ID2

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For the ISO/IEC 7810 identification card standard, see ID-2 format.
Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ID2 ; GIG8; ID2A; ID2H; bHLHb26
External IDs OMIM600386 MGI96397 HomoloGene1632 GeneCards: ID2 Gene
RNA expression pattern
PBB GE ID2 201565 s at tn.png
PBB GE ID2 201566 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3398 15902
Ensembl ENSG00000115738 ENSMUSG00000020644
UniProt Q02363 P41136
RefSeq (mRNA) NM_002166 NM_010496
RefSeq (protein) NP_002157 NP_034626
Location (UCSC) Chr 2:
8.82 – 8.82 Mb
Chr 12:
25.09 – 25.1 Mb
PubMed search [1] [2]

DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.[1]

The protein encoded by this gene belongs to the inhibitor of DNA binding (ID) family, members of which are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative manner by suppressing their heterodimerization partners through the HLH domains. This protein may play a role in negatively regulating cell differentiation. A pseudogene has been identified for this gene.[2]

See also[edit]

Interactions[edit]

ID2 has been shown to interact with MyoD[3] and NEDD9.[4]

References[edit]

  1. ^ Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, Oda K (Feb 1994). "Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts". J Biol Chem 269 (3): 2139–45. PMID 8294468. 
  2. ^ "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein". 
  3. ^ Langlands, K; Yin X; Anand G; Prochownik E V (Aug 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. (UNITED STATES) 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. ISSN 0021-9258. PMID 9242638. 
  4. ^ Law, S F; Zhang Y Z; Fashena S J; Toby G; Estojak J; Golemis E A (Oct 1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. (UNITED STATES) 252 (1): 224–35. doi:10.1006/excr.1999.4609. ISSN 0014-4827. PMID 10502414. 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.