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 1773094908  14 MHTPEALSKHFIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273     1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1773094908  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 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 1773094908  14 MHTPEALSKHFIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273     1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1773094908  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 157
Cdd:cd01273    81 PLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEKLAEEITLTIGQAFDLAYRRFLESNG 144

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773094908  27 YNAKFLGSTEVEQPK------GTEVVRDAVRKLKFAR--HIKKSEGQKIP--KVELQISIYGVKILEPKTKEVQHNCQLH 96
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKinKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1773094908  97 RISFCAD-DKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLA 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 1773094908  14 MHTPEALSKHFIPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNC 93
Cdd:cd01273     1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1773094908  94 QLHRISFCADDKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLAYRKFLESGG 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 1773094908  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKfarHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:cd00934     3 FQVKYLGSVEVGSSRGVDVVEEALKALA---AALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1773094908 107 DKRIFTFICKDSESNKHLCYVF--DSEKCAEEITLTIGQAF 145
Cdd:cd00934    80 NPNVFAFIAGEEGGSGFRCHVFqcEDEEEAEEILQAIGQAF 120

Phosphotyrosine interaction domain (PTB/PID);

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773094908  27 YNAKFLGSTEVEQPK------GTEVVRDAVRKLKFAR--HIKKSEGQKIP--KVELQISIYGVKILEPKTKEVQHNCQLH 96
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKinKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1773094908  97 RISFCAD-DKTDKRIFTFICKDSESNKHLCYVFDSEKCAEEITLTIGQAFDLA 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 1773094908  24 FIPYNAKFLGSTEVEQPKGTEVVRDAVRKlkfARHIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCAD 103
Cdd:cd13159     2 GVTFYLKYLGSTLVEKPKGEGATAEAVKT---IIAMAKASGKKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISYCTA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1773094908 104 DKTDKRIFTFICKDSESNKHLCYVF--DSEKCAEEITLTIGQAF 145
Cdd:cd13159    79 DANHDKVFAFIATNQDNEKLECHAFlcAKRKMAQAVTLTVAQAF 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 1773094908  15 HTPEALSKHF----IPYNAKFLGSTEVEQPKGTEVVRDAVRKLKFArhIKKSEGQKiPKVELQISIYGVKILEPKTKEVQ 90
Cdd:cd01215     2 KTAENLPERFrgdgVRFKAKLIGIDEVPAARGDKMCQDAMMKLKGA--VKAAGEHK-QRIWLNISLEGIKILDEKTGALL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1773094908  91 HNCQLHRISFCADDKTDKRIFTFICkdSESNKHLCYVFDSEKCAEEITLTIGQAFDLAY 149
Cdd:cd01215    79 HHHPVHKISFIARDTTDNRAFGYVC--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 1773094908  30 KFLGSteveQPKGTEVVRDAVRKLKFARHIKKSEGQKIPKVELQISIYGVKiLEPKTKEVQHNCQ----LHRISFCADDK 105
Cdd:cd13160     6 KYLGR----MPARGLWGIKHTRKPLVDALKNLPKGKTLPKTKLEVSSDGVK-LEELRGGFGSSKTvffpIHTISYGVQDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1773094908 106 TDKRIFTFICK-DSESNKHL--CYVF--DSEKCAEEITLTIGQAF 145
Cdd:cd13160    81 VHTRVFSMIVVgEQDSSNHPfeCHAFvcDSRADARNLTYWLAKAF 125

Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an 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. This cd is part of the Shc-like subgroup.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773094908  13 WMHTPEALSKH-FIPYNAKFLGSTEVEQ-------PKGTEVVRDAVRKL----KFARHIKKSEGQKI---------PK-- 69
Cdd:cd01209     2 GWLHPDQLGMGpGVSYPVRYVGCIEVLQsmrsldfNTRTQVTREAINRVceavGGAKGAKRKRKSKAlssilgksnLQfa 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773094908  70 ---VELQISIYGVKILEPKTKEVQHNCQLHRISF--CADDKTDKRIfTFICKDsESNKHLCYVFD-SEKCAEEITLTIGQ 143
Cdd:cd01209    82 gmnISLTISTDGLNLVTPDTGQIIANHHMQSISFasGGDPDTYDYV-AYVAKD-PVNQRACHVLEcGDGLAQDVIATIGQ 159

                         170
                  ....*....|
gi 1773094908 144 AFDLAYRKFL 153
Cdd:cd01209   160 AFELRFKQYL 169

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 1773094908  17 PEALSKHFIpYNAKFLGSTEVEQPKGTevvRDAVRKLKfARH----IKKSEGQKIP--KVELQISIYGVKILEPKTKEVQ 90
Cdd:cd01208     1 PEDLIDGVI-FGANYLGSTQLLSERNP---SKNVRMAQ-AQEavsrVKAPEGESQPstEVDLFISTERIKVLNADTQETM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773094908  91 HNCQLHRISFCAD-----------------DKTDKRIFTFICKDSESNKHLCYVFDSEKcAEEITLTIGQAFDLAYRKFL 153
Cdd:cd01208    76 MDHALRTISYIADignivvlmarrrmprssSQECVETTPPSQEGKRQYKMICHVFESED-AQLIAQSIGQAFSVAYQEFL 154

                  ....
gi 1773094908 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 1773094908  26 PYNAKF-----LGSTEVEQPKGTEVVRD-AVRKLKF--ARHIKKSEGQKIPKVE-------LQISIYGVKILEPKTKEVQ 90
Cdd:cd01269     4 PSNSQFfevlyCGKIKVSHKKVPPTFIDdCLEKFRLheLEKSRSGPSSVQPTDSeenrtmlFQIGRSELRLISPDTKQVL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773094908  91 HNCQLHRISFCADDKTDKRIFTFICKDSESNK---HLCYVF--DSEKCAEEITLTIGQAF 145
Cdd:cd01269    84 LEKQFKDISSCSQGIKHVDHFGFICRESSEGGgfhFVCYVFkcQSESVVDEIMLTIKQAF 143

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773094908  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKipkVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:pfam08416   2 YRVEHLTTFELDSLTGLQAVEDAIRKLQLLDAQGRVWTQE---MLLQVSDQGITLTDNETKEELESYPLDSISHCQAVLN 78

                          90       100
                  ....*....|....*....|....*
gi 1773094908 107 DKR---IFTFICKDSESNKHLCYVF 128
Cdd:pfam08416  79 DGRynsILALVCQEPGQSKPDVHLF 103

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 1773094908  31 FLGSTEVEQPKgTEVvrDAVRKLKfarhIKKSEGQKIPKVELQI--SIYG-VKILEPKTKEVQHNCQLHRISFCA---DD 104
Cdd:cd01211     8 YLGCAKVNAPR-SET--EALRIMA----ILREQSAQPIKVTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILFCArgpDG 80

                          90       100
                  ....*....|....*....|....
gi 1773094908 105 KTDKRIFTFICKDSESNKHLCYVF 128
Cdd:cd01211    81 TSESDCFAFTWSHGETAIFQCHVF 104