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_MOUSE             Reviewed;        1274 AA.
Q60520; Q570Z7; Q60820; Q62139; Q62140; Q7TPU8; Q7TSZ2;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
23-MAY-2018, entry version 178.
RecName: Full=Paired amphipathic helix protein Sin3a;
AltName: Full=Histone deacetylase complex subunit Sin3a;
AltName: Full=Transcriptional corepressor Sin3a;
Name=Sin3a; Synonyms=Kiaa4126;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=129; TISSUE=Teratocarcinoma;
PubMed=7601471; DOI=10.1016/0888-7543(95)80229-F;
Halleck M.S., Pownall S., Harder K.W., Duncan A.M.V., Jirik F.R.,
Schlegel R.A.;
"A widely distributed putative mammalian transcriptional regulator
containing multiple paired amphipathic helices, with similarity to
yeast SIN3.";
Genomics 26:403-406(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
MXI1.
STRAIN=ICR; TISSUE=Brain;
PubMed=8649810;
Rao G., Alland L., Guida P., Schreiber-Agus N., Chin L., Chen K.,
Rochelle J.M., Seldin M.F., Skoultchi A.I., DePinho R.A.;
"Mouse Sin3A interacts with and can functionally substitute for the
amino-terminal repression of the Myc antagonist Mxi1.";
Oncogene 12:1165-1172(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreatic islet;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000305, ECO:0000312|EMBL:AAH52716.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-1146 (ISOFORM 1).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52716.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH52716.1}, and
Egg {ECO:0000312|EMBL:AAH53385.1};
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1216 (ISOFORM 1), FUNCTION, AND
INTERACTION WITH MXD1.
TISSUE=Embryo;
PubMed=7889570; DOI=10.1016/0092-8674(95)90355-0;
Ayer D.E., Lawrence Q.A., Eisenman R.N.;
"Mad-Max transcriptional repression is mediated by ternary complex
formation with mammalian homologs of yeast repressor Sin3.";
Cell 80:767-776(1995).
[6]
SEQUENCE REVISION TO C-TERMINUS.
Ayer D.E., Lawrence Q.A., Eisenman R.N.;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[7]
INTERACTION WITH MXD3 AND MXD4.
PubMed=8521822;
Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
Copeland N.G., Jenkins N.A., Eisenman R.N.;
"Mad3 and Mad4: novel Max-interacting transcriptional repressors that
suppress c-myc dependent transformation and are expressed during
neural and epidermal differentiation.";
EMBO J. 14:5646-5659(1995).
[8]
ERRATUM.
PubMed=8617250;
Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
Copeland N.G., Jenkins N.A., Eisenman R.N.;
EMBO J. 15:2030-2030(1996).
[9]
INTERACTION WITH NCOR1.
PubMed=9139820; DOI=10.1038/387043a0;
Heinzel T., Lavinsky R.M., Mullen T.-M., Soederstroem M.,
Laherty C.D., Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R.,
Seto E., Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G.;
"A complex containing N-CoR, mSin3 and histone deacetylase mediates
transcriptional repression.";
Nature 387:43-48(1997).
[10] {ECO:0000305}
INTERACTION WITH SAP30 AND NCOR1.
PubMed=9702189; DOI=10.1016/S1097-2765(00)80111-2;
Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K.,
Rosenfeld M.G., Ayer D.E., Eisenman R.N.;
"SAP30, a component of the mSin3 corepressor complex involved in N-
CoR-mediated repression by specific transcription factors.";
Mol. Cell 2:33-42(1998).
[11] {ECO:0000305}
INTERACTION WITH MBD2.
PubMed=10950960; DOI=10.1074/jbc.M005929200;
Boeke J., Ammerpohl O., Kegel S., Moehren U., Renkawitz R.;
"The minimal repression domain of MBD2b overlaps with the methyl-CpG-
binding domain and binds directly to Sin3A.";
J. Biol. Chem. 275:34963-34967(2000).
[12]
FUNCTION, AND INTERACTION WITH REST.
PubMed=10734093; DOI=10.1074/jbc.275.13.9461;
Grimes J.A., Nielsen S.J., Battaglioli E., Miska E.A., Speh J.C.,
Berry D.L., Atouf F., Holdener B.C., Mandel G., Kouzarides T.;
"The co-repressor mSin3A is a functional component of the REST-CoREST
repressor complex.";
J. Biol. Chem. 275:9461-9467(2000).
[13]
INTERACTION WITH PHF12.
PubMed=11390640; DOI=10.1128/MCB.21.13.4110-4118.2001;
Yochum G.S., Ayer D.E.;
"Pf1, a novel PHD zinc finger protein that links the TLE corepressor
to the mSin3A-histone deacetylase complex.";
Mol. Cell. Biol. 21:4110-4118(2001).
[14]
INTERACTION WITH BAZ2A.
PubMed=12198165; DOI=10.1093/emboj/cdf460;
Zhou Y., Santoro R., Grummt I.;
"The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal
gene promoter and represses RNA polymerase I transcription.";
EMBO J. 21:4632-4640(2002).
[15] {ECO:0000305}
INTERACTION WITH SUDS3.
PubMed=11909966; DOI=10.1128/MCB.22.8.2743-2750.2002;
Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C.,
Hou H. Jr., Chen K., DePinho R.A.;
"Identification of mammalian Sds3 as an integral component of the
Sin3/histone deacetylase corepressor complex.";
Mol. Cell. Biol. 22:2743-2750(2002).
[16]
INTERACTION WITH RLIM.
PubMed=11882901; DOI=10.1038/416099a;
Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M.,
Scheffner M., Bach I.;
"Ubiquitination-dependent cofactor exchange on LIM homeodomain
transcription factors.";
Nature 416:99-103(2002).
[17] {ECO:0000305}
INTERACTION WITH DACH1.
PubMed=12130660; DOI=10.1126/science.1073263;
Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.;
"Tissue-specific regulation of retinal and pituitary precursor cell
proliferation.";
Science 297:1180-1183(2002).
[18]
INTERACTION WITH SETDB1.
PubMed=12398767; DOI=10.1042/BJ20020854;
Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
"An ERG (ets-related gene)-associated histone methyltransferase
interacts with histone deacetylases 1/2 and transcription co-
repressors mSin3A/B.";
Biochem. J. 369:651-657(2003).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[20]
INTERACTION WITH KLF11.
PubMed=15774581; DOI=10.1073/pnas.0409177102;
Neve B., Fernandez-Zapico M.E., Ashkenazi-Katalan V., Dina C.,
Hamid Y.H., Joly E., Vaillant E., Benmezroua Y., Durand E.,
Bakaher N., Delannoy V., Vaxillaire M., Cook T., Dallinga-Thie G.M.,
Jansen H., Charles M.-A., Clement K., Galan P., Hercberg S.,
Helbecque N., Charpentier G., Prentki M., Hansen T., Pedersen O.,
Urrutia R., Melloul D., Froguel P.;
"Role of transcription factor KLF11 and its diabetes-associated gene
variants in pancreatic beta cell function.";
Proc. Natl. Acad. Sci. U.S.A. 102:4807-4812(2005).
[21]
INTERACTION WITH SMYD2.
PubMed=16805913; DOI=10.1186/1476-4598-5-26;
Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.;
"Identification and characterization of Smyd2: a split SET/MYND
domain-containing histone H3 lysine 36-specific methyltransferase that
interacts with the Sin3 histone deacetylase complex.";
Mol. Cancer 5:26-26(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[23]
INTERACTION WITH NR4A2.
PubMed=19144721; DOI=10.1242/dev.029769;
Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L.,
Burbach J.P., Smidt M.P.;
"Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation
through release of SMRT-mediated repression.";
Development 136:531-540(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; THR-284; SER-833
AND SER-1113, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[25]
IDENTIFICATION IN A COMPLEX WITH YY1; GON4L AND HDAC1, AND SUBCELLULAR
LOCATION.
PubMed=21454521; DOI=10.1074/jbc.M110.133603;
Lu P., Hankel I.L., Hostager B.S., Swartzendruber J.A., Friedman A.D.,
Brenton J.L., Rothman P.B., Colgan J.D.;
"The developmental regulator protein Gon4l associates with protein
YY1, co-repressor Sin3a, and histone deacetylase 1 and mediates
transcriptional repression.";
J. Biol. Chem. 286:18311-18319(2011).
[26]
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).
[27]
FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER
COMPLEX.
PubMed=21680841; DOI=10.1126/science.1196766;
Duong H.A., Robles M.S., Knutti D., Weitz C.J.;
"A molecular mechanism for circadian clock negative feedback.";
Science 332:1436-1439(2011).
[28]
FUNCTION, AND INTERACTION WITH FOXK1.
PubMed=22476904; DOI=10.1007/s11010-012-1302-2;
Shi X., Garry D.J.;
"Sin3 interacts with Foxk1 and regulates myogenic progenitors.";
Mol. Cell. Biochem. 366:251-258(2012).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-866 AND LYS-876, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[30]
IDENTIFICATION IN A COMPLEX WITH SINHCAF; HDAC1; SAP30; RBBP4; OGT AND
TET1, AND INTERACTION WITH SINHCAF AND HDAC1.
PubMed=28554894; DOI=10.15252/embj.201696307;
Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B.,
Das S., Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T.,
Jammula S., Hokamp K., O'Connor D.P., Pasini D., Cagney G.,
Bracken A.P.;
"Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells
required for self-renewal.";
EMBO J. 36:2216-2232(2017).
[31]
STRUCTURE BY NMR OF 295-383 IN COMPLEX WITH MXD1, AND MUTAGENESIS OF
ALA-307; ILE-308; ASN-309; VAL-311; LYS-326; LEU-329 AND LEU-332.
PubMed=11106735; DOI=10.1016/S0092-8674(00)00168-9;
Brubaker K., Cowley S.M., Huang K., Loo L., Yochum G.S., Ayer D.E.,
Eisenman R.N., Radhakrishnan I.;
"Solution structure of the interacting domains of the Mad-Sin3
complex: implications for recruitment of a chromatin-modifying
complex.";
Cell 103:655-665(2000).
-!- 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 the 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 (PubMed:22476904).
{ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:21680841,
ECO:0000269|PubMed:22476904, ECO:0000269|PubMed:7889570,
ECO:0000269|PubMed:8649810}.
-!- 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. Interacts
with PPHLN1 (By similarity). Found in a complex with YY1, GON4L
and HDAC1 (PubMed:21454521). Interacts (via PAH2) with FOXK1
(PubMed:22476904). Found in a complex composed of at least
SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1. Interacts with
SINHCAF (PubMed:28554894). {ECO:0000250|UniProtKB:Q96ST3,
ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:10950960,
ECO:0000269|PubMed:11106735, ECO:0000269|PubMed:11390640,
ECO:0000269|PubMed:11882901, ECO:0000269|PubMed:11909966,
ECO:0000269|PubMed:12130660, ECO:0000269|PubMed:12198165,
ECO:0000269|PubMed:12398767, ECO:0000269|PubMed:15774581,
ECO:0000269|PubMed:16805913, ECO:0000269|PubMed:19144721,
ECO:0000269|PubMed:21454521, ECO:0000269|PubMed:21490601,
ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22476904,
ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:7889570,
ECO:0000269|PubMed:8521822, ECO:0000269|PubMed:8649810,
ECO:0000269|PubMed:9139820, ECO:0000269|PubMed:9702189}.
-!- INTERACTION:
O09106:Hdac1; NbExp=9; IntAct=EBI-349034, EBI-301912;
P70288:Hdac2; NbExp=7; IntAct=EBI-349034, EBI-302251;
Q9Z2D6:Mecp2; NbExp=4; IntAct=EBI-349034, EBI-1188816;
Q1EHW4:Sap25; NbExp=4; IntAct=EBI-349034, EBI-937195;
O88574:Sap30; NbExp=6; IntAct=EBI-349034, EBI-593511;
P48432:Sox2; NbExp=3; IntAct=EBI-349034, EBI-2313612;
Q8BR65:Suds3; NbExp=4; IntAct=EBI-349034, EBI-591431;
Q3URK3:Tet1; NbExp=2; IntAct=EBI-349034, EBI-4291699;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454521}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96ST3}. Note=Recruited
to the nucleolus by SAP30L. {ECO:0000250|UniProtKB:Q96ST3,
ECO:0000269|PubMed:21454521}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q60520-2; Sequence=Displayed;
Name=2;
IsoId=Q60520-1; Sequence=VSP_039918;
-!- TISSUE SPECIFICITY: Widely expressed. Highest levels in testis,
lung and thymus.
-!- PTM: SUMO1 sumoylated by TOPORS. Probably desumoylated by SENP2.
{ECO:0000250|UniProtKB:Q96ST3}.
-!- SEQUENCE CAUTION:
Sequence=AAB01610.1; Type=Miscellaneous discrepancy; Note=The cDNA contains an internal 15bp tandem duplication.; Evidence={ECO:0000305};
Sequence=AAH52716.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to an internal deletion.; Evidence={ECO:0000305};
Sequence=AAH53385.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAD90217.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L36831; AAB01610.1; ALT_SEQ; mRNA.
EMBL; U22394; AAA89119.1; -; mRNA.
EMBL; AK220292; BAD90217.1; ALT_INIT; mRNA.
EMBL; BC052716; AAH52716.1; ALT_SEQ; mRNA.
EMBL; BC053385; AAH53385.1; ALT_SEQ; mRNA.
EMBL; L38620; AAA69773.2; -; mRNA.
EMBL; L38621; AAA69772.2; -; mRNA.
CCDS; CCDS23216.1; -. [Q60520-2]
CCDS; CCDS52805.1; -. [Q60520-1]
PIR; A56068; A56068.
PIR; I61713; I61713.
RefSeq; NP_001103820.1; NM_001110350.1. [Q60520-1]
RefSeq; NP_001103821.1; NM_001110351.1. [Q60520-2]
RefSeq; NP_035508.2; NM_011378.2. [Q60520-2]
RefSeq; XP_006510953.1; XM_006510890.3. [Q60520-1]
RefSeq; XP_006510954.1; XM_006510891.3. [Q60520-1]
RefSeq; XP_006510955.1; XM_006510892.3. [Q60520-1]
RefSeq; XP_006510956.1; XM_006510893.3. [Q60520-1]
RefSeq; XP_011240985.1; XM_011242683.2. [Q60520-1]
RefSeq; XP_011240986.1; XM_011242684.2. [Q60520-1]
RefSeq; XP_011240987.1; XM_011242685.2. [Q60520-1]
RefSeq; XP_011240988.1; XM_011242686.2. [Q60520-1]
RefSeq; XP_017168720.1; XM_017313231.1.
UniGene; Mm.15755; -.
PDB; 1G1E; NMR; -; B=295-383.
PDB; 1S5Q; NMR; -; B=295-383.
PDB; 1S5R; NMR; -; B=295-383.
PDB; 2L9S; NMR; -; B=295-385.
PDB; 2LD7; NMR; -; B=456-528.
PDB; 2N2H; NMR; -; B=608-729.
PDB; 2RMR; NMR; -; A=119-189.
PDB; 2RMS; NMR; -; A=119-189.
PDBsum; 1G1E; -.
PDBsum; 1S5Q; -.
PDBsum; 1S5R; -.
PDBsum; 2L9S; -.
PDBsum; 2LD7; -.
PDBsum; 2N2H; -.
PDBsum; 2RMR; -.
PDBsum; 2RMS; -.
ProteinModelPortal; Q60520; -.
SMR; Q60520; -.
BioGrid; 203256; 74.
CORUM; Q60520; -.
DIP; DIP-469N; -.
IntAct; Q60520; 37.
MINT; Q60520; -.
STRING; 10090.ENSMUSP00000128956; -.
iPTMnet; Q60520; -.
PhosphoSitePlus; Q60520; -.
EPD; Q60520; -.
MaxQB; Q60520; -.
PaxDb; Q60520; -.
PeptideAtlas; Q60520; -.
PRIDE; Q60520; -.
Ensembl; ENSMUST00000049169; ENSMUSP00000045044; ENSMUSG00000042557. [Q60520-2]
Ensembl; ENSMUST00000167715; ENSMUSP00000130641; ENSMUSG00000042557. [Q60520-2]
Ensembl; ENSMUST00000168177; ENSMUSP00000130221; ENSMUSG00000042557. [Q60520-1]
Ensembl; ENSMUST00000168502; ENSMUSP00000128956; ENSMUSG00000042557. [Q60520-1]
Ensembl; ENSMUST00000168678; ENSMUSP00000126601; ENSMUSG00000042557. [Q60520-2]
GeneID; 20466; -.
KEGG; mmu:20466; -.
UCSC; uc009ptx.2; mouse. [Q60520-1]
UCSC; uc012gtw.1; mouse. [Q60520-2]
CTD; 25942; -.
MGI; MGI:107157; Sin3a.
eggNOG; KOG4204; Eukaryota.
eggNOG; COG5602; LUCA.
GeneTree; ENSGT00390000007239; -.
HOVERGEN; HBG060425; -.
InParanoid; Q60520; -.
KO; K11644; -.
OMA; KPCSGRD; -.
OrthoDB; EOG091G03HY; -.
PhylomeDB; Q60520; -.
TreeFam; TF106187; -.
Reactome; R-MMU-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
ChiTaRS; Sin3a; mouse.
EvolutionaryTrace; Q60520; -.
PRO; PR:Q60520; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000042557; -.
CleanEx; MM_SIN3A; -.
ExpressionAtlas; Q60520; baseline and differential.
Genevisible; Q60520; MM.
GO; GO:0000776; C:kinetochore; IDA:MGI.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016580; C:Sin3 complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IPI:MGI.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IMP:MGI.
GO; GO:0033558; F:protein deacetylase activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:MGI.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IGI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:MGI.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0034613; P:cellular protein localization; IMP:MGI.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
GO; GO:0006260; P:DNA replication; IMP:MGI.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:1901675; P:negative regulation of histone H3-K27 acetylation; ISO:MGI.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0031937; P:positive regulation of chromatin silencing; ISO:MGI.
GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0006476; P:protein deacetylation; ISO:MGI.
GO; GO:0010817; P:regulation of hormone levels; IEA:Ensembl.
GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0051595; P:response to methylglyoxal; IDA:MGI.
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.
InterPro; IPR037969; SIN3A.
PANTHER; PTHR12346:SF2; PTHR12346:SF2; 1.
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; Alternative splicing; Biological rhythms;
Coiled coil; Complete proteome; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 1274 Paired amphipathic helix protein Sin3a.
/FTId=PRO_0000121538.
DOMAIN 119 189 PAH 1. {ECO:0000255|PROSITE-
ProRule:PRU00810}.
DOMAIN 300 383 PAH 2. {ECO:0000255|PROSITE-
ProRule:PRU00810}.
DOMAIN 457 526 PAH 3. {ECO:0000255|PROSITE-
ProRule:PRU00810}.
REGION 119 196 Interaction with HCFC1.
{ECO:0000250|UniProtKB:Q96ST3}.
REGION 205 479 Interaction with REST.
{ECO:0000269|PubMed:10734093}.
REGION 459 526 Interaction with SAP30.
{ECO:0000269|PubMed:9702189}.
REGION 524 851 Interaction with NCOR1.
REGION 525 660 Interactions with SUDS3 and SAP130.
{ECO:0000250}.
REGION 688 830 Interactions with HDAC1 and ARID4B.
{ECO:0000250}.
REGION 889 968 Interaction with OGT. {ECO:0000250}.
COILED 904 933 {ECO:0000255}.
COMPBIAS 207 265 Gln-rich.
COMPBIAS 218 285 Pro-rich.
COMPBIAS 836 842 Poly-Glu.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:Q96ST3}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 284 284 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 470 470 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q96ST3}.
MOD_RES 833 833 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 861 861 Phosphoserine.
{ECO:0000250|UniProtKB:Q96ST3}.
MOD_RES 866 866 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 876 876 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 941 941 Phosphoserine.
{ECO:0000250|UniProtKB:Q96ST3}.
MOD_RES 1090 1090 Phosphoserine.
{ECO:0000250|UniProtKB:Q96ST3}.
MOD_RES 1113 1113 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96ST3}.
CROSSLNK 134 134 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96ST3}.
CROSSLNK 564 564 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96ST3}.
VAR_SEQ 1097 1097 E -> EVWT (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7601471,
ECO:0000303|Ref.3}.
/FTId=VSP_039918.
MUTAGEN 307 307 A->V: Greatly reduced binding to MAD;
when associated with D-308 and A-311.
{ECO:0000269|PubMed:11106735}.
MUTAGEN 308 308 I->D: Greatly reduced binding to MAD;
when associated with V-307 and A-311.
{ECO:0000269|PubMed:11106735}.
MUTAGEN 309 309 N->D: No effect on binding to MAD.
{ECO:0000269|PubMed:11106735}.
MUTAGEN 311 311 V->A: Greatly reduced binding to MAD;
when associated with V-307 and D-308.
{ECO:0000269|PubMed:11106735}.
MUTAGEN 326 326 K->A: No effect on binding to MAD.
{ECO:0000269|PubMed:11106735}.
MUTAGEN 329 329 L->A: Greatly reduced binding to MAD;
when associated with A-332.
{ECO:0000269|PubMed:11106735}.
MUTAGEN 332 332 L->A: Greatly reduced binding to MAD;
when associated with A-329.
{ECO:0000269|PubMed:11106735}.
CONFLICT 144 144 Y -> H (in Ref. 1; AAB01610).
{ECO:0000305}.
CONFLICT 154 154 F -> L (in Ref. 4; AAH53385).
{ECO:0000305}.
CONFLICT 303 303 E -> H (in Ref. 1; AAB01610).
{ECO:0000305}.
CONFLICT 514 514 E -> G (in Ref. 4; AAH53385).
{ECO:0000305}.
CONFLICT 720 721 EQ -> DE (in Ref. 1; AAB01610).
{ECO:0000305}.
CONFLICT 827 827 A -> D (in Ref. 2; AAA89119).
{ECO:0000305}.
CONFLICT 899 899 L -> R (in Ref. 4; AAH52716).
{ECO:0000305}.
CONFLICT 912 912 S -> F (in Ref. 4; AAH52716).
{ECO:0000305}.
CONFLICT 969 969 S -> Q (in Ref. 1; AAB01610).
{ECO:0000305}.
CONFLICT 1047 1047 L -> V (in Ref. 1; AAB01610).
{ECO:0000305}.
CONFLICT 1205 1207 KRL -> QGK (in Ref. 5; AAA69773).
{ECO:0000305}.
CONFLICT 1205 1205 K -> KK (in Ref. 5; AAA69772).
{ECO:0000305}.
CONFLICT 1215 1216 VD -> GK (in Ref. 5; AAA69772).
{ECO:0000305}.
HELIX 126 136 {ECO:0000244|PDB:2RMR}.
HELIX 137 139 {ECO:0000244|PDB:2RMS}.
HELIX 141 155 {ECO:0000244|PDB:2RMR}.
HELIX 161 171 {ECO:0000244|PDB:2RMR}.
TURN 172 174 {ECO:0000244|PDB:2RMR}.
HELIX 176 183 {ECO:0000244|PDB:2RMR}.
HELIX 302 317 {ECO:0000244|PDB:1G1E}.
TURN 318 320 {ECO:0000244|PDB:1G1E}.
HELIX 322 344 {ECO:0000244|PDB:1G1E}.
STRAND 347 349 {ECO:0000244|PDB:1S5R}.
HELIX 355 365 {ECO:0000244|PDB:1G1E}.
TURN 366 368 {ECO:0000244|PDB:1G1E}.
HELIX 370 377 {ECO:0000244|PDB:1G1E}.
TURN 457 460 {ECO:0000244|PDB:2LD7}.
HELIX 463 475 {ECO:0000244|PDB:2LD7}.
HELIX 478 492 {ECO:0000244|PDB:2LD7}.
HELIX 498 504 {ECO:0000244|PDB:2LD7}.
HELIX 506 509 {ECO:0000244|PDB:2LD7}.
HELIX 513 523 {ECO:0000244|PDB:2LD7}.
HELIX 616 641 {ECO:0000244|PDB:2N2H}.
HELIX 646 651 {ECO:0000244|PDB:2N2H}.
TURN 660 662 {ECO:0000244|PDB:2N2H}.
HELIX 663 673 {ECO:0000244|PDB:2N2H}.
HELIX 675 677 {ECO:0000244|PDB:2N2H}.
HELIX 678 685 {ECO:0000244|PDB:2N2H}.
HELIX 689 713 {ECO:0000244|PDB:2N2H}.
HELIX 715 723 {ECO:0000244|PDB:2N2H}.
SEQUENCE 1274 AA; 145088 MW; 80FE378F62ED7CB3 CRC64;
MKRRLDDQES PVYAAQQRRI PGSTEAFSHQ HRVLAPAPPV YEAVSETMQS ATGIQYSVAP
NYQVSAVPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ SHAHPAPPVA PVQGQQQFQR
LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI MKEFKSQSID TPGVISRVSQ LFKGHPDLIM
GFNTFLPPGY KIEVQTNDMV NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SSQSAPTPAQ
PAPQPTAAKV SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ
PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT PALTEQEVYA
QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV RNDHGGTVKK PQLNNKPQRP
SQNGCQIRRH SGTGATPPVK KKPKLMSLKE SSMADASKHG VGTESLFFDK VRKALRSAEA
YENFLRCLVI FNQEVISRAE LVQLVSPFLG KFPELFNWFK NFLGYKESVH LESFPKERAT
EGIAMEIDYA SCKRLGSSYR ALPKSYQQPK CTGRTPLCKE VLNDTWVSFP SWSEDSTFVS
SKKTQYEEHI YRCEDERFEL DVVLETNLAT IRVLEAIQKK LSRLSAEEQA KFRLDNTLGG
TSEVIHRKAL QRIYADKAAD IIDGLRKNPS IAVPIVLKRL KMKEEEWREA QRGFNKVWRE
QNEKYYLKSL DHQGINFKQN DTKVLRSKSL LNEIESIYDE RQEQATEENA GVPVGPHLSL
AYEDKQILED AAALIIHHVK RQTGIQKEDK YKIKQIMHHF IPDLLFAQRG DLSDVEEEEE
EEMDVDEATG APKKHNGVGG SPPKSKLLFS NTAAQKLRGM DEVYNLFYVN NNWYIFMRLH
QILCLRLLRI CSQAERQIEE ENREREWERE VLGIKRDKSD SPAIQLRLKE PMDVDVEDYY
PAFLDMVRSL LDGNIDSSQY EDSLREMFTI HAYIAFTMDK LIQSIVRQLQ HIVSDEVCVQ
VTDLYLAENN NGATGGQLNS QTSRSLLESA YQRKAEQLMS DENCFKLMFI QSQGQVQLTV
ELLDTEEENS DDPVEAERWS DYVERYMSSD TTSPELREHL AQKPVFLPRN LRRIRKCQRG
REQQEKEGKE GNSKKTMENV ESLDKLECRF KLNSYKMVYV IKSEDYMYRR TALLRAHQSH
ERVSKRLHQR FQAWVDKWTK EHVPREMAAE TSKWLMGEGL EGLVPCTTTC DTETLHFVSI
NKYRVKYGTV FKAP


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