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Conserved domains on  [gi|1907129620|ref|XP_036017003|]
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amyloid-beta A4 precursor protein-binding family B member 3 isoform X1 [Mus musculus]

Protein Classification

Fe65 family PTB domain-containing protein( domain architecture ID 10101053)

Fe65 family PTB (phosphotyrosine-binding) domain-containing protein similar to PTB domain region of Homo sapiens neuronal adaptor protein Fe65 and homologs

CATH:  2.30.29.30
Gene Ontology:  GO:0005515|GO:0001540
PubMed:  15567406|8987385|10610414
SCOP:  4002427

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 ...
 22-160 8.53e-83

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: 249.14  E-value: 8.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  22 CQCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 101
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129620 102 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 160
Cdd:cd01272    81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 189-319 1.14e-60

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: 192.05  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620 189 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTARGDRKTWVPAMLSVSDSLMTAHAIQAEagaeEEPLWQCPVRLV 268
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907129620 269 TFIGVGRDPHTFGLIADLGCQSFQCAAFWCEPHAGGLSEAVQAACMVQYQK 319
Cdd:cd01271    77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 22-160 8.53e-83

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: 249.14  E-value: 8.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  22 CQCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 101
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129620 102 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 160
Cdd:cd01272    81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 189-319 1.14e-60

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: 192.05  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620 189 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTARGDRKTWVPAMLSVSDSLMTAHAIQAEagaeEEPLWQCPVRLV 268
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907129620 269 TFIGVGRDPHTFGLIADLGCQSFQCAAFWCEPHAGGLSEAVQAACMVQYQK 319
Cdd:cd01271    77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
25-156 3.75e-47

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 157.14  E-value: 3.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  25 FAVRSLGWVEVPEEdLAPGKS--SIAVNNCIQQL-AQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 101
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVkAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907129620 102 VHIRVWGVGsSKGRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQI 156
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 21-160 6.19e-30

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: 112.02  E-value: 6.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620   21 SCQCFAVRSLGWVEVPEEDlapgkSSIAVNNCIQQLAQTrnrsqpHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQP 100
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAA------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHP 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  101 LVHIRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 160
Cdd:smart00462  71 LRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELK 128
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 192-324 4.64e-27

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: 104.32  E-value: 4.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  192 QAAQKYEALYMGILPVTKAMGMDVLNEAIGTL--TARGDRKTWVPAMLSVSDSLMTAHAIQAEAgaeeePLWQCPVRLVT 269
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-----VLHEHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907129620  270 FIGVGR-DPHTFGLIADLGCQS-FQCAAFWCEPHAGGLSEAVQAACMVQYQKCLVAS 324
Cdd:smart00462  76 FCAVGPdDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 22-160 8.53e-83

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: 249.14  E-value: 8.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  22 CQCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 101
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129620 102 VHIRVWGVGSSKGrdRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 160
Cdd:cd01272    81 HSIRVWGVGRDNG--RDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAER 137
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 189-319 1.14e-60

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: 192.05  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620 189 AVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTARGDRKTWVPAMLSVSDSLMTAHAIQAEagaeEEPLWQCPVRLV 268
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDE----EEVLVECRVRFL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907129620 269 TFIGVGRDPHTFGLIADLGCQSFQCAAFWCEPHAGGLSEAVQAACMVQYQK 319
Cdd:cd01271    77 SFMGIGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
25-156 3.75e-47

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 157.14  E-value: 3.75e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  25 FAVRSLGWVEVPEEdLAPGKS--SIAVNNCIQQL-AQTRNRSQPHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQPL 101
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVkAAKINKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907129620 102 VHIRVWGVGsSKGRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQI 156
Cdd:pfam00640  80 VSISFCADG-DPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 21-160 6.19e-30

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: 112.02  E-value: 6.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620   21 SCQCFAVRSLGWVEVPEEDlapgkSSIAVNNCIQQLAQTrnrsqpHDGTWGEGQNMLMILKKDAMSLLNPLDHSLIHCQP 100
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAA------QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHP 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  101 LVHIRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFHCDVPAKAIASALQGLCAQILSER 160
Cdd:smart00462  71 LRRISFCAVGPD--DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELK 128
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 192-324 4.64e-27

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: 104.32  E-value: 4.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  192 QAAQKYEALYMGILPVTKAMGMDVLNEAIGTL--TARGDRKTWVPAMLSVSDSLMTAHAIQAEAgaeeePLWQCPVRLVT 269
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-----VLHEHPLRRIS 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907129620  270 FIGVGR-DPHTFGLIADLGCQS-FQCAAFWCEPHAGGLSEAVQAACMVQYQKCLVAS 324
Cdd:smart00462  76 FCAVGPdDLDVFGYIARDPGSSrFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 23-150 2.16e-13

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: 66.38  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  23 QCFAVRSLGWVEVPEEDlapGKSSIAVNNCIQQLAQTRNRSQPhdgtwgegQNMLMILKKDAMSLLNPLDHSLIHCQPLV 102
Cdd:cd00934     1 ASFQVKYLGSVEVGSSR---GVDVVEEALKALAAALKSSKRKP--------GPVLLEVSSKGVKLLDLDTKELLLRHPLH 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907129620 103 HIRVWGVGSSkgRDRDFAFVAGDKDSCMLKCHVFHCD--VPAKAIASALQ 150
Cdd:cd00934    70 RISYCGRDPD--NPNVFAFIAGEEGGSGFRCHVFQCEdeEEAEEILQAIG 117
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 195-313 1.68e-04

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: 40.96  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620 195 QKYEALYMGILPVTKAMGMDVLNEAIGTL--TARGDRKTWVPAMLSVSDSlmtahAIQAEAGAEEEPLWQCPVRLVTFIG 272
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEALKALaaALKSSKRKPGPVLLEVSSK-----GVKLLDLDTKELLLRHPLHRISYCG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907129620 273 VGRD-PHTFGLIA-DLGCQSFQCAAFWCEP--HAGGLSEAVQAAC 313
Cdd:cd00934    76 RDPDnPNVFAFIAgEEGGSGFRCHVFQCEDeeEAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 197-312 2.11e-04

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: 40.69  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620 197 YEALYMGILPVTKAMGMDVLNEAIGTLTARGdrKTWVPAMLSVSDSlmtahAIQAEAGAEEEPLWQCPVRLVTFIGV-GR 275
Cdd:cd13161     4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLK--LKPKPVVLVVSSE-----GIRVVERLTGEVLTNVPIKDISFVTVdPK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907129620 276 DPHTFGLIA---DLG---CQSFQCAafwcePHAGGLSEAVQAA 312
Cdd:cd13161    77 DKKLFAFIShdpRLGritCHVFRCK-----RGAQEICDTIAEA 114
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 48-150 7.52e-03

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: 36.56  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129620  48 AVNNCIQQLAQTRNRSQPhdgtWGegQNMLMILKKDAMSLLNP-----LDH----SLIHCQPLVHIRVWgvgsskgrDRD 118
Cdd:pfam08416  20 AVEDAIRKLQLLDAQGRV----WT--QEMLLQVSDQGITLTDNetkeeLESypldSISHCQAVLNDGRY--------NSI 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907129620 119 FAFVAGDKDSCMLKCHVFHC-----DVPAKAIASALQ 150
Cdd:pfam08416  86 LALVCQEPGQSKPDVHLFQCdelgaELIAEDIESALS 122
 
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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