Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Paired amphipathic helix protein Sin3a (Histone deacetylase complex subunit Sin3a) (Transcriptional corepressor Sin3a)

 SIN3A_HUMAN             Reviewed;        1273 AA.
Q96ST3; B2RNS5; Q8N8N4; Q8NC83; Q8WV18; Q96L98; Q9UFQ1;
24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
24-OCT-2003, sequence version 2.
22-NOV-2017, entry version 165.
RecName: Full=Paired amphipathic helix protein Sin3a;
AltName: Full=Histone deacetylase complex subunit Sin3a;
AltName: Full=Transcriptional corepressor Sin3a;
Name=SIN3A {ECO:0000312|HGNC:HGNC:19353};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAP97288.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Guo J.H., Yu L.;
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000305, ECO:0000312|EMBL:AAH18973.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Uterus {ECO:0000312|EMBL:AAH18973.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1026.
TISSUE=Brain, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4] {ECO:0000305, ECO:0000312|EMBL:AAP97288.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-620.
Bu X., Fu Y., Jiang S., Avraham S., Avraham H.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 913-1273.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6] {ECO:0000305}
INTERACTION WITH SFPQ.
PubMed=11259580; DOI=10.1128/MCB.21.7.2298-2311.2001;
Mathur M., Tucker P.W., Samuels H.H.;
"PSF is a novel corepressor that mediates its effect through Sin3A and
the DNA binding domain of nuclear hormone receptors.";
Mol. Cell. Biol. 21:2298-2311(2001).
[7]
INTERACTION WITH OGT, AND FUNCTION.
PubMed=12150998; DOI=10.1016/S0092-8674(02)00810-3;
Yang X., Zhang F., Kudlow J.E.;
"Recruitment of O-GlcNAc transferase to promoters by corepressor
mSin3A: coupling protein O-GlcNAcylation to transcriptional
repression.";
Cell 110:69-80(2002).
[8] {ECO:0000305}
INTERACTION WITH SFPQ.
PubMed=11897684; DOI=10.1210/endo.143.4.8748;
Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N.,
Waterman M.R.;
"Transcriptional activation of human CYP17 in H295R adrenocortical
cells depends on complex formation among p54(nrb)/NonO, protein-
associated splicing factor, and SF-1, a complex that also participates
in repression of transcription.";
Endocrinology 143:1280-1290(2002).
[9] {ECO:0000305}
INTERACTION WITH DACH1.
PubMed=14525983; DOI=10.1074/jbc.M310021200;
Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K.,
Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.;
"DACH1 inhibits transforming growth factor-beta signaling through
binding Smad4.";
J. Biol. Chem. 278:51673-51684(2003).
[10] {ECO:0000305}
INTERACTION WITH HCFC1.
PubMed=12670868; DOI=10.1101/gad.252103;
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
methyltransferase are tethered together selectively by the cell-
proliferation factor HCF-1.";
Genes Dev. 17:896-911(2003).
[11]
INTERACTION WITH SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
PubMed=12724404; DOI=10.1128/MCB.23.10.3456-3467.2003;
Fleischer T.C., Yun U.J., Ayer D.E.;
"Identification and characterization of three new components of the
mSin3A corepressor complex.";
Mol. Cell. Biol. 23:3456-3467(2003).
[12]
INTERACTION WITH BRMS1L.
PubMed=15451426; DOI=10.1016/j.bbrc.2004.08.227;
Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.;
"Identification of a novel BRMS1-homologue protein p40 as a component
of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex.";
Biochem. Biophys. Res. Commun. 323:1216-1222(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
SUBCELLULAR LOCATION, AND INTERACTION WITH SAP30L.
PubMed=16820529; DOI=10.1093/nar/gkl401;
Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K.,
Peterson P., Maeki M., Kainulainen H., Lohi O.;
"SAP30L interacts with members of the Sin3A corepressor complex and
targets Sin3A to the nucleolus.";
Nucleic Acids Res. 34:3288-3298(2006).
[15]
INTERACTION WITH PPHLN1.
PubMed=17963697; DOI=10.1016/j.bbrc.2007.10.090;
Kurita M., Suzuki H., Kawano Y., Aiso S., Matsuoka M.;
"CR/periphilin is a transcriptional co-repressor involved in cell
cycle progression.";
Biochem. Biophys. Res. Commun. 364:930-936(2007).
[16]
INTERACTION WITH TOPORS, SUMOYLATION BY TOPORS, AND DESUMOYLATION BY
SENP2.
PubMed=17803295; DOI=10.1021/pr0703674;
Pungaliya P., Kulkarni D., Park H.J., Marshall H., Zheng H.,
Lackland H., Saleem A., Rubin E.H.;
"TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying
proteins.";
J. Proteome Res. 6:3918-3923(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-277; SER-832;
SER-940 AND SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 AND SER-1112, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-469, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832; SER-860; SER-940
AND SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
INTERACTION WITH TET1.
PubMed=21490601; DOI=10.1038/nature10066;
Williams K., Christensen J., Pedersen M.T., Johansen J.V., Cloos P.A.,
Rappsilber J., Helin K.;
"TET1 and hydroxymethylcytosine in transcription and DNA methylation
fidelity.";
Nature 473:343-348(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 AND SER-860, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-832; SER-940 AND
SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1089, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122; LYS-134 AND LYS-563,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Acts as a transcriptional repressor. Corepressor for
REST. Interacts with MXI1 to repress MYC responsive genes and
antagonize MYC oncogenic activities. Also interacts with MXD1-MAX
heterodimers to repress transcription by tethering SIN3A to DNA.
Acts cooperatively with OGT to repress transcription in parallel
with histone deacetylation. Involved in he control of the
circadian rhythms. Required for the transcriptional repression of
circadian target genes, such as PER1, mediated by the large PER
complex through histone deacetylation. Cooperates with FOXK1 to
regulate cell cycle progression probably by repressing cell cycle
inhibitor genes expression (By similarity).
{ECO:0000250|UniProtKB:Q60520, ECO:0000269|PubMed:12150998}.
-!- SUBUNIT: Interacts with ARID4B, BRMS1L, HCFC1, HDAC1, HDAC2, MXI1,
SAP30L, SAP130, SFPQ and TOPORS. Interacts with OGT (via TPRs 1-
6); the interaction mediates transcriptional repression in
parallel with histone deacetylase (By similarity). Interacts with
BAZ2A, MXD3, MXD4, MBD2, DACH1, NCOR1, NR4A2, REST, RLIM, SAP30,
SETDB1, SMYD2, and SUDS3. Interacts with PHF12 in a complex
composed of HDAC1, PHF12 and SAP30. Interacts with TET1; the
interaction recruits SIN3A to gene promoters. The large PER
complex involved in the histone deacetylation is composed of at
least HDAC1, PER2, SFPQ and SIN3A. Interacts with KLF11 (By
similarity). Interacts with PPHLN1 (PubMed:17963697). Found in a
complex with YY1, GON4L and HDAC1 (By similarity). Interacts (via
PAH2) with FOXK1 (By similarity). Found in a complex composed of
at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1.
Interacts with SINHCAF (By similarity).
{ECO:0000250|UniProtKB:Q60520, ECO:0000269|PubMed:11259580,
ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:12150998,
ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:12724404,
ECO:0000269|PubMed:14525983, ECO:0000269|PubMed:15451426,
ECO:0000269|PubMed:16820529, ECO:0000269|PubMed:17803295,
ECO:0000269|PubMed:17963697, ECO:0000269|PubMed:21490601}.
-!- INTERACTION:
Q7L2E3:DHX30; NbExp=3; IntAct=EBI-347218, EBI-1211456;
P51610:HCFC1; NbExp=6; IntAct=EBI-347218, EBI-396176;
Q13547:HDAC1; NbExp=7; IntAct=EBI-347218, EBI-301834;
Q92769:HDAC2; NbExp=5; IntAct=EBI-347218, EBI-301821;
Q9Y4K0:LOXL2; NbExp=2; IntAct=EBI-347218, EBI-7172227;
P51608:MECP2; NbExp=2; IntAct=EBI-347218, EBI-1189067;
Q9Y5X4:NR2E3; NbExp=2; IntAct=EBI-347218, EBI-7216962;
Q9UQ80:PA2G4; NbExp=4; IntAct=EBI-347218, EBI-924893;
Q16576:RBBP7; NbExp=2; IntAct=EBI-347218, EBI-352227;
P23246:SFPQ; NbExp=2; IntAct=EBI-347218, EBI-355453;
P12755:SKI; NbExp=3; IntAct=EBI-347218, EBI-347281;
P04637:TP53; NbExp=2; IntAct=EBI-347218, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00810, ECO:0000269|PubMed:16820529}. Nucleus, nucleolus
{ECO:0000269|PubMed:16820529}. Note=Recruited to the nucleolus by
SAP30L.
-!- PTM: SUMO1 sumoylated by TOPORS. Probably desumoylated by SENP2.
{ECO:0000269|PubMed:17803295}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF418569; AAP97288.1; -; mRNA.
EMBL; BC018973; AAH18973.1; -; mRNA.
EMBL; BC137098; AAI37099.1; -; mRNA.
EMBL; BC137099; AAI37100.1; -; mRNA.
EMBL; AK027559; BAB55197.1; -; mRNA.
EMBL; AK074903; BAC11280.1; -; mRNA.
EMBL; AK096477; BAC04801.1; -; mRNA.
EMBL; AY044430; AAK95854.1; -; mRNA.
EMBL; AL117513; CAB55972.1; -; mRNA.
CCDS; CCDS10279.1; -.
PIR; T17282; T17282.
RefSeq; NP_001138829.1; NM_001145357.1.
RefSeq; NP_001138830.1; NM_001145358.1.
RefSeq; NP_056292.1; NM_015477.2.
RefSeq; XP_006720528.1; XM_006720465.3.
RefSeq; XP_006720529.1; XM_006720466.3.
RefSeq; XP_006720530.1; XM_006720467.3.
UniGene; Hs.513039; -.
PDB; 1PO4; Model; -; B=295-383.
PDBsum; 1PO4; -.
ProteinModelPortal; Q96ST3; -.
SMR; Q96ST3; -.
BioGrid; 117439; 212.
CORUM; Q96ST3; -.
DIP; DIP-31515N; -.
IntAct; Q96ST3; 55.
MINT; MINT-2815493; -.
STRING; 9606.ENSP00000353622; -.
iPTMnet; Q96ST3; -.
PhosphoSitePlus; Q96ST3; -.
BioMuta; SIN3A; -.
DMDM; 37999759; -.
EPD; Q96ST3; -.
MaxQB; Q96ST3; -.
PaxDb; Q96ST3; -.
PeptideAtlas; Q96ST3; -.
PRIDE; Q96ST3; -.
Ensembl; ENST00000360439; ENSP00000353622; ENSG00000169375.
Ensembl; ENST00000394947; ENSP00000378402; ENSG00000169375.
Ensembl; ENST00000394949; ENSP00000378403; ENSG00000169375.
GeneID; 25942; -.
KEGG; hsa:25942; -.
UCSC; uc002bai.4; human.
CTD; 25942; -.
DisGeNET; 25942; -.
EuPathDB; HostDB:ENSG00000169375.15; -.
GeneCards; SIN3A; -.
H-InvDB; HIX0012443; -.
H-InvDB; HIX0019634; -.
H-InvDB; HIX0172841; -.
HGNC; HGNC:19353; SIN3A.
HPA; CAB004506; -.
HPA; HPA047213; -.
HPA; HPA062123; -.
MalaCards; SIN3A; -.
MIM; 607776; gene.
neXtProt; NX_Q96ST3; -.
OpenTargets; ENSG00000169375; -.
PharmGKB; PA134993567; -.
eggNOG; KOG4204; Eukaryota.
eggNOG; COG5602; LUCA.
GeneTree; ENSGT00390000007239; -.
HOVERGEN; HBG060425; -.
InParanoid; Q96ST3; -.
KO; K11644; -.
OMA; KPCSGRD; -.
OrthoDB; EOG091G03HY; -.
PhylomeDB; Q96ST3; -.
TreeFam; TF106187; -.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; Q96ST3; -.
ChiTaRS; SIN3A; human.
GeneWiki; SIN3A; -.
GenomeRNAi; 25942; -.
PRO; PR:Q96ST3; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000169375; -.
CleanEx; HS_SIN3A; -.
ExpressionAtlas; Q96ST3; baseline and differential.
Genevisible; Q96ST3; HS.
GO; GO:0000776; C:kinetochore; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0033558; F:protein deacetylase activity; IMP:BHF-UCL.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IEA:Ensembl.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; IMP:BHF-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0006260; P:DNA replication; IEA:Ensembl.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:1901675; P:negative regulation of histone H3-K27 acetylation; IMP:BHF-UCL.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0031937; P:positive regulation of chromatin silencing; IMP:BHF-UCL.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:BHF-UCL.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0006476; P:protein deacetylation; IMP:BHF-UCL.
GO; GO:0010817; P:regulation of hormone levels; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:Ensembl.
GO; GO:0051595; P:response to methylglyoxal; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR013194; HDAC_interact_dom.
InterPro; IPR003822; PAH.
InterPro; IPR036600; PAH_sf.
InterPro; IPR031693; Sin3_C.
Pfam; PF02671; PAH; 3.
Pfam; PF08295; Sin3_corepress; 1.
Pfam; PF16879; Sin3a_C; 1.
SMART; SM00761; HDAC_interact; 1.
SUPFAM; SSF47762; SSF47762; 3.
PROSITE; PS51477; PAH; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Biological rhythms; Coiled coil;
Complete proteome; Isopeptide bond; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 1273 Paired amphipathic helix protein Sin3a.
/FTId=PRO_0000121537.
DOMAIN 119 189 PAH 1. {ECO:0000255|PROSITE-
ProRule:PRU00810}.
DOMAIN 300 383 PAH 2. {ECO:0000255|PROSITE-
ProRule:PRU00810}.
DOMAIN 456 525 PAH 3. {ECO:0000255|PROSITE-
ProRule:PRU00810}.
REGION 119 196 Interaction with HCFC1.
{ECO:0000269|PubMed:12670868}.
REGION 205 480 Interaction with REST. {ECO:0000250}.
REGION 458 525 Interaction with SAP30.
{ECO:0000250|UniProtKB:Q60520}.
REGION 523 850 Interaction with NCOR1.
{ECO:0000250|UniProtKB:Q60520}.
REGION 524 659 Interaction with SUDS3 and SAP130.
{ECO:0000269|PubMed:12724404}.
REGION 687 829 Interaction with HDAC1 and ARID4B.
{ECO:0000269|PubMed:12724404}.
REGION 888 967 Interaction with OGT.
{ECO:0000269|PubMed:12150998}.
COILED 903 932 {ECO:0000255}.
COMPBIAS 218 285 Pro-rich.
COMPBIAS 835 841 Poly-Glu.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 284 284 Phosphothreonine.
{ECO:0000250|UniProtKB:Q60520}.
MOD_RES 469 469 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 832 832 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 860 860 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 865 865 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q60520}.
MOD_RES 875 875 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q60520}.
MOD_RES 940 940 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1089 1089 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1112 1112 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 134 134 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 563 563 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 1156 1156 M -> L (in dbSNP:rs60213317).
/FTId=VAR_062129.
CONFLICT 163 163 G -> R (in Ref. 4; AAK95854).
{ECO:0000305}.
CONFLICT 170 177 QLFKGHPD -> HYSKGPPI (in Ref. 4;
AAK95854). {ECO:0000305}.
CONFLICT 182 192 FNTFLPPGYKI -> IQHLFAPWATKM (in Ref. 4;
AAK95854). {ECO:0000305}.
CONFLICT 216 216 I -> T (in Ref. 3; BAC04801).
{ECO:0000305}.
CONFLICT 386 386 S -> F (in Ref. 4; AAK95854).
{ECO:0000305}.
CONFLICT 536 536 E -> D (in Ref. 4; AAK95854).
{ECO:0000305}.
CONFLICT 562 562 P -> G (in Ref. 4; AAK95854).
{ECO:0000305}.
CONFLICT 575 576 PL -> GV (in Ref. 4; AAK95854).
{ECO:0000305}.
CONFLICT 595 595 S -> C (in Ref. 4; AAK95854).
{ECO:0000305}.
CONFLICT 618 620 ELD -> DLM (in Ref. 4; AAK95854).
{ECO:0000305}.
CONFLICT 1009 1009 Q -> R (in Ref. 3; BAC11280).
{ECO:0000305}.
CONFLICT 1247 1248 TT -> NN (in Ref. 1; AAP97288).
{ECO:0000305}.
SEQUENCE 1273 AA; 145175 MW; E6A329BE0EAD84CD CRC64;
MKRRLDDQES PVYAAQQRRI PGSTEAFPHQ HRVLAPAPPV YEAVSETMQS ATGIQYSVTP
SYQVSAMPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ SHAHPAPPVA PVQGQQQFQR
LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI MKEFKSQSID TPGVISRVSQ LFKGHPDLIM
GFNTFLPPGY KIEVQTNDMV NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SAQSAPAPAQ
PAPQPPPAKV SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ
PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT PALTEQEVYA
QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV RNDHGGTVKK PQLNNKPQRP
SQNGCQIRRH PTGTTPPVKK KPKLLNLKDS SMADASKHGG GTESLFFDKV RKALRSAEAY
ENFLRCLVIF NQEVISRAEL VQLVSPFLGK FPELFNWFKN FLGYKESVHL ETYPKERATE
GIAMEIDYAS CKRLGSSYRA LPKSYQQPKC TGRTPLCKEV LNDTWVSFPS WSEDSTFVSS
KKTQYEEHIY RCEDERFELD VVLETNLATI RVLEAIQKKL SRLSAEEQAK FRLDNTLGGT
SEVIHRKALQ RIYADKAADI IDGLRKNPSI AVPIVLKRLK MKEEEWREAQ RGFNKVWREQ
NEKYYLKSLD HQGINFKQND TKVLRSKSLL NEIESIYDER QEQATEENAG VPVGPHLSLA
YEDKQILEDA AALIIHHVKR QTGIQKEDKY KIKQIMHHFI PDLLFAQRGD LSDVEEEEEE
EMDVDEATGA VKKHNGVGGS PPKSKLLFSN TAAQKLRGMD EVYNLFYVNN NWYIFMRLHQ
ILCLRLLRIC SQAERQIEEE NREREWEREV LGIKRDKSDS PAIQLRLKEP MDVDVEDYYP
AFLDMVRSLL DGNIDSSQYE DSLREMFTIH AYIAFTMDKL IQSIVRQLQH IVSDEICVQV
TDLYLAENNN GATGGQLNTQ NSRSLLESTY QRKAEQLMSD ENCFKLMFIQ SQGQVQLTIE
LLDTEEENSD DPVEAERWSD YVERYMNSDT TSPELREHLA QKPVFLPRNL RRIRKCQRGR
EQQEKEGKEG NSKKTMENVD SLDKLECRFK LNSYKMVYVI KSEDYMYRRT ALLRAHQSHE
RVSKRLHQRF QAWVDKWTKE HVPREMAAET SKWLMGEGLE GLVPCTTTCD TETLHFVSIN
KYRVKYGTVF KAP


Related products :

Catalog number Product name Quantity
EIAAB38491 Histone deacetylase complex subunit Sin3a,Homo sapiens,Human,Paired amphipathic helix protein Sin3a,SIN3A,Transcriptional corepressor Sin3a
EIAAB38490 Histone deacetylase complex subunit Sin3a,Kiaa4126,Mouse,Mus musculus,Paired amphipathic helix protein Sin3a,Sin3a,Transcriptional corepressor Sin3a
CSB-EL021327MO Mouse Paired amphipathic helix protein Sin3a(SIN3A) ELISA kit 96T
CSB-EL021327HU Human Paired amphipathic helix protein Sin3a(SIN3A) ELISA kit 96T
CSB-EL021327HU Human Paired amphipathic helix protein Sin3a(SIN3A) ELISA kit SpeciesHuman 96T
CSB-EL021327MO Mouse Paired amphipathic helix protein Sin3a(SIN3A) ELISA kit SpeciesMouse 96T
SIN3A_MOUSE ELISA Kit FOR Paired amphipathic helix protein Sin3a; organism: Mouse; gene name: Sin3a 96T
25-070 SIN3A is a transcriptional regulatory protein. It contains paired amphipathic helix (PAH) domains, which are important for protein-protein interactions and may mediate repression by the Mad-Max comple 0.05 mg
EIAAB38493 Histone deacetylase complex subunit Sin3b,Kiaa0700,Mouse,Mus musculus,Paired amphipathic helix protein Sin3b,Sin3b,Transcriptional corepressor Sin3b
EIAAB38492 Histone deacetylase complex subunit Sin3b,Homo sapiens,Human,KIAA0700,Paired amphipathic helix protein Sin3b,SIN3B,Transcriptional corepressor Sin3b
A1577 SIN3A Primary Antibody, SIN3A, Species: Human Recombinant Protein Source: Rabbit Polyclonal 50ug
SIN3A SIN3A Gene SIN3 homolog A, transcription regulator (yeast)
26-527 PHF12 acts as a transcriptional repressor. It is involved in recruitment of functional SIN3A complexes to DNA. PHF12 represses transcription at least in part through the activity of an associated hist 0.05 mg
RPR-707 Recombinant Human Sin3A-Associated Protein, 18kDa 5
pro-707 Recombinant Human Sin3A-Associated Protein, 18kDa 1mg
pro-707 Recombinant Human Sin3A-Associated Protein, 18kDa 5
H00025942-Q01-25 SIN3A (Human) Recombinant Protein (Q01) 25 ug
pro-707 Recombinant Human Sin3A-Associated Protein, 18kDa 20
228-11398-3 Recombinant Human Sin3A-Associated Protein, 18kDa 1 mg
228-11398-1 Recombinant Human Sin3A-Associated Protein, 18kDa 5
228-11398-2 Recombinant Human Sin3A-Associated Protein, 18kDa 20
pro-707 Recombinant Human Sin3A-Associated Protein, 18kDa SAP18 1mg
7-06316 Recombinant Human Sin3A-Associated Protein, 18kDa 2
Y052424 Anti-SAP30L (Sin3A associated protein p30-like) Antibody 100 μg
201-20-5099 SAP130{Sin3A-associated protein, 130kDa}rabbit.pAb 0.2ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur