Protein-coding gene in the species Homo sapiens
SAP18 |
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Available structures |
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PDB | Human UniProt search: PDBe RCSB |
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Identifiers |
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Aliases | SAP18, 2HOR0202, SAP18P, Sin3A associated protein 18kDa, Sin3A associated protein 18 |
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External IDs | OMIM: 602949; MGI: 3704317; HomoloGene: 4289; GeneCards: SAP18; OMA:SAP18 - orthologs |
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Gene location (Human) |
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| Chr. | Chromosome 13 (human)[1] |
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| Band | 13q12.11 | Start | 21,140,514 bp[1] |
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End | 21,149,084 bp[1] |
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Gene location (Mouse) |
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| Chr. | Chromosome 8 (mouse)[2] |
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| Band | 8|8 D1 | Start | 96,551,974 bp[2] |
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End | 96,552,762 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - internal globus pallidus
- right ventricle
- tendon
- tendon of biceps brachii
- corpus epididymis
- Achilles tendon
- caput epididymis
- bronchial epithelial cell
- biceps brachii
- Skeletal muscle tissue of biceps brachii
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| Top expressed in | - primary oocyte
- yolk sac
- embryo
- embryo
- neural tube
- stomach
- lens
- zygote
- epiblast
- proximal tubule
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| More reference expression data |
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BioGPS |
| More reference expression data |
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Gene ontology |
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Molecular function | - transcription corepressor activity
- protein binding
- histone deacetylase activity
- RNA binding
| Cellular component | - histone deacetylase complex
- nuclear speck
- exon-exon junction complex
- nucleoplasm
- ASAP complex
- nucleus
- cytoplasm
- cytosol
- nuclear body
| Biological process | - regulation of transcription, DNA-templated
- regulation of transcription by RNA polymerase II
- mRNA processing
- regulation of alternative mRNA splicing, via spliceosome
- transcription, DNA-templated
- negative regulation of mRNA splicing, via spliceosome
- RNA splicing
- positive regulation of apoptotic process
- negative regulation of nucleic acid-templated transcription
- histone deacetylation
| Sources:Amigo / QuickGO |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | | |
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RefSeq (protein) | | |
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Location (UCSC) | Chr 13: 21.14 – 21.15 Mb | Chr 8: 96.55 – 96.55 Mb |
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PubMed search | [3] | [4] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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Histone deacetylase complex subunit SAP18 is an enzyme that in humans is encoded by the SAP18 gene.[5][6]
Function
Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Multisubunit complexes catalyze histone acetylation and deacetylation. The protein encoded by this gene is a histone deacetylase complex component, including 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.[6] Additionally, SAP18s splice variants are implicated in apoptotic cycles.[7]
Interactions
SAP18 has been shown to interact with
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000150459 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000061104 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ 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.
- ^ a b "Entrez Gene: SAP18 Sin3A-associated protein, 18kDa".
- ^ 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.
- ^ 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.
- ^ 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. Bibcode:2002PNAS...99.5442C. doi:10.1073/pnas.082096999. PMC 122788. PMID 11960000.
- ^ 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
- Koipally J, Renold A, Kim J, Georgopoulos K (June 1999). "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". The EMBO Journal. 18 (11): 3090–100. doi:10.1093/emboj/18.11.3090. PMC 1171390. PMID 10357820.
- 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.
- 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. Bibcode:2002PNAS...99.5442C. doi:10.1073/pnas.082096999. PMC 122788. PMID 11960000.
- Paces-Fessy M, Boucher D, Petit E, Paute-Briand S, Blanchet-Tournier MF (March 2004). "The negative regulator of Gli, Suppressor of fused (Sufu), interacts with SAP18, Galectin3 and other nuclear proteins". The Biochemical Journal. 378 (Pt 2): 353–62. doi:10.1042/BJ20030786. PMC 1223961. PMID 14611647.
- Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (January 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
External links
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