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Conserved domains on  [gi|6671334|gb|AAF23161|]
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disabled-2 [Homo sapiens]

Protein Classification

Dab family PTB domain-containing protein( domain architecture ID 10100614)

Dab (Disabled) family PTB (phosphotyrosine-binding) domain-containing protein similar to mammalian disabled homolog 1 and 2, which are adapter proteins that function in neural development and endocytosis, respectively

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 35-172 3.00e-89

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


:

Pssm-ID: 269926  Cd Length: 147  Bit Score: 276.83  E-value: 3.00e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   35 TDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAargRSQGQHKQRIWVNISLSGIKIIDEKTGVIEH 114
Cdd:cd01215   3 TAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAV---KAAGEHKQRIWLNISLEGIKILDEKTGALLH 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6671334  115 EHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNV 172
Cdd:cd01215  80 HHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFEL 137
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 35-172 3.00e-89

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


Pssm-ID: 269926  Cd Length: 147  Bit Score: 276.83  E-value: 3.00e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   35 TDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAargRSQGQHKQRIWVNISLSGIKIIDEKTGVIEH 114
Cdd:cd01215   3 TAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAV---KAAGEHKQRIWLNISLEGIKILDEKTGALLH 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6671334  115 EHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNV 172
Cdd:cd01215  80 HHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFEL 137
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 45-171 1.18e-26

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: 105.86  E-value: 1.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334      45 GDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKgmaARGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFI 124
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR---AAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFC 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 6671334     125 ARDVTDNRAFGYVC--GGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYN 171
Cdd:smart00462  78 AVGPDDLDVFGYIArdPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYE 126
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
65-169 6.66e-07

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 49.28  E-value: 6.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334     65 GDKMSQDSMMKLKgmAARGRSQGQHK-QRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIA-RDVTDNRAFGYVCGGEG 142
Cdd:pfam00640  27 REAIRRVKAAKIN--KIRGLSGETGPgTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKA 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6671334    143 QHQF----FAIKTGqqAEPLVVDLKDLFQVI 169
Cdd:pfam00640 105 TNKFachvFESEDG--AQDIAQSIGQAFALA 133
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 35-172 3.00e-89

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


Pssm-ID: 269926  Cd Length: 147  Bit Score: 276.83  E-value: 3.00e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   35 TDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAargRSQGQHKQRIWVNISLSGIKIIDEKTGVIEH 114
Cdd:cd01215   3 TAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAV---KAAGEHKQRIWLNISLEGIKILDEKTGALLH 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6671334  115 EHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNV 172
Cdd:cd01215  80 HHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFEL 137
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 45-171 1.18e-26

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: 105.86  E-value: 1.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334      45 GDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKgmaARGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFI 124
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR---AAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFC 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 6671334     125 ARDVTDNRAFGYVC--GGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYN 171
Cdd:smart00462  78 AVGPDDLDVFGYIArdPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYE 126
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 48-166 1.32e-21

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: 90.65  E-value: 1.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   48 VKYKAKLIGIDDVPDARGDKMSQDSmmkLKGMAARGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARD 127
Cdd:cd00934   1 ASFQVKYLGSVEVGSSRGVDVVEEA---LKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRD 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6671334  128 VTDNRAFGYVCGGEGQHQF----FAIKTGQQAEPLVVDLKDLF 166
Cdd:cd00934  78 PDNPNVFAFIAGEEGGSGFrchvFQCEDEEEAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 35-170 4.45e-15

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: 72.70  E-value: 4.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   35 TDEYLLARFkgdgVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAARGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEH 114
Cdd:cd01273   3 PPEALIKGH----VAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMH 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6671334  115 EHPVNKISFIARDVTDNRAFGYVC--GGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIY 170
Cdd:cd01273  79 QFPLHRISFCADDKTDKRIFSFIAkdSESEKHLCFVFDSEKLAEEITLTIGQAFDLAY 136
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 46-145 4.98e-07

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: 49.25  E-value: 4.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   46 DGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMA-ARGRSQgqhkQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFI 124
Cdd:cd13159   1 DGVTFYLKYLGSTLVEKPKGEGATAEAVKTIIAMAkASGKKL----QKVTLTVSPKGIKVTDSATNETILEVSIYRISYC 76

                        90       100
                ....*....|....*....|.
gi 6671334  125 ARDVTDNRAFGYVcGGEGQHQ 145
Cdd:cd13159  77 TADANHDKVFAFI-ATNQDNE 96
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
65-169 6.66e-07

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 49.28  E-value: 6.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334     65 GDKMSQDSMMKLKgmAARGRSQGQHK-QRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIA-RDVTDNRAFGYVCGGEG 142
Cdd:pfam00640  27 REAIRRVKAAKIN--KIRGLSGETGPgTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKA 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 6671334    143 QHQF----FAIKTGqqAEPLVVDLKDLFQVI 169
Cdd:pfam00640 105 TNKFachvFESEDG--AQDIAQSIGQAFALA 133
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 35-150 8.86e-07

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: 48.84  E-value: 8.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   35 TDEYLLarfKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLkgmaargRSQGQHKQRIWVNISLSGIKIIDEKTGVIEH 114
Cdd:cd01268   5 ADEEAV---RSGTCSFPVKYLGCVEVGESRGMQVCEEALKKL-------KASRKKPVRAVLWVSGDGLRVVDEKTKGLIV 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6671334  115 EHPVNKISFIARDVTDNRAFGYVC-GGEGQ----HQFFAIK 150
Cdd:cd01268  75 DQTIEKVSFCAPDRNHERAFSYICrDGTTRrwmcHCFLAVK 115
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 46-137 6.49e-06

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


Pssm-ID: 269972  Cd Length: 146  Bit Score: 46.50  E-value: 6.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   46 DGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKgmaargRSQGQHKQ--RIWVNISLSGIKIIDEKTGVIEHEHPVNKISF 123
Cdd:cd01274  13 GSVNYEAHYLGSTEIKELRGTESTKKAIQKLK------KSTREMKKipTIILSISYKGVKFIDATTKNLICEHEIRNISC 86

                        90
                ....*....|....
gi 6671334  124 IARDVTDNRAFGYV 137
Cdd:cd01274  87 ACQDPEDLNTFAYI 100
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 50-138 7.27e-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: 43.00  E-value: 7.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   50 YKAKLIGIDDVPDARGDKMSQDSMMKLkgmaargRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVT 129
Cdd:cd13161   4 FEAKYLGSVPVKEPKGNDVVMAAVKRL-------KDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPK 76


                ....*....
gi 6671334  130 DNRAFGYVC 138
Cdd:cd13161  77 DKKLFAFIS 85
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
 48-170 2.91e-03

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


Pssm-ID: 269979  Cd Length: 129  Bit Score: 38.52  E-value: 2.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6671334   48 VKYKAKLIG---IDDV-PDARGDKMSQdsmmKLKGMaargRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISF 123
Cdd:cd13157   2 VSRNAQYIGsfpVSGLdVADRADSVRK----QLESL----KESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSY 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6671334  124 IARDvTDNRAFGYVC---GGEGQHQF---FAIKTGQQAEPLVVDLKDLFQVIY 170
Cdd:cd13157  74 STCR-PAHAQFAFVArnpGGPTNRQYchvFVTRSPREAQELNLLLCRAFQLAY 125
 
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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