SIN3B

Protein-coding gene in the species Homo sapiens
SIN3B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1E91, 1PD7, 2CR7, 2CZY, 2F05

Identifiers
AliasesSIN3B, Paired amphipathic helix protein Sin3b, SIN3 transcription regulator family member B
External IDsOMIM: 607777 MGI: 107158 HomoloGene: 81810 GeneCards: SIN3B
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for SIN3B
Genomic location for SIN3B
Band19p13.11Start16,829,398 bp[1]
End16,880,353 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for SIN3B
Genomic location for SIN3B
Band8 B3.3|8 35.08 cMStart73,449,913 bp[2]
End73,484,829 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right uterine tube

  • canal of the cervix

  • right lung

  • gastric mucosa

  • left uterine tube

  • sural nerve

  • left lobe of thyroid gland

  • right lobe of thyroid gland

  • upper lobe of left lung

  • anterior pituitary
Top expressed in
  • Paneth cell

  • internal carotid artery

  • external carotid artery

  • fossa

  • renal corpuscle

  • condyle

  • endocardial cushion

  • medullary collecting duct

  • testicle

  • ureter
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • transcription corepressor activity
  • histone deacetylase activity
  • chromatin binding
  • protein binding
Cellular component
  • cytoplasm
  • X chromosome
  • Y chromosome
  • autosome
  • Sin3 complex
  • nucleoplasm
  • XY body
  • nucleus
  • chromatin
Biological process
  • regulation of transcription, DNA-templated
  • negative regulation of transcription by RNA polymerase II
  • transcription, DNA-templated
  • negative regulation of transcription, DNA-templated
  • histone deacetylation
  • regulation of lipid metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23309

20467

Ensembl

ENSG00000127511

ENSMUSG00000031622

UniProt

O75182

Q62141

RefSeq (mRNA)

NM_001297595
NM_001297597
NM_015260

NM_001113248
NM_009188

RefSeq (protein)

NP_001284524
NP_001284526
NP_056075

NP_001106719
NP_033214

Location (UCSC)Chr 19: 16.83 – 16.88 MbChr 8: 73.45 – 73.48 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Paired amphipathic helix protein Sin3b is a protein that in humans is encoded by the SIN3B gene.[5][6]

Interactions

SIN3B has been shown to interact with HDAC1,[7][8] Zinc finger and BTB domain-containing protein 16,[9] SUDS3[10] and IKZF1.[8][11]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000127511 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031622 – 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. ^ Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Jun 1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 5 (3): 169–76. doi:10.1093/dnares/5.3.169. PMID 9734811.
  6. ^ "Entrez Gene: SIN3B SIN3 homolog B, transcription regulator (yeast)".
  7. ^ 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. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
  8. ^ a b Koipally J, Renold A, Kim J, Georgopoulos K (Jun 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.
  9. ^ David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A (May 1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID 9627120. S2CID 655636.
  10. ^ Alland L, David G, Shen-Li H, Potes J, Muhle R, Lee HC, Hou H, Chen K, DePinho RA (Apr 2002). "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex". Molecular and Cellular Biology. 22 (8): 2743–50. doi:10.1128/MCB.22.8.2743-2750.2002. PMC 133736. PMID 11909966.
  11. ^ Koipally J, Georgopoulos K (Aug 2002). "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry. 277 (31): 27697–705. doi:10.1074/jbc.M201694200. PMID 12015313.

Further reading

  • Ayer DE, Lawrence QA, Eisenman RN (Mar 1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. 80 (5): 767–76. doi:10.1016/0092-8674(95)90355-0. PMID 7889570. S2CID 8749951.
  • David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A (May 1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID 9627120. S2CID 655636.
  • Koipally J, Renold A, Kim J, Georgopoulos K (Jun 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.
  • Naruse Y, Aoki T, Kojima T, Mori N (Nov 1999). "Neural restrictive silencer factor recruits mSin3 and histone deacetylase complex to repress neuron-specific target genes". Proceedings of the National Academy of Sciences of the United States of America. 96 (24): 13691–6. Bibcode:1999PNAS...9613691N. doi:10.1073/pnas.96.24.13691. PMC 24126. PMID 10570134.
  • Spronk CA, Tessari M, Kaan AM, Jansen JF, Vermeulen M, Stunnenberg HG, Vuister GW (Dec 2000). "The Mad1-Sin3B interaction involves a novel helical fold". Nature Structural Biology. 7 (12): 1100–4. doi:10.1038/81944. PMID 11101889. S2CID 12451972.
  • Spronk CA, Jansen JF, Tessari M, Kaan AM, Aelen J, Lasonder E, Stunnenberg HG, Vuister GW (Apr 2001). "Sequence-specific assignment of the PAH2 domain of Sin3B free and bound to Mad1". Journal of Biomolecular NMR. 19 (4): 377–8. doi:10.1023/A:1011262214741. hdl:2066/79476. PMID 11370785. S2CID 31789681.
  • Alland L, David G, Shen-Li H, Potes J, Muhle R, Lee HC, Hou H, Chen K, DePinho RA (Apr 2002). "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex". Molecular and Cellular Biology. 22 (8): 2743–50. doi:10.1128/MCB.22.8.2743-2750.2002. PMC 133736. PMID 11909966.
  • Rayman JB, Takahashi Y, Indjeian VB, Dannenberg JH, Catchpole S, Watson RJ, te Riele H, Dynlacht BD (Apr 2002). "E2F mediates cell cycle-dependent transcriptional repression in vivo by recruitment of an HDAC1/mSin3B corepressor complex". Genes & Development. 16 (8): 933–47. doi:10.1101/gad.969202. PMC 152357. PMID 11959842.
  • Koipally J, Georgopoulos K (Aug 2002). "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry. 277 (31): 27697–705. doi:10.1074/jbc.M201694200. PMID 12015313.
  • Yang L, Mei Q, Zielinska-Kwiatkowska A, Matsui Y, Blackburn ML, Benedetti D, Krumm AA, Taborsky GJ, Chansky HA (Feb 2003). "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B". The Biochemical Journal. 369 (Pt 3): 651–7. doi:10.1042/BJ20020854. PMC 1223118. PMID 12398767.
  • Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A (May 2003). "The histone deacetylase 9 gene encodes multiple protein isoforms". The Journal of Biological Chemistry. 278 (18): 16059–72. doi:10.1074/jbc.M212935200. PMID 12590135.
  • Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W (Apr 2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes & Development. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
  • Dugast-Darzacq C, Pirity M, Blanck JK, Scherl A, Schreiber-Agus N (Nov 2004). "Mxi1-SRalpha: a novel Mxi1 isoform with enhanced transcriptional repression potential". Oncogene. 23 (55): 8887–99. doi:10.1038/sj.onc.1208107. PMID 15467743. S2CID 30045920.
  • Rampalli S, Pavithra L, Bhatt A, Kundu TK, Chattopadhyay S (Oct 2005). "Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex". Molecular and Cellular Biology. 25 (19): 8415–29. doi:10.1128/MCB.25.19.8415-8429.2005. PMC 1265755. PMID 16166625.
  • Xu Y, Sengupta PK, Seto E, Smith BD (Apr 2006). "Regulatory factor for X-box family proteins differentially interact with histone deacetylases to repress collagen alpha2(I) gene (COL1A2) expression". The Journal of Biological Chemistry. 281 (14): 9260–70. doi:10.1074/jbc.M511724200. PMC 1434794. PMID 16464847.
  • v
  • t
  • e
  • 1e91: STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS
    1e91: STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS
  • 1pd7: Extended SID of Mad1 bound to the PAH2 domain of mSin3B
    1pd7: Extended SID of Mad1 bound to the PAH2 domain of mSin3B
  • 2cr7: Solution structure of the first PAH domain of the mouse transcriptional repressor SIN3B
    2cr7: Solution structure of the first PAH domain of the mouse transcriptional repressor SIN3B
  • 2czy: Solution structure of the NRSF/REST-mSin3B PAH1 complex
    2czy: Solution structure of the NRSF/REST-mSin3B PAH1 complex
  • 2f05: Solution structure of free PAH2 domain of mSin3B
    2f05: Solution structure of free PAH2 domain of mSin3B

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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Coactivators
Corepressors
ATP-dependent remodeling factors
  • Chromatin Structure Remodeling (RSC) Complex
  • SWI/SNF


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