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Conserved domains on  [gi|1475409272|ref|NP_001352724|]
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disabled homolog 1 isoform 2 [Homo sapiens]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
25-69 1.44e-22

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01215:

Pssm-ID: 473070  Cd Length: 147  Bit Score: 84.23  E-value: 1.44e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1475409272  25 DRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLK 69
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLK 45
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
25-69 1.44e-22

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: 84.23  E-value: 1.44e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1475409272  25 DRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLK 69
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLK 45
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
37-69 3.29e-04

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: 36.52  E-value: 3.29e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1475409272   37 GEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLK 69
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR 33
 
Name Accession Description Interval E-value
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
25-69 1.44e-22

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: 84.23  E-value: 1.44e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1475409272  25 DRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLK 69
Cdd:cd01215     1 DKTAENLPERFRGDGVRFKAKLIGIDEVPAARGDKMCQDAMMKLK 45
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
37-69 3.29e-04

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: 36.52  E-value: 3.29e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1475409272   37 GEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLK 69
Cdd:smart00462   1 GSGVSFRVKYLGSVEVPEARGLQVVQEAIRKLR 33
 
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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