ING2

Protein-coding gene in the species Homo sapiens
ING2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1WES, 2G6Q

Identifiers
AliasesING2, ING1L, p33inhibitor of growth family member 2
External IDsOMIM: 604215 MGI: 1916510 HomoloGene: 20388 GeneCards: ING2
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for ING2
Genomic location for ING2
Band4q35.1Start183,505,058 bp[1]
End183,512,429 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for ING2
Genomic location for ING2
Band8|8 B1.1Start48,120,213 bp[2]
End48,128,591 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • amniotic fluid

  • jejunal mucosa

  • right adrenal gland

  • left adrenal gland

  • palpebral conjunctiva

  • bronchial epithelial cell

  • oral cavity

  • biceps brachii

  • caput epididymis

  • retinal pigment epithelium
Top expressed in
  • lens

  • islet of Langerhans

  • seminiferous tubule

  • renal corpuscle

  • yolk sac

  • bone marrow

  • retinal pigment epithelium

  • secondary oocyte

  • primitive streak

  • dermis
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • chromatin binding
  • metal ion binding
  • methylated histone binding
  • protein binding
  • phosphatidylinositol binding
  • protein-containing complex binding
Cellular component
  • Golgi apparatus
  • plasma membrane
  • Sin3 complex
  • CCAAT-binding factor complex
  • nucleus
  • nucleoplasm
  • cytosol
Biological process
  • flagellated sperm motility
  • positive regulation of transforming growth factor beta receptor signaling pathway
  • regulation of transcription, DNA-templated
  • negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
  • negative regulation of apoptotic signaling pathway
  • male meiosis I
  • transcription, DNA-templated
  • positive regulation of transcription, DNA-templated
  • male germ-line stem cell asymmetric division
  • seminiferous tubule development
  • spermatogenesis
  • spermatid development
  • regulation of growth
  • regulation of response to DNA damage stimulus
  • signal transduction
  • negative regulation of cell population proliferation
  • chromatin organization
  • positive regulation of histone deacetylation
  • regulation of apoptotic process
  • regulation of cellular senescence
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3622

69260

Ensembl

ENSG00000168556

ENSMUSG00000063049

UniProt

Q9H160

Q9ESK4

RefSeq (mRNA)

NM_001291959
NM_001564

NM_023503

RefSeq (protein)

NP_001278888
NP_001555

NP_075992

Location (UCSC)Chr 4: 183.51 – 183.51 MbChr 8: 48.12 – 48.13 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Inhibitor of growth protein 2 is a protein that in humans is encoded by the ING2 gene.[5][6]

Function

This gene is a member of the inhibitor of growth (ING) family. Members of the ING family associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and function in DNA repair and apoptosis.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000168556 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000063049 – 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. ^ Shimada Y, Saito A, Suzuki M, Takahashi E, Horie M (Mar 1999). "Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor suppressor". Cytogenetics and Cell Genetics. 83 (3–4): 232–5. doi:10.1159/000015188. PMID 10072587. S2CID 7081905.
  6. ^ a b "Entrez Gene: ING2 inhibitor of growth family, member 2".

Further reading

  • Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Nagashima M, Shiseki M, Miura K, Hagiwara K, Linke SP, Pedeux R, Wang XW, Yokota J, Riabowol K, Harris CC (Aug 2001). "DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53". Proceedings of the National Academy of Sciences of the United States of America. 98 (17): 9671–6. Bibcode:2001PNAS...98.9671N. doi:10.1073/pnas.161151798. PMC 55510. PMID 11481424.
  • Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (Feb 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Molecular and Cellular Biology. 22 (3): 835–48. doi:10.1128/MCB.22.3.835-848.2002. PMC 133546. PMID 11784859.
  • Gozani O, Karuman P, Jones DR, Ivanov D, Cha J, Lugovskoy AA, Baird CL, Zhu H, Field SJ, Lessnick SL, Villasenor J, Mehrotra B, Chen J, Rao VR, Brugge JS, Ferguson CG, Payrastre B, Myszka DG, Cantley LC, Wagner G, Divecha N, Prestwich GD, Yuan J (Jul 2003). "The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor". Cell. 114 (1): 99–111. doi:10.1016/S0092-8674(03)00480-X. PMID 12859901. S2CID 16506650.
  • Sironi E, Cerri A, Tomasini D, Sirchia SM, Porta G, Rossella F, Grati FR, Simoni G (Apr 2004). "Loss of heterozygosity on chromosome 4q32-35 in sporadic basal cell carcinomas: evidence for the involvement of p33ING2/ING1L and SAP30 genes". Journal of Cutaneous Pathology. 31 (4): 318–22. doi:10.1111/j.0303-6987.2004.0187.x. PMID 15005689. S2CID 2520678.
  • Chattopadhyay C, Hawke D, Kobayashi R, Maity SN (2004). "Human p32, interacts with B subunit of the CCAAT-binding factor, CBF/NF-Y, and inhibits CBF-mediated transcription activation in vitro". Nucleic Acids Research. 32 (12): 3632–41. doi:10.1093/nar/gkh692. PMC 484179. PMID 15243141.
  • He GH, Helbing CC, Wagner MJ, Sensen CW, Riabowol K (Jan 2005). "Phylogenetic analysis of the ING family of PHD finger proteins". Molecular Biology and Evolution. 22 (1): 104–16. doi:10.1093/molbev/msh256. PMID 15356280.
  • Chin MY, Ng KC, Li G (Apr 2005). "The novel tumor suppressor p33ING2 enhances UVB-induced apoptosis in human melanoma cells". Experimental Cell Research. 304 (2): 531–43. doi:10.1016/j.yexcr.2004.11.023. PMID 15748897.
  • Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (Mar 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
  • Pedeux R, Sengupta S, Shen JC, Demidov ON, Saito S, Onogi H, Kumamoto K, Wincovitch S, Garfield SH, McMenamin M, Nagashima M, Grossman SR, Appella E, Harris CC (Aug 2005). "ING2 regulates the onset of replicative senescence by induction of p300-dependent p53 acetylation". Molecular and Cellular Biology. 25 (15): 6639–48. doi:10.1128/MCB.25.15.6639-6648.2005. PMC 1190357. PMID 16024799.
  • Okano T, Gemma A, Hosoya Y, Hosomi Y, Nara M, Kokubo Y, Yoshimura A, Shibuya M, Nagashima M, Harris CC, Kudoh S (Mar 2006). "Alterations in novel candidate tumor suppressor genes, ING1 and ING2 in human lung cancer". Oncology Reports. 15 (3): 545–9. doi:10.3892/or.15.3.545. PMID 16465410.
  • Wang J, Chin MY, Li G (Feb 2006). "The novel tumor suppressor p33ING2 enhances nucleotide excision repair via inducement of histone H4 acetylation and chromatin relaxation". Cancer Research. 66 (4): 1906–11. doi:10.1158/0008-5472.CAN-05-3444. PMID 16488987.
  • Lu F, Dai DL, Martinka M, Ho V, Li G (Jul 2006). "Nuclear ING2 expression is reduced in human cutaneous melanomas". British Journal of Cancer. 95 (1): 80–6. doi:10.1038/sj.bjc.6603205. PMC 2360493. PMID 16755297.
  • Wang Y, Wang J, Li G (Jul 2006). "Leucine zipper-like domain is required for tumor suppressor ING2-mediated nucleotide excision repair and apoptosis". FEBS Letters. 580 (16): 3787–93. doi:10.1016/j.febslet.2006.05.065. PMID 16782091. S2CID 40317066.
  • Huang W, Zhang H, Davrazou F, Kutateladze TG, Shi X, Gozani O, Prestwich GD (May 2007). "Stabilized phosphatidylinositol-5-phosphate analogues as ligands for the nuclear protein ING2: chemistry, biology, and molecular modeling". Journal of the American Chemical Society. 129 (20): 6498–506. doi:10.1021/ja070195b. PMC 2553394. PMID 17469822.

External links

  • 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
  • v
  • t
  • e
  • 1wes: Solution structure of PHD domain in inhibitor of growth family, member 1-like
    1wes: Solution structure of PHD domain in inhibitor of growth family, member 1-like
  • 2g6q: Crystal structure of ING2 PHD domain in complex with H3K4Me3 peptide
    2g6q: Crystal structure of ING2 PHD domain in complex with H3K4Me3 peptide
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.