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Conserved domains on  [gi|568949401|ref|XP_006507297|]
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amyloid beta precursor protein binding family B member 1 isoform X6 [Mus musculus]

Protein Classification

Fe65 family protein( domain architecture ID 11093636)

Fe65 family protein contains WW and PTB (phosphotyrosine-binding) domains, similar to human protein Fe65, also called amyloid-beta A4 precursor protein-binding family B member 1, that have both coactivator and corepressor functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 109-248 2.81e-94

Fe65 N-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 N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. 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: 269970  Cd Length: 138  Bit Score: 280.34  E-value: 2.81e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 109 KCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPmAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 188
Cdd:cd01272    2 KRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDT-VGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 189 VSIRVWGVGRDSGreRDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERR 248
Cdd:cd01272   81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 276-401 9.24e-76

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: 232.49  E-value: 9.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 276 PKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQ-TEAVLGECRVRFLSFLA 354
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKdEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568949401 355 VGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQK 401
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 3-24 7.03e-04

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 36.71  E-value: 7.03e-04
                          10        20
                  ....*....|....*....|...
gi 568949401    3 VQDTSG-TYYWHIPTGTTQWEPP 24
Cdd:pfam00397   8 RWDPDGrVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 109-248 2.81e-94

Fe65 N-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 N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. 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: 269970  Cd Length: 138  Bit Score: 280.34  E-value: 2.81e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 109 KCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPmAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 188
Cdd:cd01272    2 KRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDT-VGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 189 VSIRVWGVGRDSGreRDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERR 248
Cdd:cd01272   81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 276-401 9.24e-76

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: 232.49  E-value: 9.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 276 PKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQ-TEAVLGECRVRFLSFLA 354
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKdEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568949401 355 VGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQK 401
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
111-243 6.89e-52

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 171.01  E-value: 6.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401  111 FAVRSLGWVEMTEEeLAPGRS--SVAVNNCIRQLSYHKNNLHDPMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 188
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVKAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568949401  189 VSIRVWGVGrDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKI 243
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 106-253 1.54e-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: 133.59  E-value: 1.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401   106 PGIKCFAVRSLGWVEMTEEelapgRSSVAVNNCIRQLSYHknnlhdpMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHA 185
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEA-----RGLQVVQEAIRKLRAA-------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHE 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568949401   186 QPIVSIRVWGVGRDsgRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERRNARCL 253
Cdd:smart00462  69 HPLRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 279-408 1.20e-33

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: 123.19  E-value: 1.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401   279 ELVQKFQVYYLGNVPVAKPVGVDVINGALESVLS--SSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVG 356
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAaqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568949401   357 R-DVHTFAFIMAAGPAS-FCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQ 408
Cdd:smart00462  81 PdDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 3-24 7.03e-04

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 36.71  E-value: 7.03e-04
                          10        20
                  ....*....|....*....|...
gi 568949401    3 VQDTSG-TYYWHIPTGTTQWEPP 24
Cdd:pfam00397   8 RWDPDGrVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 2-24 2.01e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.58  E-value: 2.01e-03
                         10        20
                 ....*....|....*....|....
gi 568949401   2 RVQDTSG-TYYWHIPTGTTQWEPP 24
Cdd:cd00201    6 ERWDPDGrVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 2-24 6.60e-03

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 34.11  E-value: 6.60e-03
                           10        20
                   ....*....|....*....|....
gi 568949401     2 RVQDTSG-TYYWHIPTGTTQWEPP 24
Cdd:smart00456   8 ERKDPDGrPYYYNHETKETQWEKP 31
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 109-248 2.81e-94

Fe65 N-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 N-terminal PTB domain was shown to interact with a variety of proteins, including the low density lipoprotein receptor-related protein (LRP-1), the ApoEr2 receptor, and the histone acetyltransferase Tip60. 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: 269970  Cd Length: 138  Bit Score: 280.34  E-value: 2.81e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 109 KCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPmAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 188
Cdd:cd01272    2 KRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDT-VGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 189 VSIRVWGVGRDSGreRDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERR 248
Cdd:cd01272   81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 276-401 9.24e-76

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: 232.49  E-value: 9.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 276 PKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQ-TEAVLGECRVRFLSFLA 354
Cdd:cd01271    1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKdEEEVLVECRVRFLSFMG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568949401 355 VGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQK 401
Cdd:cd01271   81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
111-243 6.89e-52

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 171.01  E-value: 6.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401  111 FAVRSLGWVEMTEEeLAPGRS--SVAVNNCIRQLSYHKNNLHDPMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPI 188
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVKAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568949401  189 VSIRVWGVGrDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKI 243
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 106-253 1.54e-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: 133.59  E-value: 1.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401   106 PGIKCFAVRSLGWVEMTEEelapgRSSVAVNNCIRQLSYHknnlhdpMAGGWGEGKDLLLQLEDETLKLVEPQNQTLLHA 185
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEA-----RGLQVVQEAIRKLRAA-------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHE 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568949401   186 QPIVSIRVWGVGRDsgRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERRNARCL 253
Cdd:smart00462  69 HPLRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 279-408 1.20e-33

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: 123.19  E-value: 1.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401   279 ELVQKFQVYYLGNVPVAKPVGVDVINGALESVLS--SSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVG 356
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAaqGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568949401   357 R-DVHTFAFIMAAGPAS-FCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQ 408
Cdd:smart00462  81 PdDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 282-395 1.09e-18

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: 81.40  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 282 QKFQVYYLGNVPVAKPVGVDVINGALESVL--SSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDV 359
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAaaLKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568949401 360 -HTFAFIMAAGPAS-FCCHMFWCEPN--AASLSEAVQAAC 395
Cdd:cd00934   81 pNVFAFIAGEEGGSgFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 110-240 1.96e-16

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: 75.24  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 110 CFAVRSLGWVEMTEEELAPgRSSVAVNNCIRQLSYHKNnlhdpmaggwgEGKDLLLQLEDETLKLVEPQNQTLLHAQPIV 189
Cdd:cd00934    2 SFQVKYLGSVEVGSSRGVD-VVEEALKALAAALKSSKR-----------KPGPVLLEVSSKGVKLLDLDTKELLLRHPLH 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568949401 190 SIRVwgVGRDSGRERDFAYVARDKLTQMLKCHVFRC--EAPAKNIATSLHEIC 240
Cdd:cd00934   70 RISY--CGRDPDNPNVFAFIAGEEGGSGFRCHVFQCedEEEAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 284-394 4.35e-11

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: 59.95  E-value: 4.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 284 FQVYYLGNVPVAKPVGVDVINGALESVLSSSSREqwTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAV-GRDVHTF 362
Cdd:cd13161    4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKP--KPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVdPKDKKLF 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568949401 363 AFIMAAGPASFC-CHMFWCEPNAASLSEAVQAA 394
Cdd:cd13161   82 AFISHDPRLGRItCHVFRCKRGAQEICDTIAEA 114
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 165-234 8.26e-05

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: 41.85  E-value: 8.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 165 LQLEDETLKLVEPQNQTLLHAQPIVSIrVWgVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIAT 234
Cdd:cd13161   42 LVVSSEGIRVVERLTGEVLTNVPIKDI-SF-VTVDPKDKKLFAFISHDPRLGRITCHVFRCKRGAQEICD 109
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 171-250 3.84e-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: 40.31  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 171 TLKLVEPQNQTLLHAQPIVSIRVWGVGRDSGRERD-FAYVARDKLTQMLKCHVFRCEAPakniatslhEICSKIMSERRN 249
Cdd:cd01211   51 SVRLYDPTSNTEIASYPIYRILFCARGPDGTSESDcFAFTWSHGETAIFQCHVFRCEIP---------EAVSKVLYSFAK 121


                 .
gi 568949401 250 A 250
Cdd:cd01211  122 A 122
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 3-24 7.03e-04

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 36.71  E-value: 7.03e-04
                          10        20
                  ....*....|....*....|...
gi 568949401    3 VQDTSG-TYYWHIPTGTTQWEPP 24
Cdd:pfam00397   8 RWDPDGrVYYYNHETGETQWEKP 30
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 107-223 9.16e-04

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: 39.21  E-value: 9.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 107 GIKCFAVRSLGWVEMTEeelapgrsSVAVNNCIRQLSYHKNNLHDPMAGgwgegkdlLLQLEDETLKLVEPQNQTLLHAQ 186
Cdd:cd01268   13 GTCSFPVKYLGCVEVGE--------SRGMQVCEEALKKLKASRKKPVRA--------VLWVSGDGLRVVDEKTKGLIVDQ 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568949401 187 PI--VSIrvwgVGRDSGRERDFAYVARDKLTQMLKCHVF 223
Cdd:cd01268   77 TIekVSF----CAPDRNHERAFSYICRDGTTRRWMCHCF 111
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 179-225 1.25e-03

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: 38.85  E-value: 1.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 568949401 179 NQTLLHaqpiVSI-RVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRC 225
Cdd:cd13159   62 NETILE----VSIyRISYCTADANHDKVFAFIATNQDNEKLECHAFLC 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 2-24 2.01e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.58  E-value: 2.01e-03
                         10        20
                 ....*....|....*....|....
gi 568949401   2 RVQDTSG-TYYWHIPTGTTQWEPP 24
Cdd:cd00201    6 ERWDPDGrVYYYNHNTKETQWEDP 29
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 284-404 4.61e-03

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: 37.64  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949401 284 FQVYYLGNVPVAKPVGVDVINGALESV-----LSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRD 358
Cdd:cd01273   14 YLVKFLGCTEVEQPKGTEVVKEAIRKLkfarqLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKT 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568949401 359 V-HTFAFImAAGPAS--FCCHMFWCEPNAASLSEAVQAACMLRYQKCLD 404
Cdd:cd01273   94 DkRIFSFI-AKDSESekHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLE 141
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 2-24 6.60e-03

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 34.11  E-value: 6.60e-03
                           10        20
                   ....*....|....*....|....
gi 568949401     2 RVQDTSG-TYYWHIPTGTTQWEPP 24
Cdd:smart00456   8 ERKDPDGrPYYYNHETKETQWEKP 31
 
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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