NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462596967|ref|XP_054205885|]
View 

amyloid beta precursor protein binding family B member 2 isoform X9 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 395-532 5.25e-105

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: 316.55  E-value: 5.25e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 395 AKCFAVRSLGWVEMAEEDLAPGKSSVAVNNCIRQLSYCKNDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 474
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596967 475 VSIRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERK 532
Cdd:cd01272    81 HSIRVWGVGRDNGRDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 561-687 7.15e-86

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: 266.39  E-value: 7.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 561 PKTELVQKFHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 640
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462596967 641 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQK 687
Cdd:cd01271    81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 292-320 1.98e-08

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: 50.20  E-value: 1.98e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596967 292 LPPGWKRVSDIAG-TYYWHIPTGTTQWERP 320
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 395-532 5.25e-105

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: 316.55  E-value: 5.25e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 395 AKCFAVRSLGWVEMAEEDLAPGKSSVAVNNCIRQLSYCKNDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 474
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596967 475 VSIRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERK 532
Cdd:cd01272    81 HSIRVWGVGRDNGRDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 561-687 7.15e-86

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: 266.39  E-value: 7.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 561 PKTELVQKFHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 640
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462596967 641 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQK 687
Cdd:cd01271    81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
398-527 1.48e-50

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 172.55  E-value: 1.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 398 FAVRSLGWVEMAEEdLAPGKS--SVAVNNCIRQLSYCK-NDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 474
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVKAAKiNKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462596967 475 VSIRVWGVG-RDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKI 527
Cdd:pfam00640  80 VSISFCADGdPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 393-535 6.46e-38

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: 137.45  E-value: 6.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967  393 PEAKCFAVRSLGWVEMAEEDlapgkSSVAVNNCIRQLSYCKndirdtVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQ 472
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAAQ------GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596967  473 PIVSIRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERKNAK 535
Cdd:smart00462  70 PLRRISFCAVGPDDLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 564-694 1.40e-36

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


Pssm-ID: 214675  Cd Length: 134  Bit Score: 133.98  E-value: 1.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967  564 ELVQKFHVQYLGMLPVDKPVGMDILNSAIENL--MTSSNKEDWLSVNMNVADATVTVISEKNEEeVLVECRVRFLSFMGV 641
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-VLHEHPLRRISFCAV 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462596967  642 G-KDVHTFAFIM-DTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQKCLVARPP 694
Cdd:smart00462  80 GpDDLDVFGYIArDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 292-320 1.98e-08

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: 50.20  E-value: 1.98e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596967 292 LPPGWKRVSDIAG-TYYWHIPTGTTQWERP 320
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 291-322 4.26e-08

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: 49.52  E-value: 4.26e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462596967  291 DLPPGWKRVSDIAG-TYYWHIPTGTTQWERPVS 322
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 293-321 1.47e-07

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: 47.91  E-value: 1.47e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596967 293 PPGWKRVSDIAG-TYYWHIPTGTTQWERPV 321
Cdd:cd00201     1 PPGWEERWDPDGrVYYYNHNTKETQWEDPR 30
 
Name Accession Description Interval E-value
PTB1_Fe65 cd01272
Fe65 N-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 395-532 5.25e-105

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: 316.55  E-value: 5.25e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 395 AKCFAVRSLGWVEMAEEDLAPGKSSVAVNNCIRQLSYCKNDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 474
Cdd:cd01272     1 AKRFAVRSLGWVEMAEEDLTPGKSSVAVNNCIRQLSYGRNDIRDTVGRWGEGKDMLMVLDDDTLKLVDPDDRSVLHSQPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596967 475 VSIRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERK 532
Cdd:cd01272    81 HSIRVWGVGRDNGRDFAYVARDKDTRVLKCHVFRCDTPAKAIATALHEICSRIMAERR 138
PTB2_Fe65 cd01271
Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is ...
 561-687 7.15e-86

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: 266.39  E-value: 7.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 561 PKTELVQKFHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMG 640
Cdd:cd01271     1 PKEEPVQKLKALYLGSTPVSKPTGMDVLNEAIDTLLSSVPKEQWTPVNVSVAPSTVTILSQKDEEEVLVECRVRFLSFMG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462596967 641 VGKDVHTFAFIMDTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQK 687
Cdd:cd01271    81 IGKDVHTFAFIMDTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
398-527 1.48e-50

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 172.55  E-value: 1.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 398 FAVRSLGWVEMAEEdLAPGKS--SVAVNNCIRQLSYCK-NDIRDTVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQPI 474
Cdd:pfam00640   1 FAVRYLGSVEVPEE-RAPDKNtrMQQAREAIRRVKAAKiNKIRGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462596967 475 VSIRVWGVG-RDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKI 527
Cdd:pfam00640  80 VSISFCADGdPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 393-535 6.46e-38

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: 137.45  E-value: 6.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967  393 PEAKCFAVRSLGWVEMAEEDlapgkSSVAVNNCIRQLSYCKndirdtVGIWGEGKDMYLILENDMLSLVDPMDRSVLHSQ 472
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEAR-----GLQVVQEAIRKLRAAQ------GSEKKEPQKVILSISSRGVKLIDEDTKAVLHEH 69

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462596967  473 PIVSIRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIATSLHEICSKIMAERKNAK 535
Cdd:smart00462  70 PLRRISFCAVGPDDLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 564-694 1.40e-36

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


Pssm-ID: 214675  Cd Length: 134  Bit Score: 133.98  E-value: 1.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967  564 ELVQKFHVQYLGMLPVDKPVGMDILNSAIENL--MTSSNKEDWLSVNMNVADATVTVISEKNEEeVLVECRVRFLSFMGV 641
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLraAQGSEKKEPQKVILSISSRGVKLIDEDTKA-VLHEHPLRRISFCAV 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462596967  642 G-KDVHTFAFIM-DTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQKCLVARPP 694
Cdd:smart00462  80 GpDDLDVFGYIArDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 397-524 2.75e-15

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: 72.54  E-value: 2.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 397 CFAVRSLGWVEMAEEDLAPGkSSVAVNNCIRQLSYCKNdirdtvgiwgEGKDMYLILENDMLSLVDPMDRSVLHSQPIVS 476
Cdd:cd00934     2 SFQVKYLGSVEVGSSRGVDV-VEEALKALAAALKSSKR----------KPGPVLLEVSSKGVKLLDLDTKELLLRHPLHR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462596967 477 IRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTP--AKAIATSLHEIC 524
Cdd:cd00934    71 ISYCGRDPDNPNVFAFIAGEEGGSGFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 567-681 1.95e-14

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: 70.23  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 567 QKFHVQYLGMLPVDKPVGMDILNSAIENLMT--SSNKEDWLSVNMNVADATVTVIsEKNEEEVLVECRVRFLSFMGVGKD 644
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAalKSSKRKPGPVLLEVSSKGVKLL-DLDTKELLLRHPLHRISYCGRDPD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462596967 645 V-HTFAFI-MDTGNQRFECHVFWCEPN--AGNVSEAVQAAC 681
Cdd:cd00934    80 NpNVFAFIaGEEGGSGFRCHVFQCEDEeeAEEILQAIGQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 569-680 4.13e-13

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: 66.50  E-value: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 569 FHVQYLGMLPVDKPVGMDILNSAIENLMTSSNKEDwlSVNMNVADATVTVIsEKNEEEVLVECRVRFLSFMGV-GKDVHT 647
Cdd:cd13161     4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKPK--PVVLVVSSEGIRVV-ERLTGEVLTNVPIKDISFVTVdPKDKKL 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462596967 648 FAFIM-DTGNQRFECHVFWCEPNAGNVSEAVQAA 680
Cdd:cd13161    81 FAFIShDPRLGRITCHVFRCKRGAQEICDTIAEA 114
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 397-518 1.57e-08

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: 53.41  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 397 CFAVRSLGWVEMAEedlaPGKSSVaVNNCIRqlsycknDIRDTvgiWGEGKDMYLILENDMLSLVDPMDRSVLHSQPIVS 476
Cdd:cd13161     3 VFEAKYLGSVPVKE----PKGNDV-VMAAVK-------RLKDL---KLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKD 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462596967 477 IRVWGVGRDNGRDFAYVARDKDTRILKCHVFRCDTPAKAIAT 518
Cdd:cd13161    68 ISFVTVDPKDKKLFAFISHDPRLGRITCHVFRCKRGAQEICD 109
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 292-320 1.98e-08

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: 50.20  E-value: 1.98e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596967 292 LPPGWKRVSDIAG-TYYWHIPTGTTQWERP 320
Cdd:pfam00397   1 LPPGWEERWDPDGrVYYYNHETGETQWEKP 30
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 291-322 4.26e-08

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: 49.52  E-value: 4.26e-08
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462596967  291 DLPPGWKRVSDIAG-TYYWHIPTGTTQWERPVS 322
Cdd:smart00456   1 PLPPGWEERKDPDGrPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 293-321 1.47e-07

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: 47.91  E-value: 1.47e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596967 293 PPGWKRVSDIAG-TYYWHIPTGTTQWERPV 321
Cdd:cd00201     1 PPGWEERWDPDGrVYYYNHNTKETQWEDPR 30
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 569-666 4.77e-05

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: 43.47  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 569 FHVQYLGMLPVDKPVGMDILNSAIENL--MTSSNKEDWLSVNMNVADATVTVISEKNEEEVLVECRVRfLSFMGVGK-DV 645
Cdd:cd13159     5 FYLKYLGSTLVEKPKGEGATAEAVKTIiaMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYR-ISYCTADAnHD 83

                          90       100
                  ....*....|....*....|..
gi 2462596967 646 HTFAFIMDTG-NQRFECHVFWC 666
Cdd:cd13159    84 KVFAFIATNQdNEKLECHAFLC 105
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 460-534 1.14e-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: 42.62  E-value: 1.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596967 460 LVDPMDRSVLHSQPIVSIRVWGVGRDNGRD---FAYVARDKDTRILKCHVFRCDTPakaiatslhEICSKIMAERKNA 534
Cdd:cd01211    54 LYDPTSNTEIASYPIYRILFCARGPDGTSEsdcFAFTWSHGETAIFQCHVFRCEIP---------EAVSKVLYSFAKA 122
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 447-527 1.66e-03

Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called DCC-interacting protein (DIP)-13alpha) Phosphotyrosine-binding (PTB) domain; APPL interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. 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: 269980  Cd Length: 135  Bit Score: 39.25  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 447 KDMYLILENDMLSLVDPMDRSVLHSQPIVSIRVWGVGRDNGRDFAYVARDKDTR----ILKCHVFRCDTPAKaiatslhE 522
Cdd:cd13158    52 TESHLLVTSDCLRLIDPQTQVTRARFPLADVVQFAAHQENKRLFGFVVRTPEGDgeepSFSCYVFESNTEGE-------K 124


                  ....*
gi 2462596967 523 ICSKI 527
Cdd:cd13158   125 ICDAI 129
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 564-689 3.38e-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: 38.41  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596967 564 ELVQKFHVQY----LGMLPVDKPVGMDILNSAIENL-----MTSSNKEDWLSVNMNVADATVTVISEKNeEEVLVECRVR 634
Cdd:cd01273     5 EALIKGHVAYlvkfLGCTEVEQPKGTEVVKEAIRKLkfarqLKKSEGAKLPKVELQISIDGVKIQDPKT-KVIMHQFPLH 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596967 635 FLSFMGVGKDV-HTFAFIM-DTGNQRFECHVFWCEPNAGNVSEAVQAACMLRYQKCL 689
Cdd:cd01273    84 RISFCADDKTDkRIFSFIAkDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFL 140
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH