ID SIN3A_HUMAN Reviewed; 1273 AA. AC Q96ST3; B2RNS5; Q8N8N4; Q8NC83; Q8WV18; Q96L98; Q9UFQ1; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 24-OCT-2003, sequence version 2. DT 27-MAR-2024, entry version 208. DE RecName: Full=Paired amphipathic helix protein Sin3a; DE AltName: Full=Histone deacetylase complex subunit Sin3a; DE AltName: Full=Transcriptional corepressor Sin3a; GN Name=SIN3A {ECO:0000312|HGNC:HGNC:19353}; 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:AAP97288.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Guo J.H., Yu L.; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH18973.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Uterus {ECO:0000312|EMBL:AAH18973.1}; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1026. RC TISSUE=Brain, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] {ECO:0000305, ECO:0000312|EMBL:AAP97288.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-620. RA Bu X., Fu Y., Jiang S., Avraham S., Avraham H.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 913-1273. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] {ECO:0000305} RP INTERACTION WITH SFPQ. RX PubMed=11259580; DOI=10.1128/mcb.21.7.2298-2311.2001; RA Mathur M., Tucker P.W., Samuels H.H.; RT "PSF is a novel corepressor that mediates its effect through Sin3A and the RT DNA binding domain of nuclear hormone receptors."; RL Mol. Cell. Biol. 21:2298-2311(2001). RN [7] RP INTERACTION WITH OGT, AND FUNCTION. RX PubMed=12150998; DOI=10.1016/s0092-8674(02)00810-3; RA Yang X., Zhang F., Kudlow J.E.; RT "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: RT coupling protein O-GlcNAcylation to transcriptional repression."; RL Cell 110:69-80(2002). RN [8] {ECO:0000305} RP INTERACTION WITH SFPQ. RX PubMed=11897684; DOI=10.1210/endo.143.4.8748; RA Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R.; RT "Transcriptional activation of human CYP17 in H295R adrenocortical cells RT depends on complex formation among p54(nrb)/NonO, protein-associated RT splicing factor, and SF-1, a complex that also participates in repression RT of transcription."; RL Endocrinology 143:1280-1290(2002). RN [9] {ECO:0000305} RP INTERACTION WITH DACH1. RX PubMed=14525983; DOI=10.1074/jbc.m310021200; RA Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K., RA Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.; RT "DACH1 inhibits transforming growth factor-beta signaling through binding RT Smad4."; RL J. Biol. Chem. 278:51673-51684(2003). RN [10] {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 [11] RP INTERACTION WITH SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2. RX PubMed=12724404; DOI=10.1128/mcb.23.10.3456-3467.2003; RA Fleischer T.C., Yun U.J., Ayer D.E.; RT "Identification and characterization of three new components of the mSin3A RT corepressor complex."; RL Mol. Cell. Biol. 23:3456-3467(2003). RN [12] RP INTERACTION WITH BRMS1L. RX PubMed=15451426; DOI=10.1016/j.bbrc.2004.08.227; RA Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.; RT "Identification of a novel BRMS1-homologue protein p40 as a component of RT the mSin3A/p33(ING1b)/HDAC1 deacetylase complex."; RL Biochem. Biophys. Res. Commun. 323:1216-1222(2004). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [14] RP SUBCELLULAR LOCATION, AND INTERACTION WITH SAP30L. RX PubMed=16820529; DOI=10.1093/nar/gkl401; RA Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., RA Peterson P., Maeki M., Kainulainen H., Lohi O.; RT "SAP30L interacts with members of the Sin3A corepressor complex and targets RT Sin3A to the nucleolus."; RL Nucleic Acids Res. 34:3288-3298(2006). RN [15] RP INTERACTION WITH PPHLN1. RX PubMed=17963697; DOI=10.1016/j.bbrc.2007.10.090; RA Kurita M., Suzuki H., Kawano Y., Aiso S., Matsuoka M.; RT "CR/periphilin is a transcriptional co-repressor involved in cell cycle RT progression."; RL Biochem. Biophys. Res. Commun. 364:930-936(2007). RN [16] RP INTERACTION WITH TOPORS, SUMOYLATION BY TOPORS, AND DESUMOYLATION BY SENP2. RX PubMed=17803295; DOI=10.1021/pr0703674; RA Pungaliya P., Kulkarni D., Park H.J., Marshall H., Zheng H., Lackland H., RA Saleem A., Rubin E.H.; RT "TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins."; RL J. Proteome Res. 6:3918-3923(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-277; SER-832; SER-940 RP AND SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 AND SER-1112, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-469, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [21] RP INTERACTION WITH SPHK2. RX PubMed=19729656; DOI=10.1126/science.1176709; RA Hait N.C., Allegood J., Maceyka M., Strub G.M., Harikumar K.B., Singh S.K., RA Luo C., Marmorstein R., Kordula T., Milstien S., Spiegel S.; RT "Regulation of histone acetylation in the nucleus by sphingosine-1- RT phosphate."; RL Science 325:1254-1257(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832; SER-860; SER-940 AND RP SER-1112, AND 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 [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [24] RP INTERACTION WITH TET1. RX PubMed=21490601; DOI=10.1038/nature10066; RA Williams K., Christensen J., Pedersen M.T., Johansen J.V., Cloos P.A., RA Rappsilber J., Helin K.; RT "TET1 and hydroxymethylcytosine in transcription and DNA methylation RT fidelity."; RL Nature 473:343-348(2011). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 AND SER-860, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-832; SER-940 AND RP SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1089, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [28] RP TISSUE SPECIFICITY, INVOLVEMENT IN WITKOS, AND VARIANT WITKOS RP 1104-ARG--PRO-1273 DEL. RX PubMed=27399968; DOI=10.1038/ng.3619; RA Witteveen J.S., Willemsen M.H., Dombroski T.C., van Bakel N.H., RA Nillesen W.M., van Hulten J.A., Jansen E.J., Verkaik D., RA Veenstra-Knol H.E., van Ravenswaaij-Arts C.M., Wassink-Ruiter J.S., RA Vincent M., David A., Le Caignec C., Schieving J., Gilissen C., Foulds N., RA Rump P., Strom T., Cremer K., Zink A.M., Engels H., de Munnik S.A., RA Visser J.E., Brunner H.G., Martens G.J., Pfundt R., Kleefstra T., RA Kolk S.M.; RT "Haploinsufficiency of MeCP2-interacting transcriptional co-repressor SIN3A RT causes mild intellectual disability by affecting the development of RT cortical integrity."; RL Nat. Genet. 48:877-887(2016). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122; LYS-134 AND LYS-563, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [30] RP INVOLVEMENT IN WITKOS. RX PubMed=30267900; DOI=10.1016/j.ejmg.2018.09.014; RA Narumi-Kishimoto Y., Araki N., Migita O., Kawai T., Okamura K., RA Nakabayashi K., Kaname T., Ozawa Y., Ozawa H., Takada F., Hata K.; RT "Novel SIN3A mutation identified in a Japanese patient with Witteveen-Kolk RT syndrome."; RL Eur. J. Med. Genet. 62:103547-103547(2019). CC -!- FUNCTION: Acts as a transcriptional repressor. Corepressor for REST. CC Interacts with MXI1 to repress MYC responsive genes and antagonize MYC CC oncogenic activities. Also interacts with MXD1-MAX heterodimers to CC repress transcription by tethering SIN3A to DNA. Acts cooperatively CC with OGT to repress transcription in parallel with histone CC deacetylation. Involved in the control of the circadian rhythms. CC Required for the transcriptional repression of circadian target genes, CC such as PER1, mediated by the large PER complex through histone CC deacetylation. Cooperates with FOXK1 to regulate cell cycle progression CC probably by repressing cell cycle inhibitor genes expression (By CC similarity). Required for cortical neuron differentiation and callosal CC axon elongation (By similarity). {ECO:0000250|UniProtKB:Q60520, CC ECO:0000269|PubMed:12150998}. CC -!- SUBUNIT: Interacts with ARID4B, BRMS1L, HCFC1, HDAC1, HDAC2, MXI1, CC SAP30L, SAP130, SFPQ and TOPORS (PubMed:11259580, PubMed:11897684, CC PubMed:12670868, PubMed:12724404, PubMed:15451426, PubMed:16820529, CC PubMed:17803295). Interacts with OGT (via TPRs 1-6); the interaction CC mediates transcriptional repression in parallel with histone CC deacetylase (PubMed:12150998). Interacts with BAZ2A, MXD1, MXD3, MXD4, CC MBD2, DACH1, NCOR1, NR4A2, REST, RLIM, SAP30, SETDB1, SMYD2, and SUDS3 CC (PubMed:14525983). Interacts with PHF12 in a complex composed of HDAC1, CC PHF12 and SAP30 (By similarity). Interacts with TET1; the interaction CC recruits SIN3A to gene promoters (PubMed:21490601). The large PER CC complex involved in the histone deacetylation is composed of at least CC HDAC1, PER2, SFPQ and SIN3A (By similarity). Interacts with KLF11 (By CC similarity). Interacts with PPHLN1 (PubMed:17963697). Found in a CC complex with YY1, GON4L and HDAC1 (By similarity). Interacts (via PAH2) CC with FOXK1 (By similarity). Interacts with FOXK2 (By similarity). Found CC in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, CC OGT and TET1. Interacts with SINHCAF (By similarity). Interacts with CC SPHK2 (PubMed:19729656). {ECO:0000250|UniProtKB:Q60520, CC ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11897684, CC ECO:0000269|PubMed:12150998, ECO:0000269|PubMed:12670868, CC ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:14525983, CC ECO:0000269|PubMed:15451426, ECO:0000269|PubMed:16820529, CC ECO:0000269|PubMed:17803295, ECO:0000269|PubMed:17963697, CC ECO:0000269|PubMed:19729656, ECO:0000269|PubMed:21490601}. CC -!- INTERACTION: CC Q96ST3; P51610: HCFC1; NbExp=6; IntAct=EBI-347218, EBI-396176; CC Q96ST3; Q13547: HDAC1; NbExp=9; IntAct=EBI-347218, EBI-301834; CC Q96ST3; Q92769: HDAC2; NbExp=6; IntAct=EBI-347218, EBI-301821; CC Q96ST3; P42858: HTT; NbExp=4; IntAct=EBI-347218, EBI-466029; CC Q96ST3; Q9H160: ING2; NbExp=2; IntAct=EBI-347218, EBI-389787; CC Q96ST3; P51608: MECP2; NbExp=2; IntAct=EBI-347218, EBI-1189067; CC Q96ST3; Q9UQ80: PA2G4; NbExp=4; IntAct=EBI-347218, EBI-924893; CC Q96ST3; P23246: SFPQ; NbExp=2; IntAct=EBI-347218, EBI-355453; CC Q96ST3; P12755: SKI; NbExp=3; IntAct=EBI-347218, EBI-347281; CC Q96ST3; P04637: TP53; NbExp=2; IntAct=EBI-347218, EBI-366083; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810, CC ECO:0000269|PubMed:16820529}. Nucleus, nucleolus CC {ECO:0000269|PubMed:16820529}. Note=Recruited to the nucleolus by CC SAP30L. CC -!- TISSUE SPECIFICITY: Expressed in the developing brain, with highest CC levels of expression detected in the ventricular zone of various CC cortical regions. {ECO:0000269|PubMed:27399968}. CC -!- PTM: SUMO1 sumoylated by TOPORS. Probably desumoylated by SENP2. CC {ECO:0000269|PubMed:17803295}. CC -!- DISEASE: Witteveen-Kolk syndrome (WITKOS) [MIM:613406]: An autosomal CC dominant syndrome characterized by global developmental delay, mild to CC severe intellectual disability, and facial dysmorphism. Additional CC features include short stature, microcephaly, joint hypermotility, and CC small hands and feet with digital abnormalities. Brain imaging shows CC dilated ventricles, thin corpus callosum and, in some cases, dysgyria CC or polymicrogyria. {ECO:0000269|PubMed:27399968, CC ECO:0000269|PubMed:30267900}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF418569; AAP97288.1; -; mRNA. DR EMBL; BC018973; AAH18973.1; -; mRNA. DR EMBL; BC137098; AAI37099.1; -; mRNA. DR EMBL; BC137099; AAI37100.1; -; mRNA. DR EMBL; AK027559; BAB55197.1; -; mRNA. DR EMBL; AK074903; BAC11280.1; -; mRNA. DR EMBL; AK096477; BAC04801.1; -; mRNA. DR EMBL; AY044430; AAK95854.1; -; mRNA. DR EMBL; AL117513; CAB55972.1; -; mRNA. DR CCDS; CCDS10279.1; -. DR PIR; T17282; T17282. DR RefSeq; NP_001138829.1; NM_001145357.1. DR RefSeq; NP_001138830.1; NM_001145358.1. DR RefSeq; NP_056292.1; NM_015477.2. DR RefSeq; XP_006720528.1; XM_006720465.3. DR RefSeq; XP_006720529.1; XM_006720466.3. DR RefSeq; XP_006720530.1; XM_006720467.3. DR AlphaFoldDB; Q96ST3; -. DR SMR; Q96ST3; -. DR BioGRID; 117439; 342. DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex. DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant. DR CORUM; Q96ST3; -. DR DIP; DIP-31515N; -. DR IntAct; Q96ST3; 84. DR MINT; Q96ST3; -. DR STRING; 9606.ENSP00000378402; -. DR GlyCosmos; Q96ST3; 8 sites, 2 glycans. DR GlyGen; Q96ST3; 10 sites, 2 O-linked glycans (10 sites). DR iPTMnet; Q96ST3; -. DR MetOSite; Q96ST3; -. DR PhosphoSitePlus; Q96ST3; -. DR SwissPalm; Q96ST3; -. DR BioMuta; SIN3A; -. DR DMDM; 37999759; -. DR EPD; Q96ST3; -. DR jPOST; Q96ST3; -. DR MassIVE; Q96ST3; -. DR MaxQB; Q96ST3; -. DR PaxDb; 9606-ENSP00000378402; -. DR PeptideAtlas; Q96ST3; -. DR ProteomicsDB; 78146; -. DR Pumba; Q96ST3; -. DR Antibodypedia; 3857; 307 antibodies from 37 providers. DR DNASU; 25942; -. DR Ensembl; ENST00000360439.8; ENSP00000353622.4; ENSG00000169375.17. DR Ensembl; ENST00000394947.8; ENSP00000378402.3; ENSG00000169375.17. DR Ensembl; ENST00000394949.8; ENSP00000378403.4; ENSG00000169375.17. DR Ensembl; ENST00000564778.6; ENSP00000455204.2; ENSG00000169375.17. DR Ensembl; ENST00000565264.2; ENSP00000454296.2; ENSG00000169375.17. DR Ensembl; ENST00000704312.1; ENSP00000515834.1; ENSG00000169375.17. DR GeneID; 25942; -. DR KEGG; hsa:25942; -. DR MANE-Select; ENST00000394947.8; ENSP00000378402.3; NM_001145358.2; NP_001138830.1. DR UCSC; uc002bai.4; human. DR AGR; HGNC:19353; -. DR CTD; 25942; -. DR DisGeNET; 25942; -. DR GeneCards; SIN3A; -. DR HGNC; HGNC:19353; SIN3A. DR HPA; ENSG00000169375; Low tissue specificity. DR MalaCards; SIN3A; -. DR MIM; 607776; gene. DR MIM; 613406; phenotype. DR neXtProt; NX_Q96ST3; -. DR OpenTargets; ENSG00000169375; -. DR Orphanet; 94065; 15q24 microdeletion syndrome. DR Orphanet; 500166; SIN3A-related intellectual disability syndrome due to a point mutation. DR Orphanet; 500163; Witteveen-Kolk syndrome. DR PharmGKB; PA134993567; -. DR VEuPathDB; HostDB:ENSG00000169375; -. DR eggNOG; KOG4204; Eukaryota. DR GeneTree; ENSGT00940000155491; -. DR HOGENOM; CLU_001360_0_1_1; -. DR InParanoid; Q96ST3; -. DR OMA; MCEEVIK; -. DR OrthoDB; 199155at2759; -. DR PhylomeDB; Q96ST3; -. DR TreeFam; TF106187; -. DR PathwayCommons; Q96ST3; -. DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha. 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-9022538; Loss of MECP2 binding ability to 5mC-DNA. DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity. DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels. DR Reactome; R-HSA-9022702; MECP2 regulates transcription of neuronal ligands. DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes. DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling. DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; Q96ST3; -. DR SIGNOR; Q96ST3; -. DR BioGRID-ORCS; 25942; 709 hits in 1173 CRISPR screens. DR ChiTaRS; SIN3A; human. DR GeneWiki; SIN3A; -. DR GenomeRNAi; 25942; -. DR Pharos; Q96ST3; Tbio. DR PRO; PR:Q96ST3; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q96ST3; Protein. DR Bgee; ENSG00000169375; Expressed in secondary oocyte and 174 other cell types or tissues. DR ExpressionAtlas; Q96ST3; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB. DR GO; GO:0000776; C:kinetochore; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0070822; C:Sin3-type complex; IDA:UniProtKB. DR GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; IEA:Ensembl. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0003714; F:transcription corepressor activity; IMP:BHF-UCL. DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:BHF-UCL. DR GO; GO:0002218; P:activation of innate immune response; IMP:BHF-UCL. DR GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0021895; P:cerebral cortex neuron differentiation; ISS:UniProtKB. DR GO; GO:0006260; P:DNA replication; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl. DR GO; GO:0031507; P:heterochromatin formation; IMP:BHF-UCL. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal. DR GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:BHF-UCL. DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; NAS:ComplexPortal. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:BHF-UCL. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB. DR GO; GO:0010817; P:regulation of hormone levels; IEA:Ensembl. DR GO; GO:0051595; P:response to methylglyoxal; IEA:Ensembl. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IMP:BHF-UCL. DR Gene3D; 1.20.1160.11; Paired amphipathic helix; 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:SF2; PAIRED AMPHIPATHIC HELIX PROTEIN SIN3A; 1. DR PANTHER; PTHR12346; SIN3B-RELATED; 1. DR Pfam; PF02671; PAH; 3. DR Pfam; PF08295; Sin3_corepress; 1. DR Pfam; PF16879; Sin3a_C; 1. DR SMART; SM00761; HDAC_interact; 1. DR SUPFAM; SSF47762; PAH2 domain; 3. DR PROSITE; PS51477; PAH; 3. DR Genevisible; Q96ST3; HS. PE 1: Evidence at protein level; KW Acetylation; Biological rhythms; Coiled coil; Disease variant; Dwarfism; KW Intellectual disability; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..1273 FT /note="Paired amphipathic helix protein Sin3a" FT /id="PRO_0000121537" FT DOMAIN 119..189 FT /note="PAH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810" FT DOMAIN 300..383 FT /note="PAH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810" FT DOMAIN 456..525 FT /note="PAH 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 87..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 119..196 FT /note="Interaction with HCFC1" FT /evidence="ECO:0000269|PubMed:12670868" FT REGION 205..480 FT /note="Interaction with REST" FT /evidence="ECO:0000250" FT REGION 205..297 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 398..446 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 458..525 FT /note="Interaction with SAP30" FT /evidence="ECO:0000250|UniProtKB:Q60520" FT REGION 523..850 FT /note="Interaction with NCOR1" FT /evidence="ECO:0000250|UniProtKB:Q60520" FT REGION 524..659 FT /note="Interaction with SUDS3 and SAP130" FT /evidence="ECO:0000269|PubMed:12724404" FT REGION 687..829 FT /note="Interaction with HDAC1 and ARID4B" FT /evidence="ECO:0000269|PubMed:12724404" FT REGION 888..967 FT /note="Interaction with OGT" FT /evidence="ECO:0000269|PubMed:12150998" FT REGION 1136..1156 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 903..932 FT /evidence="ECO:0000255" FT COMPBIAS 216..250 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 264..282 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 283..297 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 408..430 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 284 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q60520" FT MOD_RES 469 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 832 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 860 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 865 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q60520" FT MOD_RES 875 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q60520" FT MOD_RES 940 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1089 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1112 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 122 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 134 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 563 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 1104..1273 FT /note="Missing (in WITKOS)" FT /evidence="ECO:0000269|PubMed:27399968" FT /id="VAR_081785" FT VARIANT 1156 FT /note="M -> L (in dbSNP:rs60213317)" FT /id="VAR_062129" FT CONFLICT 163 FT /note="G -> R (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 170..177 FT /note="QLFKGHPD -> HYSKGPPI (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 182..192 FT /note="FNTFLPPGYKI -> IQHLFAPWATKM (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="I -> T (in Ref. 3; BAC04801)" FT /evidence="ECO:0000305" FT CONFLICT 386 FT /note="S -> F (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 536 FT /note="E -> D (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 562 FT /note="P -> G (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 575..576 FT /note="PL -> GV (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 595 FT /note="S -> C (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 618..620 FT /note="ELD -> DLM (in Ref. 4; AAK95854)" FT /evidence="ECO:0000305" FT CONFLICT 1009 FT /note="Q -> R (in Ref. 3; BAC11280)" FT /evidence="ECO:0000305" FT CONFLICT 1247..1248 FT /note="TT -> NN (in Ref. 1; AAP97288)" FT /evidence="ECO:0000305" SQ 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 //