ID2

Protein-coding gene in the species Homo sapiens
ID2
Available structures
PDBOrtholog search: PDBe RCSB
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
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for ID2
Genomic location for ID2
Band2p25.1Start8,678,845 bp[1]
End8,684,461 bp[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 cMStart25,143,798 bp[2]
End25,147,139 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • popliteal artery

  • saphenous vein

  • pericardium

  • right lobe of liver

  • trachea

  • lower lobe of lung

  • renal medulla

  • seminal vesicula

  • vena cava

  • urethra
Top expressed in
  • vas deferens

  • seminal vesicula

  • cerebellar vermis

  • abdominal wall

  • dermis

  • left lung lobe

  • hand

  • parotid gland

  • gallbladder

  • adrenal gland
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein dimerization activity
  • transmembrane transporter binding
  • protein binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • DNA-binding transcription factor activity
  • transcription factor binding
Cellular component
  • nucleus
  • cytosol
  • cytoplasm
  • protein-containing complex
Biological process
  • regulation of G1/S transition of mitotic cell cycle
  • rhythmic process
  • negative regulation of DNA-binding transcription factor activity
  • regulation of transcription, DNA-templated
  • positive regulation of transcription involved in G1/S transition of mitotic cell cycle
  • multicellular organism development
  • negative regulation of transcription, DNA-templated
  • transcription, DNA-templated
  • negative regulation of transcription by RNA polymerase II
  • metanephros development
  • natural killer cell differentiation
  • thigmotaxis
  • leukocyte differentiation
  • membranous septum morphogenesis
  • bundle of His development
  • heart development
  • circadian rhythm
  • adult locomotory behavior
  • entrainment of circadian clock
  • positive regulation of gene expression
  • negative regulation of gene expression
  • oligodendrocyte development
  • regulation of lipid metabolic process
  • olfactory bulb development
  • circadian regulation of gene expression
  • mammary gland epithelial cell proliferation
  • regulation of circadian rhythm
  • entrainment of circadian clock by photoperiod
  • enucleate erythrocyte differentiation
  • negative regulation of DNA binding
  • locomotor rhythm
  • negative regulation of B cell differentiation
  • positive regulation of fat cell differentiation
  • positive regulation of erythrocyte differentiation
  • positive regulation of macrophage differentiation
  • negative regulation of neuron differentiation
  • negative regulation of osteoblast differentiation
  • positive regulation of blood pressure
  • positive regulation of transcription, DNA-templated
  • cell development
  • cell maturation
  • Peyer's patch development
  • embryonic digestive tract morphogenesis
  • positive regulation of smooth muscle cell proliferation
  • neuron fate commitment
  • cell morphogenesis involved in neuron differentiation
  • positive regulation of astrocyte differentiation
  • negative regulation of oligodendrocyte differentiation
  • adipose tissue development
  • mammary gland alveolus development
  • epithelial cell differentiation involved in mammary gland alveolus development
  • endodermal digestive tract morphogenesis
  • cellular response to lithium ion
  • cellular senescence
  • negative regulation of neural precursor cell proliferation
  • neuron differentiation
  • regulation of cell cycle
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 a protein that in humans is encoded by the ID2 gene.[5]

Function

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 of glioblastoma, the most aggressive of brain cancers.[7]

Interactions

ID2 has been shown to interact with MyoD[8] and NEDD9.[9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115738 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020644 – Ensembl, 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, 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. 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, Sang Bae; Frattini, Veronique; Bansal, Mukesh; Castano, Angelica M.; Sherman, Dan; Hutchinson, Keino; Bruce, Jeffrey N.; Califano, Andrea; Liu, Guangchao; Cardozo, Timothy; Iavarone, Antonio; Lasorella, Anna (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 (Aug 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. PMID 9242638.
  9. ^ Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (Oct 1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. 252 (1): 224–35. doi:10.1006/excr.1999.4609. PMID 10502414.

Further reading

  • Biggs J, Murphy EV, Israel MA (1992). "A human Id-like helix-loop-helix protein expressed during early development". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1512–6. Bibcode:1992PNAS...89.1512B. doi:10.1073/pnas.89.4.1512. PMC 48481. PMID 1741406.
  • Iavarone A, Garg P, Lasorella A, Hsu J, Israel MA (1994). "The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein". Genes Dev. 8 (11): 1270–84. doi:10.1101/gad.8.11.1270. PMID 7926730.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Kurabayashi M, Jeyaseelan R, Kedes L (1993). "Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2". Gene. 133 (2): 305–6. doi:10.1016/0378-1119(93)90658-P. PMID 8224921.
  • Mathew S, Chen W, Murty VV, Benezra R, Chaganti RS (1996). "Chromosomal assignment of human ID1 and ID2 genes". Genomics. 30 (2): 385–7. doi:10.1006/geno.1995.0037. PMID 8586447.
  • Lasorella A, Iavarone A, Israel MA (1996). "Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins". Mol. Cell. Biol. 16 (6): 2570–8. doi:10.1128/MCB.16.6.2570. PMC 231247. PMID 8649364.
  • Hara E, Hall M, Peters G (1997). "Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors". EMBO J. 16 (2): 332–42. doi:10.1093/emboj/16.2.332. PMC 1169639. PMID 9029153.
  • Langlands K, Yin X, Anand G, Prochownik EV (1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. doi:10.1074/jbc.272.32.19785. PMID 9242638.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Yates PR, Atherton GT, Deed RW, Norton JD, Sharrocks AD (1999). "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors". EMBO J. 18 (4): 968–76. doi:10.1093/emboj/18.4.968. PMC 1171189. PMID 10022839.
  • Yokota Y, Mansouri A, Mori S, Sugawara S, Adachi S, Nishikawa S, Gruss P (1999). "Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2". Nature. 397 (6721): 702–6. Bibcode:1999Natur.397..702Y. doi:10.1038/17812. PMID 10067894. S2CID 4428856.
  • Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. 252 (1): 224–35. doi:10.1006/excr.1999.4609. PMID 10502414.
  • Moldes M, Boizard M, Liepvre XL, Fève B, Dugail I, Pairault J (2000). "Functional antagonism between inhibitor of DNA binding (Id) and adipocyte determination and differentiation factor 1/sterol regulatory element-binding protein-1c (ADD1/SREBP-1c) trans-factors for the regulation of fatty acid synthase promoter in adipocytes". Biochem. J. 344 (3): 873–80. doi:10.1042/0264-6021:3440873. PMC 1220711. PMID 10585876.
  • Liu J, Shi W, Warburton D (2000). "A cysteine residue in the helix-loop-helix domain of Id2 is critical for homodimerization and function". Biochem. Biophys. Res. Commun. 273 (3): 1042–7. doi:10.1006/bbrc.2000.3055. PMID 10891368.
  • Lasorella A, Noseda M, Beyna M, Yokota Y, Iavarone A (2000). "Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins". Nature. 407 (6804): 592–8. Bibcode:2000Natur.407..592L. doi:10.1038/35036504. PMID 11034201. S2CID 4335368.
  • Roberts EC, Deed RW, Inoue T, Norton JD, Sharrocks AD (2001). "Id Helix-Loop-Helix Proteins Antagonize Pax Transcription Factor Activity by Inhibiting DNA Binding". Mol. Cell. Biol. 21 (2): 524–33. doi:10.1128/MCB.21.2.524-533.2001. PMC 86614. PMID 11134340.
  • Wang S, Sdrulla A, Johnson JE, Yokota Y, Barres BA (2001). "A role for the helix-loop-helix protein Id2 in the control of oligodendrocyte development". Neuron. 29 (3): 603–14. doi:10.1016/S0896-6273(01)00237-9. PMID 11301021. S2CID 7978661.
  • Wong J, Funes-Duran M, Ahlberg J, Round J, O'Connell R, Miller R, Chen E, Richmond PA, Vierra CA (2001). "Characterization of a basic helix-loop-helix protein, ABF-1: nuclear localization, transcriptional properties, and interaction with Id-2". DNA Cell Biol. 20 (8): 465–71. doi:10.1089/104454901316976091. PMID 11560778.
  • Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y (2001). "Protein–Protein Interaction Panel Using Mouse Full-Length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.

External links

  • ID2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • Overview of all the structural information available in the PDB for UniProt: Q02363 (DNA-binding protein inhibitor ID-2) at the PDBe-KB.

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

  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine 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) Helix-turn-helix domains
(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
see also transcription factor/coregulator deficiencies


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