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Conserved domains on  [gi|160333775|ref|NP_663529|]
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low density lipoprotein receptor adapter protein 1 [Mus musculus]

Protein Classification

low density lipoprotein receptor adapter protein 1 family protein( domain architecture ID 10192159)

low density lipoprotein receptor adapter protein 1 family protein similar to human low density lipoprotein receptor adapter protein 1 (LDLRAP1) which is an adaptor protein needed for efficient endocytosis of low density lipoprotein receptor (LDLR); contains a Phosphotyrosine-binding (PTB) domain/Phosphotyrosine-interaction (PI) domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 43-165 1.13e-82

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: 245.32  E-value: 1.13e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  43 EGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADK 122
Cdd:cd13159    1 DGVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 160333775 123 MHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFK 165
Cdd:cd13159   81 NHDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
 
Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 43-165 1.13e-82

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: 245.32  E-value: 1.13e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  43 EGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADK 122
Cdd:cd13159    1 DGVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 160333775 123 MHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFK 165
Cdd:cd13159   81 NHDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 43-174 8.29e-37

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: 128.20  E-value: 8.29e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775    43 EGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADK 122
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160333775   123 MHDKVFAYIAQSQQNESLECHAFLCTkrKVAQAVTLTVAQAFKVAFEFWQVS 174
Cdd:smart00462  82 DDLDVFGYIARDPGSSRFACHVFRCE--KAAEDIALAIGQAFQLAYELKLKA 131
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
47-169 7.80e-16

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 74.04  E-value: 7.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775   47 FSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLqKVTLKVSPRGIILTdslTSQ--LIENVSiYRISYCTADKMH 124
Cdd:pfam14719   2 YKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKSGT-KMKLTVTRSGLKAT---TKEhgLTEYWS-HRITYCSAPPNY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 160333775  125 DKVFAYIAQSQ---QNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFE 169
Cdd:pfam14719  77 PRVFCWVYRHEgrkLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQ 124
 
Name Accession Description Interval E-value
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 43-165 1.13e-82

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: 245.32  E-value: 1.13e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  43 EGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADK 122
Cdd:cd13159    1 DGVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTADA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 160333775 123 MHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFK 165
Cdd:cd13159   81 NHDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 45-164 2.25e-37

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: 129.17  E-value: 2.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  45 MVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADKMH 124
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 160333775 125 DKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAF 164
Cdd:cd00934   81 PNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 43-174 8.29e-37

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: 128.20  E-value: 8.29e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775    43 EGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADK 122
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 160333775   123 MHDKVFAYIAQSQQNESLECHAFLCTkrKVAQAVTLTVAQAFKVAFEFWQVS 174
Cdd:smart00462  82 DDLDVFGYIARDPGSSRFACHVFRCE--KAAEDIALAIGQAFQLAYELKLKA 131
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 37-168 4.05e-28

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: 105.82  E-value: 4.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  37 TRETLLEG-MVFSLKYLGMTLVERPKGEELSAAAVKRIVAT---AKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSI 112
Cdd:cd01273    3 PPEALIKGhVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFArqlKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 160333775 113 YRISYCTADKMHDKVFAYIAQSQQNESLECHAFLCTkrKVAQAVTLTVAQAFKVAF 168
Cdd:cd01273   83 HRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSE--KLAEEITLTIGQAFDLAY 136
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 46-169 1.02e-26

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: 101.56  E-value: 1.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  46 VFSLKYLGMTLVERPKGEELSAAAVKRIvataKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADKMHD 125
Cdd:cd13161    3 VFEAKYLGSVPVKEPKGNDVVMAAVKRL----KDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 160333775 126 KVFAYIAQSQQNESLECHAFLCTKRkvAQAVTLTVAQAFKVAFE 169
Cdd:cd13161   79 KLFAFISHDPRLGRITCHVFRCKRG--AQEICDTIAEAFKAAAE 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 33-169 1.51e-17

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: 77.71  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  33 NWTDTRETLLEGMV-FSLKYLGMTLVERPKGEELSAAAVKRIVaTAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVS 111
Cdd:cd01274    2 QWRHSPEKLITGSVnYEAHYLGSTEIKELRGTESTKKAIQKLK-KSTREMKKIPTIILSISYKGVKFIDATTKNLICEHE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 160333775 112 IYRISYCTADKMHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFE 169
Cdd:cd01274   81 IRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQ 138
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 32-169 6.05e-17

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: 75.80  E-value: 6.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  32 ENWTDTRETLLEGMV-FSLKYLGMTLVERPKGEELSAAAVKRIvataKASGKKLQKVTLKVSPRGIILTDSLTSQLIENV 110
Cdd:cd01268    1 HQWQADEEAVRSGTCsFPVKYLGCVEVGESRGMQVCEEALKKL----KASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQ 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 160333775 111 SIYRISYCTADKMHDKVFAYIAQSQQNESLECHAFLCTKrKVAQAVTLTVAQAFKVAFE 169
Cdd:cd01268   77 TIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVK-DSGERLSHAVGCAFAACLE 134
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 46-164 1.17e-16

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects 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 insects, ticks, sea urchins, and nematodes.


Pssm-ID: 269982  Cd Length: 125  Bit Score: 74.68  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  46 VFSLKYLGmtlVERPKGEELSAAAVKRIVATAK--ASGKKLQKVTLKVSPRGI---ILTDSLTSQLIENVSIYRISYCTA 120
Cdd:cd13160    2 VFTVKYLG---RMPARGLWGIKHTRKPLVDALKnlPKGKTLPKTKLEVSSDGVkleELRGGFGSSKTVFFPIHTISYGVQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 160333775 121 DKMHDKVFAYI---AQSQQNESLECHAFLCTKRKVAQAVTLTVAQAF 164
Cdd:cd13160   79 DLVHTRVFSMIvvgEQDSSNHPFECHAFVCDSRADARNLTYWLAKAF 125
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
47-169 7.80e-16

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 74.04  E-value: 7.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775   47 FSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLqKVTLKVSPRGIILTdslTSQ--LIENVSiYRISYCTADKMH 124
Cdd:pfam14719   2 YKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQGKSGT-KMKLTVTRSGLKAT---TKEhgLTEYWS-HRITYCSAPPNY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 160333775  125 DKVFAYIAQSQ---QNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFE 169
Cdd:pfam14719  77 PRVFCWVYRHEgrkLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQ 124
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
47-167 2.73e-15

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 71.24  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775   47 FSLKYLGMTLVERPKGEELSAA------AVKRIVATAKASGKKL-------QKVTLKVSPRGIILTDSLTSQLIENVSIY 113
Cdd:pfam00640   1 FAVRYLGSVEVPEERAPDKNTRmqqareAIRRVKAAKINKIRGLsgetgpgTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 160333775  114 RISYCT-ADKMHDKVFAYIAQSQQNESLECHAFLCTKRkvAQAVTLTVAQAFKVA 167
Cdd:pfam00640  81 SISFCAdGDPDLMRYFAYIARDKATNKFACHVFESEDG--AQDIAQSIGQAFALA 133
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 51-162 5.96e-14

Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; The function of FAM43A is currently unknown. Human FAM43A is located on chromosome 3 at location 3q29. It encodes a 3182 base pair mRNA which possesses one Pleckstrin homology-like domain. The mRNA translates into LOC131583, a hydrophilic protein that is predicted to localize in the nucleus. The FAM43A gene is conserved through a broad range of vertebrates. It is highly conserved from chimpanzees to zebrafish. 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: 269925  Cd Length: 125  Bit Score: 67.32  E-value: 5.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  51 YLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTdslTSQ--LIENVSiYRISYCTADKMHDKVF 128
Cdd:cd01214   12 YLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKAT---TKQhgLTEYWL-HRITYCSAPPNYPRVF 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 160333775 129 AYIAQSQ---QNESLECHAFLCTKRKVAQAVTLTVAQ 162
Cdd:cd01214   88 CWIYRHEgrkLKVELRCHAVLCSKESKARAIALLLYQ 124
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 44-166 1.02e-12

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: 65.38  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  44 GMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGI-----------ILTDSLTSQLIENVSI 112
Cdd:cd01270   28 GITFQAKYIGSLEVPRPSSRVEIVAAMRRIRYEFKAKNIKKKKVTITVSVDGVkvvlrkkkkkkGWTWDESKLLLMQHPI 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 160333775 113 YRISYCTADkMHD-KVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFKV 166
Cdd:cd01270  108 YRIFYVSHD-SQDlKIFSYIARDGSSNVFKCNVFKSKKKSQAMRIVRTIGQAFEV 161
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 43-169 4.17e-12

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: 62.66  E-value: 4.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  43 EGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADK 122
Cdd:cd01215   14 DGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDT 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 160333775 123 MHDKVFAYIAQSQQNeslecHAFLCTKR-KVAQAVTLTVAQAFKVAFE 169
Cdd:cd01215   94 TDNRAFGYVCGLDGG-----HRFFAIKTaKAAEPVVLDLRDLFQVVFE 136
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 46-165 9.92e-09

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: 52.64  E-value: 9.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  46 VFS-LKYLGMTLVERPKGEelsaAAVKRIVATAKASGKKLQKVTLKV--SPRG-IILTDSLTSQLIENVSIYRISYC--- 118
Cdd:cd01211    2 IFNgVTYLGCAKVNAPRSE----TEALRIMAILREQSAQPIKVTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILFCarg 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 160333775 119 ---TADKmhdKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFK 165
Cdd:cd01211   78 pdgTSES---DCFAFTWSHGETAIFQCHVFRCEIPEAVSKVLYSFAKAFR 124
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 50-168 3.01e-07

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: 48.54  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  50 KYLGMTLVERPKGEElSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTADKMHdKVFA 129
Cdd:cd13157    7 QYIGSFPVSGLDVAD-RADSVRKQLESLKESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCRPAH-AQFA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 160333775 130 YIAQSQQNES--LECHAFLCTKRKVAQAVTLTVAQAFKVAF 168
Cdd:cd13157   85 FVARNPGGPTnrQYCHVFVTRSPREAQELNLLLCRAFQLAY 125
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 69-169 3.86e-05

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: 43.35  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  69 AVKRI-VATAKASGKKLQK-------------VTLKVSPRGIILTDSLTSQLIENVSIYRISYCTA-DKMHDKVFAYIAQ 133
Cdd:cd01209   53 AVGGAkGAKRKRKSKALSSilgksnlqfagmnISLTISTDGLNLVTPDTGQIIANHHMQSISFASGgDPDTYDYVAYVAK 132

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 160333775 134 SQQNESlECHAFLCTKRkVAQAVTLTVAQAFKVAFE 169
Cdd:cd01209  133 DPVNQR-ACHVLECGDG-LAQDVIATIGQAFELRFK 166
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 85-154 6.05e-05

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.


Pssm-ID: 429984  Cd Length: 131  Bit Score: 41.95  E-value: 6.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160333775   85 QKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTAD---KMHDKVFAYIAQSQQNESLECHAFLCTKRKVAQ 154
Cdd:pfam08416  40 QEMLLQVSDQGITLTDNETKEELESYPLDSISHCQAVlndGRYNSILALVCQEPGQSKPDVHLFQCDELGAEL 112
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 107-169 1.25e-03

PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like fold; P-CLI1 (also called Phosphotyrosine interaction domain-containing protein 1) increases proliferation of preadipocytes without affecting adipocytic differentiation. It forms a complex with PID1/PCLI1, LRP1 and CUBNI. It is found in subcutaneous fat, heart, skeletal muscle, brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. P-CLI1 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.


Pssm-ID: 269988  Cd Length: 139  Bit Score: 38.43  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775 107 IENVSIYRISYCTADkmHD---KVFAYIAQsQQNESL----ECHAFLCTKRKVAQAVTLTVAQAFKVAFE 169
Cdd:cd13167   70 MDTFQVARIAYCTAD--HNispNIFAWVYR-EINDDLsfqmDCHAVECESKLEAKKLAHAMMEAFKKTFH 136
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 46-147 6.33e-03

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. 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: 269969  Cd Length: 127  Bit Score: 36.04  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333775  46 VFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASgkKLQKVTLKVSPRGI-ILTDSLTSQLIENVSIYRISYCTADKmH 124
Cdd:cd01271    8 KLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKE--QWTPVNVSVAPSTVtILSQKDEEEVLVECRVRFLSFMGIGK-D 84

                         90       100
                 ....*....|....*....|...
gi 160333775 125 DKVFAYIAQSQQNeSLECHAFLC 147
Cdd:cd01271   85 VHTFAFIMDTGPQ-LFQCHVFWC 106
 
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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