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ID2

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
For the ISO/IEC 7810 identification card standard, seeID-2 format. For the upcoming electric car, seeVolkswagen ID. Polo.

ID2
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

4AYA

Identifiers
AliasesID2, GIG8, ID2A, ID2H, bHLHb26, inhibitor of DNA binding 2, HLH protein, inhibitor of DNA binding 2
External IDsOMIM:600386;MGI:96397;HomoloGene:1632;GeneCards:ID2;OMA:ID2 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for ID2
Genomic location for ID2
Band2p25.1Start8,678,845bp[1]
End8,684,461bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for ID2
Genomic location for ID2
Band12 A1.3|12 8.57 cMStart25,143,798bp[2]
End25,147,139bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • popliteal artery

  • tibial arteries

  • saphenous vein

  • pericardium

  • right lobe of liver

  • granulocyte

  • trachea

  • lower lobe of lung

  • renal medulla

  • seminal vesicula
Top expressed in
  • vas deferens

  • seminal vesicula

  • lobe of cerebellum

  • migratory enteric neural crest cell

  • cerebellar vermis

  • abdominal wall

  • dermis

  • left lung lobe

  • hand

  • parotid gland
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
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: 8.68 – 8.68 MbChr 12: 25.14 – 25.15 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DNA-binding protein inhibitor ID-2 is aprotein that in humans is encoded by theID2gene.[5]

Function

[edit]

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.[6]The ID2 protein may play a role in the development and resistance to therapies ofglioblastoma, the most aggressive of brain cancers.[7]

Interactions

[edit]

ID2 has been shown tointeract withMyoD[8] andNEDD9.[9]

See also

[edit]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000115738Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000020644Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, et al. (January 1994)."Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts".The Journal of Biological Chemistry.269 (3):2139–2145.doi:10.1016/S0021-9258(17)42146-6.PMID 8294468.
  6. ^"Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".
  7. ^Lee SB, Frattini V, Bansal M, Castano AM, Sherman D, Hutchinson K, et al. (January 2016)."An ID2-dependent mechanism for VHL inactivation in cancer".Nature.529 (7585):172–177.Bibcode:2016Natur.529..172L.doi:10.1038/nature16475.PMC 5384647.PMID 26735018.
  8. ^Langlands K, Yin X, Anand G, Prochownik EV (August 1997)."Differential interactions of Id proteins with basic-helix-loop-helix transcription factors".The Journal of Biological Chemistry.272 (32):19785–19793.doi:10.1074/jbc.272.32.19785.PMID 9242638.
  9. ^Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (October 1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain".Experimental Cell Research.252 (1):224–235.doi:10.1006/excr.1999.4609.PMID 10502414.

Further reading

[edit]

External links

[edit]

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

(1) Basic domains
(1.1) Basicleucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3)bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2)Zinc finger DNA-binding domains
(2.1)Nuclear receptor(Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3.1)Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3)Fork head /winged helix
(3.4)Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4)β-Scaffold factors with minor groove contacts
(4.1)Rel homology region
(4.2)STAT
(4.3) p53-like
(4.4)MADS box
(4.6)TATA-binding proteins
(4.7)High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3)Pocket domain
(0.5)AP-2/EREBP-related factors
(0.6) Miscellaneous
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