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Sin3A-associated protein, 30kDa
Available structures
PDB Ortholog search: PDBe, RCSB
Symbol SAP30
External IDs OMIM603378 MGI1929129 HomoloGene2869 GeneCards: SAP30 Gene
RNA expression pattern
PBB GE SAP30 204899 s at tn.png
PBB GE SAP30 204900 x at tn.png
More reference expression data
Species Human Mouse
Entrez 8819 60406
Ensembl ENSG00000164105 ENSMUSG00000031609
UniProt O75446 O88574
RefSeq (mRNA) NM_003864 NM_021788
RefSeq (protein) NP_003855 NP_068560
Location (UCSC) Chr 4:
173.37 – 173.38 Mb
Chr 8:
57.48 – 57.49 Mb
PubMed search [1] [2]

Sin3A-associated protein, 30kDa, also known as SAP30, is a protein which in humans is encoded by the SAP30 gene.[1]


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 SIN3A, SAP18, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones. A pseudogene of this gene is located on chromosome 3.[1]

Mammals have one paralog of SAP30, named SAP30-like (SAP30L), which shares 70% sequence identity with SAP30.[2] SAP30 and SAP30L together constitute a well-conserved SAP30 protein family. Also SAP30L interacts with several components of the Sin3A corepressor complex and induces transcriptional repression via recruitment of Sin3A and histone deacetylases.[3]

Proteins of the SAP30 family (SAP30 proteins) have a functional nucleolar localization signal and they are able to target Sin3A to the nucleolus.[3] SAP30 proteins have sequence-independent contact with DNA by their N-terminal zinc-dependent module and their acidic central region contributes to histone and nucleosome interactions. The DNA binding of SAP30 proteins is regulated by the nuclear signalling lipids, phosphoinositides (PI).[4] SAP30 proteins provide the first example in which the DNA and PIs seem to stand in a mutually antagonizing interrelationship in regard to their interaction with zinc finger proteins and thus exemplifies the molecular mechanism how these lipids can contribute for gene regulation.[4][5]


SAP30 has been shown to interact with HDAC1,[6][7][8][9][10][11] Histone deacetylase 2,[7][8][11] SIN3A,[7][8][10][11][12][13] RBBP7,[7][8][11] Nuclear receptor co-repressor 1,[13][14] RBBP4,[7][8][11] ING1[11] and YY1.[6]


  1. ^ a b "Entrez Gene: SAP30 Sin3A-associated protein, 30kDa". 
  2. ^ Lindfors K, Viiri KM, Niittynen M, Heinonen TY, Mäki M, Kainulainen H (December 2003). "TGF-beta induces the expression of SAP30L, a novel nuclear protein". BMC Genomics 4: 53. doi:10.1186/1471-2164-4-53. PMC 319701. PMID 14680513. 
  3. ^ a b Viiri KM, Korkeamäki H, Kukkonen MK, Nieminen LK, Lindfors K, Peterson P, Mäki M, Kainulainen H, Lohi O (2006). "SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus". Nucleic Acids Res. 34 (11): 3288–98. doi:10.1093/nar/gkl401. PMC 1500868. PMID 16820529. 
  4. ^ a b Viiri KM, Jänis J, Siggers T, Heinonen TY, Valjakka J, Bulyk ML, Mäki M, Lohi O (January 2009). "DNA-binding and -bending activities of SAP30L and SAP30 are mediated by a zinc-dependent module and monophosphoinositides". Mol. Cell. Biol. 29 (2): 342–56. doi:10.1128/MCB.01213-08. PMC 2612513. PMID 19015240. 
  5. ^
  6. ^ a b Huang, Nu En; Lin Ching Hui; Lin Young Sun; Yu Winston C Y (June 2003). "Modulation of YY1 activity by SAP30". Biochem. Biophys. Res. Commun. (United States) 306 (1): 267–75. doi:10.1016/S0006-291X(03)00966-5. ISSN 0006-291X. PMID 12788099. 
  7. ^ a b c d e Zhang, Y; Sun Z W; Iratni R; Erdjument-Bromage H; Tempst P; Hampsey M; Reinberg D (June 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell (UNITED STATES) 1 (7): 1021–31. doi:10.1016/S1097-2765(00)80102-1. ISSN 1097-2765. PMID 9651585. 
  8. ^ a b c d e Zhang, Y; Ng H H; Erdjument-Bromage H; Tempst P; Bird A; Reinberg D (August 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. (UNITED STATES) 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. ISSN 0890-9369. PMC 316920. PMID 10444591. 
  9. ^ Swanson, Kurt A; Knoepfler Paul S; Huang Kai; Kang Richard S; Cowley Shaun M; Laherty Carol D; Eisenman Robert N; Radhakrishnan Ishwar (August 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nat. Struct. Mol. Biol. (United States) 11 (8): 738–46. doi:10.1038/nsmb798. ISSN 1545-9993. PMID 15235594. 
  10. ^ a b Yochum, G S; Ayer D E (July 2001). "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex". Mol. Cell. Biol. (United States) 21 (13): 4110–8. doi:10.1128/MCB.21.13.4110-4118.2001. ISSN 0270-7306. PMC 87072. PMID 11390640. 
  11. ^ a b c d e f Kuzmichev, A; Zhang Y; Erdjument-Bromage H; Tempst P; Reinberg D (February 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Mol. Cell. Biol. (United States) 22 (3): 835–48. doi:10.1128/MCB.22.3.835-848.2002. ISSN 0270-7306. PMC 133546. PMID 11784859. 
  12. ^ Fleischer, Tracey C; Yun Ui Jeong; Ayer Donald E (May 2003). "Identification and characterization of three new components of the mSin3A corepressor complex". Mol. Cell. Biol. (United States) 23 (10): 3456–67. doi:10.1128/MCB.23.10.3456-3467.2003. ISSN 0270-7306. PMC 164750. PMID 12724404. 
  13. ^ a b Laherty, C D; Billin A N, Lavinsky R M, Yochum G S, Bush A C, Sun J M, Mullen T M, Davie J R, Rose D W, Glass C K, Rosenfeld M G, Ayer D E, Eisenman R N (July 1998). "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors". Mol. Cell (UNITED STATES) 2 (1): 33–42. doi:10.1016/S1097-2765(00)80111-2. ISSN 1097-2765. PMID 9702189. 
  14. ^ Underhill, C; Qutob M S; Yee S P; Torchia J (Dec 2000). "A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1". J. Biol. Chem. (UNITED STATES) 275 (51): 40463–70. doi:10.1074/jbc.M007864200. ISSN 0021-9258. PMID 11013263. 

Further reading[edit]