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Conserved domains on  [gi|1173933921|gb|OQR85457|]
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hypothetical protein ACHHYP_11801 [Achlya hypogyna]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RING_Ubox super family cl17238
The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING ...
204-246 2.96e-14

The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well. C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC finger. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are close to RING-H2 finger. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerated RING fingers from Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16454:

Pssm-ID: 354325 [Multi-domain]  Cd Length: 43  Bit Score: 64.63  E-value: 2.96e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16454     2 CAICLEEFED-GEEVRVLPCNHLFHSNCIDPWLEQHATCPLCR 43
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
46-138 2.31e-05

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


:

Pssm-ID: 132768  Cd Length: 106  Bit Score: 41.96  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921  46 YTVYIMQI-LSSNVLWVVRHRYSALASTRALLLKTVNMVPrkdyssraavaalvepLREFPRKYLF-MDTPRVVNDRKKG 123
Cdd:cd06093    17 YVVYIIEVtTQGGEEWTVYRRYSDFEELHEKLKKKFPGVI----------------LPPLPPKKLFgNLDPEFIEERRKQ 80
                          90
                  ....*....|....*
gi 1173933921 124 LAMFVQAMFHVRDLC 138
Cdd:cd06093    81 LEQYLQSLLNHPELR 95
PEX10 super family cl27118
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
144-247 1.37e-03

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5574:

Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 39.11  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921 144 SNGENTLLLVIAKGIIEKIETTLQIPvlqkEEDHKwrlqtlamvpvepplnmaddgdrdgCSICLENLHDLgvssVQLAC 223
Cdd:COG5574   187 SNNLHTLFQVITKENLSKKNGLPFIP----LADYK-------------------------CFLCLEEPEVP----SCTPC 233
                          90       100
                  ....*....|....*....|....*.
gi 1173933921 224 SHAFHRGCVAEWLARQST--CPLCRA 247
Cdd:COG5574   234 GHLFCLSCLLISWTKKKYefCPLCRA 259
 
Name Accession Description Interval E-value
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
204-246 2.96e-14

RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3 which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer.


Pssm-ID: 319368 [Multi-domain]  Cd Length: 43  Bit Score: 64.63  E-value: 2.96e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16454     2 CAICLEEFED-GEEVRVLPCNHLFHSNCIDPWLEQHATCPLCR 43
zf-RING_2 pfam13639
Ring finger domain;
204-246 1.73e-13

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 62.80  E-value: 1.73e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:pfam13639   3 CPICLEEFEE-GDKVVILPCGHHFHRECLDKWLRSSNTCPLCR 44
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
204-245 3.38e-07

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 45.58  E-value: 3.38e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1173933921  204 CSICLENLHDlgvSSVQLACSHAFHRGCVAEWL-ARQSTCPLC 245
Cdd:smart00184   1 CPICLEEYLK---DPVILPCGHTFCRSCIRKWLeSGNNTCPIC 40
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
179-249 8.34e-07

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 49.20  E-value: 8.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921 179 WRL--QTLAMVPVEPPLNMADDgdrDG-CSICLENL---------HDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:COG5243   265 RRAtkDLNAMYPTATEEQLTNS---DRtCTICMDEMfhpdheplpRGLDMTPKRLPCGHILHLHCLKNWLERQQTCPICR 341

                  ...
gi 1173933921 247 ASL 249
Cdd:COG5243   342 RPV 344
PHA02929 PHA02929
N1R/p28-like protein; Provisional
204-246 8.69e-07

N1R/p28-like protein; Provisional


Pssm-ID: 222944  Cd Length: 238  Bit Score: 48.24  E-value: 8.69e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1173933921 204 CSICLENLHDLGVSSVQLA----CSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:PHA02929  177 CAICMEKVYDKEIKNMYFGilsnCNHVFCIECIDIWKKEKNTCPVCR 223
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
46-138 2.31e-05

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768  Cd Length: 106  Bit Score: 41.96  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921  46 YTVYIMQI-LSSNVLWVVRHRYSALASTRALLLKTVNMVPrkdyssraavaalvepLREFPRKYLF-MDTPRVVNDRKKG 123
Cdd:cd06093    17 YVVYIIEVtTQGGEEWTVYRRYSDFEELHEKLKKKFPGVI----------------LPPLPPKKLFgNLDPEFIEERRKQ 80
                          90
                  ....*....|....*
gi 1173933921 124 LAMFVQAMFHVRDLC 138
Cdd:cd06093    81 LEQYLQSLLNHPELR 95
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
204-248 3.84e-04

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 40.76  E-value: 3.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSIClenlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCRAS 248
Cdd:TIGR00599  29 CHIC----KDFFDVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAE 69
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
144-247 1.37e-03

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 39.11  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921 144 SNGENTLLLVIAKGIIEKIETTLQIPvlqkEEDHKwrlqtlamvpvepplnmaddgdrdgCSICLENLHDLgvssVQLAC 223
Cdd:COG5574   187 SNNLHTLFQVITKENLSKKNGLPFIP----LADYK-------------------------CFLCLEEPEVP----SCTPC 233
                          90       100
                  ....*....|....*....|....*.
gi 1173933921 224 SHAFHRGCVAEWLARQST--CPLCRA 247
Cdd:COG5574   234 GHLFCLSCLLISWTKKKYefCPLCRA 259
 
Name Accession Description Interval E-value
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
204-246 2.96e-14

RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3 which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer.


Pssm-ID: 319368 [Multi-domain]  Cd Length: 43  Bit Score: 64.63  E-value: 2.96e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16454     2 CAICLEEFED-GEEVRVLPCNHLFHSNCIDPWLEQHATCPLCR 43
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
204-246 5.62e-14

RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar proteins; TTC3, also known as protein DCRR1, or TPR repeat protein D, or TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. TTC3 contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.TTC3, also known as protein DCRR1, TPR repeat protein D, TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It also affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. TTC3 contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.


Pssm-ID: 319395 [Multi-domain]  Cd Length: 42  Bit Score: 63.91  E-value: 5.62e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLGVSsvQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16481     2 CSICHEELKPGTVR--KLDCGHRFHKGCIRQWLKEQSTCPTCR 42
zf-RING_2 pfam13639
Ring finger domain;
204-246 1.73e-13

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 62.80  E-value: 1.73e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:pfam13639   3 CPICLEEFEE-GDKVVILPCGHHFHRECLDKWLRSSNTCPLCR 44
RING-H2 cd16448
H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of ...
204-246 3.20e-12

H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well. This family corresponds to H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319362 [Multi-domain]  Cd Length: 44  Bit Score: 59.39  E-value: 3.20e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDLGVSSVQLACSHAFHRGCVAEWLARQS-TCPLCR 246
Cdd:cd16448     1 CAICLEEFEEGDCPVRLLPCGHVFHKSCIDKWLESGNrTCPLCR 44
RING-H2_RNF126_like cd16667
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; ...
204-246 6.22e-11

RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; The family includes RING finger proteins RNF126, RNF115, and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. RNF115 and RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319581 [Multi-domain]  Cd Length: 43  Bit Score: 55.79  E-value: 6.22e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLhDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16667     2 CAVCKEDF-KVGEKVRQLPCNHVFHPDCIVPWLEQHNTCPVCR 43
zf-rbx1 pfam12678
RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be ...
202-246 8.55e-11

RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be the conserved residues involved in zinc binding. The protein, of which this domain is the conserved region, participates in diverse functions relevant to chromosome metabolism and cell cycle control.


Pssm-ID: 315369 [Multi-domain]  Cd Length: 55  Bit Score: 55.78  E-value: 8.55e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1173933921 202 DGCSICLENLHDL----------GVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:pfam12678   1 DTCAICRNPFEEPcpecqapgddECPVVWGECGHAFHLHCISRWLKTNNTCPLCR 55
RING-H2_EL5_like cd16461
RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; ...
204-246 5.51e-10

RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; EL5, also known as protein ELICITOR 5, is an E3 ubiquitin-protein ligase containing an N-terminal transmembrane domain and a C3H2C3-type RING-H2 finger that is a binding site for ubiquitin-conjugating enzyme (E2). It can be rapidly induced by N-acetylchitooligosaccharide elicitor. EL5 catalyzes polyubiquitination via the Lys48 residue of ubiquitin, and thus plays a crucial role as a membrane-anchored E3 in the maintenance of cell viability after the initiation of root primordial formation in rice. It also acts as an anti-cell death enzyme that might be responsible for mediating the degradation of cytotoxic proteins produced in root cells after the actions of phytohormones. Moreover, EL5 interacts with UBC5b, a rice ubiquitin carrier protein, through its RING-H2 finger. EL5 is an unstable protein, and its degradation is regulated by the C3H2C3-type RING-H2 finger in a proteasome-independent manner.


Pssm-ID: 319375 [Multi-domain]  Cd Length: 43  Bit Score: 53.08  E-value: 5.51e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16461     2 CPICLEDFED-GELVRLLKCGHVFHKECIDLWLRSHSTCPLCR 43
RING-HC_RNFT1_like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
204-246 6.60e-10

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 319446 [Multi-domain]  Cd Length: 40  Bit Score: 53.06  E-value: 6.60e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16532     2 CPICQDEFKD----PIKLRCKHIFCEDCVSEWFDRERTCPLCR 40
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
202-249 1.91e-09

RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR, also known as AMF receptor, or RING finger protein 45, or ER-protein gp78, is an internalizing cell surface glycoprotein localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). It is involved in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. AMFR also functions as a RING finger-dependent ubiquitin protein ligase (E3) implicated in degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain.


Pssm-ID: 319369 [Multi-domain]  Cd Length: 44  Bit Score: 51.60  E-value: 1.91e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1173933921 202 DGCSICLENLHdlgvSSVQLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16455     1 DDCAICWESMQ----TARKLPCGHLFHNSCLRSWLEQDTSCPTCRRSL 44
RING-H2_RNF215 cd16670
RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This ...
202-249 2.38e-09

RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This family includes uncharacterized protein RNF215 and similar proteins. Although its biological function remains unclear, RNF215 shares high sequence similarity with PA-TM-RING ubiquitin ligases, which have been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain.


Pssm-ID: 319584 [Multi-domain]  Cd Length: 50  Bit Score: 51.82  E-value: 2.38e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1173933921 202 DGCSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16670     1 ESCAVCLDQFHKNQCLRV-LPCLHEFHRDCVDPWLLLQQTCPLCKRNV 47
RING-H2_RNF145 cd16684
RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; ...
202-245 2.44e-09

RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; RNF145 is an uncharacterized RING finger protein encoded by RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139, an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. Like RNF139, RNF145 contains a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 319598 [Multi-domain]  Cd Length: 43  Bit Score: 51.60  E-value: 2.44e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 202 DGCSICLENLHdlgvSSVQLACSHAFHRGCVAEWLARQSTCPLC 245
Cdd:cd16684     3 DICSICYQDMK----SAVITPCSHFFHAGCLKKWLYVQETCPLC 42
RING-H2_RNF126 cd16801
RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; ...
204-246 2.66e-09

RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). Moreover, RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. In addition, RNF126 and the related protein, RNF115 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF126 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319715 [Multi-domain]  Cd Length: 44  Bit Score: 51.49  E-value: 2.66e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16801     2 CPVCKED-YAVGENVRQLPCNHLFHNDCIVPWLEQHDTCPVCR 43
RING-H2_RNF24_like cd16469
RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; ...
202-249 3.46e-09

RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; The family includes RNF24, RNF122, and similar proteins. RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, ?3, ?4, ?5, ?6, and ?7, and affects TRPC intracellular trafficking without affecting their activity. RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergoes degradation through its RING finger in a proteasome-dependent manner. Both RNF24 and RNF122 contain an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319383 [Multi-domain]  Cd Length: 47  Bit Score: 51.30  E-value: 3.46e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1173933921 202 DGCSICLE---NLHDLGVssvqLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16469     1 DTCAVCLEdfkKKEELGV----CPCGHAFHRKCLLKWLEVRNVCPMCNSPV 47
RING-H2_RNF111_like cd16474
RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; ...
204-246 4.17e-09

RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; The family includes RING finger proteins RNF111, RNF165, and similar proteins. RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It also interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. The N-terminal half of RNF111 harbors three SUMO-interacting motifs (SIMs). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). RNF165, also known as Arkadia-like 2, or Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It thus acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. Both RNF165 and RNF111 contain a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319388 [Multi-domain]  Cd Length: 46  Bit Score: 50.77  E-value: 4.17e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16474     3 CTICLSEFED-GEEVRRLPCMHLFHQACVDQWLATNKRCPICR 44
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
204-246 4.48e-09

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated- (FHA) and a C3HC4-type RING-HC finger.


Pssm-ID: 319417 [Multi-domain]  Cd Length: 44  Bit Score: 50.87  E-value: 4.48e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlgVSSVQlACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16503     5 CSICQDLLHD--CVSLQ-PCMHNFCAGCYSEWMERSSLCPQCR 44
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
204-246 5.60e-09

RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; RNF151 is a testis-specific RING finger protein that interacts with dysbindin, a synaptic and microtubular protein that binds brain snapin, a SNARE-binding protein that mediated intracellular membrane fusion in both neuronal and non-neuronal cells. Thus, it may be involved in acrosome formation of spermatids through interacting with multiple proteins participating in membrane biogenesis and microtubule organization. RNF151 contains a C3HC4-type RING finger domain, a putative nuclear localization signal (NLS), and a TNF receptor associated factor (TRAF)-type zinc finger domain.


Pssm-ID: 319461 [Multi-domain]  Cd Length: 39  Bit Score: 50.59  E-value: 5.60e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSIClenlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16547     1 CSIC----HGVLKCPYMLPCSHIFCKKCILQWLKRQETCPCCR 39
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
202-246 5.92e-09

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting the crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, Synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, Synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of Synoviolin may represent a protective response against neurodegeneration in Parkinson"s disease (PD). In addition, Synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 319393 [Multi-domain]  Cd Length: 43  Bit Score: 50.37  E-value: 5.92e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 202 DGCSICLEnlhDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16479     2 DTCIICRE---EMVSGAKKLPCGHIFHLSCLRSWLQRQQTCPTCR 43
RING-H2_RNF6 cd16673
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 ...
204-246 8.03e-09

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity through modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Moreover, RNF6 regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 also binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. Furthermore, RNF6 acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF6 contains an N-terminal coiled-coil domain, a Lys-X-X-Leu/Ile-X-X-Leu/Ile (KIL) motif, and a C-terminal C3H2C3-type RING-H2 finger which is responsible for its ubiquitin ligase activity. The KIL motif is present in a subset of RING-H2 proteins from organisms as evolutionarily diverse as human, mouse, chicken, Drosophila, Caenorhabditis elegans, and Arabidopsis thaliana.


Pssm-ID: 319587 [Multi-domain]  Cd Length: 45  Bit Score: 50.02  E-value: 8.03e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLeNLHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16673     3 CSVCI-NEYATGNKLRRLPCAHEFHIHCIDRWLSENSTCPICR 44
RING-H2_RNF181 cd16669
RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; ...
204-249 9.16e-09

RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; RNF181, also known as HSPC238, is a platelet E3 ubiquitin-protein ligase containing a C3H2C3-type RING-H2 finger. It interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3, suggesting a role for RNF181-mediated ubiquitination in integrin and platelet signaling. It also suppresses the tumorigenesis of hepatocellular carcinoma (HCC) through the inhibition of extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) signaling in the liver.


Pssm-ID: 319583 [Multi-domain]  Cd Length: 46  Bit Score: 50.06  E-value: 9.16e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLhDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16669     2 CPVCLLEF-EEGEEVKEMPCKHSFHSGCILPWLKKTNSCPLCRHEL 46
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
202-246 1.02e-08

RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It ubiquitinates GluA2 and regulates its surface expression, and thus acts as a selective regulator of AMPAR-mediated neurotransmission. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. RNF167 is widely conserved in metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, two transmembrane domains (TM1 and TM2), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319711 [Multi-domain]  Cd Length: 46  Bit Score: 50.04  E-value: 1.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 202 DGCSICLENLHDlGVSSVQLACSHAFHRGCVAEWLAR-QSTCPLCR 246
Cdd:cd16797     1 DVCAICLDEYEE-GDKLRVLPCSHAYHSKCVDPWLTQtKKTCPVCK 45
RING-H2_RNF43 cd16798
RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 ...
204-245 1.09e-08

RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 is a transmembrane E3 ubiquitin-protein ligase that plays an important role in frizzled-dependent regulation of the Wnt/beta-catenin pathway. It functions as a tumor suppressor that inhibits Wnt/beta-catenin signaling by ubiquitinating Frizzled receptor and targeting it to the lysosomal pathway for degradation. miR-550a-5p directly targeted the 3?-UTR of gene RNF43 and regulated its expression. Moreover, RNF43 interacts with NEDD-4-like ubiquitin-protein ligase-1 (NEDL1) and regulates p53-mediated transcription. It may also be involved in cell growth control potentially through the interaction with HAP95, a chromatin-associated protein interfacing the nuclear envelope. Mutations of RNF43 have been identified in various tumors, including colorectal cancer (CRC), endometrial cancer, mucinous ovarian tumors, gastric adenocarcinoma, pancreatic ductal adenocarcinoma, liver fluke-associated cholangiocarcinoma, hepatocellular carcinoma, and glioma. RNF43 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region.


Pssm-ID: 319712 [Multi-domain]  Cd Length: 47  Bit Score: 49.94  E-value: 1.09e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLC 245
Cdd:cd16798     3 CAICLEEFSE-GQELRIISCAHEFHRECVDPWLHQHRTCPLC 43
RING-H2_RNF115 cd16800
RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; ...
204-249 1.92e-08

RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. Furthermore, RNF115 and the related protein, RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF115 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319714 [Multi-domain]  Cd Length: 47  Bit Score: 49.22  E-value: 1.92e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16800     3 CPVCKED-YTVEEQVRQLPCNHFFHSDCIVPWLELHDTCPVCRKSL 47
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
204-246 2.07e-08

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 319449 [Multi-domain]  Cd Length: 42  Bit Score: 48.96  E-value: 2.07e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLEnlhdLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16535     4 CSICSE----LFIEAVTLNCSHSFCSYCITEWMKRKKECPICR 42
RING1-H2_RNF32 cd16677
RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
204-246 2.35e-08

RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, the protein with double RING-H2 fingers may act as a scaffold for binding several proteins that function in the same pathway. This family corresponds to the first RING-H2 finger.


Pssm-ID: 319591 [Multi-domain]  Cd Length: 44  Bit Score: 48.86  E-value: 2.35e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLEnlhDLGVSS-VQLACSHAFHRGCVA--EWLARQSTCPLCR 246
Cdd:cd16677     2 CVICKE---DFGLQQqVLLSCSHVFHRACLEsfERFSGKKTCPMCR 44
RING-H2_RNF43_like cd16666
RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; ...
204-246 2.56e-08

RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; RNF43 and ZNRF3 (also known as RNF203) are transmembrane E3 ubiquitin-protein ligases that belong to the PA-TM-RING ubiquitin ligases family, which has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region. Both RNF43 and RNF203 function as tumor suppressors involved in the regulation of Wnt/beta-catenin signaling. They negatively regulate Wnt signaling through interacting with complexes of frizzled receptors (FZD) and low-density lipoprotein receptor-related protein (LRP) 5/6, which leads to ubiquitination of Frizzled receptors (FZD) and endocytosis of the Wnt receptor. Dishevelled (DVL), a positive Wnt regulator, is required for ZNRF3/RNF43-mediated ubiquitination and degradation of FZD. They also associate with R-spondin 1 (RSPO1). This interaction may block Frizzled ubiquitination and enhances Wnt signaling.


Pssm-ID: 319580 [Multi-domain]  Cd Length: 45  Bit Score: 48.59  E-value: 2.56e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16666     2 CAICLEEFKDGQELRV-LPCSHEFHRHCVDPWLLQNRTCPLCL 43
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
204-246 2.68e-08

RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) and similar proteins; DZIP3, also known as RNA-binding ubiquitin ligase of 138 kDa (RUL138) or 2A-HUB protein, is an RNA-binding E3 ubiquitin-protein ligase that interacts with coactivator-associated arginine methyltransferase 1 (CARM1) and acts as a transcriptional coactivator of estrogen receptor (ER) alpha. It is also a histone H2A ubiquitin ligase that catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatoric component of the repression machinery required for repressing a specific chemokine gene expression program, critically modulating migratory responses to Toll-like receptors (TLR) activation. DZIP3 contains a C3H2C3-type RING-H2 finger at the C-terminus.


Pssm-ID: 319374 [Multi-domain]  Cd Length: 43  Bit Score: 48.48  E-value: 2.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLGVSSvqLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16460     3 CVICHENLSPENLSV--LPCAHKFHSQCIRPWLMQQRTCPTCR 43
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
202-249 3.36e-08

RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL). It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF130 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319717 [Multi-domain]  Cd Length: 49  Bit Score: 48.43  E-value: 3.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1173933921 202 DGCSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16803     1 DHCAVCIEGYKQNDVVRI-LPCKHVFHKSCVDPWLNEHCTCPMCKLNI 47
RING-H2_PJA1_2 cd16465
RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and ...
204-249 5.56e-08

RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and similar proteins; The family includes two highly similar E3 ubiquitin-protein ligases Praja-1 and Praja-2. Praja-1, also known as RING finger protein 70, is a RING-H2 finger ubiquitin ligase encoded by gene PJA1, a novel human X chromosome gene abundantly expressed in brain. It has been implicated in bone and liver development, as well as memory formation and X-linked mental retardation (MRX). Praja-1 interacts with and activates the ubiquitin-conjugating enzyme UbcH5B, and shows E2-dependent E3 ubiquitin ligase activity. It is a 3-deazaneplanocin A (DZNep)-induced ubiquitin ligase that directly ubiquitinates individual polycomb repressive complex 2 (PRC2) subunits in a cell free system, which leads to their proteasomal degradation. It also plays an important role in neuronal plasticity, which is the basis for learning and memory. Moreover, Praja-1 ubiquitinates embryonic liver fodrin (ELF) and Smad3, but not Smad4, in a transforming growth factor-beta (TGF-beta)-dependent manner. It controls ELF abundance through ubiquitin-mediated degradation, and further regulates TGF-beta signaling, which plays a key role in the suppression of gastric carcinoma. Furthermore, Praja-1 regulates the transcription function of the homeodomain protein Dlx5 by controlling the stability of the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1, via an ubiquitin-dependent degradation pathway. Praja-2, also known as RING finger protein 131, or NEURODAP1, or KIAA0438, is an E2-dependent E3 ubiquitin ligase that interacts with and activates the ubiquitin-conjugating enzyme UbcH5B. It functions as an A-kinase anchoring protein (AKAP)-like E3 ubiquitin ligase that plays a critical role in controlling cyclic AMP (cAMP) dependent PKA activity and pro-survival signaling, and further promotes cell proliferation and growth. Praja-2 is also involved in protein sorting at the postsynaptic density region of axosomatic synapses and possibly plays a role in synaptic communication and plasticity. Moreover, Praja-2, together with the AMPK-related kinase SIK2 and the CDK5 activator CDK5R1/p35, forms a SIK2-p35-PJA2 complex that plays an essential role for glucose homeostasis in pancreatic beta cell functional compensation. Furthermore, Praja-2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumor-suppressor Hippo signaling. Both Praja-1 and Praja-2 contain a potential nuclear localization signal (NLS) and a C-terminal C3H2C3-type RING-H2 motif.


Pssm-ID: 319379 [Multi-domain]  Cd Length: 46  Bit Score: 47.76  E-value: 5.56e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16465     2 CPICCCE-YVKDEIATELPCHHLFHKLCITAWLQKSGTCPVCRHVL 46
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
204-246 6.83e-08

RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger.


Pssm-ID: 319371 [Multi-domain]  Cd Length: 44  Bit Score: 47.66  E-value: 6.83e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLGVSSVQLACSHAFHRGCVAEWlaRQSTCPLCR 246
Cdd:cd16457     3 CPVCLERMDESVSGILTILCNHSFHCDCLKRW--GDSTCPVCR 43
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
204-246 9.45e-08

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1, or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway through interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319387 [Multi-domain]  Cd Length: 46  Bit Score: 47.29  E-value: 9.45e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENlHDLGVSSVQLACSHAFHRGCVAEWLARQS-TCPLCR 246
Cdd:cd16473     2 CVICLEN-YEEGCLLCGLPCGHVFHQNCIDVWLTRDNhCCPVCR 44
RING-H2_GRAIL cd16668
RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL ...
204-247 1.17e-07

RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL transmembrane proteins family includes RING finger proteins RNF128 (also known as GRAIL), RNF130, RNF133, RNF148, RNF149, and RNF150, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF128 is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128. It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression regulated by histone deacetylases. RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that induces the ubiquitination of wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF) and promotes its proteasome-dependent degradation. RNF150 is a RING finger protein that its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. The family also includes Drosophila melanogaster protein goliath (d-goliath), also known as protein g1, which is one of the funding members of the family. It was originally identified as a transcription factor involved in the embryo mesoderm formation.


Pssm-ID: 319582 [Multi-domain]  Cd Length: 48  Bit Score: 46.96  E-value: 1.17e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCRA 247
Cdd:cd16668     2 CAVCIEPYKPGDVVRI-LPCKHIFHKSCVDPWLLEHRTCPMCKL 44
mRING-H2-C3H2C2D_ZSWM2 cd16486
Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing ...
204-246 1.27e-07

Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins; ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3 and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It also acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination, and two modified RING-H2 fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This family corresponds to the second RING-H2 finger, which is not a canonical C3H2C3-type, but a modified C3H2C2D-type.


Pssm-ID: 319400 [Multi-domain]  Cd Length: 44  Bit Score: 46.84  E-value: 1.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHdLGVSSVQLACSHAFHRGCVAEWLARQ-STCPLCR 246
Cdd:cd16486     2 CRICLRDFQ-AGQVLRKLPCKHKFHRDCIDSWLTHSrPTCPLCG 44
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
204-247 1.27e-07

RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region , as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 319497 [Multi-domain]  Cd Length: 46  Bit Score: 46.81  E-value: 1.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQS-----TCPLCRA 247
Cdd:cd16583     2 CPICLDPLKE----PVSTTCGHVFCRGCIAQHLEKASvsgvlCCPVCRK 46
RING-H2_RNF149 cd16804
RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; ...
203-246 2.04e-07

RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that interacts with wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF), a RING domain-containing E3 ubiquitin ligase involved in control of gene transcription, translation, cytoskeletal organization, cell adhesion, and epithelial development. RNF149 induces the ubiquitination of wild-type BRAF and promotes its proteasome-dependent degradation. Mutated RNF149 has been found in some human breast, ovarian, and colorectal cancers. RNF149 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319718 [Multi-domain]  Cd Length: 48  Bit Score: 46.43  E-value: 2.04e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 203 GCSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16804     1 NCAVCIENYKPKDVVRI-LPCKHIFHRICIDPWLLEHRTCPMCK 43
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
204-246 2.67e-07

RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; RNF141, also known as zinc finger protein 230 (ZNF230), is a RING finger protein present primarily in the nuclei of spermatogonia, the acrosome, and the tail of spermatozoa. It may have a broad function during early development of vertebrates. It plays an important role in spermatogenesis, including spermatogenic cell proliferation and sperm maturation, as well as motility and fertilization. It also exhibits DNA binding activity. RNF141 corresponding ZNF230 gene mutation may be associated with azoospermia. RNF141 contains a C3HC4-type RING finger domain that may function as an activator module in transcription.


Pssm-ID: 319459 [Multi-domain]  Cd Length: 39  Bit Score: 45.86  E-value: 2.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLEnlhdlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16545     2 CCICMD-----RKPDTILPCAHSFCQKCIDKWSVRHRTCPICR 39
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
204-245 3.38e-07

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 45.58  E-value: 3.38e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1173933921  204 CSICLENLHDlgvSSVQLACSHAFHRGCVAEWL-ARQSTCPLC 245
Cdd:smart00184   1 CPICLEEYLK---DPVILPCGHTFCRSCIRKWLeSGNNTCPIC 40
RING-H2_RNF165 cd16682
RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; ...
204-249 4.47e-07

RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; RNF165, also known as Arkadia-like 2, or Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It thus acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. RNF165 contains two serine rich domains, a nuclear localization signal, a NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is responsible for the enhancement of BMP-Smad1/5/8 signaling in the spinal cord.


Pssm-ID: 319596 [Multi-domain]  Cd Length: 51  Bit Score: 45.46  E-value: 4.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16682     3 CTICLSMLED-GEDVRRLPCMHLFHQLCVDQWLAMSKKCPICRVDI 47
RING-H2_RNF12 cd16674
RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, ...
204-246 7.31e-07

RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, also known as LIM domain-interacting RING finger protein or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Its functional activity is regulated by phosphorylation-dependent nucleocytoplasmic shuttling. It is negatively regulated by pluripotency factors in embryonic stem cells. p53 represses its transcription through Sp1. RNF12 is the primary factor responsible for X chromosome inactivation (XCI) in female placental mammals. It is an indispensable factor in up-regulation of Xist transcription, thereby leading to initiation of random XCI. It also targets REX1, an inhibitor of XCI, for proteasomal degradation. Moreover, RNF12 acts as a co-regulator of a range of transcription factors, particularly those containing a LIM homeodomain, and modulates the formation of transcriptional multiprotein complexes. It is a negative regulator of Smad7, which in turn negatively regulates the type I receptors in transforming growth factor beta (TGF-beta) superfamily signaling. In addition, paternal RNF12 is a critical survival factor for milk-producing alveolar cells. RNF12 contains an nuclear localization signal (NLS) and a C3H2C3-type RING-H2 finger.


Pssm-ID: 319588 [Multi-domain]  Cd Length: 45  Bit Score: 44.67  E-value: 7.31e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16674     3 CSVCITE-YTEGNKLRKLPCSHEYHVHCIDRWLSENSTCPICR 44
RING-H2_RNF128_like cd16802
RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This ...
202-246 8.03e-07

RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This subfamily includes RING finger proteins RNF128, RNF133, RNF148, and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL), is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. It inhibits cytokine gene transcription is expressed in anergic CD4+ T cells, and has been implicated in primary T cell activation, survival, and differentiation, as well as in T cell anergy and oral tolerance. It induces T cell anergy through the ubiquitination activity of its cytosolic RING finger. It regulates expression of the costimulatory molecule CD40L on CD4 T cells, and ubiquitinates the costimulatory molecule CD40 ligand (CD40L) during the induction of T cell anergy. Moreover, RNF128 interacts with the luminal/extracellular portion of both CD151 and the related tetraspanin CD81 via its PA domain, which promoted ubiquitination of cytosolic lysine residues. It also down-modulates the expression of CD83 (previously described as a cell surface marker for mature dendritic cells) on CD4 T cells. Furthermore, Rho guanine dissociation inhibitor (RhoGDI) has been identified as a potential substrate of RNF128, suggesting a role for Rho effector molecules in T cell anergy. In addition, RNF128 plays a role in environmental stress responses. It promotes environmental salinity tolerance in euryhaline tilapia. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that is mainly present in the cytoplasm of elongated spermatids. It may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression regulated by histone deacetylases.


Pssm-ID: 319716 [Multi-domain]  Cd Length: 49  Bit Score: 44.81  E-value: 8.03e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 202 DGCSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16802     1 DSCAVCIEPYKPNDVVRI-LTCNHFFHKSCIDPWLLEHRTCPMCK 44
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
179-249 8.34e-07

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 49.20  E-value: 8.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921 179 WRL--QTLAMVPVEPPLNMADDgdrDG-CSICLENL---------HDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:COG5243   265 RRAtkDLNAMYPTATEEQLTNS---DRtCTICMDEMfhpdheplpRGLDMTPKRLPCGHILHLHCLKNWLERQQTCPICR 341

                  ...
gi 1173933921 247 ASL 249
Cdd:COG5243   342 RPV 344
RING-H2_Pirh2 cd16464
RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; ...
204-246 8.48e-07

RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; Pirh2, also known as RING finger and CHY zinc finger domain-containing protein 1 (Rchy1), androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, RING finger protein 199 (RNF199), or zinc finger protein 363 (ZNF363), is a p53 inducible E3 ubiquitin-protein ligase that functions as a negative regulator of p53. It ubiquitylates preferably the tetrameric form of p53 in vitro and in vivo, suggesting a role of Pirh2 in downregulating the transcriptionally active form of p53 in the cell. Moreover, Pirh2 inhibits p73, a homolog of the tumor suppressor p53, transcriptional activity by promoting its ubiquitination. It also monoubiquitinates DNA polymerase eta (PolH) to suppress translesion DNA synthesis. Furthermore, Pirh2 functions as a negative regulator of the cyclin-dependent kinase inhibitor p27(Kip1) function by promoting ubiquitin-dependent proteasomal degradation. In addition, Pirh2 enhances androgen receptor (AR) signaling through inhibition of histone deacetylase 1 (HDAC1) and is overexpressed in prostate cancer. Pirh2 also interacts with TIP60 and the TIP60-Pirh2 association may regulate Pirh2 stability. In addition, the oncoprotein pleomorphic adenoma gene like 2 (PLAGL2) can bind to Pirh2 dimer and therefore control the stability of Pirh2. Pirh2 contains a total of nine zinc-binding sites with six located at the N-terminal region, two in the C3H2C3-type RING-H2 domain, and one in the C-terminal region. Nine zinc binding sites comprise three different zinc coordination schemes, including RING type cross-brace zinc coordination, C4 zinc finger, and a novel left-handed beta-spiral zinc-binding motif formed by three recurrent CCHC sequence motifs.


Pssm-ID: 319378  Cd Length: 45  Bit Score: 44.49  E-value: 8.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDLGVSSVQLACSHAFHRGCVAEWLARQS-TCPLCR 246
Cdd:cd16464     2 CPVCLEDLFTSREPVHVLPCGHLMHSTCFEEYLKSGNyRCPLCS 45
PHA02929 PHA02929
N1R/p28-like protein; Provisional
204-246 8.69e-07

N1R/p28-like protein; Provisional


Pssm-ID: 222944  Cd Length: 238  Bit Score: 48.24  E-value: 8.69e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1173933921 204 CSICLENLHDLGVSSVQLA----CSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:PHA02929  177 CAICMEKVYDKEIKNMYFGilsnCNHVFCIECIDIWKKEKNTCPVCR 223
RING-HC_LNX3_like cd16512
RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; ...
204-246 9.90e-07

RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4, or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for the substrate-binding. This family corresponds to LNX3/LNX4-like proteins, which contains a typical C3HC4-type RING-HC finger and two PDZ domains.


Pssm-ID: 319426 [Multi-domain]  Cd Length: 41  Bit Score: 44.04  E-value: 9.90e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQSTCPL-CR 246
Cdd:cd16512     2 CSICLEVLED----PLTTPCGHVFCSGCILPWLVQNGSCPVkCR 41
RING-H2_RNF11 cd16468
RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 ...
204-245 1.21e-06

RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It is the downstream of an enzymatic cascade for the ubiquitination of specific substrates. It is also a molecular adaptor of homologous to E6-associated protein C-terminus (HECT)-type ligases. RNF11 has been implicated in the regulation of several signaling pathways. It enhances the transforming growth factor receptor (TGFR) signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM), a de-ubiquitinating enzyme that enhances transforming growth factor-beta (TGF-beta) signaling and epidermal growth factor receptor (EGFR) endosomal recycling. It also acts directly on Smad4 to enhance Smad4 function, and plays a role in prolonged TGF-beta signaling. Moreover, RNF11 functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation. It also interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex, thus participating in the regulation of lysosomal degradation of EGFR. Furthermore, RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family. In addition, RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi, and further restricts antiviral signaling and type I interferon (IFN)-beta production. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch, Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2), and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13.


Pssm-ID: 319382 [Multi-domain]  Cd Length: 43  Bit Score: 43.96  E-value: 1.21e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1173933921 204 CSICLENLhDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLC 245
Cdd:cd16468     2 CVICMNDF-VYGDPIRFLPCMHIYHKDCIDDWLMRSFTCPSC 42
RING-H2_RNF139 cd16683
RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins; ...
202-245 1.58e-06

RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins; RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. The mutation of RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF139 physically and functionally interacts with von Hippel-Lindau (VHL), which is part of an SCF related E3-ubiquitin ligase complex with "gatekeeper" function in renal carcinoma and is defective in most sporadic clear-cell renal cell carcinomas (ccRCC). It suppresses growth and functions with VHL in a common pathway. RNF139 also suppresses tumorigenesis through targeting heme oxygenase-1 for ubiquitination and degradation. Moreover, RNF139 is a target of Translin (TSN), a posttranscriptional regulator of genes transcribed by the transcription factor CREM-tau in postmeiotic male germ cells, suggesting a role of RNF139 in dysgerminoma. Furthermore, RNF139 physically and functionally interacts with von Hippel-Lindau (VHL), which is part of an SCF related E3-ubiquitin ligase complex with "gatekeeper" function in renal carcinoma and is defective in most sporadic clear-cell renal cell carcinomas (ccRCC). It suppresses growth and functions with VHL in a common pathway. In addition, RNF139 forms an integral part of a novel multi-protein ER complex, containing MHC I, US2, and signal peptide peptidase, which is associated with ER-associated degradation (ERAD) pathway. It is required for the ubiquitination of MHC class I molecules before dislocation from the ER. As a novel sterol-sensing ER membrane protein, RNF139 hinders sterol regulatory element-binding protein-2 (SREBP-2) processing through interaction with SREBP-2 and SREBP cleavage-activated protein (SCAP), regulating its own turnover rate via its E3 ubiquitin ligase activity. RNF139 shows two regions of similarity with the receptor for sonic hedgehog (SHH), Patched. The first region corresponds to the second extracellular domain of Patched, which is involved in binding SHH. The second region is a putative sterol-sensing domain (SSD). In addition, the C-terminal half of RNF139 contains a C3H2C3-type RING-H2 finger with E3-ubiquitin ligase activity in vitro.


Pssm-ID: 319597 [Multi-domain]  Cd Length: 42  Bit Score: 43.83  E-value: 1.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 202 DGCSICLenlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLC 245
Cdd:cd16683     1 DVCAICY---QEFTTSARITPCNHYFHALCLRKWLYIQDTCPMC 41
RING-H2_RNF6_like cd16467
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar ...
204-246 1.68e-06

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity through modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Moreover, RNF6 regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 also binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. Furthermore, RNF6 acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF12, also known as LIM domain-interacting RING finger protein, or RING finger LIM domain-binding protein (R-LIM), is E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Both RNF6 and RNF12 contain a well conserved C3H2C3-type RING-H2 finger.


Pssm-ID: 319381 [Multi-domain]  Cd Length: 43  Bit Score: 43.66  E-value: 1.68e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16467     2 CSVCISE-YVTGNKLRKLPCSHEFHVHCIDRWLSENSTCPICR 43
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
204-246 1.77e-06

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 319488 [Multi-domain]  Cd Length: 40  Bit Score: 43.39  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLGVSSVqlaCSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16574     1 CPICLGEFENKSFLDS---CFHSFCFGCILEWSKVKAECPLCK 40
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
204-246 1.78e-06

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, or HIP116, or RING finger protein 80, or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 319423 [Multi-domain]  Cd Length: 43  Bit Score: 43.44  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLAR--QSTCPLCR 246
Cdd:cd16509     3 CPICLDSLKD----PVITPCAHVFCRGCIEQVIQRepNAKCPLCR 43
RING-H2_RNF32 cd16471
RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 ...
204-246 1.83e-06

RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, the protein with double RING-H2 fingers may act as a scaffold for binding several proteins that function in the same pathway.


Pssm-ID: 319385 [Multi-domain]  Cd Length: 49  Bit Score: 43.75  E-value: 1.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1173933921 204 CSICLENLHDlgVSSVQLACSHAFHRGCVAEWLA-------RQSTCPLCR 246
Cdd:cd16471     2 CPICLEEFDQ--DSQARLSCSHVFHQACFLSYLAyshservSQTQCPMCR 49
RING-H2_ZNRF3 cd16799
RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ...
204-246 2.03e-06

RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ZNRF3, also known as RING finger protein 203 (RNF203), is a homolog of Ring finger protein 43 (RNF43). It is a transmembrane E3 ubiquitin-protein ligase that is associated with the Wnt receptor complex, and negatively regulates Wnt signaling by promoting the turnover of frizzled and lipoprotein receptor-related protein LRP6 in an R-spondin-sensitive manner. It inhibits gastric cancer cell growth and promotes the cell apoptosis by affecting the Wnt/beta-catenin/TCF signaling pathway. ZNRF3 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region.


Pssm-ID: 319713 [Multi-domain]  Cd Length: 45  Bit Score: 43.48  E-value: 2.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16799     2 CAICLEKYID-GEELRVIPCTHRFHKKCVDPWLLQHHTCPHCR 43
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
200-246 2.08e-06

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 319364 [Multi-domain]  Cd Length: 49  Bit Score: 43.42  E-value: 2.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1173933921 200 DRDGCSICLENLHDLG---VSSvqLACSHAFHRGCVAEWLARQ-STCPLCR 246
Cdd:cd16450     1 EGDTCPICFEPWTNSGshrLCS--LKCGHLFGRSCIEKWLKGQgGKCPQCN 49
RING-H2_RNF139_like cd16476
RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; ...
202-245 2.55e-06

RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. The mutation of RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF145 is an uncharacterized RING finger protein encoded by RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139. Both RNF139 and RNF145 contain a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 319390 [Multi-domain]  Cd Length: 41  Bit Score: 43.23  E-value: 2.55e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 202 DGCSICLENLHDLGVSSvqlaCSHAFHRGCVAEWLARQSTCPLC 245
Cdd:cd16476     1 DVCAICYQEMKNARITP----CQHYFHGVCLRKWLYVQDRCPLC 40
mRING-H2-C3H2C2D_RBX1 cd16485
modified RING finger, H2 subclass (C3H2C2D-type), found in RING-box protein 1 (RBX1) and ...
202-245 3.83e-06

modified RING finger, H2 subclass (C3H2C2D-type), found in RING-box protein 1 (RBX1) and similar proteins; RBX1, also known as Hrt1, protein ZYP, RING finger protein 75 (RNF75), or regulator of cullins 1 (ROC1), is an E3 ubiquitin-protein ligase necessary for ubiquitin ligation activity of the multimeric cullin (Cul)-RING E3 ligases (CRLs). RBX1-containing CRLs are involved in NEDD8 pathway and RBX1 specifically regulate NEDD8ylation of Cul1-4. It can also bind and activate HIV-1 Vif-Cullin5 E3 ligase complex in vitro. Moreover, RBX1 is an essential element of Skp1/Cullins/F-box (SCF) E3-ubiquitin ligase complex that targets diverse proteins for proteasome-mediated degradation. It is a direct functional target of miR-194 and plays an important role in proliferation and migration of gastric cancer (GC) cells. RBX1 is also an essential component of KEAP1/CUL3/RBX1 E3-ubiquitin ligase complex that functions as a regulator of NFE2-related factor 2 (NRF2) and plays a key role in NRF2 pathway deregulation in multiple tumor types, including ovarian carcinomas (OVCA) and papillary thyroid carcinoma (PTC). Furthermore, RBX1 associates with DDB1, Cul4A, and Fbxw5 to form the Fbxw5-DDB1-Cul4A-Rbx1 complex that may function as a dual SUMO/ubiquitin ligase suppressing c-Myb activity through sumoylation or ubiquitination. RBX1 contains a C-terminal modified RING-H2 finger that is C3H2C2D-type, rather than the canonical C3H2C3-type. The modified RING-H2 finger is essential for its ligase activity.


Pssm-ID: 319399 [Multi-domain]  Cd Length: 62  Bit Score: 43.13  E-value: 3.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1173933921 202 DGCSICLENLHDLGV-------SSVQLACS-------HAFHRGCVAEWLARQSTCPLC 245
Cdd:cd16485     1 DNCAICRNHIMDLCIecqanqaSATSEECTvawgvcnHAFHFHCISRWLKTRQVCPLD 58
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
204-246 4.91e-06

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 319655 [Multi-domain]  Cd Length: 40  Bit Score: 42.23  E-value: 4.91e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16741     2 CPICQAEFQK----PILLICQHIFCEECISLWFNREKTCPLCR 40
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
204-249 5.04e-06

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 46.53  E-value: 5.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQS-TCPLCRASL 249
Cdd:COG5540   326 CAICMSNFIK-NDRLRVLPCDHRFHVGCVDKWLLGYSnKCPVCRTAI 371
RING-H2_RNF13_like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
202-246 5.25e-06

RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins; This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA; also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, induces calnexin ubiquitination, and p97-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin turnover. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and involved in spermatogenesis.


Pssm-ID: 319579 [Multi-domain]  Cd Length: 46  Bit Score: 42.39  E-value: 5.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 202 DGCSICLENLHDlGVSSVQLACSHAFHRGCVAEWLAR-QSTCPLCR 246
Cdd:cd16665     1 DVCAICLDDYEE-GDKLRILPCSHAYHCKCIDPWLTQnRRTCPVCK 45
RING-H2_APC11 cd16456
RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar ...
222-247 6.82e-06

RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar proteins; APC11, also known as cyclosome subunit 11, or hepatocellular carcinoma-associated RING finger protein, is a C3H2C3-type RING-H2 protein that facilitates ubiquitin chain formation by recruiting ubiquitin-charged ubiquitin conjugating enzymes (E2) through its RING-H2 domain. APC11 and its partner the cullin-like subunit APC2 form the dynamic catalytic core of the gigantic, multisubunit 1.2-MDa anaphase-promoting complex/cyclosome (APC), also known as the cyclosome, which is a ubiquitin-protein ligase (E3) composed of at least 12 subunits and controls cell division by ubiquitinating cell cycle regulators, such as cyclin B and securin, to drive their timely degradation. APC11 can be inhibited by hydrogen peroxide, which may contributes to the delay in cell cycle progression through mitosis that is characteristic of cells subjected to oxidative stress. APC11 contains a canonical RING-H2-finger domain, which includes one histidine and seven cysteine residues that coordinate two Zn2+ ions. In addition, it contains a third Zn2+-binding site and the third Zn2+ ion is not essential for its ligase activity.


Pssm-ID: 319370 [Multi-domain]  Cd Length: 63  Bit Score: 42.26  E-value: 6.82e-06
                          10        20
                  ....*....|....*....|....*....
gi 1173933921 222 ACSHAFHRGCVAEWLARQST---CPLCRA 247
Cdd:cd16456    31 KCSHAFHMHCILKWLNSQQVqqqCPMCRQ 59
RING-H2_RNF122 cd16676
RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; ...
204-245 7.20e-06

RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergoes degradation through its RING finger in a proteasome-dependent manner. It interacts with calcium-modulating cyclophilin ligand (CAML), which is not a substrate, but a stabilizer of RNF122. RNF122 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319590 [Multi-domain]  Cd Length: 47  Bit Score: 41.93  E-value: 7.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENL---HDLGVssvqLACSHAFHRGCVAEWLARQSTCPLC 245
Cdd:cd16676     3 CAVCLEDFkvkDELGV----LPCQHAFHRKCLVKWLEVRCVCPMC 43
RING-HC_RNF219 cd16562
RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; ...
204-246 8.03e-06

RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; RNF219 may function as a modulator of late-onset Alzheimer"s disease (LOAD) associated amyloid beta A4 precursor protein (APP) endocytosis and metabolism. It genetically interacts with apolipoprotein E epsilon4 allele (APOE4). Thus a genetic variant within RNF219 was found to affect amyloid deposition in human brain and LOAD age-of-onset. Moreover, common genetic variants at the RNF219 locus had been associated with alternations in lipid metabolism, cognitive performance and central nervous system ventricle volume. RNF219 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319476 [Multi-domain]  Cd Length: 42  Bit Score: 41.59  E-value: 8.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16562     4 CHICLGKVKQ----PVICPNNHVFCSSCMDLWLKRNNQCPACR 42
RING-H2_RNF111 cd16681
RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; ...
204-246 8.43e-06

RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It acts as an amplifier of Nodal signals, and enhances the dorsalizing activity of limiting amounts of Xnr1, a Nodal homolog, and requires Nodal signaling for its function. The loss of RNF111 results in early embryonic lethality, with defects attributed to compromised Nodal signaling. Moreover, RNF111 regulates tumor metastasis by modulation of the TGF-beta pathway. Its ubiquitination can be modulated by the four and a half LIM-only protein 2 (FHL2) that activates TGF-beta signal transduction. Furthermore, RNF111 interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. In addition, RNF111 has been identified as a small ubiquitin-like modifier (SUMO)-binding protein with clustered SUMO-interacting motifs (SIMs) that together form a SUMO-binding domain (SBD). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). The N-terminal half of RNF111 harbors three SIMs. Its C-terminal half show high sequence similarity with RING finger protein 165 (RNF165), where it contains two serine rich domains, two nuclear localization signals, a NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is required for polyubiqutination and proteasome-dependent degradation of phosphorylated forms of Smad2/3 and three major negative regulators of TGF-beta signaling, Smad7, SnoN and c-Ski.


Pssm-ID: 319595 [Multi-domain]  Cd Length: 46  Bit Score: 41.99  E-value: 8.43e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16681     3 CTICLSILEE-GEDVRRLPCMHLFHQVCVDQWLITNKKCPICR 44
RING-H2_RNF121_like cd16475
RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; ...
204-246 9.02e-06

RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; The family includes RNF121, RNF175 and similar proteins. RNF121 is an E3-ubiquitin ligase present in the endoplasmic reticulum (ER) and cis-Golgi compartments. It is a novel regulator of apoptosis. It also facilitates the degradation and membrane localization of voltage-gated sodium (NaV) channels, and thus plays a role in the quality control of NaV channels during their synthesis and subsequent transport to the membrane. Moreover, RNF121 acts as a broad regulator of nuclear factor kappaB (NF-kappaB) signaling since its silencing also dampens NF-kappaB activation following stimulation of toll-like receptors (TLRs), nod-like receptors (NLRs), RIG-I-like Receptors (RLRs) or after DNA damages. RNF121 contains five conserved transmembrane (TM) domains and a C3H2C2-type RING-H2 finger. RNF175 is an uncharacterized RING finger protein that shows high sequence similarity with RNF121. This family also includes Arabidopsis RING finger E3 ligase RHA2A, RHA2B, and their homologs. RHA2A is a novel positive regulator of abscisic acid (ABA) signaling during seed germination and early seedling development. RHA2B may play a role in the ubiquitin-dependent proteolysis pathway that respond to proteasome inhibition. All family members contain a C3H2C3-type RING-H2 finger, which is responsible for E3-ubiquitin ligase activity.


Pssm-ID: 319389 [Multi-domain]  Cd Length: 55  Bit Score: 41.89  E-value: 9.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1173933921 204 CSICLENL------HDLGVSSVQLACSHAFHRGCVAEW--LARQSTCPLCR 246
Cdd:cd16475     3 CAICGQELdvddneEGIIEKTYQLSCGHVFHEFCIRGWciVGKKQTCPYCK 53
RING-H2_RNF150 cd16805
RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; ...
202-249 1.11e-05

RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; RNF150 is a RING finger protein that its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. Further studies with larger numbers of participants worldwide are needed for validation of the relationships between RNF150 genetic variants and the pathogenesis of COPD. RNF150 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319719 [Multi-domain]  Cd Length: 49  Bit Score: 41.55  E-value: 1.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1173933921 202 DGCSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16805     1 DNCAVCIEGYKPNDVVRI-LPCRHLFHKSCVDPWLLDHRTCPMCKMNI 47
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
223-246 1.13e-05

Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation protein-1 (Nrdp1) and similar proteins; Nrdp1 (referred to as FLRF in mice), also known as RING finger protein 41 (RNF41), is an E3 ubiquitin-protein ligase that plays a critical role in the regulation of cell growth and apoptosis, inflammation and production of reactive oxygen species (ROS), as well as in doxorubicin (DOX)-induced cardiac injury. It promoten and degradation of the epidermal growth factor receptor (EGFR/ErbB) family member, ErbB3, which is independent of growth factor stimulation. It also promotes M2 macrophage polarization by ubiquitinating and activating transcription factor CCAAT/enhancer-binding Protein beta (C/EBPbeta) via Lys-63-linked ubiquitination. Moreover, Nrdp1 interacts with and modulates activity of Parkin, a causative protein for early onset recessive juvenile parkinsonism (AR-JP). It also interacts with ubiquitin-specific protease 8 (USP8), which is involved in trafficking of various transmembrane proteins. Furthermore, Nrdp1 inhibits basal lysosomal degradation and enhances ectodomain shedding of JAK2-associated cytokine receptors. Its phosphorylation by the kinase Par-1b (also known as MARK2) is required for epithelial cell polarity. Nrdp1 contains an N-terminal modified C3HC3D-type RING-HC finger required for enhancing ErbB3 degradation, a B-box, a coiled-coil domain responsible for Nrdp1 oligomerization, and a C-terminal ErbB3-binding domain.


Pssm-ID: 319548 [Multi-domain]  Cd Length: 43  Bit Score: 41.26  E-value: 1.13e-05
                          10        20
                  ....*....|....*....|....
gi 1173933921 223 CSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16634    20 CEHAFCNACITEWLSRQQTCPVDR 43
RING2-H2_RNF32 cd16678
RING finger 2, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
204-247 1.22e-05

RING finger 2, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, the protein with double RING-H2 fingers may act as a scaffold for binding several proteins that function in the same pathway. This family corresponds to the second RING-H2 finger.


Pssm-ID: 319592 [Multi-domain]  Cd Length: 60  Bit Score: 41.60  E-value: 1.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1173933921 204 CSICLENLHDLGVSSVQ---------LACSHAFHRGCVAEW----LARQSTCPLCRA 247
Cdd:cd16678     2 CPICLMPLSSSSLSTVAgglsrktvlLSCSHVFHATCLQAFeefsEGEKNVCPVCRS 58
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
204-245 1.24e-05

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 333836 [Multi-domain]  Cd Length: 40  Bit Score: 41.19  E-value: 1.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLgvsSVQLACSHAFHRGCVAEWL-ARQSTCPLC 245
Cdd:pfam00097   1 CPICLEEPKDP---VTILPCGHLFCSKCILSWLeSGNVTCPLC 40
RING-H2_RNF38_like cd16472
RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; ...
203-246 1.35e-05

RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; The family includes RING finger proteins RNF38, RNF44, and similar proteins. RNF38 is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38. Both RNF38 and RNF44 contain a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger. In addition, RNF38 harbors two potential nuclear localization signals.


Pssm-ID: 319386 [Multi-domain]  Cd Length: 45  Bit Score: 41.31  E-value: 1.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 203 GCSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16472     3 SCVVCMCDFEARQLLRV-LPCSHEFHAKCVDKWLKTNRTCPICR 45
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
204-246 1.55e-05

RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome.


Pssm-ID: 319441 [Multi-domain]  Cd Length: 40  Bit Score: 40.66  E-value: 1.55e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16527     2 CSLCLESRRH----PTATPCGHLFCWSCITEWCNEKPECPLCR 40
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
204-246 1.99e-05

RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319513 [Multi-domain]  Cd Length: 44  Bit Score: 40.69  E-value: 1.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAE-WLARQSTCPLCR 246
Cdd:cd16599     4 CPICYDPFRE----AVTLRCGHNFCKGCVSRsWEVRSHTCPVCK 43
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
46-138 2.31e-05

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768  Cd Length: 106  Bit Score: 41.96  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921  46 YTVYIMQI-LSSNVLWVVRHRYSALASTRALLLKTVNMVPrkdyssraavaalvepLREFPRKYLF-MDTPRVVNDRKKG 123
Cdd:cd06093    17 YVVYIIEVtTQGGEEWTVYRRYSDFEELHEKLKKKFPGVI----------------LPPLPPKKLFgNLDPEFIEERRKQ 80
                          90
                  ....*....|....*
gi 1173933921 124 LAMFVQAMFHVRDLC 138
Cdd:cd06093    81 LEQYLQSLLNHPELR 95
RING-CH-C4HC3_LTN1 cd16491
RING-CH finger, H2 subclass (C4HC3-type), found in E3 ubiquitin-protein ligase listerin and ...
204-246 2.32e-05

RING-CH finger, H2 subclass (C4HC3-type), found in E3 ubiquitin-protein ligase listerin and similar proteins; Listerin, also known as RING finger protein 160 or zinc finger protein 294, is the mammalian homolog of yeast Ltn1. It is widely expressed in all tissues, but motor and sensory neurons and neuronal processes in the brainstem and spinal cord are primarily affected in the mutant. Listerin is required for embryonic development and plays an important role in neurodegeneration. It also functions as a critical E3 ligase involving quality control of nonstop proteins. It mediates ubiquitylation of aberrant proteins that become stalled on ribosomes during translation. Ltn1 works with several cofactors to form a large ribosomal subunit-associated quality control complex (RQC), whick mediates the ubiquitylation and extraction of ribosome-stalled nascent polypeptide chains for proteasomal degradation. It appears to first associate with nascent chain-stalled 60S subunits together with two proteins of unknown function, Tae2 and Rqc1. Listerin contains a long stretch of HEAT (Huntingtin, Elongation factor 3, PR65/A subunit of protein phosphatase 2A, and TOR) or ARM (Armadillo) repeats in the N terminus and middle region, and a catalytic RING-CH finger, also known as vRING or RINGv, with an unusual arrangement of zinc-coordinating residues in the C-terminus . Its cysteines and histidines are arranged in the sequence as C4HC3-type, rather than the C3H2C3-type in canonical RING-H2 finger.


Pssm-ID: 319405 [Multi-domain]  Cd Length: 50  Bit Score: 40.72  E-value: 2.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1173933921 204 CSICLENLH--DLGVSSVQLA-CSHAFHRGCVAEWL--ARQSTCPLCR 246
Cdd:cd16491     3 CPICYSVIHgsNHSLPKLKCKtCKNKFHSACLYKWFssSNKSTCPLCR 50
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
202-246 2.35e-05

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2); RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 319656 [Multi-domain]  Cd Length: 41  Bit Score: 40.58  E-value: 2.35e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 202 DGCSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16742     1 DICAICQAEFRE----PLILICQHVFCEECLCLWFDRERTCPLCR 41
RING-HC_TRIM4_C-IV_like cd16590
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM4, TRIM75, ...
204-246 3.74e-05

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM4, TRIM75, tripartite motif family-like protein 1 (TRIML1) and similar proteins; TRIM4 and TRIM75, two closely related tripartite motif-containing proteins, belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that it had recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at mitochondria. TRIM75 mainly localizes within spindles, suggesting it may function in spindle organization and thereby affect meiosis. The family also includes TRIML1 that is identical to TRIM11 and TRIM17 except for the absence of B-box domain. TRIML1, also known as RING finger protein 209 (RNF209), is a probable E3 ubiquitin-protein ligase expressed in embryo before implantation. It plays an important role in blastocyst development. By interacting with USP5 (also known as isoT), TRIML1 may exerts its influence on debranching ubiquitin from multi-chains on the stability and activity of protein substrates in the preimplantation embryo.


Pssm-ID: 319504 [Multi-domain]  Cd Length: 45  Bit Score: 39.77  E-value: 3.74e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAE-WLARQS--TCPLCR 246
Cdd:cd16590     4 CSICLDYFKD----PVTIECGHNFCRGCILQsWENLNTpfSCPECR 45
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of ...
204-245 4.09e-05

HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to HC subclass of RING (RING-HC) finger proteins that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319363 [Multi-domain]  Cd Length: 39  Bit Score: 39.76  E-value: 4.09e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLgvssVQLACSHAFHRGCVAEWL-ARQSTCPLC 245
Cdd:cd16449     1 CPICLELLKDP----VLLPCGHTFCRSCLRRLLkEGKKKCPIC 39
RING-H2_RNF24 cd16675
RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 ...
204-245 6.59e-05

RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, ?3, ?4, ?5, ?6, and ?7, and affects TRPC intracellular trafficking without affecting their activity. RNF24 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319589 [Multi-domain]  Cd Length: 47  Bit Score: 39.21  E-value: 6.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENLH---DLGVSSvqlaCSHAFHRGCVAEWLARQSTCPLC 245
Cdd:cd16675     3 CAVCLEEFKpkdELGICP----CKHAFHRKCLIKWLEVRKVCPLC 43
RING-HC_MID_C-I cd16575
RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; ...
204-246 6.74e-05

RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is highly related to MID1. It associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis and the functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319489 [Multi-domain]  Cd Length: 52  Bit Score: 39.44  E-value: 6.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQST------------CPLCR 246
Cdd:cd16575     1 CPICLELFED----PILLPCSHNLCKSCAERLVVSHCGsgesgetresfrCPTCR 51
RING-H2_RNF38 cd16679
RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 ...
204-247 6.87e-05

RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 is a nuclear E3 ubiquitin protein ligase that is widely expressed throughout the body in human, especially highly expressed in the heart, brain, placenta and the testis. It recognizes p53 as a substrate for ubiquitination, and thus plays a role in regulating p53. The overexpression of RNF38 increases p53 ubiquitination and alters p53 localization. It is also capable of autoubiquitination. Moreover, RNF38 expression is negatively regulated by the serotonergic system. Induction of RNF38 may be involved in the anxiety-like behavior or non-cell autonomous by the decline of serotonin (5-HT) levels. RNF38 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger, as well as two potential nuclear localization signals.


Pssm-ID: 319593 [Multi-domain]  Cd Length: 49  Bit Score: 39.27  E-value: 6.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCRA 247
Cdd:cd16679     5 CVVCMCDFESRQLLRV-LPCNHEFHAKCVDKWLKANRTCPICRA 47
RING-HC_RNF5_like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
204-246 7.84e-05

RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 and RNF185 are E3 ubiquitin-protein ligases that are anchored to the outer membrane of the endoplasmic reticulum (ER). RNF5 acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis, and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. RNF185 controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical endoplasmic reticulum-associated degradation (ERAD) model substrates. Moreover, both RNF5 and RNF185 play important roles in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) are also included in this family. They possess E3 ubiquitin-protein ligase activity and may play a role in the growth and development of Arabidopsis. All members in this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 319448 [Multi-domain]  Cd Length: 43  Bit Score: 38.95  E-value: 7.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLHDLGVSsvqlACSHAFHRGCVAEWLARQS---TCPLCR 246
Cdd:cd16534     2 CNICLDTAKDAVVS----MCGHLFCWPCLHQWLETRPdrpTCPVCK 43
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
204-245 8.45e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 316445 [Multi-domain]  Cd Length: 40  Bit Score: 38.94  E-value: 8.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1173933921 204 CSICLENLHDlgvSSVQLACSHAFHRGCVAEWLARQSTCPLC 245
Cdd:pfam13923   2 CPICLDMLKD---PSTTTPCGHVFCQKCILRALRSGNECPLC 40
RING-H2_RNF13 cd16796
RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; RING ...
202-246 8.89e-05

RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. It functions as an important regulator of Inositol-requiring transmembrane kinase/endonuclease IRE1alpha, mediating endoplasmic reticulum (ER) stress-induced apoptosis through the activation of the IRE1alpha-TRAF2-JNK signaling pathway. Moreover, RNF13 is involved in the regulation of the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) complex via the ubiquitination of snapin, a SNAP25-interacting protein, which thereby controls synaptic function. In addition, RNF13 participates in regulating the function of satellite cells by modulating cytokine composition. RNF13 is evolutionarily conserved among many metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319710 [Multi-domain]  Cd Length: 49  Bit Score: 38.87  E-value: 8.89e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 202 DGCSICLENLHDlGVSSVQLACSHAFHRGCVAEWLAR-QSTCPLCR 246
Cdd:cd16796     2 DVCAICLDEYEE-GDKLRILPCSHAYHCKCVDPWLTKtKKTCPVCK 46
APC11 COG5194
Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational ...
202-246 9.96e-05

Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational modification, protein turnover, chaperones / Cell division and chromosome partitioning];


Pssm-ID: 227521 [Multi-domain]  Cd Length: 88  Bit Score: 39.82  E-value: 9.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1173933921 202 DGCSICLENLHDLGVSSVQLA------------CSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:COG5194    21 DVCAICRNHIMGTCPECQFGMtpgdecpvvwgvCNHAFHDHCIYRWLDTKGVCPLDR 77
RING-H2_RNF44 cd16680
RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 ...
204-246 1.26e-04

RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38, which is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C2-type RING-H2 finger.


Pssm-ID: 319594 [Multi-domain]  Cd Length: 45  Bit Score: 38.50  E-value: 1.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLGVSSVqLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16680     4 CVVCFSDFESRQLLRV-LPCNHEFHTKCVDKWLKTNRTCPICR 45
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
204-243 1.26e-04

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 (WDR24) and similar proteins; WDR24 is a component of GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea3/WDR59, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR24 contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea2 is the yeast counterpart of WDR24. It is not included in this subfamily.


Pssm-ID: 319607  Cd Length: 46  Bit Score: 38.40  E-value: 1.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1173933921 204 CSICLENLHdlGVSSVQLACSHAFHRGCVAEWLARQSTCP 243
Cdd:cd16693     2 CAVCHLPVK--GLYVWCQGCGHGGHLEHIQEWFSDNSECP 39
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
204-246 1.35e-04

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319523 [Multi-domain]  Cd Length: 47  Bit Score: 38.24  E-value: 1.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQS------TCPLCR 246
Cdd:cd16609     3 CSICLELFTD----PVTLPCGHNFCGECIRDHWDKCElikkgySCPQCR 47
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
204-249 1.47e-04

RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, also known as small nuclear ring finger protein (SNURF), is a SUMO-targeted E3 ubiquitin-protein ligase with a pivotal function in the DNA damage response (DDR) through interacting with the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, and further facilitating DNA repair. It plays a novel role in preventing the loss of intact chromosomes and ensures the maintenance of chromosome integrity. Moreover, RNF4 is responsible for the UbcH5A-catalyzed formation of K48 chains that target SUMO-modified promyelocytic leukemia (PML) protein for proteasomal degradation in response to arsenic treatment. It also interacts with telomeric repeat binding factor 2 (TRF2) in a small ubiquitin-like modifiers (SUMO)-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination through SUMO-interacting motifs (SIMs). Furthermore, RNF4 can form a complex with a Ubc13-ubiquitin conjugate and Ube2V2. It catalyzes K63-linked polyubiquitination by the Ube2V2-Ubc13 (ubiquitin-loaded) complex. Meanwhile, RNF4 negatively regulates nuclear factor kappa B (NF-kappaB) signaling by down-regulating transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1)-TAK1-binding protein2 (TAB2). RNF4 contains four SIMs followed by a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 319447 [Multi-domain]  Cd Length: 54  Bit Score: 38.59  E-value: 1.47e-04
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gi 1173933921 204 CSICLENLHDLGVSSVQLA---CSHAFHRGCVAEWLARQSTCPLCRASL 249
Cdd:cd16533     6 CPICMDGYSEIVQSGRLLVstiCGHVFCSQCIRDSIKNAHTCPTCRKKL 54
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
204-246 1.90e-04

RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability as well as functions in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This family corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s).


Pssm-ID: 319411 [Multi-domain]  Cd Length: 46  Bit Score: 37.86  E-value: 1.90e-04
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gi 1173933921 204 CSIClenlHDLGVSSVQLACSHAFHRGCVAEW--LARQSTCPLCR 246
Cdd:cd16497     3 CHCC----YDLLVNPTTLNCGHSFCRHCLALWwlSSKKTECPECR 43
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
204-246 2.07e-04

RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319509 [Multi-domain]  Cd Length: 48  Bit Score: 37.82  E-value: 2.07e-04
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gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCV------AEWLARQSTCPLCR 246
Cdd:cd16595     4 CSICLDYFKD----PVILRCGHNFCRACItqfwekQGGLQGKLTCPECR 48
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
204-246 2.64e-04

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of acetylcholine receptor (AChR) in the postsynaptic membrane of the motor endplate (EP). AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate acetylcholine-receptor deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site.


Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 37.41  E-value: 2.64e-04
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gi 1173933921 204 CSICLENLHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16478     4 CGMCGESIGEKNESLQALPCSHIFHLKCLQTNLNGTRGCPNCR 46
RING-HC_TRIM11_like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM11 and TRIM27, ...
204-246 2.72e-04

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM11 and TRIM27, and similar proteins; TRIM11 and TRIM27, two closely related tripartite motif-containing proteins, belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) through mediating the degradation of congenital central hypoventilation syndrome-associated polyalanine-expanded Phox2b. Trim11 modulates the function of neurogenic transcription factor Pax6 through ubiquitin-proteosome system, and thus plays an essential role for the Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer"s disease-relevant insults, through the ubiquitin-proteasome system, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. Furthermore, TRIM27 promote a non-canonical polyubiquitinations of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. In addition, TRIM27 forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is also a component of an estrogen receptor 1 (ESR1) regulatory complex, and is involved in estrogen receptor-mediated transcription in MCF-7 cells. Meanwhile, TRIM27 interacts with the hinge region of chromosome 3 protein (SMC3), a component of the multimeric cohesin complex that holds sister chromatids together and prevents their premature separation during mitosis.


Pssm-ID: 319508 [Multi-domain]  Cd Length: 45  Bit Score: 37.45  E-value: 2.72e-04
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gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAE-W--LARQSTCPLCR 246
Cdd:cd16594     4 CPVCLEYFTD----PVILDCGHNFCRACILRcWetRATPVSCPQCR 45
mRING-CH-C4HC2H_ZNRF cd16489
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; This ZNRF family ...
204-243 2.88e-04

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; This ZNRF family includes zinc/RING finger proteins ZNRF1, ZNRF2, and similar proteins. It has been characterized by containing a unique combination zinc finger-RING finger motif in the C-terminal region, which is evolutionarily conserved in a wide range of species, including Caenorhabditis elegans and Drosophila. The ZNRF family of proteins function as an E3 ubiquitin ligase and are highly expressed in central nervous system (CNS) and peripheral nervous system (PNS) neurons, particularly during development and in adulthood. In neurons, ZNRF1 and ZNRF2 are differentially localized within the synaptic region. ZNRF1 is associated with synaptic vesicle membranes, whereas ZNRF2 is present in presynaptic plasma membranes. They are N-myrisotoylated and also located in the endosome-lysosome compartment in fibroblasts. ZNRF proteins may play a role in the establishment and maintenance of neuronal transmission and plasticity via their ubiquitin ligase activity, as well as in regulating Ca2+-dependent exocytosis. The RING fingers found in ZNRF proteins are modified as C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of RING-H2 finger.


Pssm-ID: 319403 [Multi-domain]  Cd Length: 43  Bit Score: 37.26  E-value: 2.88e-04
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gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCP 243
Cdd:cd16489     2 CVICLEELLA-GDTIARLPCLCIYHKKCIDDWFEVNRSCP 40
mRING-CH-C4HC2H_ZNRF2 cd16695
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 2 (ZNRF2) ...
204-243 3.02e-04

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 2 (ZNRF2) and similar proteins; ZNRF2, also known as protein Ells2 or RING finger protein 202 (RNF202), is an E3 ubiquitin-protein ligase that is highly expressed in the nervous system during development and is present in presynaptic plasma membranes. It is N-myrisotoylated and also located in the endosome-lysosome compartment in fibroblasts. It contains an N-terminal MAGE domain, and a special C-terminal domain that combines a zinc finger and a modified C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of RING-H2 finger. Only the RING finger of the zinc finger-RING finger motif is required for its E3 ubiquitin ligase activity. Together with its sister protein ZNRF1, ZNRF2 regulates the ubiquitous Na+/K+ pump (Na+/K+ATPase).


Pssm-ID: 319609 [Multi-domain]  Cd Length: 45  Bit Score: 37.31  E-value: 3.02e-04
                          10        20        30        40
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gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCP 243
Cdd:cd16695     2 CAICLEELQQ-GDTIARLPCLCIYHKGCIDEWFEVNRSCP 40
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
204-246 3.67e-04

RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulates Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation through translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail.


Pssm-ID: 319460 [Multi-domain]  Cd Length: 40  Bit Score: 36.98  E-value: 3.67e-04
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gi 1173933921 204 CSICLENLhdlgVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16546     2 CAICLQTC----VHPVRLPCGHIFCYLCVKGVAWQSKRCALCR 40
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
204-248 3.84e-04

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 40.76  E-value: 3.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSIClenlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCRAS 248
Cdd:TIGR00599  29 CHIC----KDFFDVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAE 69
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
204-246 3.85e-04

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 319412 [Multi-domain]  Cd Length: 48  Bit Score: 37.00  E-value: 3.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQST---CPLCR 246
Cdd:cd16498     7 CPICLDLMKN----PVSTKCDHQFCRFCILKLLSRKKGsapCPLCK 48
RING-H2_TRAIP cd16480
RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; ...
204-246 3.88e-04

RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; TRAIP, also known as RING finger protein 206 (RNF206) or TRIP, is a ubiquitously expressed nucleolar E3 ubiquitin ligase important for cellular proliferation and differentiation. It is found near mitotic chromosomes and functions as a regulator of the spindle assembly checkpoint. TRAIP interacts with tumor necrosis factor (TNF)-receptor-associated factor (TRAF) proteins and inhibits TNF-alpha-mediated nuclear factor (NF)-kappaB activation. It also interacts with two tumor suppressors CYLD and spleen tyrosine kinase (Syk), and DNA polymerase eta, which facilitates translesional synthesis after DNA damage. TRAIP contains an N-terminal C3H2C2-type RING-H2 finger and an extended coiled-coil domain.


Pssm-ID: 319394 [Multi-domain]  Cd Length: 45  Bit Score: 37.15  E-value: 3.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1173933921 204 CSIClenlHDLGVSSVQLA---CSHAFHRGCVAEWL--ARQSTCPLCR 246
Cdd:cd16480     2 CTIC----SDFFDNSRDVAaihCGHTFHYECLLQWFetAPSRTCPQCR 45
RING_Ubox cd00162
The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING ...
204-245 4.26e-04

The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well. C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC finger. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are close to RING-H2 finger. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerated RING fingers from Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319361 [Multi-domain]  Cd Length: 40  Bit Score: 36.67  E-value: 4.26e-04
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gi 1173933921 204 CSICLENLHDlgvSSVQLACSHAFHRGCVAEWL-ARQSTCPLC 245
Cdd:cd00162     1 CPICRELMKD---PVVLPSCGHTFCYSCIARWLeSSDQTCPFC 40
RING-H2_PHR cd16463
RING finger, H2 subclass, found in the PHR protein family; The PHR protein family represents ...
202-246 4.29e-04

RING finger, H2 subclass, found in the PHR protein family; The PHR protein family represents an evolutionally conserved family of large proteins including human E3 ubiquitin ligase protein associated with Myc (Pam) and its homologs, Phr1 (for Pam/Highwire/RPM-1) in mouse, Highwire (HIW) in Drosophila, RPM-1 (regulator of presynaptic morphology 1) in Caenorhabditis elegans, and Esrom in zebrafish. Those proteins are large E3 ubiquitin ligases containing regulator of chromosome condensation (RCC) homology domains (RHD-1 and RHD-2) with inferred guanine exchange factor (GEF) activity, a Myc-binding domain, a B-box zinc finger, and a C-terminal C3H2C3-type RING-H2 finger with E3 ubiquitin (Ub) ligase activity. They play an important role in axon guidance and synaptogenesis. They regulate synapse formation and growth in mammals, zebrafish, Drosophila, and Caenorhabditis elegans, and may control a variety of signaling pathways, including cAMP signaling in mammalian cells, JNK/p38 MAPK signaling in Drosophila and C. elegans, and bone morphogenetic protein signaling in Drosophila. Pam also known as Myc-binding protein 2 (MYCBP2), or Pam/highwire/rpm-1 protein (PHR1), negatively regulates neuronal growth, synaptogenesis and synaptic plasticity by modulating several signaling pathways including the p38 MAPK signaling cascade. It also participates in receptor and ion channel internalization, such as regulating internalization of transient receptor potential vanilloid receptor 1 (TRPV1) in peripheral sensory neurons, as well as duration of thermal hyperalgesia through p38 MAPK. It interacts with neuron-specific electroneutral potassium (K+) and chloride (Cl-) cotransporter KCC2 and modulates its function. Moreover, Pam genetically interacts with Robo2 to modulate axon guidance in the olfactory system. It also associates with tuberous sclerosis complex (TSC) proteins, ubiquitinating TSC2 and regulating mammalian/mechanistic target of rapamycin (mTOR) signaling. Furthermore, Pam is the longest lasting nontranscriptional regulator of adenylyl cyclase activity, and can mediate sustained inhibition of cAMP signaling by sphingosine-1-phosphate. It is also involved in spinal nociceptive processing. Phr1 is an essential regulator of retinal ganglion cell projection during both dorsal lateral geniculate nucleus (dLGN) and superior colliculus (SC) topographic map development. RPM-1 positively regulates a Rab GTPase pathway to promote vesicular trafficking via late endosomes, thereby regulating synapse formation and axon termination. Esrom has E3 ligase activity and modulates the amount of phosphorylated Tuberin, a tumor suppressor, in growth cones. It is required in formation of the retinotectal projection.


Pssm-ID: 319377  Cd Length: 55  Bit Score: 37.29  E-value: 4.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1173933921 202 DGCSICLenLHDLGVS-SVQLACSHAFHRGCVAEWLARQ----------STCPLCR 246
Cdd:cd16463     2 DMCMICF--TEALSAApAIQLQCGHVFHLHCCRRVLEKRwpgpritfgfLKCPICK 55
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
204-245 4.45e-04

RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of nuclear TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.


Pssm-ID: 319494 [Multi-domain]  Cd Length: 44  Bit Score: 36.86  E-value: 4.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLEnlhdLGVSSVQLACSHAFHRGCVAEWLARQST---CPLC 245
Cdd:cd16580     3 CPICLH----VFVEPVQLPCKHNFCRGCIGEAWAKEAGlvrCPEC 43
zf-RING_11 pfam17123
RING-like zinc finger;
204-232 4.70e-04

RING-like zinc finger;


Pssm-ID: 339895 [Multi-domain]  Cd Length: 29  Bit Score: 36.34  E-value: 4.70e-04
                          10        20
                  ....*....|....*....|....*....
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCV 232
Cdd:pfam17123   2 CSICLDEFEP-GQALRVLPCSHVFHYKCI 29
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
204-246 4.87e-04

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. Furthermore, TRIM62 is involved in the regulation of apical-basal polarity and acinar morphogenesis. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) through binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319522 [Multi-domain]  Cd Length: 50  Bit Score: 36.96  E-value: 4.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQST-----CPLCR 246
Cdd:cd16608     6 CSICLSIYQD----PVSFGCEHYFCRKCITEHWSRQEHqgtrdCPECR 49
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
204-246 5.90e-04

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may associate with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can forms huge ring-shaped oligomeric complex.


Pssm-ID: 319475 [Multi-domain]  Cd Length: 41  Bit Score: 36.31  E-value: 5.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLAR--QSTCPLCR 246
Cdd:cd16561     1 CSICLEDPKD----PVSLPCDHIHCLTCLRQWFRPvgQMHCPTCR 41
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
204-243 6.51e-04

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 338747 [Multi-domain]  Cd Length: 38  Bit Score: 36.21  E-value: 6.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlgvssVQLACSHAFHRGCVAEWLARQS---TCP 243
Cdd:pfam13445   1 CPICLELFTD-----PVLPCGHTFCRECLEEMSLLKGgrfKCP 38
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
204-246 6.61e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 319495 [Multi-domain]  Cd Length: 45  Bit Score: 36.28  E-value: 6.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENLHDLGVssvqLACSHAFHRGCVAEWLARQST--CPLCR 246
Cdd:cd16581     5 CSICLDIFNDPRV----LPCLHTFCKNCLEGRAAESGPlkCPTCR 45
RING2-HC_LONFs cd16514
RING finger 2, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
204-246 6.72e-04

RING finger 2, HC subclass, found in the LON peptidase N-terminal domain and RING finger proteins family; The LON peptidase N-terminal domain and RING finger proteins family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192 or RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and one N-terminal domain of the ATP-dependent protease La (LON) domain at the C-terminus. Their biological function remain unclear. This family corresponds to the second RING-HC finger.


Pssm-ID: 319428 [Multi-domain]  Cd Length: 42  Bit Score: 36.15  E-value: 6.72e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16514     4 CSLCMRLLYE----PVTTPCGHTFCKKCLERCLDHSPKCPLCK 42
RING-H2_RBX2 cd16466
RING finger, H2 subclass, found in RING-box protein 2 (RBX2) and similar proteins; RBX2, also ...
223-246 6.92e-04

RING finger, H2 subclass, found in RING-box protein 2 (RBX2) and similar proteins; RBX2, also known as CKII beta-binding protein 1 (CKBBP1), RING finger protein 7 (RNF7), regulator of cullins 2 (ROC2), or sensitive to apoptosis gene protein (SAG), is an E3 ubiquitin-protein ligase that protects cells from apoptosis, confers radioresistance, and plays an essential and non-redundant role in embryogenesis and vasculogenesis. It promotes ubiquitination and degradation of a number of protein substrates, including c-JUN, DEPTOR, HIF-1alpha, IkappaBalpha, NF1, NOXA, p27, and procaspase-3, thus regulating various signaling pathways and biological processes. RBX2 is necessary for ubiquitin ligation activity of the multimeric cullin (Cul)-RING E3 ligases (CRLs). RBX2-containing CRLs are involved in NEDD8 pathway and RBX2 specifically regulate NEDD8ylation of Cul5. It can bind and activate HIV-1 Vif-Cullin5 E3 ligase complex in vitro. It is also a substrate of NEDD4-1 E3 ubiquitin ligase and mediates NEDD4-1 induced chemosensitization. The inactivation of RBX2 E3 ubiquitin ligase activity triggers senescence and inhibits Kras-induced immortalization. Endothelial deletion of RBX2 causes embryonic lethality and blocks tumor angiogenesis, suggesting a way for anti-angiogenesis therapy of human cancer. Moreover, as a component of Cullin 5-RING E3 ubiquitin ligase (CRL5) complex, RBX2 regulates neuronal migration through different CRL5 adaptors, such as SOCS7. Furthermore, RBX2 functions as a redox inducible antioxidant protein that scavenges oxygen radicals by forming inter- and intra-molecular disulfide bonds when acting alone. RBX2 contains a C-terminal C3H2C3-type RING-H2 finger that is essential for its ligase activity.


Pssm-ID: 319380 [Multi-domain]  Cd Length: 60  Bit Score: 36.73  E-value: 6.92e-04
                          10        20
                  ....*....|....*....|....
gi 1173933921 223 CSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16466    34 CNHSFHNCCMSLWVKQNNRCPLCQ 57
RING-HC_RAD16_like cd16567
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ...
204-245 7.30e-04

RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, Schizosaccharomyces pombe rhp16, and similar proteins; Budding yeast RAD16, also known as ATP-dependent helicase RAD16, is encoded by a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation. It is a component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) that removes DNA damage from non-transcribing DNA. RAD16 is involved in differential repair of DNA after UV damage, and repairs preferentially the MAT-alpha locus compared with the HML-alpha locus. Fission yeast rhp16, also known as ATP-dependent helicase rhp16, is a RAD16 homolog. It is involved in GGR via nucleotide excision repair (NER), in conjunction with rhp7, after UV irradiation. Both RAD16 and rhp16 contain a C3HC4-type RING-HC finger, as well as a DEAD-like helicase domain and a helicase superfamily C-terminal domain.


Pssm-ID: 319481 [Multi-domain]  Cd Length: 47  Bit Score: 36.27  E-value: 7.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSIClenlHDLGVSSVQLACSHAFHRGCVAEWL----ARQSTCPLC 245
Cdd:cd16567     2 CGIC----NDPAEDPVVSRCHHAFCRLCVTEYIesapGGEVTCPRC 43
mRING-CH-C4HC2H_ZNRF1 cd16694
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 1 (ZNRF1) ...
204-243 7.70e-04

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 1 (ZNRF1) and similar proteins; ZNRF1, also known as Nerve injury-induced gene 283 protein (nin283), or peripheral nerve injury protein (PNIP), is an E3 ubiquitin-protein ligase that is highly expressed in the nervous system during development and is associated with synaptic vesicle membranes. It is N-myrisotoylated and also located in the endosome-lysosome compartment in fibroblasts, suggesting it may participate in ubiquitin-mediated protein modification. It contains an N-terminal MAGE domain, and a special C-terminal domain that combines a zinc finger and a modified C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of RING-H2 finger. Only the RING finger of the zinc finger-RING finger motif is required for its E3 ubiquitin ligase activity. ZNRF1 regulates Schwann cell differentiation by proteasomal degradation of glutamine synthetase (GS). It also mediates regulation of neuritogenesis via interaction with beta-tubulin type 2 (Tubb2). Moreover, ZNRF1 promotes Wallerian degeneration by degrading AKT to induce glycogen synthase kinase-3beta (GSK3B)-dependent CRMP2 phosphorylation. Furthermore, ZNRF1 and its sister protein ZNRF2 regulate the ubiquitous Na+/K+ pump (Na+/K+ATPase). In addition, ZNRF1 may be associated with leukemogenesis of acute lymphoblastic leukemia (ALL) with paired box domain gene 5 (PAX5) alteration.


Pssm-ID: 319608 [Multi-domain]  Cd Length: 46  Bit Score: 36.10  E-value: 7.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1173933921 204 CSICLENLHDlGVSSVQLACSHAFHRGCVAEWLARQSTCP 243
Cdd:cd16694     3 CVICLEELLQ-GDTIARLPCLCIYHKSCIDSWFEVNRSCP 41
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
191-247 8.71e-04

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 39.69  E-value: 8.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1173933921 191 PPLNMADDGDRdgCSIClenlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCRA 247
Cdd:COG5432    17 PSLKGLDSMLR--CRIC----DCRISIPCETTCGHTFCSLCIRRHLGTQPFCPVCRE 67
COG5219 COG5219
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
204-249 9.54e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227544  Cd Length: 1525  Bit Score: 40.04  E-value: 9.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1173933921  204 CSIC--LENLHDLGVSSVQLA-CSHAFHRGCVAEWLAR--QSTCPLCRASL 249
Cdd:COG5219   1472 CAICysVLDMVDRSLPSKRCAtCKNKFHTRCLYKWFASsaRSNCPLCRSEI 1522
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
204-243 9.86e-04

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 (WDR59) and similar proteins; WDR59 is a component of GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR59 contains an N-terminal WD40 domain followed by a RWD domain, and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea3 is the yeast counterpart of WDR59. It is not included in this subfamily.


Pssm-ID: 319606  Cd Length: 47  Bit Score: 36.15  E-value: 9.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1173933921 204 CSICLENLHdlGVSSVQLACSHAFHRGCVAEWLARQSTCP 243
Cdd:cd16692     3 CAICHLAVK--GSSNFCLSCGHGGHTSHMMEWFRTHTVCP 40
mRING-HC-C3HC3D_PHRF1 cd16635
Modified RING finger, HC subclass (C3HC3D-type), found in PHD and RING finger ...
204-246 1.07e-03

Modified RING finger, HC subclass (C3HC3D-type), found in PHD and RING finger domain-containing protein 1(PHRF1) and similar proteins; PHRF1, also known as KIAA1542, or CTD-binding SR-like protein rA9, is a ubiquitin ligase which induces the ubiquitination of TGIF (TG-interacting factor) at lysine 130. It acts as a tumor suppressor that promotes the transforming growth factor (TGF)-beta cytostatic program through selective release of TGIF-driven promyelocytic leukemia protein (PML) inactivation. PHRF1 contains a plant homeodomain (PHD) finger and a modified C3HC3D-type RING-HC finger.


Pssm-ID: 319549 [Multi-domain]  Cd Length: 44  Bit Score: 35.87  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLGVSSVQlACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16635     3 CPICLNEFTDQAVGTPE-SCDHYFCLDCILEWSKNVNTCPVDR 44
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
204-246 1.13e-03

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319512 [Multi-domain]  Cd Length: 45  Bit Score: 35.63  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQST---CPLCR 246
Cdd:cd16598     4 CSICLDYLRD----PVTIDCGHVFCRSCTTDIRPISGNrpvCPLCK 45
RING-HC_TRIM7_C-IV cd16592
RING finger, HC subclass, found in tripartite motif-containing protein 7 (TRIM7) and similar ...
204-246 1.15e-03

RING finger, HC subclass, found in tripartite motif-containing protein 7 (TRIM7) and similar proteins; TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM7 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319506 [Multi-domain]  Cd Length: 45  Bit Score: 35.92  E-value: 1.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAE-WLARQST--CPLCR 246
Cdd:cd16592     4 CSICLDLFRD----PVSIPCGHNFCRACIRRcWELQGSTfsCPQCR 45
RING-H2_Vps11 cd16688
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog ...
204-246 1.16e-03

RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins; Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport) protein complexes. CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absent of Vps11, resulting in a massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis in Saccharomyces cerevisiae. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole.


Pssm-ID: 319602  Cd Length: 44  Bit Score: 35.74  E-value: 1.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLenlHDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16688     3 CSICN---SPLDLPSVHFLCGHSFHQRCLEDYEENDNECPLCA 42
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
144-247 1.37e-03

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 39.11  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921 144 SNGENTLLLVIAKGIIEKIETTLQIPvlqkEEDHKwrlqtlamvpvepplnmaddgdrdgCSICLENLHDLgvssVQLAC 223
Cdd:COG5574   187 SNNLHTLFQVITKENLSKKNGLPFIP----LADYK-------------------------CFLCLEEPEVP----SCTPC 233
                          90       100
                  ....*....|....*....|....*.
gi 1173933921 224 SHAFHRGCVAEWLARQST--CPLCRA 247
Cdd:COG5574   234 GHLFCLSCLLISWTKKKYefCPLCRA 259
RING-HC_AtRMA_like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
204-247 1.62e-03

RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins; AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region.


Pssm-ID: 319659 [Multi-domain]  Cd Length: 45  Bit Score: 35.36  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1173933921 204 CSICLENLHDLGVSSvqlaCSHAFHRGCVAEWLARQS---TCPLCRA 247
Cdd:cd16745     3 CNICLDLASDPVVTL----CGHLFCWPCLYRWLQRHSenrECPVCKA 45
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) protein family; The MKRN protein family ...
204-246 1.69e-03

RING finger, HC subclass, found in the makorin (MKRN) protein family; The MKRN protein family includes the ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


Pssm-ID: 319435 [Multi-domain]  Cd Length: 51  Bit Score: 35.37  E-value: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1173933921 204 CSICLENLHDLGVSSVQL-ACSHAFHRGCVAEWLARQS-------TCPLCR 246
Cdd:cd16521     1 CGICLEVVLPSERRFGILpNCDHPFCLACIRDWRGSKDqektvvrACPICR 51
zf-ANAPC11 pfam12861
Anaphase-promoting complex subunit 11 RING-H2 finger; Apc11 is one of the subunits of the ...
223-248 1.71e-03

Anaphase-promoting complex subunit 11 RING-H2 finger; Apc11 is one of the subunits of the anaphase-promoting complex or cyclosome. The APC subunits are cullin family proteins with ubiquitin ligase activity. Polyubiquitination marks proteins for degradation by the 26S proteasome and is carried out by a cascade of enzymes that includes ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s). Apc11 acts as an E3 enzyme and is responsible for recruiting E2s to the APC and for mediating the subsequent transfer of ubiquitin to APC substrates in vivo. In Saccharomyces cerevisiae this RING-H2 finger protein defines the minimal ubiquitin ligase activity of the APC, and the integrity of the RING-H2 finger is essential for budding yeast cell viability.


Pssm-ID: 289620 [Multi-domain]  Cd Length: 85  Bit Score: 36.31  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|....*....
gi 1173933921 223 CSHAFHRGCVAEWLARQST---CPLCRAS 248
Cdd:pfam12861  52 CSHNFHMHCILKWLHTETSkglCPMCRQT 80
RING-HC_TRIM41_like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
204-246 1.76e-03

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain.


Pssm-ID: 319516 [Multi-domain]  Cd Length: 41  Bit Score: 35.23  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAE-WLarqsTCPLCR 246
Cdd:cd16602     5 CAICLDYFRD----PVSIGCGHNFCRVCVTQlWF----TCPQCR 40
RING-H2_Vps cd16484
RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, ...
204-246 1.96e-03

RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, Vps18, Vps41, and similar proteins; This family corresponds to a group of vacuolar protein sorting-associated proteins containing a C-terminal C3H2C3-type RING-H2 finger, which includes Vps8, Vps11, Vps18, and Vps41. Vps11 and Vps18 associate with Vps16 and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport) protein complexes. CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form.


Pssm-ID: 319398  Cd Length: 46  Bit Score: 35.16  E-value: 1.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENL--HDLGVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16484     2 CSICNKPLkeRGRADPVVVFFCGHMYHETCLENYERSRATCPICS 46
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
204-246 2.84e-03

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319507 [Multi-domain]  Cd Length: 49  Bit Score: 34.60  E-value: 2.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQS-------TCPLCR 246
Cdd:cd16593     4 CPICQGTLRE----PVTIDCGHNFCRACLTRYCEIPGpdleeppTCPLCK 49
RING-HC_LNX3 cd16718
RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ ...
204-246 2.88e-03

RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ domain-containing RING finger protein 3 (PDZRN3), or Semaphorin cytoplasmic domain-associated protein 3 (SEMACAP3), is an E3 ubiquitin-protein ligase that was first identified as a Semaphorin-binding partner. It is also responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX3 acts as a negative regulator of osteoblast differentiation by inhibiting Wnt-beta-catenin signaling. LNX3 also plays an important role in neuromuscular junction formation. It interacts with and ubiquitinates the muscle specific tyrosine kinase (MuSK), thus promoting its endocytosis and negatively regulating the cell surface expression of this key regulator of postsynaptic assembly. LNX3 contains an N-terminal typical C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 319632 [Multi-domain]  Cd Length: 42  Bit Score: 34.57  E-value: 2.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQSTCPL-CR 246
Cdd:cd16718     2 CNLCNKVLED----PLTTPCGHVFCAGCVLPWVVQQGSCPVkCQ 41
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
204-245 3.00e-03

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcriptions, which is induced by inflammatory stimulants such as tumor necrosis factor alpha (TNFalpha). Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319515 [Multi-domain]  Cd Length: 44  Bit Score: 34.64  E-value: 3.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEW---LARQSTCPLC 245
Cdd:cd16601     4 CSVCLEYLKE----PVIIECGHNFCKACITRWwedLERDFPCPVC 44
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
204-246 3.15e-03

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 319443 [Multi-domain]  Cd Length: 42  Bit Score: 34.55  E-value: 3.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHdlgVSSVQLACSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16529     3 CPICFDYFD---TAPMITPCSHNFCSLCIRRHLSYKTQCPTCR 42
RING-HC_Cbl_like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
204-246 3.93e-03

RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor proteins family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity, which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-c, as well as two invertebrate Cbl-family proteins, D-Cbl in Drosophila and Sli-1 in C. elegans. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating the activated tyrosine kinases and targeting them for degradation. D-Cbl associates with the Drosophila epidermal growth factor receptor (EGFR) and overexpression of D-Cbl in the eye of Drosophila embryos inhibits EGFR dependent photoreceptor cell development. Sli-1 is a negative regulator of the Let-23 receptor tyrosine kinase, an EGFR homolog, in vulva development. Cbl proteins in this family consist of a highly conserved N-terminal half that includes a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain) and a C3HC4-type RING-HC finger, both of which are required for Cbl-mediated downregulation of RTKs, and a divergent C-terminal region.


Pssm-ID: 319416 [Multi-domain]  Cd Length: 43  Bit Score: 34.25  E-value: 3.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1173933921 204 CSICLENLHDlgvssVQL-ACSHAFHRGCVAEWLARQS-TCPLCR 246
Cdd:cd16502     4 CKICAENDKD-----VRIePCGHLLCTPCLTSWQDSDGqTCPFCR 43
RING-HC_RNF125 cd16542
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as ...
204-246 4.04e-03

RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as T-cell RING activation protein 1 (TRAC-1), is an E3 ubiquitin-protein ligase that is predominantly expressed in lymphoid cells, and functions as a positive regulator of T cell activation. It also down-modulates HIV replication and inhibits pathogen-induced cytokine production. It negatively regulates type I interferon signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I. Further, RNF125 conjugates ubiquitin to melanoma differentiation-associated gene 5 (MDA5), a family protein of RIG-I. It thus acts as a negative regulator of RIG-I signaling, and is a direct target of miR-15b in the context of Japanese encephalitis virus (JEV) infection. Moreover, RNF125 binds to and ubiquitinates JAK1, prompting its degradation and inhibition of receptor tyrosine kinase (RTK) expression. It also negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. Mutations in RNF125 may lead to overgrowth syndromes (OGS). RNF125, together with three closely related proteins: RNF114, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM). The UIM of RNF125 binds K48-linked poly-ubiquitin chains and is, together with the RING domain, required for auto-ubiquitination.


Pssm-ID: 319456 [Multi-domain]  Cd Length: 42  Bit Score: 34.00  E-value: 4.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVAEWLARQS-TCPLCR 246
Cdd:cd16542     3 CAICLEVLHQ----PVRTRCGHVFCRTCIITSLKNNTwTCPYCR 42
RING-HC_TRIM60_like_C-IV cd16607
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61 and ...
204-246 4.50e-03

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61 and similar proteins; TRIM60 and TRIM61 are two closely related tripartite motif-containing proteins. TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. RNF33 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM60 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast to TRIM60, TRIM61 belongs to the C-V subclass of TRIM family that contains RBCC domains only. Its biological function remains unclear.


Pssm-ID: 319521 [Multi-domain]  Cd Length: 47  Bit Score: 34.18  E-value: 4.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLHDlgvsSVQLACSHAFHRGCVA-EWLARQST--CPLCR 246
Cdd:cd16607     4 CPICLEYLKD----PVTINCGHNFCRSCLIvSWKDLDDTfpCPVCR 45
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
204-246 4.62e-03

RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), was defined as a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3 delta ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.


Pssm-ID: 319418 [Multi-domain]  Cd Length: 46  Bit Score: 34.16  E-value: 4.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1173933921 204 CSICLENLHDLGVSSvqlaCSHAFHRGCVAEWLARQSTCPLCR 246
Cdd:cd16504     5 CPICFDIIEEAYMTK----CGHSFCYKCIRTSLEQSNRCPKCN 43
RING-CH-C4HC3_ZSWM2 cd16494
RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein ...
202-246 5.11e-03

RING-CH finger, H2 subclass (C4HC3-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins; ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3, and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It also acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination and two RING fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This family corresponds to the first RING finger, which is a C4HC3-type RING-CH finger, also known as vRING or RINGv, rather than the canonical C3H2C3-type RING-H2 finger.


Pssm-ID: 319408  Cd Length: 58  Bit Score: 34.20  E-value: 5.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1173933921 202 DGCSICLENLHD--LGVSSVQLACSHAFHRGCVAEWLARQST-------CPLCR 246
Cdd:cd16494     2 DVCPICQEELLEksEPLTYCRFGCGNSIHIKCMKVWAEHQRSsgeetikCPLCR 55
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
46-67 5.52e-03

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132785  Cd Length: 116  Bit Score: 35.72  E-value: 5.52e-03
                          10        20
                  ....*....|....*....|..
gi 1173933921  46 YTVYIMQILSSNVLWVVRHRYS 67
Cdd:cd06875    17 YTVYIIEVKVGSVEWTVKHRYS 38
RING-HC_TRIM47_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
203-246 6.18e-03

RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), belongs a subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis.


Pssm-ID: 319518 [Multi-domain]  Cd Length: 47  Bit Score: 33.64  E-value: 6.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1173933921 203 GCSICLENLHDlgvsSVQLACSHAFHRGCVAEWLAR------QSTCPLCR 246
Cdd:cd16604     2 TCPICLDALRD----PVTLPCGHNYCLACLQHLWEKngsrggAYRCPECQ 47
RING-HC_ScPSH1_like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
204-246 6.65e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1), Arabidopsis thaliana Protein KEEP ON GOING (AtKEG) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain. AtKEG is an E3 ubiquitin ligase essential for Arabidopsis growth and development. It maintains low levels of ABSCISIC ACID-INSENSITIVE5 (ABI5) in the absence of stress and thus functions as a negative regulator of abscisic acid (ABA) signaling. AtKEG is a multidomain protein that includes a C3HC4-type RING-HC finger, a kinase domain, ankyrin repeats, and 12 HERC2-like (for HECT and RCC1-like) repeats.


Pssm-ID: 319482 [Multi-domain]  Cd Length: 45  Bit Score: 33.63  E-value: 6.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1173933921 204 CSIClenlHD-LGVSSVQLACSHAFHRGCVAEWLARQS----TCPLCR 246
Cdd:cd16568     2 CSVC----HDrLNEVPMMLPCGHGFCKKCLNKMFSTSSdkrlACPTCR 45
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
204-246 8.20e-03

Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.


Pssm-ID: 319533 [Multi-domain]  Cd Length: 43  Bit Score: 33.09  E-value: 8.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1173933921 204 CSICLENLHDlgvssVQL--ACSHAFHRGCVAEWLARQ-STCPLCR 246
Cdd:cd16619     3 CFICMEKLRD-----ARLcpHCSKLCCFSCIRRWLTEQrSQCPHCR 43
RING-H2_DTX1_like cd16459
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), ...
204-247 9.03e-03

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase Deltex1 (DTX1), Deltex2 (DTX2), Deltex4 (DTX4), and similar proteins; This family includes Drosophila melanogaster Deltex, its vertebrate homologs, DTX1, DTX2, and DTX4, and other similar proteins mainly from eumetazoa. Deltex is a ubiquitously expressed cytoplasmic ubiquitin E3 ligase that mediates Notch activation in Drosophila. It selectively suppresses T-cell activation through degradation of a key signaling molecule, MAP kinase kinase kinase 1 (MEKK1). It also inhibits Jun-mediated transcription at the stage of Ras-dependent Jun N-terminal protein kinase (JNK) activation. Deltex contains N-terminal two Notch-binding WWE domains that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a RING finger at the C-terminus. The vertebrate homologs of Deltex have been involved in Notch signaling and neurogenesis. The mammalian DTX1 is most closely related to the Drosophila Deltex. Both of them bind to SH3-domain containing protein Grb2 and further inhibit E2A. DTX1 functions as a Notch downstream transcription regulator. It interacts with the transcription coactivator p300 and inhibits transcription activation mediated by the neural specific transcription factor MASH1. It is also a transcription target of nuclear factor of activated T cells (NFAT) and participated in T cell anergy and Foxp3 protein level maintenance in vivo. Moreover, DTX1 promotes protein kinase C theta degradation and sustains Casitas B-lineage lymphoma expression. DTX4, also known as RING finger protein 155, shares the highest degree of sequence similarity with DTX1. So it likely interacts with the intracellular domain of Notch as well. Like DTX1 and DTX4, DTX2 is expressed in thymocytes. It interacts with the intracellular domain of Notch receptors and acts as a negative regulator of Notch signals in T cells. However, the endogenous levels of DTX1 and DTX2 is not important for regulating Notch signals during thymocyte development. In contrast to other DTXs, DTX3 does not contain N-terminal two Notch-binding WWE domains, but a short unique N-terminal domain. It does not interact with intracellular domain of Notch. In addition, it has a different class of RING finger (C3HC4 type or RING-HC subclass) than do the other DTXs which harbor a C3H2C3-type RING-H2 finger. Thus DTX3 is not included in this family.


Pssm-ID: 319373  Cd Length: 64  Bit Score: 33.90  E-value: 9.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173933921 204 CSICLENLHD---------LGVSSV-QL-ACSHAFHRGCVAEWLARQS-----TCPLCRA 247
Cdd:cd16459     2 CPICMEKLCAasgyeetasSGSSAVcKLnRCGHVFHHACLVAMYSSGPkdgslQCPTCKT 61
FANCL_C pfam11793
FANCL C-terminal domain; This domain is found at the C-terminus of the Fancl protein in humans ...
204-249 9.33e-03

FANCL C-terminal domain; This domain is found at the C-terminus of the Fancl protein in humans which is the putative E3 ubiquitin ligase subunit of the FA complex (Fanconi anaemia). Eight subunits of the Fanconi anaemia gene products form a multisubunit nuclear complex which is required for mono-ubiquitination of a downstream FA protein, FANCD2.


Pssm-ID: 314629  Cd Length: 70  Bit Score: 33.95  E-value: 9.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173933921 204 CSICLENLHDLGVSSVQLA----CSHAFHRGCVAEWLA-----RQS------TCPLCRASL 249
Cdd:pfam11793   5 CGICYAYRLDGGEIPDIVCdnpkCGLPFHIACLYEWLRtlrdsRQSfnvsfgNCPYCKAKI 65
zf-RING_5 pfam14634
zinc-RING finger domain;
204-247 9.56e-03

zinc-RING finger domain;


Pssm-ID: 339304 [Multi-domain]  Cd Length: 43  Bit Score: 33.17  E-value: 9.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1173933921 204 CSICLEnLHDLGVSSVQLACSHAFHRGCVAEwLARQSTCPLCRA 247
Cdd:pfam14634   2 CNKCFK-PLSKTRPFYLTSCGHIFCEECLTK-LLKERQCPICRK 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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