ID SDS3_MOUSE Reviewed; 328 AA. AC Q8BR65; Q3UC92; Q6P6K1; Q7TNT0; Q8BRR7; Q8K5B4; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 14-OCT-2015, entry version 113. DE RecName: Full=Sin3 histone deacetylase corepressor complex component SDS3; DE AltName: Full=Suppressor of defective silencing 3 protein homolog; GN Name=Suds3; Synonyms=Sds3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM22676.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH SIN3A RP AND SIN3B, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6 {ECO:0000312|EMBL:AAM22676.1}; RX PubMed=11909966; DOI=10.1128/MCB.22.8.2743-2750.2002; RA Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., RA Hou H. Jr., Chen K., DePinho R.A.; RT "Identification of mammalian Sds3 as an integral component of the RT Sin3/histone deacetylase corepressor complex."; RL Mol. Cell. Biol. 22:2743-2750(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Aorta, Bone marrow macrophage, Brain cortex, RC Corpora quadrigemina, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] {ECO:0000312|EMBL:AAH62176.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain, and Limb {ECO:0000312|EMBL:AAH62176.1}; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-49, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-237, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND SER-234, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Regulatory protein which represses transcription and CC augments histone deacetylase activity of HDAC1. May have a CC potential role in tumor suppressor pathways through regulation of CC apoptosis. May function in the assembly and/or enzymatic activity CC of the mSin3A corepressor complex or in mediating interactions CC between the complex and other regulatory complexes (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with HCFC1 (By similarity). Homodimer. CC Component of the SIN3 histone deacetylase (HDAC) corepressor CC complex. Interacts with SIN3A. Interaction with SIN3B enhances the CC interaction between SIN3B and HDAC1 to form a complex. Component CC of a mSin3A corepressor complex that contains SIN3A, SAP130, CC SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with CC USP17L2; the interaction is direct (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-591431, EBI-591431; CC Q60520:Sin3a; NbExp=4; IntAct=EBI-591431, EBI-349034; CC Q62141:Sin3b; NbExp=5; IntAct=EBI-591431, EBI-591450; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in all newborn tissues tested, CC including brain, kidney and liver. {ECO:0000269|PubMed:11909966}. CC -!- DOMAIN: The C-terminus is involved in transcriptional repression CC by HDAC-independent mechanisms. {ECO:0000250}. CC -!- PTM: Polyubiquitinated. 'Lys-63'-polyubiquitinated SUDS3 CC positively regulates histone deacetylation. Regulated through CC deubiquitination by USP17L2/USP17 that cleaves 'Lys-63'-linked CC ubiquitin chains (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SDS3 family. {ECO:0000305}. 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; AF469109; AAM22676.1; -; mRNA. DR EMBL; AK043652; BAC31608.1; -; mRNA. DR EMBL; AK045475; BAC32387.1; -; mRNA. DR EMBL; AK138947; BAE23831.1; -; mRNA. DR EMBL; AK150633; BAE29722.1; -; mRNA. DR EMBL; BC055764; AAH55764.2; -; mRNA. DR EMBL; BC062176; AAH62176.1; -; mRNA. DR CCDS; CCDS39232.1; -. DR RefSeq; NP_001116138.1; NM_001122666.2. DR RefSeq; NP_848737.3; NM_178622.5. DR UniGene; Mm.34456; -. DR PDB; 2N2H; NMR; -; A=205-228. DR PDB; 4ZQA; X-ray; 1.65 A; A=90-172. DR PDBsum; 2N2H; -. DR PDBsum; 4ZQA; -. DR ProteinModelPortal; Q8BR65; -. DR BioGrid; 215053; 9. DR IntAct; Q8BR65; 3. DR MINT; MINT-4112013; -. DR STRING; 10090.ENSMUSP00000130535; -. DR PhosphoSite; Q8BR65; -. DR MaxQB; Q8BR65; -. DR PaxDb; Q8BR65; -. DR PRIDE; Q8BR65; -. DR Ensembl; ENSMUST00000086471; ENSMUSP00000083662; ENSMUSG00000066900. DR GeneID; 71954; -. DR KEGG; mmu:71954; -. DR UCSC; uc008zff.3; mouse. DR CTD; 64426; -. DR MGI; MGI:1919204; Suds3. DR eggNOG; NOG311652; -. DR GeneTree; ENSGT00530000063177; -. DR HOGENOM; HOG000007054; -. DR HOVERGEN; HBG108465; -. DR InParanoid; Q8BR65; -. DR KO; K19201; -. DR OrthoDB; EOG7VQJFB; -. DR PhylomeDB; Q8BR65; -. DR TreeFam; TF323740; -. DR Reactome; R-MMU-3214815; HDACs deacetylate histones. DR NextBio; 335040; -. DR PRO; PR:Q8BR65; -. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; Q8BR65; -. DR Genevisible; Q8BR65; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IPI:MGI. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR013907; Sds3. DR Pfam; PF08598; Sds3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Apoptosis; Chromatin regulator; KW Coiled coil; Complete proteome; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9H7L9}. FT CHAIN 2 328 Sin3 histone deacetylase corepressor FT complex component SDS3. FT /FTId=PRO_0000097653. FT REGION 2 170 Mediates interaction with USP17L2. FT {ECO:0000250}. FT REGION 188 226 Sin3 interaction domain (SID). FT COILED 66 171 {ECO:0000255}. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000250|UniProtKB:Q9H7L9}. FT MOD_RES 32 32 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H7L9}. FT MOD_RES 45 45 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 49 49 Phosphothreonine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 53 53 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H7L9}. FT MOD_RES 228 228 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9H7L9}. FT MOD_RES 234 234 Phosphoserine. FT {ECO:0000244|PubMed:19144319, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 237 237 Phosphoserine. FT {ECO:0000244|PubMed:19144319}. FT MOD_RES 244 244 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q9H7L9}. FT CROSSLNK 69 69 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:Q9H7L9}. FT CONFLICT 142 142 K -> N (in Ref. 2; BAC31608). FT {ECO:0000305}. FT CONFLICT 186 186 R -> W (in Ref. 1; AAM22676). FT {ECO:0000305}. FT CONFLICT 326 328 SAA -> KFLTYRD (in Ref. 3; AAH62176). FT {ECO:0000305}. SQ SEQUENCE 328 AA; 38107 MW; 05C22EA578C318E8 CRC64; MSAAGLLAPA PAPAAAPAAP EYYPEDEEEL ESAEDDERSC RGRESDEDTE DASETDLAKH DEEDYVEMKE QMYQDKLASL KRQLQQLQEG TLQEYQKRMK KLDQQYRERI RNAELFLQLE TEQVERNYIK EKKAAVKEFE DKKVELKENL IAELEEKKKM IENEKLTMEL TGDSMEVKPI MTRKLRRRPN DPVPIPDKRR KPAPAQLNYL LTDEQIMEDL RTLNKLKSPK RPASPSSPEH LPATPAESPA QRFEARIEDG KLYYDKRWYH KSQAIYLESK DNQKLSCVIS SVGANEIWVR KTSDSTKMRI YVGQLQRGLF VIRRRSAA //