SIN3B

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SIN3B
Protein SIN3B PDB 1e91.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSIN3B, Paired amphipathic helix protein Sin3b, SIN3 transcription regulator family member B
External IDsMGI: 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
Band19p13.11Start16,829,400 bp[1]
End16,880,353 bp[1]
RNA expression pattern
PBB GE SIN3B 209352 s at fs.png

PBB GE SIN3B 39705 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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: 72.72 – 72.76 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[edit]

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[edit]

References[edit]

  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:".
  4. ^ "Mouse PubMed Reference:".
  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.
  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[edit]

External links[edit]

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