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Conserved domains on  [gi|1839705760|ref|XP_034120574|]
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PTB domain-containing adapter protein ced-6 isoform X2 [Drosophila guanche]

Protein Classification

CED-6 family protein( domain architecture ID 10101057)

CED-6 (cell death protein 6) family protein is a PTB (phosphotyrosine-binding) domain-containing protein, similar to Caenorhabditis elegans CED-6 and its mammalian homolog PTB domain-containing engulfment adapter protein 1 (GULP1), which may function as adapter proteins required for efficient phagocytosis of apoptotic cells

Gene Ontology:  GO:0005515|GO:0006915
PubMed:  15567406|8987385|10610414

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 77-245 2.03e-80

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: 247.58  E-value: 2.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  77 LHTPEQLISGHAVYLVKFFGNLSVDQPKGIEVVKEAIRKLQFAQQMKKaatGTQEKFTKLEITISIKGVAIQEPRTHKIL 156
Cdd:cd01273     1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKK---SEGAKLPKVELQISIDGVKIQDPKTKVIM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760 157 HQFPLYNISYCADEKGVKKFFSFIAKTVKTregeltttsnghtngsgspkteESHECFVFISNKLASDITLTIGQAFDLA 236
Cdd:cd01273    78 HQFPLHRISFCADDKTDKRIFSFIAKDSES----------------------EKHLCFVFDSEKLAEEITLTIGQAFDLA 135


                  ....*....
gi 1839705760 237 YRKYMDSTE 245
Cdd:cd01273   136 YRRFLESNG 144
 
Name Accession Description Interval E-value
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 77-245 2.03e-80

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: 247.58  E-value: 2.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  77 LHTPEQLISGHAVYLVKFFGNLSVDQPKGIEVVKEAIRKLQFAQQMKKaatGTQEKFTKLEITISIKGVAIQEPRTHKIL 156
Cdd:cd01273     1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKK---SEGAKLPKVELQISIDGVKIQDPKTKVIM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760 157 HQFPLYNISYCADEKGVKKFFSFIAKTVKTregeltttsnghtngsgspkteESHECFVFISNKLASDITLTIGQAFDLA 236
Cdd:cd01273    78 HQFPLHRISFCADDKTDKRIFSFIAKDSES----------------------EKHLCFVFDSEKLAEEITLTIGQAFDLA 135


                  ....*....
gi 1839705760 237 YRKYMDSTE 245
Cdd:cd01273   136 YRRFLESNG 144
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 90-245 6.90e-25

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: 100.08  E-value: 6.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760   90 YLVKFFGNLSVDQPKGIEVVKEAIRKLqfaqqmKKAATGTQEKFTKLEITISIKGVAIQEPRTHKILHQFPLYNISYCAD 169
Cdd:smart00462   6 FRVKYLGSVEVPEARGLQVVQEAIRKL------RAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAV 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705760  170 EKGVKKFFSFIAKtvktregeltttsngHTNGSGspkteesHECFVFISNKLASDITLTIGQAFDLAYRKYMDSTE 245
Cdd:smart00462  80 GPDDLDVFGYIAR---------------DPGSSR-------FACHVFRCEKAAEDIALAIGQAFQLAYELKLKARS 133
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
90-236 7.99e-19

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 82.80  E-value: 7.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  90 YLVKFFGNLSVDQPK------GIEVVKEAIRKLQFAQQMKKA-ATGTQEKFTKLEITISIKGVAIQEPRTHKILHQFPLY 162
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKINKIRgLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1839705760 163 NISYCAD-EKGVKKFFSFIAKTVKTREgeltttsnghtngsgspkteesHECFVFISNKLASDITLTIGQAFDLA 236
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNK----------------------FACHVFESEDGAQDIAQSIGQAFALA 133
 
Name Accession Description Interval E-value
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 77-245 2.03e-80

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: 247.58  E-value: 2.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  77 LHTPEQLISGHAVYLVKFFGNLSVDQPKGIEVVKEAIRKLQFAQQMKKaatGTQEKFTKLEITISIKGVAIQEPRTHKIL 156
Cdd:cd01273     1 IHPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKK---SEGAKLPKVELQISIDGVKIQDPKTKVIM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760 157 HQFPLYNISYCADEKGVKKFFSFIAKTVKTregeltttsnghtngsgspkteESHECFVFISNKLASDITLTIGQAFDLA 236
Cdd:cd01273    78 HQFPLHRISFCADDKTDKRIFSFIAKDSES----------------------EKHLCFVFDSEKLAEEITLTIGQAFDLA 135


                  ....*....
gi 1839705760 237 YRKYMDSTE 245
Cdd:cd01273   136 YRRFLESNG 144
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 90-245 6.90e-25

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: 100.08  E-value: 6.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760   90 YLVKFFGNLSVDQPKGIEVVKEAIRKLqfaqqmKKAATGTQEKFTKLEITISIKGVAIQEPRTHKILHQFPLYNISYCAD 169
Cdd:smart00462   6 FRVKYLGSVEVPEARGLQVVQEAIRKL------RAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAV 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705760  170 EKGVKKFFSFIAKtvktregeltttsngHTNGSGspkteesHECFVFISNKLASDITLTIGQAFDLAYRKYMDSTE 245
Cdd:smart00462  80 GPDDLDVFGYIAR---------------DPGSSR-------FACHVFRCEKAAEDIALAIGQAFQLAYELKLKARS 133
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
90-236 7.99e-19

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 82.80  E-value: 7.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  90 YLVKFFGNLSVDQPK------GIEVVKEAIRKLQFAQQMKKA-ATGTQEKFTKLEITISIKGVAIQEPRTHKILHQFPLY 162
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAIRRVKAAKINKIRgLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1839705760 163 NISYCAD-EKGVKKFFSFIAKTVKTREgeltttsnghtngsgspkteesHECFVFISNKLASDITLTIGQAFDLA 236
Cdd:pfam00640  81 SISFCADgDPDLMRYFAYIARDKATNK----------------------FACHVFESEDGAQDIAQSIGQAFALA 133
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 88-233 8.13e-19

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: 82.17  E-value: 8.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  88 AVYLVKFFGNLSVDQPKGIEVVKEAIRKLQFAQQMKKaatgtqEKFTKLEITISIKGVAIQEPRTHKILHQFPLYNISYC 167
Cdd:cd00934     1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSK------RKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYC 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1839705760 168 ADEKGVKKFFSFIAKTvktregeltttsnghtngsgspKTEESHECFVFISNK--LASDITLTIGQAF 233
Cdd:cd00934    75 GRDPDNPNVFAFIAGE----------------------EGGSGFRCHVFQCEDeeEAEEILQAIGQAF 120
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 75-238 8.31e-19

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: 83.10  E-value: 8.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  75 NWLHTPEQLISGHAVYLVKFFGNLSVDQPKGIEVVKEAIRKLqfaqqmkKAATGTQEKFTKLEITISIKGVAIQEPRTHK 154
Cdd:cd01274     2 QWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKL-------KKSTREMKKIPTIILSISYKGVKFIDATTKN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760 155 ILHQFPLYNISYCADEKGVKKFFSFIAKTVKTRegeltttsnghtngsgspkteeSHECFVF--ISNKLASDITLTIGQA 232
Cdd:cd01274    75 LICEHEIRNISCACQDPEDLNTFAYITKDLKTD----------------------HHYCHVFcvLTVDLATEIILTLGQA 132


                  ....*.
gi 1839705760 233 FDLAYR 238
Cdd:cd01274   133 FEVAYQ 138
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 90-233 1.77e-16

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: 75.83  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  90 YLVKFFGNLSVDQPKGIEVVKEAIRKlqfAQQMKKAATGTQEKFTkleITISIKGVAIQEPRTHKILHQFPLYNISYCAD 169
Cdd:cd13159     5 FYLKYLGSTLVEKPKGEGATAEAVKT---IIAMAKASGKKLQKVT---LTVSPKGIKVTDSATNETILEVSIYRISYCTA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705760 170 EKGVKKFFSFIAktvktregeltttSNGHTngsgspkteESHECFVFI--SNKLASDITLTIGQAF 233
Cdd:cd13159    79 DANHDKVFAFIA-------------TNQDN---------EKLECHAFLcaKRKMAQAVTLTVAQAF 122
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 88-238 4.14e-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: 66.12  E-value: 4.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  88 AVYLVKFFGNLSVDQPKGIEVVKEAIRKLQFAQQMKKAATgtqekftkleITISIKGVAIQEPRTHKILHQFPLYNISY- 166
Cdd:cd13161     2 GVFEAKYLGSVPVKEPKGNDVVMAAVKRLKDLKLKPKPVV----------LVVSSEGIRVVERLTGEVLTNVPIKDISFv 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1839705760 167 CADEKGvKKFFSFIAKTVKTRegeltttsnghtngsgspkteeSHECFVFISNKLASDITLTIGQAFDLAYR 238
Cdd:cd13161    72 TVDPKD-KKLFAFISHDPRLG----------------------RITCHVFRCKRGAQEICDTIAEAFKAAAE 120
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 87-232 6.08e-08

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: 51.58  E-value: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  87 HAVYLVKFFGNLSVDQPKGIEVVKEAIRklqfaQQMKKAATGTQEKFTKLEITISIKGVAIQEPRTHKILHQFPLYNISY 166
Cdd:cd13158    10 QQLFIVRFLGSMEVKSDRTSEVIYEAMR-----QVLAARAIHNIFRMTESHLLVTSDCLRLIDPQTQVTRARFPLADVVQ 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705760 167 CADEKGVKKFFSFIAKTVKTREGELTTTsnghtngsgspkteesheCFVFISNKLASDITLTIGQA 232
Cdd:cd13158    85 FAAHQENKRLFGFVVRTPEGDGEEPSFS------------------CYVFESNTEGEKICDAIALA 132
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
 76-241 5.65e-06

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.


Pssm-ID: 269920  Cd Length: 170  Bit Score: 46.82  E-value: 5.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  76 WLHTPEQLISGHAV-YLVKFFGNLSVDQ-------PKGIEVVKEAIRKLQFAQQMKKAAT------GTQEKFTK------ 135
Cdd:cd01209     2 GWLHPDQLGMGPGVsYPVRYVGCIEVLQsmrsldfNTRTQVTREAINRVCEAVGGAKGAKrkrkskALSSILGKsnlqfa 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760 136 ---LEITISIKGVAIQEPRTHKILHQFPLYNISY-------CADekgvkkFFSFIAKT-VKTREgeltttsnghtngsgs 204
Cdd:cd01209    82 gmnISLTISTDGLNLVTPDTGQIIANHHMQSISFasggdpdTYD------YVAYVAKDpVNQRA---------------- 139

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1839705760 205 pkteesheCFVF-ISNKLASDITLTIGQAFDLAYRKYM 241
Cdd:cd01209   140 --------CHVLeCGDGLAQDVIATIGQAFELRFKQYL 169
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 75-187 2.17e-05

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: 44.22  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  75 NWLHTPEQLISGHAVYLVKFFGNLSVDQPKGIEVVKEAIRKLQFAQQMKKAAtgtqekftklEITISIKGVAIQEPRTHK 154
Cdd:cd01268     2 QWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKASRKKPVRA----------VLWVSGDGLRVVDEKTKG 71

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1839705760 155 ILHQFPLYNISYCADEKGVKKFFSFIAKTVKTR 187
Cdd:cd01268    72 LIVDQTIEKVSFCAPDRNHERAFSYICRDGTTR 104
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 93-168 2.92e-05

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: 44.17  E-value: 2.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705760  93 KFFGNLSVDQPKGIEVVKEAIRKLqfaqqmKKAATGTQEKFTKLEITISIKGVAIQEPRTHKILHQFPLYNISYCA 168
Cdd:cd01215    21 KLIGIDEVPAARGDKMCQDAMMKL------KGAVKAAGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIA 90
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
 93-234 1.32e-04

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain; CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have 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 is part of the Dab-like subgroup.


Pssm-ID: 269968  Cd Length: 179  Bit Score: 43.04  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705760  93 KFFGNLSVDQPKG-IEVVkEAIRKLQF---AQQMKKaatgtqekfTKLEITISIKGVAI--QEPRTHK---------ILH 157
Cdd:cd01270    34 KYIGSLEVPRPSSrVEIV-AAMRRIRYefkAKNIKK---------KKVTITVSVDGVKVvlRKKKKKKgwtwdesklLLM 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1839705760 158 QFPLYNISYCADEKGVKKFFSFIAktvktREGelttTSNghtngsgspkteeSHECFVFISNK--LASDITLTIGQAFD 234
Cdd:cd01270   104 QHPIYRIFYVSHDSQDLKIFSYIA-----RDG----SSN-------------VFKCNVFKSKKksQAMRIVRTIGQAFE 160
 
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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