SAP18

Histone deacetylase complex subunit SAP18 is an enzyme that in humans is encoded by the SAP18 gene.[4][5]

SAP18
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesSAP18, 2HOR0202, SAP18P, Sin3A associated protein 18kDa, Sin3A associated protein 18
External IDsOMIM: 602949 MGI: 3704317 HomoloGene: 4289 GeneCards: SAP18
Gene location (Human)
Chr.Chromosome 13 (human)[1]
Band13q12.11Start21,140,514 bp[1]
End21,149,084 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

10284

100041953

Ensembl

ENSG00000150459

n/a

UniProt

O00422

n/a

RefSeq (mRNA)

NM_005870
NM_001366643

NM_001142441

RefSeq (protein)

NP_005861
NP_001353572

n/a

Location (UCSC)Chr 13: 21.14 – 21.15 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Function

Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. The protein encoded by this gene is a component of the histone deacetylase complex, which includes SIN3, SAP30, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This protein directly interacts with SIN3 and enhances SIN3-mediated transcriptional repression when tethered to the promoter.[5] Additionally, SAP18s splice variants are implicated in apoptotic cycles.[6]

Interactions

SAP18 has been shown to interact with

References
  1. GRCh38: Ensembl release 89: ENSG00000150459 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/S0092-8674(00)80216-0. PMID 9150135.
  5. "Entrez Gene: SAP18 Sin3A-associated protein, 18kDa".
  6. Michelle L, Cloutier A, Toutant J, Shkreta L, Thibault P, Durand M, Garneau D, Gendron D, Lapointe E, Couture S, Le Hir H, Klinck R, Elela SA, Prinos P, Chabot B (March 2012). "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators". Molecular and Cellular Biology. 32 (5): 954–67. doi:10.1128/MCB.06130-11. PMC 3295189. PMID 22203037.
  7. Wada M, Miyazawa H, Wang RS, Mizuno T, Sato A, Asashima M, Hanaoka F (March 2002). "The second largest subunit of mouse DNA polymerase epsilon, DPE2, interacts with SAP18 and recruits the Sin3 co-repressor protein to DNA". Journal of Biochemistry. 131 (3): 307–11. doi:10.1093/oxfordjournals.jbchem.a003104. PMID 11872158.
  8. Cheng SY, Bishop JM (April 2002). "Suppressor of Fused represses Gli-mediated transcription by recruiting the SAP18-mSin3 corepressor complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (8): 5442–7. doi:10.1073/pnas.082096999. PMC 122788. PMID 11960000.
  9. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading
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