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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963  14 MHTPEALSKHYIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273    1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568906963  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 157
Cdd:cd01273   81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963  14 MHTPEALSKHYIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273    1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568906963  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 157
Cdd:cd01273   81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963   27 YNAKFLGSTEVEQPK------GTEVVRDAVRKLKFAR--HIKKSEGQKIP--KVELQISIYGVKILEPKTKEVQHNCQLH 96
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKinKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568906963   97 RISFCAD-DKTDKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLA 148
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963  14 MHTPEALSKHYIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273    1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568906963  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 157
Cdd:cd01273   81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

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 568906963  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKfarHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:cd00934    3 FQVKYLGSVEVGSSRGVDVVEEALKALA---AALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568906963 107 DKRIFTFICKDSESNKHLCFVF--DSEKCAEEITLTIGQAF 145
Cdd:cd00934   80 NPNVFAFIAGEEGGSGFRCHVFqcEDEEEAEEILQAIGQAF 120

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963   27 YNAKFLGSTEVEQPK------GTEVVRDAVRKLKFAR--HIKKSEGQKIP--KVELQISIYGVKILEPKTKEVQHNCQLH 96
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKinKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568906963   97 RISFCAD-DKTDKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLA 148
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDGAQDIAQSIGQAFALA 133

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 568906963  25 IPYNAKFLGSTEVEQPKGTEVVRDAVRKlkfARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADD 104
Cdd:cd13159    3 VTFYLKYLGSTLVEKPKGEGATAEAVKT---IIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTAD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568906963 105 KTDKRIFTFICKDSESNKHLCFVF--DSEKCAEEITLTIGQAF 145
Cdd:cd13159   80 ANHDKVFAFIATNQDNEKLECHAFlcAKRKMAQAVTLTVAQAF 122

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 568906963  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFArhIKKSEGQKiPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:cd01215   18 FKAKLIGIDEVPAARGDKMCQDAMMKLKGA--VKAAGEHK-QRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTT 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568906963 107 DKRIFTFICkdSESNKHLCFVFDSEKCAEEITLTIGQAFDLAY 149
Cdd:cd01215   95 DNRAFGYVC--GLDGGHRFFAIKTAKAAEPVVLDLRDLFQVVF 135

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects 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 insects, ticks, sea urchins, and nematodes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963  30 KFLGSteveQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKiLEPKTKEVQHNCQ----LHRISFCADDK 105
Cdd:cd13160    6 KYLGR----MPARGLWGIKHTRKPLVDALKNLPKGKTLPKTKLEVSSDGVK-LEELRGGFGSSKTvffpIHTISYGVQDL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568906963 106 TDKRIFTFICK-DSESNKHL--C--FVFDSEKCAEEITLTIGQAF 145
Cdd:cd13160   81 VHTRVFSMIVVgEQDSSNHPfeChaFVCDSRADARNLTYWLAKAF 125

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963  29 AKFLGSTEVEQPKGTEVVRDAVRKLKFARHI----KKSEGQkipkveLQISIYGVKILEPKTKEVQHNCQLHRISFCADD 104
Cdd:cd13158   15 VRFLGSMEVKSDRTSEVIYEAMRQVLAARAIhnifRMTESH------LLVTSDCLRLIDPQTQVTRARFPLADVVQFAAH 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568906963 105 KTDKRIFTFICKDSES----NKHLCFVFDSEKCAEEITLTIGQA 144
Cdd:cd13158   89 QENKRLFGFVVRTPEGdgeePSFSCYVFESNTEGEKICDAIALA 132

X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is unknown to date. X11 has a PTB domain followed by two PDZ 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 568906963  17 PEALSKHYIpYNAKFLGSTEVEQPKGTevvRDAVRKLKfARH----IKKSEGQKIP--KVELQISIYGVKILEPKTKEVQ 90
Cdd:cd01208    1 PEDLIDGVI-FGANYLGSTQLLSERNP---SKNVRMAQ-AQEavsrVKAPEGESQPstEVDLFISTERIKVLNADTQETM 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963  91 HNCQLHRISFCAD-----------------DKTDKRIFTFICKDSESNKHLCFVFDSEKcAEEITLTIGQAFDLAYRKFL 153
Cdd:cd01208   76 MDHALRTISYIADignivvlmarrrmprssSQECVETTPPSQEGKRQYKMICHVFESED-AQLIAQSIGQAFSVAYQEFL 154

                 ....
gi 568906963 154 ESGG 157
Cdd:cd01208  155 RANG 158

TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. 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 568906963  26 PYNAKF-----LGSTEVEQPKGTEVVRD-AVRKLKF--ARHIKKSEGQKIPKVE-------LQISIYGVKILEPKTKEVQ 90
Cdd:cd01269    4 PSNSQFfevlyCGKIKVSHKKVPPTFIDdCLEKFRLheLEKSRSGPSSVQPTDSeenrtmlFQIGRSELRLISPDTKQVL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963  91 HNCQLHRISFCADDKTDKRIFTFICKDSESNK---HLCFVF--DSEKCAEEITLTIGQAF 145
Cdd:cd01269   84 LEKQFKDISSCSQGIKHVDHFGFICRESSEGGgfhFVCYVFkcQSESVVDEIMLTIKQAF 143

uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of LOC417372 and its related proteins are unknown to date. Members here contain a N-terminal RUN domain, followed by a PDZ domain, and a C-terminal PTB domain. The RUN domain is involved in Ras-like GTPase signaling. The PDZ domain (also called DHR/Dlg homologous region or GLGF after its conserved sequence motif) binds C-terminal polypeptides, internal (non-C-terminal) polypeptides, and lipids. 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 568906963  25 IPYNAKFLGSTEVEQPKGTEVVRDAvrklkfARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADD 104
Cdd:cd13168    1 ALYKALYLGQVEVGEDGGVEQIESA------AIIVVLESDLTPKEVLLELGEIGVTVWDKSTSEVLFKHSFPEISSCGRR 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568906963 105 KTDKRIFTFICKD---SESNKHLCFVFDSEKCAE--EITLTIGQAFD 146
Cdd:cd13168   75 VDDPNYFAYIAGDtpcSLAKHFVCYVFEAADEEEaeTILQGIAQGFK 121

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906963  31 FLGSTEVEQPKgTEVvrDAVRKLKfarhIKKSEGQKIPKVELQI--SIYG-VKILEPKTKEVQHNCQLHRISFCA---DD 104
Cdd:cd01211    8 YLGCAKVNAPR-SET--EALRIMA----ILREQSAQPIKVTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILFCArgpDG 80

                         90       100
                 ....*....|....*....|....
gi 568906963 105 KTDKRIFTFICKDSESNKHLCFVF 128
Cdd:cd01211   81 TSESDCFAFTWSHGETAIFQCHVF 104