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Conserved domains on  [gi|323276659|ref|NP_001191008|]
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ankyrin repeat and sterile alpha motif domain-containing protein 1B isoform j [Homo sapiens]

Protein Classification

Anks family PTB domain-containing protein( domain architecture ID 10101078)

Anks (ankyrin repeat and sterile alpha motif domain-containing protein) family PTB (phosphotyrosine-binding) domain-containing protein similar to PTB domain region of mammalian ankyrin repeat and sterile alpha motif domain-containing protein 1B, a brain-specific protein highly enriched at neuronal synapses

Gene Ontology:  GO:0005515

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
77-226 1.58e-103

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: 298.04  E-value: 1.58e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  77 QYWQHHPEKLIFQSCDYKAFYLGSMLIKELRGTESTQDACAKMRancqKSTEQMKKVPTIILSVSYKGVKFIDATNKNII 156
Cdd:cd01274    1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLK----KSTREMKKIPTIILSISYKGVKFIDATTKNLI 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659 157 AEHEIRNISCAAQDPEDLSTFAYITKDLKSNHHYCHVFTAFDVNLAYEIILTLGQAFEVAYQLALQARKG 226
Cdd:cd01274   77 CEHEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
77-226 1.58e-103

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: 298.04  E-value: 1.58e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  77 QYWQHHPEKLIFQSCDYKAFYLGSMLIKELRGTESTQDACAKMRancqKSTEQMKKVPTIILSVSYKGVKFIDATNKNII 156
Cdd:cd01274    1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLK----KSTREMKKIPTIILSISYKGVKFIDATTKNLI 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659 157 AEHEIRNISCAAQDPEDLSTFAYITKDLKSNHHYCHVFTAFDVNLAYEIILTLGQAFEVAYQLALQARKG 226
Cdd:cd01274   77 CEHEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
89-225 4.83e-35

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: 123.19  E-value: 4.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659    89 QSCDYKAFYLGSMLIKELRGTESTQDACAKMRAncqKSTEQMKKVPTIILSVSYKGVKFIDATNKNIIAEHEIRNISCAA 168
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRA---AQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCA 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 323276659   169 QDPEDLSTFAYITKDLKSNHHYCHVFTAFDVnlAYEIILTLGQAFEVAYQLALQARK 225
Cdd:smart00462  79 VGPDDLDVFGYIARDPGSSRFACHVFRCEKA--AEDIALAIGQAFQLAYELKLKARS 133
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
93-216 8.91e-16

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 72.40  E-value: 8.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659   93 YKAFYLGSMLIKELR------GTESTQDA--CAKMRANCQKSTEQMKKVP--TIILSVSYKGVKFIDATNKNIIAEHEIR 162
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAirRVKAAKINKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 323276659  163 NIS-CAAQDPEDLSTFAYITKDLKSNHHYCHVFTAFDvnLAYEIILTLGQAFEVA 216
Cdd:pfam00640  81 SISfCADGDPDLMRYFAYIARDKATNKFACHVFESED--GAQDIAQSIGQAFALA 133
 
Name Accession Description Interval E-value
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
77-226 1.58e-103

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: 298.04  E-value: 1.58e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  77 QYWQHHPEKLIFQSCDYKAFYLGSMLIKELRGTESTQDACAKMRancqKSTEQMKKVPTIILSVSYKGVKFIDATNKNII 156
Cdd:cd01274    1 TQWRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLK----KSTREMKKIPTIILSISYKGVKFIDATTKNLI 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659 157 AEHEIRNISCAAQDPEDLSTFAYITKDLKSNHHYCHVFTAFDVNLAYEIILTLGQAFEVAYQLALQARKG 226
Cdd:cd01274   77 CEHEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVDLATEIILTLGQAFEVAYQLALRAQKS 146
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
89-225 4.83e-35

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: 123.19  E-value: 4.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659    89 QSCDYKAFYLGSMLIKELRGTESTQDACAKMRAncqKSTEQMKKVPTIILSVSYKGVKFIDATNKNIIAEHEIRNISCAA 168
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRA---AQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCA 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 323276659   169 QDPEDLSTFAYITKDLKSNHHYCHVFTAFDVnlAYEIILTLGQAFEVAYQLALQARK 225
Cdd:smart00462  79 VGPDDLDVFGYIARDPGSSRFACHVFRCEKA--AEDIALAIGQAFQLAYELKLKARS 133
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
93-213 6.95e-25

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: 96.42  E-value: 6.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  93 YKAFYLGSMLIKELRGTESTQDACAKMRANCQKSTEQMKKVptiILSVSYKGVKFIDATNKNIIAEHEIRNISCAAQDPE 172
Cdd:cd00934    3 FQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPV---LLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 323276659 173 DLSTFAYITKDLKSNHHYCHVFTAFDVNLAYEIILTLGQAF 213
Cdd:cd00934   80 NPNVFAFIAGEEGGSGFRCHVFQCEDEEEAEEILQAIGQAF 120
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
81-222 1.44e-22

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: 90.80  E-value: 1.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  81 HHPEKLIFQSCDYKAFYLGSMLIKELRGTESTQDACAKMRANCQKSTEQMKKVPTIILSVSYKGVKFIDATNKNIIAEHE 160
Cdd:cd01273    2 HPPEALIKGHVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSEGAKLPKVELQISIDGVKIQDPKTKVIMHQFP 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323276659 161 IRNISCAAQDPEDLSTFAYITKDLKSNHHYCHVFTAfdVNLAYEIILTLGQAFEVAYQLALQ 222
Cdd:cd01273   82 LHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDS--EKLAEEITLTIGQAFDLAYRRFLE 141
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
93-218 1.27e-16

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: 74.21  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  93 YKAFYLGSMLIKELRGTESTQDACAKMRAncqksteQMKKVPTIILSVSYKGVKFIDATNKNIIAEHEIRNISCAAQDPE 172
Cdd:cd13161    4 FEAKYLGSVPVKEPKGNDVVMAAVKRLKD-------LKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPK 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 323276659 173 DLSTFAYITKDLKSNHHYCHVFTAFDVnlAYEIILTLGQAFEVAYQ 218
Cdd:cd13161   77 DKKLFAFISHDPRLGRITCHVFRCKRG--AQEICDTIAEAFKAAAE 120
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
93-216 8.91e-16

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 72.40  E-value: 8.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659   93 YKAFYLGSMLIKELR------GTESTQDA--CAKMRANCQKSTEQMKKVP--TIILSVSYKGVKFIDATNKNIIAEHEIR 162
Cdd:pfam00640   1 FAVRYLGSVEVPEERapdkntRMQQAREAirRVKAAKINKIRGLSGETGPgtKVDLFISTDGLKLLNPDTQELIHDHPLV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 323276659  163 NIS-CAAQDPEDLSTFAYITKDLKSNHHYCHVFTAFDvnLAYEIILTLGQAFEVA 216
Cdd:pfam00640  81 SISfCADGDPDLMRYFAYIARDKATNKFACHVFESED--GAQDIAQSIGQAFALA 133
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
93-214 2.06e-15

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: 71.21  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  93 YKAFYLGSMLIKELRGTESTQDACAKMRAnCQKSTEqmKKVPTIILSVSYKGVKFIDATNKNIIAEHEIRNIS-CAAqDP 171
Cdd:cd13159    5 FYLKYLGSTLVEKPKGEGATAEAVKTIIA-MAKASG--KKLQKVTLTVSPKGIKVTDSATNETILEVSIYRISyCTA-DA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 323276659 172 EDLSTFAYITKDLKSNHHYCHVFTAFDVNLAYEIILTLGQAFE 214
Cdd:cd13159   81 NHDKVFAFIATNQDNEKLECHAFLCAKRKMAQAVTLTVAQAFN 123
PTB_Shc cd01209
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ...
135-222 6.02e-14

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: 68.39  E-value: 6.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659 135 TIILSVSYKGVKFIDATNKNIIAEHEIRNISCAA-QDPEDLSTFAYITKDlKSNHHYCHVFTAFDvNLAYEIILTLGQAF 213
Cdd:cd01209   84 NISLTISTDGLNLVTPDTGQIIANHHMQSISFASgGDPDTYDYVAYVAKD-PVNQRACHVLECGD-GLAQDVIATIGQAF 161

                 ....*....
gi 323276659 214 EVAYQLALQ 222
Cdd:cd01209  162 ELRFKQYLK 170
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
77-196 2.12e-13

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: 65.79  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  77 QYWQHHPEKLIFQSCDYKAFYLGSMLIKELRGTESTQDACAKMRANcqksteqMKKVPTIILSVSYKGVKFIDATNKNII 156
Cdd:cd01268    1 HQWQADEEAVRSGTCSFPVKYLGCVEVGESRGMQVCEEALKKLKAS-------RKKPVRAVLWVSGDGLRVVDEKTKGLI 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 323276659 157 AEHEIRNISCAAQDPEDLSTFAYITKDLKSNHHYCHVFTA 196
Cdd:cd01268   74 VDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLA 113
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
92-219 4.49e-11

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: 59.58  E-value: 4.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  92 DYKAFYLGSMLIKELRGTESTQDACAKMRaNCQKSTEQMKKvpTIILSVSYKGVKFIDATNKNIIAEHEIRNISCAAQDP 171
Cdd:cd01215   17 RFKAKLIGIDEVPAARGDKMCQDAMMKLK-GAVKAAGEHKQ--RIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDT 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 323276659 172 EDLSTFAYITKdLKSNHHYCHVFTAfdvNLAYEIILTLGQAFEVAYQL 219
Cdd:cd01215   94 TDNRAFGYVCG-LDGGHRFFAIKTA---KAAEPVVLDLRDLFQVVFEL 137
PTB_tensin-related cd13157
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ...
93-217 1.08e-09

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


Pssm-ID: 269979  Cd Length: 129  Bit Score: 55.47  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  93 YKAFYLGSMLIKELRGTESTQdacakmraNCQKSTEQMKKVPT----IILSVSYKGVKFIDATNKNIIAEHEIRNISCAA 168
Cdd:cd13157    4 RNAQYIGSFPVSGLDVADRAD--------SVRKQLESLKESGSrgrpVILSVSLSGIKICSEDGKVVLMAHALRRVSYST 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 323276659 169 QDPEDlSTFAYITKDLKS--NHHYCHVFTAFDVNLAYEIILTLGQAFEVAY 217
Cdd:cd13157   76 CRPAH-AQFAFVARNPGGptNRQYCHVFVTRSPREAQELNLLLCRAFQLAY 125
PTB_CAPON-like cd01270
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ...
82-228 1.63e-09

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: 56.14  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  82 HPEKLIFQSCDYKAFYLGSMLIKelRGTeSTQDACAKMRA---NCQKSTEQMKKVpTIILSVSykGVKFI---------- 148
Cdd:cd01270   20 HNEEAFQHGITFQAKYIGSLEVP--RPS-SRVEIVAAMRRiryEFKAKNIKKKKV-TITVSVD--GVKVVlrkkkkkkgw 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659 149 -DATNKNIIAEHEIRNISCAAQDPEDLSTFAYITKDLKSNHHYCHVFTAFDVNLAYEIILTLGQAFEVAYQLALQARKGG 227
Cdd:cd01270   94 tWDESKLLLMQHPIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKKSQAMRIVRTIGQAFEVCHKLSLQHMQGN 173

                 .
gi 323276659 228 H 228
Cdd:cd01270  174 A 174
PTB_LOC417372 cd13168
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ...
93-213 2.95e-06

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.


Pssm-ID: 269989  Cd Length: 125  Bit Score: 45.40  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  93 YKAFYLGSMLIKELRGTESTQDAcakmrANCQKSTEQMKKVPTIILsVSYKGVKFIDATNKNIIAEHEIRNISCAAQDPE 172
Cdd:cd13168    3 YKALYLGQVEVGEDGGVEQIESA-----AIIVVLESDLTPKEVLLE-LGEIGVTVWDKSTSEVLFKHSFPEISSCGRRVD 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 323276659 173 DLSTFAYITKDL---KSNHHYCHVFTAFDVNLAYEIILTLGQAF 213
Cdd:cd13168   77 DPNYFAYIAGDTpcsLAKHFVCYVFEAADEEEAETILQGIAQGF 120
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
97-194 4.15e-05

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.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 42.24  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  97 YLGSMLIKELRGTESTQDACAKMRANCQKSTEqmkkvptIILSV--SYKG-VKFIDATNKNIIAEHEIRNIS-CA--AQD 170
Cdd:cd01211    8 YLGCAKVNAPRSETEALRIMAILREQSAQPIK-------VTLSVpnSSEGsVRLYDPTSNTEIASYPIYRILfCArgPDG 80
                         90       100
                 ....*....|....*....|....
gi 323276659 171 PEDLSTFAYITKDLKSNHHYCHVF 194
Cdd:cd01211   81 TSESDCFAFTWSHGETAIFQCHVF 104
PTB_X11 cd01208
X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is ...
95-223 9.84e-05

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.


Pssm-ID: 269919  Cd Length: 161  Bit Score: 41.89  E-value: 9.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  95 AFYLGSMLIKELRGTEST------QDACAKMRA---NCQKSTEqmkkvptIILSVSYKGVKFIDATNKNIIAEHEIRNIS 165
Cdd:cd01208   12 ANYLGSTQLLSERNPSKNvrmaqaQEAVSRVKApegESQPSTE-------VDLFISTERIKVLNADTQETMMDHALRTIS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323276659 166 CAA-----------------QDPEDLSTFAYITKDLKSNHHYCHVFTAFDVNLayeIILTLGQAFEVAYQLALQA 223
Cdd:cd01208   85 YIAdignivvlmarrrmprsSSQECVETTPPSQEGKRQYKMICHVFESEDAQL---IAQSIGQAFSVAYQEFLRA 156
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
97-213 7.21e-04

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.


Pssm-ID: 269982  Cd Length: 125  Bit Score: 38.86  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659  97 YLGSMLIKELRGTESTQDACAKMRANCQKSteqmKKVPTIILSVSYKGVKFIDATNK------NIIAEHEirnISCAAQD 170
Cdd:cd13160    7 YLGRMPARGLWGIKHTRKPLVDALKNLPKG----KTLPKTKLEVSSDGVKLEELRGGfgssktVFFPIHT---ISYGVQD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 323276659 171 PEDLSTFAYITK-DLKSNHHY--CHVFTAFDVNLAYEIILTLGQAF 213
Cdd:cd13160   80 LVHTRVFSMIVVgEQDSSNHPfeCHAFVCDSRADARNLTYWLAKAF 125
PTB_TBC1D1_like cd01269
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ...
153-213 6.93e-03

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.


Pssm-ID: 269967  Cd Length: 143  Bit Score: 36.12  E-value: 6.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323276659 153 KNIIAEHEIRNISCAAQDPEDLSTFAYITKDLKSN---HHYCHVFTAFDVNLAYEIILTLGQAF 213
Cdd:cd01269   80 KQVLLEKQFKDISSCSQGIKHVDHFGFICRESSEGggfHFVCYVFKCQSESVVDEIMLTIKQAF 143
PTB_JIP cd01212
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ...
116-194 8.73e-03

JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a mitogen-activated protein kinase scaffold protein. JIP consists of a C-terminal SH3 domain, followed by a 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: 269923  Cd Length: 149  Bit Score: 36.10  E-value: 8.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323276659 116 CAKMRANCQK-STEQMKKVP-TIILSVSYKGVKFIDATNKNIIA-------EHEIRNIS-CAAQdPEDLSTFAYITK--D 183
Cdd:cd01212   25 CQAMQKIATArRLTVHLRPPqSCILEISDRGLKMVDRSKPNKKDgkpcihyFYSLKNISfCGFH-PRNSRYFGFITKhpL 103
                         90
                 ....*....|.
gi 323276659 184 LKSNHhyCHVF 194
Cdd:cd01212  104 LQRFA--CHVF 112
 
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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