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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  35 TDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGrsqGQHKQRIWVNISLSGIKIIDEKTGVIEH 114
Cdd:cd01215     3 TAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGALLH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748150 115 EHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYN 171
Cdd:cd01215    80 HHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFE 136

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  35 TDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGrsqGQHKQRIWVNISLSGIKIIDEKTGVIEH 114
Cdd:cd01215     3 TAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGALLH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748150 115 EHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYN 171
Cdd:cd01215    80 HHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFE 136

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  65 GDKMSQDSMMKLKgmAAAGRSQGQHK-QRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIA-RDVTDNRAFGYVCGGEG 142
Cdd:pfam00640  27 REAIRRVKAAKIN--KIRGLSGETGPgTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKA 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039748150 143 QHQF----FAIKTGqqAEPLVVDLKDLFQVI 169
Cdd:pfam00640 105 TNKFachvFESEDG--AQDIAQSIGQAFALA 133

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  35 TDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGrsqGQHKQRIWVNISLSGIKIIDEKTGVIEH 114
Cdd:cd01215     3 TAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGAVKAA---GEHKQRIWLNISLEGIKILDEKTGALLH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039748150 115 EHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYN 171
Cdd:cd01215    80 HHPVHKISFIARDTTDNRAFGYVCGLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVFE 136

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  48 VKYKAKLIGIDDVPDARGDKMSQDSmmkLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARD 127
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEA---LKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039748150 128 VTDNRAFGYVCGGEGQHQF----FAIKTGQQAEPLVVDLKDLF 166
Cdd:cd00934    78 PDNPNVFAFIAGEEGGSGFrchvFQCEDEEEAEEILQAIGQAF 120

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  46 DGVKYKAKLIGIDDVPDARGDKMSQDSmmkLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIA 125
Cdd:cd13159     1 DGVTFYLKYLGSTLVEKPKGEGATAEA---VKTIIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCT 77

                          90       100
                  ....*....|....*....|
gi 1039748150 126 RDVTDNRAFGYVcGGEGQHQ 145
Cdd:cd13159    78 ADANHDKVFAFI-ATNQDNE 96

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  65 GDKMSQDSMMKLKgmAAAGRSQGQHK-QRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIA-RDVTDNRAFGYVCGGEG 142
Cdd:pfam00640  27 REAIRRVKAAKIN--KIRGLSGETGPgTKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCAdGDPDLMRYFAYIARDKA 104

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039748150 143 QHQF----FAIKTGqqAEPLVVDLKDLFQVI 169
Cdd:pfam00640 105 TNKFachvFESEDG--AQDIAQSIGQAFALA 133

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  50 YKAKLIGIDDVPDARGDKMSQDSMMKLkgmaaagRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVT 129
Cdd:cd13161     4 FEAKYLGSVPVKEPKGNDVVMAAVKRL-------KDLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPK 76

                  ....*....
gi 1039748150 130 DNRAFGYVC 138
Cdd:cd13161    77 DKKLFAFIS 85

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039748150  48 VKYKAKLIG---IDDV-PDARGDKMSQdsmmKLKGMaaagRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISF 123
Cdd:cd13157     2 VSRNAQYIGsfpVSGLdVADRADSVRK----QLESL----KESGSRGRPVILSVSLSGIKICSEDGKVVLMAHALRRVSY 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039748150 124 IARDvTDNRAFGYVC---GGEGQHQF---FAIKTGQQAEPLVVDLKDLFQVIY 170
Cdd:cd13157    74 STCR-PAHAQFAFVArnpGGPTNRQYchvFVTRSPREAQELNLLLCRAFQLAY 125