SIN3B_HUMAN
ID SIN3B_HUMAN Reviewed; 1162 AA.
AC O75182; Q2NL91; Q68GC2; Q6P4B8; Q8TB34; Q9BSC8;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Paired amphipathic helix protein Sin3b;
DE AltName: Full=Histone deacetylase complex subunit Sin3b;
DE AltName: Full=Transcriptional corepressor Sin3b;
GN Name=SIN3B {ECO:0000312|HGNC:HGNC:19354}; Synonyms=KIAA0700;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAU01916.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ali M., Batra H., Saluja D.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAU01916.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH05113.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 743-1162 (ISOFORMS 1/2).
RC TISSUE=Duodenum {ECO:0000312|EMBL:AAH63531.1},
RC Lung {ECO:0000312|EMBL:AAH05113.1}, Lymph, and
RC Skin {ECO:0000312|EMBL:AAH25026.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP INTERACTION WITH HCFC1.
RX PubMed=12670868; DOI=10.1101/gad.252103;
RA Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT methyltransferase are tethered together selectively by the cell-
RT proliferation factor HCF-1.";
RL Genes Dev. 17:896-911(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP INTERACTION WITH C6ORF89.
RC TISSUE=Adipocyte;
RX PubMed=23460338; DOI=10.1002/jcp.24355;
RA Lalioti V.S., Vergarajauregui S., Villasante A., Pulido D., Sandoval I.V.;
RT "C6orf89 encodes three distinct HDAC enhancers that function in the
RT nucleolus, the Golgi and the midbody.";
RL J. Cell. Physiol. 228:1907-1921(2013).
CC -!- FUNCTION: Acts as a transcriptional repressor. Interacts with MXI1 to
CC repress MYC responsive genes and antagonize MYC oncogenic activities.
CC Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer
CC then represses transcription by tethering SIN3B to DNA. Also forms a
CC complex with FOXK1 which represses transcription. With FOXK1, regulates
CC cell cycle progression probably by repressing cell cycle inhibitor
CC genes expression. {ECO:0000250|UniProtKB:Q62141}.
CC -!- SUBUNIT: Interacts with FOXK1/MNF, MXI, MAD, NCOR1 and SAP30.
CC Interaction with SUDS3 enhances the interaction with HDAC1 to form a
CC complex. Interacts with CRY1, HCFC1, MAD3, MAD4, MAEL, REST, RNF220 and
CC SETDB1. Interacts with C6orf89 (PubMed:23460338). Interacts with MYT1L
CC (By similarity). {ECO:0000250|UniProtKB:Q62141,
CC ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:23460338}.
CC -!- INTERACTION:
CC O75182; P01106: MYC; NbExp=7; IntAct=EBI-540462, EBI-447544;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=O75182-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9734811};
CC IsoId=O75182-2; Sequence=VSP_014186;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=O75182-3; Sequence=VSP_014185;
CC -!- PTM: Ubiquitinated by RNF220 that leads to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31675.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY706204; AAU01916.1; -; mRNA.
DR EMBL; AB014600; BAA31675.2; ALT_INIT; mRNA.
DR EMBL; CH471106; EAW84565.1; -; Genomic_DNA.
DR EMBL; BC005113; AAH05113.1; -; mRNA.
DR EMBL; BC025026; AAH25026.1; -; mRNA.
DR EMBL; BC063531; AAH63531.1; -; mRNA.
DR EMBL; BC110821; AAI10822.1; -; mRNA.
DR CCDS; CCDS32946.1; -. [O75182-1]
DR CCDS; CCDS74308.1; -. [O75182-2]
DR RefSeq; NP_001284524.1; NM_001297595.1. [O75182-2]
DR RefSeq; NP_001284526.1; NM_001297597.1.
DR RefSeq; NP_056075.1; NM_015260.3. [O75182-1]
DR AlphaFoldDB; O75182; -.
DR SMR; O75182; -.
DR BioGRID; 116901; 127.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR CORUM; O75182; -.
DR IntAct; O75182; 40.
DR MINT; O75182; -.
DR STRING; 9606.ENSP00000369131; -.
DR iPTMnet; O75182; -.
DR PhosphoSitePlus; O75182; -.
DR BioMuta; SIN3B; -.
DR EPD; O75182; -.
DR jPOST; O75182; -.
DR MassIVE; O75182; -.
DR MaxQB; O75182; -.
DR PaxDb; O75182; -.
DR PeptideAtlas; O75182; -.
DR PRIDE; O75182; -.
DR ProteomicsDB; 49855; -. [O75182-1]
DR ProteomicsDB; 49856; -. [O75182-2]
DR ProteomicsDB; 49857; -. [O75182-3]
DR Antibodypedia; 27459; 245 antibodies from 26 providers.
DR DNASU; 23309; -.
DR Ensembl; ENST00000248054.10; ENSP00000248054.4; ENSG00000127511.10. [O75182-2]
DR Ensembl; ENST00000379803.5; ENSP00000369131.1; ENSG00000127511.10. [O75182-1]
DR Ensembl; ENST00000596802.5; ENSP00000473039.1; ENSG00000127511.10. [O75182-3]
DR GeneID; 23309; -.
DR KEGG; hsa:23309; -.
DR MANE-Select; ENST00000248054.10; ENSP00000248054.4; NM_001297595.2; NP_001284524.1. [O75182-2]
DR UCSC; uc002new.4; human. [O75182-1]
DR CTD; 23309; -.
DR DisGeNET; 23309; -.
DR GeneCards; SIN3B; -.
DR HGNC; HGNC:19354; SIN3B.
DR HPA; ENSG00000127511; Low tissue specificity.
DR MIM; 607777; gene.
DR neXtProt; NX_O75182; -.
DR OpenTargets; ENSG00000127511; -.
DR Orphanet; 500166; SIN3A-related intellectual disability syndrome due to a point mutation.
DR PharmGKB; PA134909030; -.
DR VEuPathDB; HostDB:ENSG00000127511; -.
DR eggNOG; KOG4204; Eukaryota.
DR GeneTree; ENSGT00940000159560; -.
DR HOGENOM; CLU_001360_0_1_1; -.
DR InParanoid; O75182; -.
DR OMA; MRWFFGT; -.
DR OrthoDB; 253485at2759; -.
DR PhylomeDB; O75182; -.
DR TreeFam; TF106187; -.
DR PathwayCommons; O75182; -.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha. [O75182-1]
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1. [O75182-1]
DR SignaLink; O75182; -.
DR SIGNOR; O75182; -.
DR BioGRID-ORCS; 23309; 42 hits in 1087 CRISPR screens.
DR ChiTaRS; SIN3B; human.
DR GeneWiki; SIN3B; -.
DR GenomeRNAi; 23309; -.
DR Pharos; O75182; Tbio.
DR PRO; PR:O75182; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75182; protein.
DR Bgee; ENSG00000127511; Expressed in body of uterus and 174 other tissues.
DR ExpressionAtlas; O75182; baseline and differential.
DR Genevisible; O75182; HS.
DR GO; GO:0030849; C:autosome; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; IBA:GO_Central.
DR GO; GO:0000805; C:X chromosome; IEA:Ensembl.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0000806; C:Y chromosome; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.1160.11; -; 3.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR PANTHER; PTHR12346; PTHR12346; 1.
DR Pfam; PF02671; PAH; 3.
DR Pfam; PF08295; Sin3_corepress; 2.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 3.
DR PROSITE; PS51477; PAH; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1162
FT /note="Paired amphipathic helix protein Sin3b"
FT /id="PRO_0000121539"
FT DOMAIN 37..107
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 153..238
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 292..369
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 1..308
FT /note="Interaction with CRY1"
FT /evidence="ECO:0000250"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..105
FT /note="Interaction with REST"
FT /evidence="ECO:0000250"
FT REGION 246..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..540
FT /note="Interaction with NCOR1"
FT /evidence="ECO:0000250|UniProtKB:Q62141"
FT REGION 392..591
FT /note="Interaction with SUDS3 and HDAC1"
FT /evidence="ECO:0000250"
FT REGION 706..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62141"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62141"
FT VAR_SEQ 354..1162
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014185"
FT VAR_SEQ 423..454
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_014186"
SQ SEQUENCE 1162 AA; 133066 MW; 03D3B24AF1CF40B6 CRC64;
MAHAGGGSGG SGAGGPAGRG LSGARWGRSG SAGHEKLPVH VEDALTYLDQ VKIRFGSDPA
TYNGFLEIMK EFKSQSIDTP GVIRRVSQLF HEHPDLIVGF NAFLPLGYRI DIPKNGKLNI
QSPLTSQENS HNHGDGAEDF KQQVPYKEDK PQVPLESDSV EFNNAISYVN KIKTRFLDHP
EIYRSFLEIL HTYQKEQLNT RGRPFRGMSE EEVFTEVANL FRGQEDLLSE FGQFLPEAKR
SLFTGNGPCE MHSVQKNEHD KTPEHSRKRS RPSLLRPVSA PAKKKMKLRG TKDLSIAAVG
KYGTLQEFSF FDKVRRVLKS QEVYENFLRC IALFNQELVS GSELLQLVSP FLGKFPELFA
QFKSFLGVKE LSFAPPMSDR SGDGISREID YASCKRIGSS YRALPKTYQQ PKCSGRTAIC
KELDHWTLLQ GSWTDDYCMS KFKNTCWIPG YSAGVLNDTW VSFPSWSEDS TFVSSKKTPY
EEQLHRCEDE RFELDVVLET NLATIRVLES VQKKLSRMAP EDQEKFRLDD SLGGTSEVIQ
RRAIYRIYGD KAPEIIESLK KNPVTAVPVV LKRLKAKEEE WREAQQGFNK IWREQYEKAY
LKSLDHQAVN FKQNDTKALR SKSLLNEIES VYDEHQEQHS EGRSAPSSEP HLIFVYEDRQ
ILEDAAALIS YYVKRQPAIQ KEDQGTIHQL LHQFVPSLFF SQQLDLGASE ESADEDRDSP
QGQTTDPSER KKPAPGPHSS PPEEKGAFGD APATEQPPLP PPAPHKPLDD VYSLFFANNN
WYFFLRLHQT LCSRLLKIYR QAQKQLLEYR TEKEREKLLC EGRREKGSDP AMELRLKQPS
EVELEEYYPA FLDMVRSLLE GSIDPTQYED TLREMFTIHA YVGFTMDKLV QNIARQLHHL
VSDDVCLKVV ELYLNEKKRG AAGGNLSSRC VRAARETSYQ WKAERCMADE NCFKVMFLQR
KGQVIMTIEL LDTEEAQTED PVEVQHLARY VEQYVGTEGA SSSPTEGFLL KPVFLQRNLK
KFRRRWQSEQ ARALRGEARS SWKRLVGVES ACDVDCRFKL STHKMVFIVN SEDYMYRRGT
LCRAKQVQPL VLLRHHQHFE EWHSRWLEDN VTVEAASLVQ DWLMGEEDED MVPCKTLCET
VHVHGLPVTR YRVQYSRRPA SP
