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Conserved domains on  [gi|1952677825|ref|XP_038528387|]
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ankyrin repeat and SAM domain-containing protein 1A isoform X3 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 940-1085 2.76e-100

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 269972  Cd Length: 146  Bit Score: 313.83  E-value: 2.76e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  940 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 1019
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825 1020 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1085
Cdd:cd01274     81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-296 8.56e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.53  E-value: 8.56e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   62 NVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrvneqntleik 141
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  142 efkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLS 221
Cdd:COG0666    113 -----------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  222 CNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 296
Cdd:COG0666    182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 711-777 9.08e-37

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


:

Pssm-ID: 188898  Cd Length: 67  Bit Score: 132.81  E-value: 9.08e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  711 LEQSVGEWLEAVGLQQYESKLLLNGFDDVRFLGSNVMEEQDLRDIGITDPQHRRKLLQAAKSLPKVK 777
Cdd:cd09499      1 VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK 67
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 782-846 8.05e-36

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


:

Pssm-ID: 188899  Cd Length: 65  Bit Score: 129.73  E-value: 8.05e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVHLLGHRKRIIASLADR 846
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 940-1085 2.76e-100

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269972  Cd Length: 146  Bit Score: 313.83  E-value: 2.76e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  940 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 1019
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825 1020 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1085
Cdd:cd01274     81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-296 8.56e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.53  E-value: 8.56e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   62 NVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrvneqntleik 141
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  142 efkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLS 221
Cdd:COG0666    113 -----------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  222 CNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 296
Cdd:COG0666    182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 711-777 9.08e-37

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188898  Cd Length: 67  Bit Score: 132.81  E-value: 9.08e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  711 LEQSVGEWLEAVGLQQYESKLLLNGFDDVRFLGSNVMEEQDLRDIGITDPQHRRKLLQAAKSLPKVK 777
Cdd:cd09499      1 VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK 67
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 952-1085 3.85e-36

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 133.21  E-value: 3.85e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   952 ESCGYEANYLGSMLIKDLRGTESTQDACAKMRKS-TEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDP 1030
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  1031 EDLCTFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQLALQAQKS 1085
Cdd:smart00462   82 DDLDVFGYIARDPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARSE 134
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 782-846 8.05e-36

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 129.73  E-value: 8.05e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVHLLGHRKRIIASLADR 846
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
197-288 5.43e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 5.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  197 LDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDaGMDSNYQTEKGSALHEAALFGKTDVVQI 276
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1952677825  277 LLAAGIDVNIKD 288
Cdd:pfam12796   80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-254 3.18e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 3.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   59 RGPNVNCVDSTGYTPLHHAALN--GHKDVVEVLLRNDALTNVADSKGCYPLHLAAW--KGDAQIVRLLIHQGpshTRVNE 134
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKG---VDINA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  135 QNtlEIKEFKKYGpFDpyINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLN 214
Cdd:PHA03100   172 KN--RVNYLLSYG-VP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1952677825  215 AHPNLlscNTKKHTPLHLAARN----------GHKAVVQVLLDAGMDSNY 254
Cdd:PHA03100   247 NGPSI---KTIIETLLYFKDKDlntitkikmlKKSIMYMFLLDPGFYKNR 293
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
956-1075 1.66e-14

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 71.63  E-value: 1.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  956 YEANYLGSM-------LIKDLRgTESTQDA--CAKM------RKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEI 1020
Cdd:pfam00640    1 FAVRYLGSVevpeeraPDKNTR-MQQAREAirRVKAakinkiRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825 1021 RNIS-CAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDvnLTYEIILTLGQAFEVA 1075
Cdd:pfam00640   80 VSISfCADGDPDLMRYFAYIARDKATNKFACHVFESED--GAQDIAQSIGQAFALA 133
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 714-773 1.70e-13

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 66.55  E-value: 1.70e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLgsNVMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLL--LLTSEEDLKELGITKLGHRKKILKAIQKL 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 782-843 4.17e-13

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 64.98  E-value: 4.17e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFlSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 843
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAI 60
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 713-773 1.69e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 63.44  E-value: 1.69e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  713 QSVGEWLEAVGLQQYEsKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:pfam00536    6 EDVGEWLESIGLGQYI-DSFRAGYIDGDALLQ--LTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 781-843 8.80e-12

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 61.54  E-value: 8.80e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952677825   781 YDGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVkNLWELELVNVLKVHLLGHRKRIIASL 843
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLL-LLTSEEDLKELGITKLGHRKKILKAI 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 160-295 8.13e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 8.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  160 NETALHCAAQYGHTEVVKVLLE-ELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLL-----SCNTKKHTPLHLA 233
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  234 ARNGHKAVVQVLLDAGMDSNYQTEKGSA---------------LHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 295
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 70-98 3.22e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.22e-05
                            10        20
                    ....*....|....*....|....*....
gi 1952677825    70 GYTPLHHAALNGHKDVVEVLLRNDALTNV 98
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 25-279 3.04e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   25 GSSFRNGFVGFCSLLVY--VTSVRVSLDQSNLRsiwrgpNVNCVDSTGYTPLHHAAL-NGHKDVVEVLLRNDALTNVADS 101
Cdd:TIGR00870   11 ESPLSDEEKAFLPAAERgdLASVYRDLEEPKKL------NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  102 KgcypLHLAAwKGDAQIVRLLIhqgpshtrvneqnTLEIKEFKKYGPFdPYINAKNNDNE----TALHCAAQYGHTEVVK 177
Cdd:TIGR00870   85 L----LHAIS-LEYVDAVEAIL-------------LHLLAAFRKSGPL-ELANDQYTSEFtpgiTALHLAAHRQNYEIVK 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  178 VLLEELTD-----------PTMRNNKF---ETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAA-----RNGH 238
Cdd:TIGR00870  146 LLLERGASvparacgdffvKSQGVDSFyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefKAEY 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  239 KAVVQ------VLLDAGMDS--------NYQTEKGSALheAALFGKTDVVQILLA 279
Cdd:TIGR00870  226 EELSCqmynfaLSLLDKLRDskelevilNHQGLTPLKL--AAKEGRIVLFRLKLA 278
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 940-1085 2.76e-100

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269972  Cd Length: 146  Bit Score: 313.83  E-value: 2.76e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  940 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHE 1019
Cdd:cd01274      1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLKKSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825 1020 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKS 1085
Cdd:cd01274     81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-296 8.56e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.53  E-value: 8.56e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   62 NVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrvneqntleik 141
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD------------- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  142 efkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLS 221
Cdd:COG0666    113 -----------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  222 CNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 296
Cdd:COG0666    182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGkTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-295 1.67e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 1.67e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   60 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrvneqntle 139
Cdd:COG0666     77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD----------- 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  140 ikefkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNL 219
Cdd:COG0666    146 -------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  220 LSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 295
Cdd:COG0666    213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-316 2.43e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 2.43e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   71 YTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPshtrvneqntleikefkkygpfd 150
Cdd:COG0666     22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA----------------------- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  151 pYINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPL 230
Cdd:COG0666     79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  231 HLAARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALDTVRElpsQKSQQI 309
Cdd:COG0666    158 HLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE---NGNLEI 234


                   ....*..
gi 1952677825  310 AALIEDH 316
Cdd:COG0666    235 VKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-263 1.75e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 1.75e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   59 RGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrvneqntl 138
Cdd:COG0666    109 AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD---------- 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  139 eikefkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPN 218
Cdd:COG0666    179 --------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1952677825  219 LLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEKGSALH 263
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 711-777 9.08e-37

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188898  Cd Length: 67  Bit Score: 132.81  E-value: 9.08e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  711 LEQSVGEWLEAVGLQQYESKLLLNGFDDVRFLGSNVMEEQDLRDIGITDPQHRRKLLQAAKSLPKVK 777
Cdd:cd09499      1 VVQSVGQWLESIGLPQYESKLLLNGFDDVDFLGSGVMEDQDLKEIGITDEQHRQIILQAARSLPKKK 67
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 952-1085 3.85e-36

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 133.21  E-value: 3.85e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   952 ESCGYEANYLGSMLIKDLRGTESTQDACAKMRKS-TEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDP 1030
Cdd:smart00462    2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  1031 EDLCTFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQLALQAQKS 1085
Cdd:smart00462   82 DDLDVFGYIARDPGSSRFACHVFRCEKAA--EDIALAIGQAFQLAYELKLKARSE 134
SAM_AIDA1AB-like_repeat2 cd09500
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ...
 782-846 8.05e-36

SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188899  Cd Length: 65  Bit Score: 129.73  E-value: 8.05e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVHLLGHRKRIIASLADR 846
Cdd:cd09500      1 DGNSPASVSEWLDSIGLGDYIETFLKHGYTSMERVKRIWEVELTNVLEINKLGHRKRILASLADR 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-295 1.18e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.42  E-value: 1.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  152 YINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLH 231
Cdd:COG0666     13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  232 LAARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 295
Cdd:COG0666     93 AAARNGDLEIVKLLLEAGADVNARDKDGeTPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 954-1072 1.85e-24

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 99.51  E-value: 1.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  954 CGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPT-IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPED 1032
Cdd:cd00934      1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGpVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1952677825 1033 LCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAF 1072
Cdd:cd00934     81 PNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
Ank_2 pfam12796
Ankyrin repeats (3 copies);
197-288 5.43e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 5.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  197 LDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDaGMDSNYQTEKGSALHEAALFGKTDVVQI 276
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1952677825  277 LLAAGIDVNIKD 288
Cdd:pfam12796   80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-254 3.18e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 3.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   59 RGPNVNCVDSTGYTPLHHAALN--GHKDVVEVLLRNDALTNVADSKGCYPLHLAAW--KGDAQIVRLLIHQGpshTRVNE 134
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKG---VDINA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  135 QNtlEIKEFKKYGpFDpyINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLN 214
Cdd:PHA03100   172 KN--RVNYLLSYG-VP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1952677825  215 AHPNLlscNTKKHTPLHLAARN----------GHKAVVQVLLDAGMDSNY 254
Cdd:PHA03100   247 NGPSI---KTIIETLLYFKDKDlntitkikmlKKSIMYMFLLDPGFYKNR 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
164-255 5.35e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 5.35e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  164 LHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNaHPNlLSCNTKKHTPLHLAARNGHKAVVQ 243
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HAD-VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1952677825  244 VLLDAGMDSNYQ 255
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-295 6.09e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.79  E-value: 6.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   60 GPNVNCVDSTGYTPLH---HAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGD-AQIVRLLIhqgpshtrvneq 135
Cdd:PHA03095    37 GADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLI------------ 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  136 ntleikefkKYGpfdPYINAKNNDNETALH--CAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDlaALYGR----LEVV 209
Cdd:PHA03095   105 ---------KAG---ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELL 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  210 KMLLNAHPNLLSCNTKKHTPLHLAARNGH--KAVVQVLLDAGMDSNYQTEKG-SALHEAALFG--KTDVVQILLAAGIDV 284
Cdd:PHA03095   171 RLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGnTPLHSMATGSscKRSLVLPLLIAGISI 250

                          250
                   ....*....|.
gi 1952677825  285 NIKDNRGLTAL 295
Cdd:PHA03095   251 NARNRYGQTPL 261
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-328 9.60e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.49  E-value: 9.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   60 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGpshtrvneqntle 139
Cdd:PHA02874   114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG------------- 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  140 ikefkkygpfdPYINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNL 219
Cdd:PHA02874   181 -----------AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASIND 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  220 LSCNtkKHTPLHLAArnghkavvqvlldagmdsNYQTEKgsalheaalfgktDVVQILLAAGIDVNIKDNRGLTALDTVR 299
Cdd:PHA02874   250 QDID--GSTPLHHAI------------------NPPCDI-------------DIIDILLYHKADISIKDNKGENPIDTAF 296

                          250       260
                   ....*....|....*....|....*....
gi 1952677825  300 ELPSQKSqqiaaLIEDHMTGKRSAKEVDK 328
Cdd:PHA02874   297 KYINKDP-----VIKDIIANAVLIKEADK 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
74-190 2.00e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 2.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   74 LHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIhqgpSHTRVNEQntleikefkkygpfdpyi 153
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLK------------------ 58

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1952677825  154 naknNDNETALHCAAQYGHTEVVKVLLEELTDPTMRN 190
Cdd:pfam12796   59 ----DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 944-1081 9.18e-19

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269971  Cd Length: 144  Bit Score: 83.87  E-value: 9.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  944 HQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMrKSTEHMK-----KIPTIILSITYKGVKFIDASNKNVIAEH 1018
Cdd:cd01273      2 HPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKL-KFARQLKksegaKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952677825 1019 EIRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFstVDVNLTYEIILTLGQAFEVAYQLALQ 1081
Cdd:cd01273     81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVF--DSEKLAEEITLTIGQAFDLAYRRFLE 141
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 60-289 1.29e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 1.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   60 GPNVNCVDSTGYTPLHHAALNGH-----KDVVEVLLRNDALTNVADSKGCYPLHLAAWK--GDAQIVRLLIHQGpshtrv 132
Cdd:PHA03100    58 GADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG------ 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  133 neqntleIKefkkygpfdpyINAKNNDNETALHCAAQYGH--TEVVKVLLEELTDPTMRNNkfetpldlaalygrlevVK 210
Cdd:PHA03100   132 -------AN-----------VNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  211 MLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEKGSA-LHEAALFGKTDVVQILLAAGIDVNIKDN 289
Cdd:PHA03100   177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTpLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 708-771 2.38e-16

SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance.


Pssm-ID: 188890  Cd Length: 63  Bit Score: 74.48  E-value: 2.38e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952677825  708 SRTLEQSVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnVMEEqDLRDIGITDPQHRRKLLQAAK 771
Cdd:cd09491      1 SLSWPKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSD-ITEE-DLEEAGVTNPAHKRRLLDSLQ 62
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 77-358 2.54e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.73  E-value: 2.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   77 AALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQG------------PSHTRVNEQNTLEIKEFK 144
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaipdvkypdiesELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  145 KYGPF-DPYINAKNNdneTALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLN--AHPNLLS 221
Cdd:PHA02875    89 DLGKFaDDVFYKDGM---TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDhkACLDIED 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  222 CntKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEKG--SALHEAALFGKTDVVQILLAAGIDVNIK---DNRGLTALD 296
Cdd:PHA02875   166 C--CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcvAALCYAIENNKIDIVRLFIKRGADCNIMfmiEGEECTILD 243

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  297 TVRELPSQ-KSQQIAALIEDHMTGKRSakevdKTLRSQGPLISNMDSISQKSQ-GDV-EKAVTEL 358
Cdd:PHA02875   244 MICNMCTNlESEAIDALIADIAIRIHK-----KTIRRDEGFKNNMSTIEDKEEfKDVfEKCIIEL 303
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
956-1075 1.66e-14

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 71.63  E-value: 1.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  956 YEANYLGSM-------LIKDLRgTESTQDA--CAKM------RKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEI 1020
Cdd:pfam00640    1 FAVRYLGSVevpeeraPDKNTR-MQQAREAirRVKAakinkiRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825 1021 RNIS-CAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDvnLTYEIILTLGQAFEVA 1075
Cdd:pfam00640   80 VSISfCADGDPDLMRYFAYIARDKATNKFACHVFESED--GAQDIAQSIGQAFALA 133
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 956-1077 2.00e-14

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269983  Cd Length: 120  Bit Score: 70.74  E-value: 2.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  956 YEANYLGSMLIKDLRGTESTQDACAKMRksteHMKKIPT-IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPEDLC 1034
Cdd:cd13161      4 FEAKYLGSVPVKEPKGNDVVMAAVKRLK----DLKLKPKpVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1952677825 1035 TFAYITKDLQTSHHYCHVFSTVDVNltYEIILTLGQAFEVAYQ 1077
Cdd:cd13161     80 LFAFISHDPRLGRITCHVFRCKRGA--QEICDTIAEAFKAAAE 120
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-133 5.26e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 5.26e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825   57 IWRGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNvaDSKGCYPLHLAAWKGDAQIVRLLIHQGPSHTRVN 133
Cdd:pfam12796   17 LENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-295 8.48e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.45  E-value: 8.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   57 IWRGPNVNCVDSTGYTPLH-HAA-LNGHKDVVEVLLRNDALTNVADSKGCYPLH--LAAWKGDAQIVRLLIHQGpshtrv 132
Cdd:PHA03095   104 IKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAG------ 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  133 neqntleikefkkygpFDPYinAKNNDNETALHCAAQYGHT--EVVKVLLEELTDPTMRNNKFETPLDLAALYGrlevvk 210
Cdd:PHA03095   178 ----------------ADVY--AVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGS------ 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  211 mllnahpnllSCNtkkhtplhlaarnghKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDN 289
Cdd:PHA03095   234 ----------SCK---------------RSLVLPLLIAGISINARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSS 288


                   ....*.
gi 1952677825  290 RGLTAL 295
Cdd:PHA03095   289 DGNTPL 294
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 714-773 1.70e-13

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 66.55  E-value: 1.70e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLgsNVMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:smart00454    8 SVADWLESIGLEQYADNFRKNGIDGALLL--LLTSEEDLKELGITKLGHRKKILKAIQKL 65
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 956-1073 1.93e-13

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 68.13  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  956 YEANYLGSMLIKDLRGTESTQDACA---KMRKSTEhmKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNIS-CAAqDPE 1031
Cdd:cd13159      5 FYLKYLGSTLVEKPKGEGATAEAVKtiiAMAKASG--KKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISyCTA-DAN 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1952677825 1032 DLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFE 1073
Cdd:cd13159     82 HDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 152-295 3.46e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 3.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  152 YINAKNNDNETALHCAAQYGHT-----EVVKVLLEELTDPTMRNNKFETPLDLAALY--GRLEVVKMLLNAHPNLLSCNT 224
Cdd:PHA03100    60 DINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952677825  225 KKHTPLHLAARNGH--KAVVQVLLDAGMDSNyqtekgsalheaalfgKTDVVQILLAAGIDVNIKDNRGLTAL 295
Cdd:PHA03100   140 DGENLLHLYLESNKidLKILKLLIDKGVDIN----------------AKNRVNYLLSYGVPINIKDVYGFTPL 196
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 782-843 4.17e-13

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 64.98  E-value: 4.17e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFlSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 843
Cdd:pfam00536    1 DGWSVEDVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLK-LGVTLLGHRKKILYAI 60
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 60-293 9.89e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 9.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   60 GPNVNCVDSTGYTPLHHAALNGH-KDVVEVLLRNDALTNVADSKGCYPLHLAAWKG-DAQIVRLLIHQGPShtrVNEQNT 137
Cdd:PHA02876   263 GFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGAD---VNAADR 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  138 LEIKEFKKYGPFDPY-------------INAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAaLYG 204
Cdd:PHA02876   340 LYITPLHQASTLDRNkdivitllelganVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCG 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  205 R--LEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKA-VVQVLLDAGMDSNYQTEKGSALHEAALfGKTDVVQILLAAG 281
Cdd:PHA02876   419 TnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLLIAL-EYHGIVNILLHYG 497

                          250
                   ....*....|..
gi 1952677825  282 IDvnIKDNRGLT 293
Cdd:PHA02876   498 AE--LRDSRVLH 507
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 713-773 1.69e-12

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 63.44  E-value: 1.69e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  713 QSVGEWLEAVGLQQYEsKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:pfam00536    6 EDVGEWLESIGLGQYI-DSFRAGYIDGDALLQ--LTEDDLLKLGVTLLGHRKKILYAIQRL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
174-295 2.29e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.21  E-value: 2.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  174 EVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSN 253
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1952677825  254 YQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 295
Cdd:COG0666     82 AKDDGGnTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
713-773 2.32e-12

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 63.06  E-value: 2.32e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  713 QSVGEWLEAVGLQQYESKLLLNGFDDVRFLgsNVMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:pfam07647    7 ESVADWLRSIGLEQYTDNFRDQGITGAELL--LRLTLEDLKRLGITSVGHRRKILKKIQEL 65
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 781-843 8.80e-12

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 61.54  E-value: 8.80e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952677825   781 YDGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVkNLWELELVNVLKVHLLGHRKRIIASL 843
Cdd:smart00454    1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLL-LLTSEEDLKELGITKLGHRKKILKAI 62
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 940-1057 3.22e-11

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 241298  Cd Length: 135  Bit Score: 61.94  E-value: 3.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  940 QSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTehmKKIPTIILSITYKGVKFIDASNKNVIAEHE 1019
Cdd:cd01268      1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASR---KKPVRAVLWVSGDGLRVVDEKTKGLIVDQT 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1952677825 1020 IRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVD 1057
Cdd:cd01268     78 IEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVK 115
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 714-771 3.50e-11

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 59.56  E-value: 3.50e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLgsnVMEEQDLRDIGITDPQHRRKLLQAAK 771
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRKNEIDGDALL---LLTDEDLKELGITSPGHRKKILRAIQ 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
162-213 7.75e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 7.75e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  162 TALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLL 213
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 958-1076 7.84e-11

Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269979  Cd Length: 129  Bit Score: 60.86  E-value: 7.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  958 ANYLGSMLIKDLrgteSTQDACAKMRKSTEHMKKIPT----IILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPEDl 1033
Cdd:cd13157      6 AQYIGSFPVSGL----DVADRADSVRKQLESLKESGSrgrpVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAH- 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1952677825 1034 CTFAYITKDLQ--TSHHYCHVFSTVDVNLTYEIILTLGQAFEVAY 1076
Cdd:cd13157     81 AQFAFVARNPGgpTNRQYCHVFVTRSPREAQELNLLLCRAFQLAY 125
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-213 1.14e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   57 IWRGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWK-GDAQIVRLLIHQGpshTRVNEQ 135
Cdd:PHA02878   188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG---VDVNAK 264

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952677825  136 NTLEikefkkygpfdpyinaknndNETALHCAAQygHTEVVKVLLEELTDPTMRNNKFETPLDLAAL-YGRLEVVKMLL 213
Cdd:PHA02878   265 SYIL--------------------GLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILI 321
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 80-297 1.38e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 1.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   80 NGHKDVVEVLLRNDA-LTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPSHTRVNEQNTLEIKEFKKYGPFDPYINAKNN 158
Cdd:PHA02874    11 SGDIEAIEKIIKNKGnCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  159 DNETALHCAAQYgHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGH 238
Cdd:PHA02874    91 GVDTSILPIPCI-EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  239 KAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALDT 297
Cdd:PHA02874   170 FDIIKLLLEKGAYANVKDNNGeSPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
SAM_SASH-like cd09493
SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like ...
 713-772 1.98e-10

SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. Proteins of this subfamily are known to be involved in preventing DN thymocytes from premature initiation of programmed cell death and in B cells activation and differentiation. They have been found downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues.


Pssm-ID: 188892  Cd Length: 60  Bit Score: 57.51  E-value: 1.98e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  713 QSVGEWLEAVGLQQYESKLLLNGFDDVRFLgsNVMEEQDLRDIGITDPQHRRKLLQAAKS 772
Cdd:cd09493      3 KTVEELLERINLQEHTSTLLLNGYETLEDF--KDLKESHLNELNITDPEHRAKLLTAAEL 60
PHA03095 PHA03095
ankyrin-like protein; Provisional
 174-296 2.86e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 2.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  174 EVVKVLLEELTDPTMRNNKFETPLDLAALYG---RLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKA-VVQVLLDAG 249
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  250 MDSNYQTEKG-SALHeAALFGK---TDVVQILLAAGIDVNIKDNRGLTALD 296
Cdd:PHA03095   108 ADVNAKDKVGrTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLA 157
Ank_4 pfam13637
Ankyrin repeats (many copies);
70-123 1.61e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1952677825   70 GYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLI 123
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 994-1081 1.80e-09

Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Shc-like subgroup.


Pssm-ID: 269920  Cd Length: 170  Bit Score: 57.99  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  994 TIILSITYKGVKFIDASNKNVIAEHEIRNISCAA-QDPEDLCTFAYITKDlQTSHHYCHVFSTVDvNLTYEIILTLGQAF 1072
Cdd:cd01209     84 NISLTISTDGLNLVTPDTGQIIANHHMQSISFASgGDPDTYDYVAYVAKD-PVNQRACHVLECGD-GLAQDVIATIGQAF 161


                   ....*....
gi 1952677825 1073 EVAYQLALQ 1081
Cdd:cd01209    162 ELRFKQYLK 170
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 785-843 2.49e-09

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 54.16  E-value: 2.49e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952677825  785 SPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 843
Cdd:cd09488      1 AFRSVGEWLESIKMGRYKENFTAAGYTSLDAVAQMTAEDLTR-LGVTLVGHQKKILNSI 58
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 132-289 2.73e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 2.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  132 VNEQNTLEIKEFKKYGPFDPYINAKNN-DNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGR----- 205
Cdd:PHA03100     6 VLTKSRIIKVKNIKYIIMEDDLNDYSYkKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdv 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  206 LEVVKMLLNAHPNLLSCNTKKHTPLHLAARN--GHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFG--KTDVVQILLAA 280
Cdd:PHA03100    86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGeNLLHLYLESNkiDLKILKLLIDK 165


                   ....*....
gi 1952677825  281 GIDVNIKDN 289
Cdd:PHA03100   166 GVDINAKNR 174
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 783-840 5.38e-09

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 53.84  E-value: 5.38e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  783 GNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNL-WE-LElvnVLKVHLLGHRKRII 840
Cdd:cd09498      4 DYPPNDLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLtWEdLQ---DIGITKLGHQKKLM 60
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
781-845 5.55e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 53.43  E-value: 5.55e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  781 YDGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASLAD 845
Cdd:pfam07647    1 VESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRL-TLEDLKRLGITSVGHRRKILKKIQE 64
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 60-235 5.66e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 5.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   60 GPNVNCVD-STGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGpshtrvneqntl 138
Cdd:PHA02878   157 GADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG------------ 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  139 eikefkkygpfdPYINAKNNDNETALHCAAQY-GHTEVVKVLLEELTDPtmrnNKFETPLDLAALYGRL---EVVKMLLN 214
Cdd:PHA02878   225 ------------ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDV----NAKSYILGLTALHSSIkseRKLKLLLE 288

                          170       180
                   ....*....|....*....|...
gi 1952677825  215 --AHPNLLscNTKKHTPLHLAAR 235
Cdd:PHA02878   289 ygADINSL--NSYKLTPLSSAVK 309
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-295 6.23e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 6.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   57 IWRGPNVNCVDSTGYTPLH----HAALNGHKDVVEVLLRND-ALTNVADSKGCYplhlaawKGDAQIVRLLIhqgpshtr 131
Cdd:PHA02878    57 LTRGHNVNQPDHRDLTPLHiickEPNKLGMKEMIRSINKCSvFYTLVAIKDAFN-------NRNVEIFKIIL-------- 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  132 vneqntleIKEFKK-YGPFDPYINAKNNDNETalhcaaqygHTEVVKVLLEELTDPTMRN-NKFETPLDLAALYGRLEVV 209
Cdd:PHA02878   122 --------TNRYKNiQTIDLVYIDKKSKDDII---------EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLT 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  210 KMLL--NAHPNLLscNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEKGSA-LHEAALFGKT-DVVQILLAAGIDVN 285
Cdd:PHA02878   185 ELLLsyGANVNIP--DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTpLHISVGYCKDyDILKLLLEHGVDVN 262

                          250
                   ....*....|.
gi 1952677825  286 IKDN-RGLTAL 295
Cdd:PHA02878   263 AKSYiLGLTAL 273
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 41-288 6.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 6.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   41 YVTSVRVSLDQSNLRS----IWRGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDA 116
Cdd:PHA02876   145 YMKLIKERIQQDELLIaemlLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  117 QIVRLLIhQGPSHTRVNEQNTLE----------------------IKEFKK----YGPFDPY--------------INAK 156
Cdd:PHA02876   225 DTIKAII-DNRSNINKNDLSLLKairnedletslllydagfsvnsIDDCKNtplhHASQAPSlsrlvpkllergadVNAK 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  157 NNDNETALHCAAQYGH-TEVVKVLLEELTDPTMRNNKFETPLDLAALYGRL-EVVKMLLNAHPNLLSCNTKKHTPLHLAA 234
Cdd:PHA02876   304 NIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAA 383

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  235 RNGHKAVVQVLLDAGMDSNYQTEK-GSALHeAALFGKTDV--VQILLAAGIDVNIKD 288
Cdd:PHA02876   384 VRNNVVIINTLLDYGADIEALSQKiGTALH-FALCGTNPYmsVKTLIDRGANVNSKN 439
Ank_4 pfam13637
Ankyrin repeats (many copies);
195-246 7.11e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 7.11e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  195 TPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLL 246
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
62-110 1.11e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 1.11e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1952677825   62 NVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLA 110
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_SAMSN1 cd09561
SAM domain of SAMSN1 subfamily; SAM (sterile alpha motif) domain of SAMSN1 (also known as ...
 709-773 1.81e-08

SAM domain of SAMSN1 subfamily; SAM (sterile alpha motif) domain of SAMSN1 (also known as HACS1 or NASH1) proteins is a predicted protein-protein interaction domain. Members of this group are putative signaling/adaptor proteins. They appear to mediate signal transduction in lymphoid tissues. Murine HACS1 protein likely plays a role in B cell activation and differentiation. Potential binding partners of HACS1 are SLAM, DEC205 and PIR-B receptors and also some unidentified tyrosine-phosphorylated proteins. Proteins of this group were found preferentially expressed in normal hematopietic tissues and in some malignancies including lymphoma, myeloid leukemia and myeloma.


Pssm-ID: 188960  Cd Length: 66  Bit Score: 52.17  E-value: 1.81e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  709 RTLEQSVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09561      2 RPKPKTLQELLERIHLQEYTSTLLLNGYETLEDLKD--LKESHLIELNITDPEDRARLLSAAENL 64
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 782-843 2.19e-08

SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design.


Pssm-ID: 188942  Cd Length: 70  Bit Score: 52.15  E-value: 2.19e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASL 843
Cdd:cd09543      1 EGVPFRTVAEWLESIKMQQYTEHFMAAGYNSIDKVLQM-TQEDIKHIGVRLPGHQKRIAYSI 61
Ank_4 pfam13637
Ankyrin repeats (many copies);
228-278 3.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.51e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  228 TPLHLAARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILL 278
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
145-200 3.96e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 3.96e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  145 KYGPFDPyiNAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLA 200
Cdd:pfam13857    3 EHGPIDL--NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 714-773 4.37e-08

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 51.14  E-value: 4.37e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLGSNVMEeqDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09498      9 DLLEWLSLLGLPQYHKVLVENGYDSIDFVTDLTWE--DLQDIGITKLGHQKKLMLAIKKL 66
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 715-773 4.52e-08

SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188926  Cd Length: 63  Bit Score: 50.91  E-value: 4.52e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952677825  715 VGEWLEAVGLQQYESKLLLNGFDDVRFlgSNVMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09527      5 VYDWLRTLQLEQYAEKFVDNGYDDLEV--CKQIGDPDLDAIGVMNPAHRKRILEAVRRL 61
Ank_5 pfam13857
Ankyrin repeats (many copies);
245-296 5.41e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 5.41e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1952677825  245 LLDAG-MDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 296
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGyTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 67-180 5.91e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 5.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   67 DSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIH---------QGPSHTRVNEQNT 137
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfasisdphaAGDLLCTAAKRND 634

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1952677825  138 LE-IKEFKKYGpFDpyINAKNNDNETALHCAAQYGHTEVVKVLL 180
Cdd:PLN03192   635 LTaMKELLKQG-LN--VDSEDHQGATALQVAMAEDHVDMVRLLI 675
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 160-295 8.13e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 8.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  160 NETALHCAAQYGHTEVVKVLLE-ELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLL-----SCNTKKHTPLHLA 233
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  234 ARNGHKAVVQVLLDAGMDSNYQTEKGSA---------------LHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL 295
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 956-1092 9.21e-08

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain; CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269968  Cd Length: 179  Bit Score: 53.44  E-value: 9.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  956 YEANYLGSMLIKdlRGTeSTQDACAKMR------KSTEHMKKIPTIILSITykGVKFI-----------DASNKNVIAEH 1018
Cdd:cd01270     31 FQAKYIGSLEVP--RPS-SRVEIVAAMRriryefKAKNIKKKKVTITVSVD--GVKVVlrkkkkkkgwtWDESKLLLMQH 105

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952677825 1019 EIRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKSRPLGASA 1092
Cdd:cd01270    106 PIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKKSQAMRIVRTIGQAFEVCHKLSLQHMQGNADDEAE 179
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 73-298 2.45e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   73 PLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWK----GDAQIVRLLIHQGPSHT------------------ 130
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTlvaikdafnnrnveifki 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  131 ----RVNEQNTLEIKEFKK-----------------YGPfDPYINAKNNDNeTALHCAAQYGHTEVVKVLLEELTDPTMR 189
Cdd:PHA02878   120 iltnRYKNIQTIDLVYIDKkskddiieaeitklllsYGA-DINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  190 NNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLA-ARNGHKAVVQVLLDAGMDSNYQTE--KGSALHEAa 266
Cdd:PHA02878   198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYilGLTALHSS- 276

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1952677825  267 lFGKTDVVQILLAAGIDVNIKDNRGLTALDTV 298
Cdd:PHA02878   277 -IKSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 956-1049 2.82e-07

Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which binds to the cytoplasmic tails of lipoprotein receptors, such as ApoER2 and VLDLR, via its PTB domain. The dab PTB domain has a preference for unphosphorylated tyrosine within an NPxY motif. Additionally, the Dab PTB domain, which is structurally similar to PH domains, binds to phosphatidlyinositol phosphate 4,5 bisphosphate in a manner characteristic of phosphoinositide binding PH domains. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269926  Cd Length: 147  Bit Score: 51.10  E-value: 2.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  956 YEANYLGSMLIKDLRGTESTQDACAKM----RKSTEHMKKIptiILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPE 1031
Cdd:cd01215     18 FKAKLIGIDEVPAARGDKMCQDAMMKLkgavKAAGEHKQRI---WLNISLEGIKILDEKTGALLHHHPVHKISFIARDTT 94

                           90
                   ....*....|....*...
gi 1952677825 1032 DLCTFAYITKdLQTSHHY 1049
Cdd:cd01215     95 DNRAFGYVCG-LDGGHRF 111
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 788-845 2.92e-07

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.


Pssm-ID: 188945  Cd Length: 66  Bit Score: 48.77  E-value: 2.92e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952677825  788 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASLAD 845
Cdd:cd09546      5 SVGEWLEAIKMGRYTEIFMENGYSSMDAVAQV-TLEDLRRLGVTLVGHQKKIMNSIQE 61
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 788-843 3.25e-07

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 48.34  E-value: 3.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  788 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASL 843
Cdd:cd09547      5 TVSDWLDSIKMGQYKNNFMAAGFTTLDMVSRM-TIDDIRRIGVTLIGHQRRIVSSI 59
SAM_SASH3 cd09560
SAM domain of SASH3 subfamily; SAM (sterile alpha motif) domain of SAHS3 (also known as SLY) ...
 709-773 8.52e-07

SAM domain of SASH3 subfamily; SAM (sterile alpha motif) domain of SAHS3 (also known as SLY) proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative signaling/adaptor proteins. In addition to SAM, they contain SLY and SH3 domains. They appear to mediate signal transduction in lymphoid tissues. Murine SASH3 is involved in preventing DN thymocytes from premature initiation of programmed cell death and in mTOR (mammalian target of rapamycin) activation via signal integration of the Notch receptor and preTCR (T cell receptor) pathways.


Pssm-ID: 188959  Cd Length: 68  Bit Score: 47.39  E-value: 8.52e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  709 RTLEQSVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09560      2 RPKPKTLHELLERIGLEEHTSTLLLNGYQTLEDFKE--LRETHLNELNIMDPQHRAKLLTAAELL 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 108-213 9.64e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 9.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  108 HLAAwKGDAQIVRLLIHQGPshtrvneqntleikefkkygpfDPyiNAKNNDNETALHCAAQYGHTEVVKVLLEELTDPT 187
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGA----------------------DP--NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT 142

                           90       100
                   ....*....|....*....|....*.
gi 1952677825  188 MRNNKFETPLDLAALYGRLEVVKMLL 213
Cdd:PTZ00322   143 LLDKDGKTPLELAEENGFREVVQLLS 168
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 715-773 1.02e-06

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 47.02  E-value: 1.02e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  715 VGEWLEAVGLQQYESKLLLNgfdDVRflGSNVM--EEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09507     10 VGAWLESLQLGEYRDIFARN---DIR--GSELLhlERRDLKDLGITKVGHVKRILQAIKDL 65
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 135-293 1.52e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 52.45  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  135 QNTLEIKEF-----KKYGPFDPYINA----KNNDNETALHCAAQYGHTEVVKVLLEELTD-----------PTMRNNKF- 193
Cdd:cd22194    107 ENTKEIVRIllafaEENGILDRFINAeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvffnPKYKHEGFy 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  194 --ETPLDLAALYGRLEVVKMLL-NAHPNLLSCNTKKHTPLH---LAARNGH------KAVVQVLLDAGMDSNYQT---EK 258
Cdd:cd22194    187 fgETPLALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLHalvTVAEDSKtqndfvKRMYDMILLKSENKNLETirnNE 266

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1952677825  259 G-SALHEAALFGKTDVVQILLaaGIDVNIKDNRGLT 293
Cdd:cd22194    267 GlTPLQLAAKMGKAEILKYIL--SREIKEKPNRSLS 300
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 714-773 1.78e-06

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 46.40  E-value: 1.78e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09549      9 SVGEWLEALDLCRYKDNFAAAGYGSLEAVAR--MTAQDVLSLGITSLEHQELLLAGIQAL 66
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 60-129 2.51e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.51e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   60 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPSH 129
Cdd:PTZ00322   105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
SAM_SASH1_repeat1 cd09559
SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins ...
 713-773 2.75e-06

SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers, relative to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis.


Pssm-ID: 188958  Cd Length: 66  Bit Score: 45.78  E-value: 2.75e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  713 QSVGEWLEAVGLQQYESKLLLNGFDDVRFLgsNVMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09559      4 KSVEDLLDRINLKEHMPTFLFNGYEDLDTF--KLLEEEDLDELNIRDPEHRAVLLTAVELL 62
SAM_SASH1_repeat2 cd09492
SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins ...
 714-773 3.58e-06

SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis.


Pssm-ID: 188891  Cd Length: 70  Bit Score: 45.58  E-value: 3.58e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09492      9 SVSDWLVSIGLPMYSPPLLEAGFSTLSRVSS--LSETCLREAGITEERHIRKLLSAARLV 66
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 59-213 3.93e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 3.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   59 RGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKgDAQIVRLLIHQGPshtrvneqntl 138
Cdd:PHA02874   179 KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNAS----------- 246

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  139 eikefkkygpfdpyINAKNNDNETALHCAAQYG-HTEVVKVLLEELTDPTMRNNKFETPLDLAALY-GRLEVVKMLL 213
Cdd:PHA02874   247 --------------INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
60-90 6.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 6.04e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1952677825   60 GPNVNCVDSTGYTPLHHAALNGHKDVVEVLL 90
Cdd:pfam13637   24 GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTB_JIP cd01212
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ...
 980-1077 6.26e-06

JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a mitogen-activated protein kinase scaffold protein. JIP consists of a C-terminal SH3 domain, followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269923  Cd Length: 149  Bit Score: 47.27  E-value: 6.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  980 AKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIA-------EHEIRNIS-CAAQdPEDLCTFAYITK--DLQTSHhy 1049
Cdd:cd01212     32 ATARRLTVHLRPPQSCILEISDRGLKMVDRSKPNKKDgkpcihyFYSLKNISfCGFH-PRNSRYFGFITKhpLLQRFA-- 108

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1952677825 1050 CHVF----STVDVNltyEIIltlGQAFEVAYQ 1077
Cdd:cd01212    109 CHVFvsqeSTRPVA---ESV---GRAFQRFYQ 134
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 167-343 6.34e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 6.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  167 AAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLL 246
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  247 DAGMDSNYQTeKGSALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL---------DTVRELPSQKSQQIAALIEDHM 317
Cdd:PLN03192   612 HFASISDPHA-AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALqvamaedhvDMVRLLIMNGADVDKANTDDDF 690

                          170       180
                   ....*....|....*....|....*.
gi 1952677825  318 TGKRSAKEVDKtlRSQGPLISNMDSI 343
Cdd:PLN03192   691 SPTELRELLQK--RELGHSITIVDSV 714
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 782-845 6.40e-06

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 45.02  E-value: 6.40e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVHLLGHRKRIIASLAD 845
Cdd:cd09553      2 DYTTFTTVGDWLDAIKMGRYKENFVSAGFASFDLVAQMTAEDLLRI-GVTLAGHQKKILSSIQD 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
262-301 1.27e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 1.27e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1952677825  262 LHEAALFGKTDVVQILLAAGIDVNIKDNRGLTAL---------DTVREL 301
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALhlaaknghlEIVKLL 49
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-180 1.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.30e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  106 PLHLAAWKGDAQIVRLLIHQGPShtrvneqntleikefkkygpfdpyINAKNNDNETALHCAAQYGHTEVVKVLL 180
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGAD------------------------INAVDGNGETALHFAASNGNVEVLKLLL 54
SAM_EPH-R cd09488
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ...
 714-773 1.36e-05

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.


Pssm-ID: 188887  Cd Length: 61  Bit Score: 43.76  E-value: 1.36e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGF---DDVRFlgsnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09488      4 SVGEWLESIKMGRYKENFTAAGYtslDAVAQ-----MTAEDLTRLGVTLVGHQKKILNSIQAL 61
SAM_SARM1-like_repeat2 cd09502
SAM domain of SARM1-like, repeat 2; SAM (sterile alpha motif) domain repeat 2 of SARM1-like ...
 717-771 1.36e-05

SAM domain of SARM1-like, repeat 2; SAM (sterile alpha motif) domain repeat 2 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.


Pssm-ID: 188901  Cd Length: 70  Bit Score: 44.21  E-value: 1.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  717 EWLEAVG--LQQYESKLLLNGFDdvRFLGSNVMEEQDLRDIGITDPQHRRKLLQAAK 771
Cdd:cd09502     12 NWLQSLGpeYSQYTYQMLNAGID--RNSLPSLTEDQLLEDCGITNGIHRLRILNAIK 66
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 714-773 1.44e-05

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 43.87  E-value: 1.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09551      8 SVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQ--MTSEDLLRIGVTLAGHQKKILNSIQSM 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 174-295 1.45e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  174 EVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLN--AHPNLlscNTKKH-TPLHLAARNGH-----KAVVQVL 245
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDngADINS---STKNNsTPLHYLSNIKYnltdvKEIVKLL 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1952677825  246 LDAGMDSNYQTEKG-SALHEAA--LFGKTDVVQILLAAGIDVNIKDNRGLTAL 295
Cdd:PHA03100    93 LEYGANVNAPDNNGiTPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLL 145
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
 955-1072 1.91e-05

uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of LOC417372 and its related proteins are unknown to date. Members here contain a N-terminal RUN domain, followed by a PDZ domain, and a C-terminal PTB domain. The RUN domain is involved in Ras-like GTPase signaling. The PDZ domain (also called DHR/Dlg homologous region or GLGF after its conserved sequence motif) binds C-terminal polypeptides, internal (non-C-terminal) polypeptides, and lipids. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269989  Cd Length: 125  Bit Score: 45.40  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  955 GYEANYLGSMLIKDLRGTESTQDACAKMRKStEHMKKIP-TIILSITykGVKFIDASNKNVIAEHEIRNISCAAQDPEDL 1033
Cdd:cd13168      2 LYKALYLGQVEVGEDGGVEQIESAAIIVVLE-SDLTPKEvLLELGEI--GVTVWDKSTSEVLFKHSFPEISSCGRRVDDP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1952677825 1034 CTFAYITKDLQTS---HHYCHVFSTVDVNLTYEIILTLGQAF 1072
Cdd:cd13168     79 NYFAYIAGDTPCSlakHFVCYVFEAADEEEAETILQGIAQGF 120
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 714-773 1.97e-05

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 43.70  E-value: 1.97e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLgSNVmEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09554      5 SVGEWLRAIKMERYEDSFLQAGFTTFQLV-SQI-STEDLLRMGVTLAGHQKKILSSIQAM 62
SAM_EPH-A4 cd09545
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 714-773 2.06e-05

SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.


Pssm-ID: 188944  Cd Length: 71  Bit Score: 43.79  E-value: 2.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09545      5 SVDDWLQAIKMERYKDNFTAAGYTTLEAVVH--MNQDDLARIGISAIAHQNKILSSVQGM 62
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 717-768 2.06e-05

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 43.40  E-value: 2.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1952677825  717 EWLEAVGLQQYESKLLLNGFDdvrfLGS-NVMEEQDLRDIGITDPQHRRKLLQ 768
Cdd:cd09497      9 DWLREFGLEEYTPNFIKAGYD----LPTiSRMTPEDLTAIGITKPGHRKKLKS 57
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 61-126 2.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 2.09e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825   61 PNVNCVDSTgyTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQG 126
Cdd:PHA02875   128 PDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
SAM_EPH-B4 cd09554
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 788-843 2.54e-05

SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design.


Pssm-ID: 188953  Cd Length: 67  Bit Score: 43.31  E-value: 2.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  788 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 843
Cdd:cd09554      5 SVGEWLRAIKMERYEDSFLQAGFTTFQLVSQISTEDLLR-MGVTLAGHQKKILSSI 59
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 788-843 2.77e-05

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 42.93  E-value: 2.77e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  788 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASL 843
Cdd:cd09550      4 SVDDWLDSIKMGRYKDHFAAGGYSSLGMVMRM-NIEDIRRLGITLMGHQKKILTSI 58
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 70-98 3.22e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.22e-05
                            10        20
                    ....*....|....*....|....*....
gi 1952677825    70 GYTPLHHAALNGHKDVVEVLLRNDALTNV 98
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 70-94 3.70e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 3.70e-05
                           10        20
                   ....*....|....*....|....*
gi 1952677825   70 GYTPLHHAALNGHKDVVEVLLRNDA 94
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGA 26
SAM_EPH-A7 cd09548
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 782-843 3.97e-05

SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188947  Cd Length: 70  Bit Score: 42.71  E-value: 3.97e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLwELELVNVLKVHLLGHRKRIIASL 843
Cdd:cd09548      3 DFTSFCSVGEWLEAIKMERYKDNFTAAGYNSLESVARM-TIEDVMSLGITLVGHQKKIMSSI 63
Ank_4 pfam13637
Ankyrin repeats (many copies);
260-296 4.18e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.18e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1952677825  260 SALHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALD 296
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALH 39
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-233 4.76e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.76e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1952677825  185 DPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLA 233
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTB_X11 cd01208
X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is ...
 958-1082 4.77e-05

X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is unknown to date. X11 has a PTB domain followed by two PDZ domains. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269919  Cd Length: 161  Bit Score: 44.97  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  958 ANYLGSMLIKdlrgTESTQDACAKMRKSTEHMKKIPT----------IILSITYKGVKFIDASNKNVIAEHEIRNISCAA 1027
Cdd:cd01208     12 ANYLGSTQLL----SERNPSKNVRMAQAQEAVSRVKApegesqpsteVDLFISTERIKVLNADTQETMMDHALRTISYIA 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952677825 1028 -----------------QDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLtyeIILTLGQAFEVAYQLALQA 1082
Cdd:cd01208     88 dignivvlmarrrmprsSSQECVETTPPSQEGKRQYKMICHVFESEDAQL---IAQSIGQAFSVAYQEFLRA 156
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 788-843 5.33e-05

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 42.30  E-value: 5.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952677825  788 SVPSWLDSLGLQDYVHSFLSSGyssIDTVKNLWEL--ELVNVLKVHLLGHRKRIIASL 843
Cdd:cd09542      6 SVSEWLESIRMKRYILHFRSAG---LDTMECVLELtaEDLTQMGITLPGHQKRILCSI 60
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 70-246 6.08e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.31  E-value: 6.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   70 GYTPLHHAALNGHKDVVEVLLRND-ALTNVADS----KGCYPLHLAAWKGDAQIVRLLIHQGPSHTRVNEQNTLeikefk 144
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAApELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTF------ 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  145 kygpFDPYINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVK----MLLNAHPNLL 220
Cdd:cd22192    125 ----FRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEDD 200

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1952677825  221 SC------NTKKHTPLHLAARNGHKAVVQVLL 246
Cdd:cd22192    201 LQpldlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
SAM_EPH-A5 cd09546
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 713-773 6.13e-05

SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression.


Pssm-ID: 188945  Cd Length: 66  Bit Score: 42.23  E-value: 6.13e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  713 QSVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09546      4 RSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQ--VTLEDLRRLGVTLVGHQKKIMNSIQEM 62
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 77-251 8.60e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.78  E-value: 8.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   77 AALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPShtrvneqntleikefkkygpfdpyINAK 156
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN------------------------VHIR 587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  157 NNDNETALHCAAQYGHTEVVKVL--LEELTDPTMRNNKfetpLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAA 234
Cdd:PLN03192   588 DANGNTALWNAISAKHHKIFRILyhFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663

                          170
                   ....*....|....*..
gi 1952677825  235 RNGHKAVVQVLLDAGMD 251
Cdd:PLN03192   664 AEDHVDMVRLLIMNGAD 680
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 159-191 8.87e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 8.87e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1952677825  159 DNETALHCAA-QYGHTEVVKVLLEELTDPTMRNN 191
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_EPH-B3 cd09553
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 714-773 9.42e-05

SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth.


Pssm-ID: 188952  Cd Length: 69  Bit Score: 41.56  E-value: 9.42e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09553      8 TVGDWLDAIKMGRYKENFVSAGFASFDLVAQ--MTAEDLLRIGVTLAGHQKKILSSIQDM 65
SAM_EPH-B1 cd09551
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 782-843 9.69e-05

SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders.


Pssm-ID: 188950  Cd Length: 68  Bit Score: 41.56  E-value: 9.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVHLLGHRKRIIASL 843
Cdd:cd09551      2 DFTAFTSVEDWLSAIKMSQYRDNFLSSGFTSLQLVAQMTSEDLLRI-GVTLAGHQKKILNSI 62
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 227-254 1.09e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 1.09e-04
                            10        20
                    ....*....|....*....|....*...
gi 1952677825   227 HTPLHLAARNGHKAVVQVLLDAGMDSNY 254
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 712-773 1.09e-04

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 41.04  E-value: 1.09e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952677825  712 EQSVGEWLEAVGLQQYESKLLLNGFDdvrflGSNVME-EQD-LRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09534      3 EEFVEEWLNELNCGQYLDIFEKNLIT-----GDLLLElDKEaLKELGITKVGDRIRLLRAIKSL 61
SAM_EPH-B2 cd09552
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 782-843 1.09e-04

SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it.


Pssm-ID: 188951  Cd Length: 71  Bit Score: 41.53  E-value: 1.09e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952677825  782 DGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVHLLGHRKRIIASL 843
Cdd:cd09552      2 DYTSFSTVDEWLDAIKMGQYKESFANAGFTSFDVVSQMTMEDILRV-GVTLAGHQKKILNSI 62
SAM_Samd5 cd09527
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ...
 789-839 1.11e-04

SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown.


Pssm-ID: 188926  Cd Length: 63  Bit Score: 41.28  E-value: 1.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  789 VPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELvNVLKVHLLGHRKRI 839
Cdd:cd09527      5 VYDWLRTLQLEQYAEKFVDNGYDDLEVCKQIGDPDL-DAIGVMNPAHRKRI 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 218-295 1.18e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  218 NLLSCNTKKHTPLHLA------ARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAALFGKTDVVQILLAAGIDVNIKDNR 290
Cdd:PLN03192   511 DLLGDNGGEHDDPNMAsnlltvASTGNAALLEELLKAKLDPDIGDSKGrTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590


                   ....*
gi 1952677825  291 GLTAL 295
Cdd:PLN03192   591 GNTAL 595
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 70-100 1.34e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.34e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952677825   70 GYTPLHHAAL-NGHKDVVEVLLRNDALTNVAD 100
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-126 1.51e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   43 TSVRVSLDqsnlrsiwRGPNVNCVDSTGYTPLHHAALNGHK-DVVEVLLRNDALTNVADSKGCYPLHLAAwkGDAQIVRL 121
Cdd:PHA02876   423 MSVKTLID--------RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNI 492


                   ....*
gi 1952677825  122 LIHQG 126
Cdd:PHA02876   493 LLHYG 497
SAM_KIF24-like cd09541
SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a ...
 717-773 1.79e-04

SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a putative protein-protein interaction domain. This subfamily includes proteins related to human kinesin-like protein KIF24. SAM domain is located at the N-terminus followed by kinesin motor domain. Kinesins are proteins involved in a number of different cell processes including microtubule dynamics and axonal transport. Kinesins of this group belong to N-type; they drive microtubule plus end-directed transport. SAM apparently plays the role of adaptor or scaffold domain. In many cases SAM is known as a mediator of dimerization/oligomerization.


Pssm-ID: 188940  Cd Length: 60  Bit Score: 40.74  E-value: 1.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952677825  717 EWLEAVGLQQYESKLLLNGFDDVRFLGSNVMeeQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09541      5 EWLEEAGLQHYYPAFAAGGVTSIEALAQLTM--QDYASLGVQDMEDKQKLFRLIQTL 59
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 260-289 1.97e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1952677825  260 SALHEAAL-FGKTDVVQILLAAGIDVNIKDN 289
Cdd:pfam00023    4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-257 2.26e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.26e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1952677825  227 HTPLHLAA-RNGHKAVVQVLLDAGMDSNYQTE 257
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_EPH-A6 cd09547
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 714-773 2.40e-04

SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers.


Pssm-ID: 188946  Cd Length: 64  Bit Score: 40.26  E-value: 2.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09547      5 TVSDWLDSIKMGQYKNNFMAAGFTTLDMVSR--MTIDDIRRIGVTLIGHQRRIVSSIQTL 62
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 25-279 3.04e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   25 GSSFRNGFVGFCSLLVY--VTSVRVSLDQSNLRsiwrgpNVNCVDSTGYTPLHHAAL-NGHKDVVEVLLRNDALTNVADS 101
Cdd:TIGR00870   11 ESPLSDEEKAFLPAAERgdLASVYRDLEEPKKL------NINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  102 KgcypLHLAAwKGDAQIVRLLIhqgpshtrvneqnTLEIKEFKKYGPFdPYINAKNNDNE----TALHCAAQYGHTEVVK 177
Cdd:TIGR00870   85 L----LHAIS-LEYVDAVEAIL-------------LHLLAAFRKSGPL-ELANDQYTSEFtpgiTALHLAAHRQNYEIVK 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  178 VLLEELTD-----------PTMRNNKF---ETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAA-----RNGH 238
Cdd:TIGR00870  146 LLLERGASvparacgdffvKSQGVDSFyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefKAEY 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  239 KAVVQ------VLLDAGMDS--------NYQTEKGSALheAALFGKTDVVQILLA 279
Cdd:TIGR00870  226 EELSCqmynfaLSLLDKLRDskelevilNHQGLTPLKL--AAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 159-188 3.17e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.17e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1952677825   159 DNETALHCAAQYGHTEVVKVLLEELTDPTM 188
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 960-1055 3.44e-04

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 41.85  E-value: 3.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  960 YLGSMLIKDLRGTESTQDACAKMRKSTEhmKKIPtIILSI--TYKG-VKFIDASNKNVIAEHEIRNIS-CA---AQDPED 1032
Cdd:cd01211      8 YLGCAKVNAPRSETEALRIMAILREQSA--QPIK-VTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILfCArgpDGTSES 84

                           90       100
                   ....*....|....*....|...
gi 1952677825 1033 LCtFAYITKDLQTSHHYCHVFST 1055
Cdd:cd01211     85 DC-FAFTWSHGETAIFQCHVFRC 106
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 715-769 4.37e-04

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 39.61  E-value: 4.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  715 VGEWLEAVGLQQYESKLLLNGFD-DVRFLgsnvMEEQDLRDIGITDPQHRRKLLQA 769
Cdd:cd09533      2 VADWLSSLGLPQYEDQFIENGITgDVLVA----LDHEDLKEMGITSVGHRLTILKA 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 228-253 5.67e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 5.67e-04
                           10        20
                   ....*....|....*....|....*.
gi 1952677825  228 TPLHLAARNGHKAVVQVLLDAGMDSN 253
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADIN 29
PHA02791 PHA02791
ankyrin-like protein; Provisional
 54-253 8.82e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 42.72  E-value: 8.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825   54 LRSIWRGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKgcYPLHLAAWKGDAQIVRLLIHQGpshtrvn 133
Cdd:PHA02791    14 LKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSG------- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  134 eqntLEIKEFKKYGpfdpyinaknndnETALHCAAQYGHTEVVKVLLEELTDPTMRNNK-FETPLDLAALYGRLEVVKML 212
Cdd:PHA02791    85 ----MDDSQFDDKG-------------NTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTgWKTSFYHAVMLNDVSIVSYF 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1952677825  213 LNAHPN------LLSCntkkhtpLHLAARNGHKAVVQVLLDAGMDSN 253
Cdd:PHA02791   148 LSEIPStfdlaiLLSC-------IHITIKNGHVDMMILLLDYMTSTN 187
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 713-773 1.20e-03

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.


Pssm-ID: 188974  Cd Length: 65  Bit Score: 38.39  E-value: 1.20e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  713 QSVGEWLEAVGLQQYESKLLLNgfdDVRFLGSNVMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09575      8 EEVAAWLEHLSLCEYKDIFTRH---DVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 791-844 1.26e-03

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 38.39  E-value: 1.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952677825  791 SWLDSLGLQDYVHSFLSSGYssidtvkNLWEL-----ELVNVLKVHLLGHRKRIIASLA 844
Cdd:cd09497      9 DWLREFGLEEYTPNFIKAGY-------DLPTIsrmtpEDLTAIGITKPGHRKKLKSEIA 60
SAM_liprin-beta1,2_repeat1 cd09563
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 713-772 1.52e-03

SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.


Pssm-ID: 188962  Cd Length: 64  Bit Score: 37.98  E-value: 1.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  713 QSVGEWLEAVGLQQYESKLLLNGFDDVRFLGsnvMEEQDL-RDIGITDPQHRRKLLQAAKS 772
Cdd:cd09563      7 EQVCDWLAELGLGQYVDECRRWVKSGQTLLK---ASPQELeKELGIKHPLHRKKLQLALQA 64
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 714-767 1.96e-03

SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia.


Pssm-ID: 188889  Cd Length: 63  Bit Score: 37.66  E-value: 1.96e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVR-FLGSNvmeEQDLRDIGITDPQHRRKLL 767
Cdd:cd09490      5 DIAEWLASIHLEQYLDLFREHGYVTATdCQGIN---DSRLKQIGISPTGHRRRIL 56
SAM_EPH-A2 cd09543
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ...
 713-766 2.52e-03

SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design.


Pssm-ID: 188942  Cd Length: 70  Bit Score: 37.51  E-value: 2.52e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1952677825  713 QSVGEWLEAVGLQQYESKLLLNGFDDVRFLgsNVMEEQDLRDIGITDPQHRRKL 766
Cdd:cd09543      6 RTVAEWLESIKMQQYTEHFMAAGYNSIDKV--LQMTQEDIKHIGVRLPGHQKRI 57
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 139-296 2.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  139 EIKEFKKYGPFdpyINAKNNDNETALH-CAAQ-YGHTEVVKVLLEELTDPT--MRNNKFeTPLDLAALYGR---LEVVKM 211
Cdd:PHA02859    33 DIEGVKKWIKF---VNDCNDLYETPIFsCLEKdKVNVEILKFLIENGADVNfkTRDNNL-SALHHYLSFNKnvePEILKI 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  212 LLNAHPNLLSCNTKKHTPLH--LAARNGHKAVVQVLLDAGmDSNYQTEK--GSALHEAALFGKTD-VVQILLAAGIDVNI 286
Cdd:PHA02859   109 LIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSG-VSFLNKDFdnNNILYSYILFHSDKkIFDFLTSLGIDINE 187

                          170
                   ....*....|
gi 1952677825  287 KDNRGLTALD 296
Cdd:PHA02859   188 TNKSGYNCYD 197
SAM_Arap1,2,3 cd09490
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ...
 788-843 2.87e-03

SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia.


Pssm-ID: 188889  Cd Length: 63  Bit Score: 37.27  E-value: 2.87e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  788 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELvNVLKVHLLGHRKRIIASL 843
Cdd:cd09490      5 DIAEWLASIHLEQYLDLFREHGYVTATDCQGINDSRL-KQIGISPTGHRRRILKQL 59
SAM_Ship2 cd09491
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ...
 786-845 3.21e-03

SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance.


Pssm-ID: 188890  Cd Length: 63  Bit Score: 37.12  E-value: 3.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  786 PPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVlKVHLLGHRKRIIASLAD 845
Cdd:cd09491      5 PKTVSEWLMNLGLQQYEEGLMHNGWDSLEFLSDITEEDLEEA-GVTNPAHKRRLLDSLQD 63
SAM_EPH-B6 cd09555
SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 717-767 3.22e-03

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.


Pssm-ID: 188954  Cd Length: 69  Bit Score: 37.22  E-value: 3.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1952677825  717 EWLEAVGLQQYE---SKLLLNGFDDVrflgsNVMEEQDLRDIGITDPQHRRKLL 767
Cdd:cd09555     11 AWLSAIGLECYQdnfSKFGLCTFSDV-----AQLSLEDLPALGITLAGHQKKLL 59
SAM_EPH-A1 cd09542
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 713-767 4.28e-03

SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell.


Pssm-ID: 188941  Cd Length: 63  Bit Score: 36.91  E-value: 4.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  713 QSVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLL 767
Cdd:cd09542      5 RSVSEWLESIRMKRYILHFRSAGLDTMECVLE--LTAEDLTQMGITLPGHQKRIL 57
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 195-219 4.68e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.68e-03
                            10        20
                    ....*....|....*....|....*
gi 1952677825   195 TPLDLAALYGRLEVVKMLLNAHPNL 219
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADI 28
SAM_AIDA1AB-like_repeat1 cd09499
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ...
 788-840 5.19e-03

SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions.


Pssm-ID: 188898  Cd Length: 67  Bit Score: 36.51  E-value: 5.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  788 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKN--LWELELVNVlKVHLLGHRKRII 840
Cdd:cd09499      4 SVGQWLESIGLPQYESKLLLNGFDDVDFLGSgvMEDQDLKEI-GITDEQHRQIIL 57
SAM_EPH-A10 cd09549
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 788-843 5.43e-03

SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers.


Pssm-ID: 188948  Cd Length: 70  Bit Score: 36.77  E-value: 5.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952677825  788 SVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNvLKVHLLGHRKRIIASL 843
Cdd:cd09549      9 SVGEWLEALDLCRYKDNFAAAGYGSLEAVARMTAQDVLS-LGITSLEHQELLLAGI 63
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 231-300 5.61e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 5.61e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952677825  231 HLAArNGHKAVVQVLLDAGMDSNYQTEKGSA-LHEAALFGKTDVVQILLAAGIDVNIKDNRGLTALDTVRE 300
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 159-181 5.71e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 5.71e-03
                           10        20
                   ....*....|....*....|...
gi 1952677825  159 DNETALHCAAQYGHTEVVKVLLE 181
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLE 23
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 153-297 5.72e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  153 INAKNNDNETALHCAAQYGH--TEVVKVLLEELTDPTMRNNKFETPLdLAALYGRLEVVKMLLNAHPNLLSCNTKKHTP- 229
Cdd:PHA02716   205 VNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPI-MTYIINIDNINPEITNIYIESLDGNKVKNIPm 283

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952677825  230 -LHL---AARNGHKAVVQVLLDAGMDSNYQTEKG-SALHEAAL--FGKTDVVQILLAAGIDVNIKDNRGLTALDT 297
Cdd:PHA02716   284 iLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGrTCLHQYILrhNISTDIIKLLHEYGNDLNEPDNIGNTVLHT 358
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 102-136 6.85e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 6.85e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1952677825  102 KGCYPLHLAAWK-GDAQIVRLLIHQGPShtrVNEQN 136
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGAD---VNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 102-128 7.08e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 7.08e-03
                            10        20
                    ....*....|....*....|....*..
gi 1952677825   102 KGCYPLHLAAWKGDAQIVRLLIHQGPS 128
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 260-286 7.67e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.67e-03
                           10        20
                   ....*....|....*....|....*..
gi 1952677825  260 SALHEAALFGKTDVVQILLAAGIDVNI 286
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 713-773 9.01e-03

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 36.14  E-value: 9.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952677825  713 QSVGEWLEAVGLQQYESKlllngFDDVRFLGSNV--MEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09506      8 DDVGDWLESLNLGEHRER-----FMDNEIDGSHLpnLDKEDLTELGVTRVGHRMNIERALKKL 65
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 144-231 9.12e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 9.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  144 KKYGPFDPYINAKNND----NETALHCAAQYGHTEVVKVLLEELTD-----------PTMRNNKF---ETPLDLAALYGR 205
Cdd:cd22193     56 EKTDNLKRFINAEYTDeyyeGQTALHIAIERRQGDIVALLVENGADvhahakgrffqPKYQGEGFyfgELPLSLAACTNQ 135

                           90       100
                   ....*....|....*....|....*....
gi 1952677825  206 LEVVKMLL-NAHP--NLLSCNTKKHTPLH 231
Cdd:cd22193    136 PDIVQYLLeNEHQpaDIEAQDSRGNTVLH 164
SAM_EPH-A8 cd09550
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ...
 714-773 1.00e-02

SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions.


Pssm-ID: 188949  Cd Length: 65  Bit Score: 36.00  E-value: 1.00e-02
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952677825  714 SVGEWLEAVGLQQYESKLLLNGFDDVRFLGSnvMEEQDLRDIGITDPQHRRKLLQAAKSL 773
Cdd:cd09550      4 SVDDWLDSIKMGRYKDHFAAGGYSSLGMVMR--MNIEDIRRLGITLMGHQKKILTSIQVM 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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