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Conserved domains on  [gi|768009707|ref|XP_011525354|]
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epidermal growth factor receptor kinase substrate 8-like protein 1 isoform X5 [Homo sapiens]

Protein Classification

EPS8 family PTB domain-containing protein( domain architecture ID 10100535)

epidermal growth factor receptor kinase substrate 8 (EPS8) family protein similar to PTB domain region of human EPS8, a signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTB_EPS8 cd01210
Epidermal growth factor receptor kinase substrate (EPS8)-like Phosphotyrosine-binding (PTB) ...
 32-162 1.85e-70

Epidermal growth factor receptor kinase substrate (EPS8)-like Phosphotyrosine-binding (PTB) domain; EPS8 is a regulator of Rac signaling. It consists of a PTB and an SH3 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: 269921  Cd Length: 131  Bit Score: 219.73  E-value: 1.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009707  32 DVSQYPVNHLVTFCLGEDDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPDHVTLLDPASKEELESYPLGAIVRCDAVM 111
Cdd:cd01210    1 DTSQYRVEHLATFTLGREEGVQTVEDALRKLKELDAKGRIWSQEMLLQVNDGWVLLLDIETKEELESFPLSSIQECTAVL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768009707 112 PPGRSRSLLLLVCQEPERAQPDVHFFQGLRLGAELIREDIQGALHNYRSGR 162
Cdd:cd01210   81 STCSYNSILLLVVQEPDQPKPEMHLFQCDEVGAELLVEDLQKALSGKRSGR 131
 
Name Accession Description Interval E-value
PTB_EPS8 cd01210
Epidermal growth factor receptor kinase substrate (EPS8)-like Phosphotyrosine-binding (PTB) ...
 32-162 1.85e-70

Epidermal growth factor receptor kinase substrate (EPS8)-like Phosphotyrosine-binding (PTB) domain; EPS8 is a regulator of Rac signaling. It consists of a PTB and an SH3 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: 269921  Cd Length: 131  Bit Score: 219.73  E-value: 1.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009707  32 DVSQYPVNHLVTFCLGEDDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPDHVTLLDPASKEELESYPLGAIVRCDAVM 111
Cdd:cd01210    1 DTSQYRVEHLATFTLGREEGVQTVEDALRKLKELDAKGRIWSQEMLLQVNDGWVLLLDIETKEELESFPLSSIQECTAVL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768009707 112 PPGRSRSLLLLVCQEPERAQPDVHFFQGLRLGAELIREDIQGALHNYRSGR 162
Cdd:cd01210   81 STCSYNSILLLVVQEPDQPKPEMHLFQCDEVGAELLVEDLQKALSGKRSGR 131
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 35-165 5.49e-66

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


Pssm-ID: 429984  Cd Length: 131  Bit Score: 207.97  E-value: 5.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009707   35 QYPVNHLVTFCLGEDDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPDHVTLLDPASKEELESYPLGAIVRCDAVMPPG 114
Cdd:pfam08416   1 QYRVEHLTTFELDSLTGLQAVEDAIRKLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEELESYPLDSISHCQAVLNDG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768009707  115 RSRSLLLLVCQEPERAQPDVHFFQGLRLGAELIREDIQGALHNYRSGRGER 165
Cdd:pfam08416  81 RYNSILALVCQEPGQSKPDVHLFQCDELGAELIAEDIESALSDVRLGKPKK 131
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 35-138 3.27e-08

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: 52.32  E-value: 3.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009707    35 QYPVNHLVTFCLGEDDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPDHVTLLDPASKEELESYPLGAIVRCDAVMPPG 114
Cdd:smart00462   5 SFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDL 84

                           90       100
                   ....*....|....*....|....
gi 768009707   115 RsrsLLLLVCQEPERAQPDVHFFQ 138
Cdd:smart00462  85 D---VFGYIARDPGSSRFACHVFR 105
 
Name Accession Description Interval E-value
PTB_EPS8 cd01210
Epidermal growth factor receptor kinase substrate (EPS8)-like Phosphotyrosine-binding (PTB) ...
 32-162 1.85e-70

Epidermal growth factor receptor kinase substrate (EPS8)-like Phosphotyrosine-binding (PTB) domain; EPS8 is a regulator of Rac signaling. It consists of a PTB and an SH3 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: 269921  Cd Length: 131  Bit Score: 219.73  E-value: 1.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009707  32 DVSQYPVNHLVTFCLGEDDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPDHVTLLDPASKEELESYPLGAIVRCDAVM 111
Cdd:cd01210    1 DTSQYRVEHLATFTLGREEGVQTVEDALRKLKELDAKGRIWSQEMLLQVNDGWVLLLDIETKEELESFPLSSIQECTAVL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768009707 112 PPGRSRSLLLLVCQEPERAQPDVHFFQGLRLGAELIREDIQGALHNYRSGR 162
Cdd:cd01210   81 STCSYNSILLLVVQEPDQPKPEMHLFQCDEVGAELLVEDLQKALSGKRSGR 131
PTB pfam08416
Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also ...
 35-165 5.49e-66

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


Pssm-ID: 429984  Cd Length: 131  Bit Score: 207.97  E-value: 5.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009707   35 QYPVNHLVTFCLGEDDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPDHVTLLDPASKEELESYPLGAIVRCDAVMPPG 114
Cdd:pfam08416   1 QYRVEHLTTFELDSLTGLQAVEDAIRKLQLLDAQGRVWTQEMLLQVSDQGITLTDNETKEELESYPLDSISHCQAVLNDG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768009707  115 RSRSLLLLVCQEPERAQPDVHFFQGLRLGAELIREDIQGALHNYRSGRGER 165
Cdd:pfam08416  81 RYNSILALVCQEPGQSKPDVHLFQCDELGAELIAEDIESALSDVRLGKPKK 131
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 36-154 2.39e-16

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: 74.85  E-value: 2.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009707  36 YPVNHLVTFCLGEDDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPDHVTLLDPASKEELESYPLGAIVRCDAVmppGR 115
Cdd:cd00934    3 FQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRD---PD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 768009707 116 SRSLLLLVCQEPERAQPDVHFFQGLR-LGAELIREDIQGA 154
Cdd:cd00934   80 NPNVFAFIAGEEGGSGFRCHVFQCEDeEEAEEILQAIGQA 119
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 35-138 3.27e-08

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: 52.32  E-value: 3.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768009707    35 QYPVNHLVTFCLGEDDGVHTVEDASRKLAVMDSQGRVWAQEMLLRVSPDHVTLLDPASKEELESYPLGAIVRCDAVMPPG 114
Cdd:smart00462   5 SFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDL 84

                           90       100
                   ....*....|....*....|....
gi 768009707   115 RsrsLLLLVCQEPERAQPDVHFFQ 138
Cdd:smart00462  85 D---VFGYIARDPGSSRFACHVFR 105
 
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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