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Conserved domains on  [gi|170292158]
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Chain A, DCC-interacting protein 13 alpha

Protein Classification

PTB_APPL domain-containing protein( domain architecture ID 10192158)

PTB_APPL domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 6-141 1.14e-86

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: 249.57  E-value: 1.14e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158   6 SGETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLP 85
Cdd:cd13158    1 SSEDEDSLLQQLFIVRFLGSMEVKSDRTSEVIYEAMRQVLAARAIHNIFRMTESHLLVTSDCLRLIDPQTQVTRARFPLA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 170292158  86 CVVLYATHQENKRLFGFVLRTSSGRSESNlSSVCYIFESNNEGEKICDSVGLAKQI 141
Cdd:cd13158   81 DVVQFAAHQENKRLFGFVVRTPEGDGEEP-SFSCYVFESNTEGEKICDAIALAKQI 135
 
Name Accession Description Interval E-value
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 6-141 1.14e-86

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: 249.57  E-value: 1.14e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158   6 SGETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLP 85
Cdd:cd13158    1 SSEDEDSLLQQLFIVRFLGSMEVKSDRTSEVIYEAMRQVLAARAIHNIFRMTESHLLVTSDCLRLIDPQTQVTRARFPLA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 170292158  86 CVVLYATHQENKRLFGFVLRTSSGRSESNlSSVCYIFESNNEGEKICDSVGLAKQI 141
Cdd:cd13158   81 DVVQFAAHQENKRLFGFVVRTPEGDGEEP-SFSCYVFESNTEGEKICDAIALAKQI 135
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 15-150 1.62e-11

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: 58.09  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158    15 HQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIfRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQ 94
Cdd:smart00462   3 GVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKK-EPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 170292158    95 ENKRLFGFVLRTSSGRSESnlssvCYIFESNNEGEKICDSVGLAKQIALHAELDRR 150
Cdd:smart00462  82 DDLDVFGYIARDPGSSRFA-----CHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
18-142 2.25e-06

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 44.66  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158   18 FIVRFLGSMEVKSDDHPD------VVYETMRQILAA------RAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLP 85
Cdd:pfam00640   1 FAVRYLGSVEVPEERAPDkntrmqQAREAIRRVKAAkinkirGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 170292158   86 CVVLYA-THQENKRLFGFVLRtssGRSESNLSsvCYIFESNNEGEKICDSVGLAKQIA 142
Cdd:pfam00640  81 SISFCAdGDPDLMRYFAYIAR---DKATNKFA--CHVFESEDGAQDIAQSIGQAFALA 133
 
Name Accession Description Interval E-value
PTB_APPL cd13158
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif (APPL; also called ...
 6-141 1.14e-86

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: 249.57  E-value: 1.14e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158   6 SGETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLP 85
Cdd:cd13158    1 SSEDEDSLLQQLFIVRFLGSMEVKSDRTSEVIYEAMRQVLAARAIHNIFRMTESHLLVTSDCLRLIDPQTQVTRARFPLA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 170292158  86 CVVLYATHQENKRLFGFVLRTSSGRSESNlSSVCYIFESNNEGEKICDSVGLAKQI 141
Cdd:cd13158   81 DVVQFAAHQENKRLFGFVVRTPEGDGEEP-SFSCYVFESNTEGEKICDAIALAKQI 135
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 16-138 4.75e-20

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: 80.25  E-value: 4.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158  16 QLFIVRFLGSMEVKSDDHPDVVYETMRqILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQE 95
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALK-ALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 170292158  96 NKRLFGFVLRTSSGRsesnlSSVCYIFESNN--EGEKICDSVGLA 138
Cdd:cd00934   80 NPNVFAFIAGEEGGS-----GFRCHVFQCEDeeEAEEILQAIGQA 119
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 15-150 1.62e-11

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: 58.09  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158    15 HQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIfRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQ 94
Cdd:smart00462   3 GVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKK-EPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 170292158    95 ENKRLFGFVLRTSSGRSESnlssvCYIFESNNEGEKICDSVGLAKQIALHAELDRR 150
Cdd:smart00462  82 DDLDVFGYIARDPGSSRFA-----CHVFRCEKAAEDIALAIGQAFQLAYELKLKAR 132
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 15-142 9.97e-09

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: 51.12  E-value: 9.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158  15 HQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNI--FRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYAT 92
Cdd:cd01273   11 HVAYLVKFLGCTEVEQPKGTEVVKEAIRKLKFARQLKKSegAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCAD 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 170292158  93 HQENKRLFGFVLRTSSGRSESnlssvCYIFESNNEGEKICDSVGLAKQIA 142
Cdd:cd01273   91 DKTDKRIFSFIAKDSESEKHL-----CFVFDSEKLAEEITLTIGQAFDLA 135
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
18-142 2.25e-06

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 44.66  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158   18 FIVRFLGSMEVKSDDHPD------VVYETMRQILAA------RAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLP 85
Cdd:pfam00640   1 FAVRYLGSVEVPEERAPDkntrmqQAREAIRRVKAAkinkirGLSGETGPGTKVDLFISTDGLKLLNPDTQELIHDHPLV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 170292158   86 CVVLYA-THQENKRLFGFVLRtssGRSESNLSsvCYIFESNNEGEKICDSVGLAKQIA 142
Cdd:pfam00640  81 SISFCAdGDPDLMRYFAYIAR---DKATNKFA--CHVFESEDGAQDIAQSIGQAFALA 133
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 17-142 2.92e-05

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: 41.08  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170292158  17 LFIVRFLGSMEVKSDDHPDVVYEtmrqilAARAIHNIFRM-TESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQE 95
Cdd:cd13161    3 VFEAKYLGSVPVKEPKGNDVVMA------AVKRLKDLKLKpKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 170292158  96 NKRLFGFVLRTSSGRSesnlsSVCYIFESNNEGEKICDSVGLAKQIA 142
Cdd:cd13161   77 DKKLFAFISHDPRLGR-----ITCHVFRCKRGAQEICDTIAEAFKAA 118
 
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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