SAP30

Sin3A-associated protein, 30kDa
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbol SAP30
External IDs OMIM: 603378 MGI: 1929129 HomoloGene: 2869 GeneCards: SAP30 Gene
RNA expression pattern
More reference expression data
Orthologs
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

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

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 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]

Interactions

SAP30 has been shown to interact with:

References

  1. 1 2 "Entrez Gene: SAP30 Sin3A-associated protein, 30kDa".
  2. ↑ Lindfors K, Viiri KM, Niittynen M, Heinonen TY, Mäki M, Kainulainen H (Dec 2003). "TGF-beta induces the expression of SAP30L, a novel nuclear protein". BMC Genomics 4 (1): 53. doi:10.1186/1471-2164-4-53. PMC 319701. PMID 14680513.
  3. 1 2 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 Research 34 (11): 3288–98. doi:10.1093/nar/gkl401. PMC 1500868. PMID 16820529.
  4. 1 2 Viiri KM, Jänis J, Siggers T, Heinonen TY, Valjakka J, Bulyk ML, Mäki M, Lohi O (Jan 2009). "DNA-binding and -bending activities of SAP30L and SAP30 are mediated by a zinc-dependent module and monophosphoinositides". Molecular and Cellular Biology 29 (2): 342–56. doi:10.1128/MCB.01213-08. PMC 2612513. PMID 19015240.
  5. ↑ http://acta.uta.fi/teos.php?id=11179
  6. 1 2 Huang NE, Lin CH, Lin YS, Yu WC (Jun 2003). "Modulation of YY1 activity by SAP30". Biochemical and Biophysical Research Communications 306 (1): 267–75. PMID 12788099.
  7. 1 2 3 4 5 Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (Jun 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Molecular Cell 1 (7): 1021–31. PMID 9651585.
  8. 1 2 3 4 5 Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (Aug 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes & Development 13 (15): 1924–35. PMC 316920. PMID 10444591.
  9. ↑ Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I (Aug 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nature Structural & Molecular Biology 11 (8): 738–46. doi:10.1038/nsmb798. PMID 15235594.
  10. 1 2 Yochum GS, Ayer DE (Jul 2001). "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex". Molecular and Cellular Biology 21 (13): 4110–8. doi:10.1128/MCB.21.13.4110-4118.2001. PMC 87072. PMID 11390640.
  11. 1 2 3 4 5 6 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. PMC 133546. PMID 11784859.
  12. 1 2 Laherty CD, Billin AN, Lavinsky RM, Yochum GS, Bush AC, Sun JM, Mullen TM, Davie JR, Rose DW, Glass CK, Rosenfeld MG, Ayer DE, Eisenman RN (Jul 1998). "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors". Molecular Cell 2 (1): 33–42. PMID 9702189.
  13. ↑ Underhill C, Qutob MS, Yee SP, 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". The Journal of Biological Chemistry 275 (51): 40463–70. doi:10.1074/jbc.M007864200. PMID 11013263.
  14. ↑ Fleischer TC, Yun UJ, Ayer DE (May 2003). "Identification and characterization of three new components of the mSin3A corepressor complex". Molecular and Cellular Biology 23 (10): 3456–67. PMC 164750. PMID 12724404.

Further reading

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