SDS3_MOUSE
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 03-AUG-2022, entry version 151.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 AND
RP SIN3B, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {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., Hou H. Jr.,
RA 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, Corpora quadrigemina,
RC 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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/6J; 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 project:
RT 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, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulatory protein which represses transcription and augments
CC histone deacetylase activity of HDAC1. May have a potential role in
CC tumor suppressor pathways through regulation of apoptosis. May function
CC in the assembly and/or enzymatic activity of the mSin3A corepressor
CC complex or in mediating interactions between the complex and other
CC regulatory complexes (By similarity). {ECO:0000250|UniProtKB:Q9H7L9,
CC ECO:0000269|PubMed:11909966}.
CC -!- SUBUNIT: Interacts with HCFC1 (By similarity). Homodimer. Component of
CC the SIN3 histone deacetylase (HDAC) corepressor complex. Interacts with
CC SIN3A. Interaction with SIN3B enhances the interaction between SIN3B
CC and HDAC1 to form a complex. Component of a mSin3A corepressor complex
CC that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and
CC HDAC2. Interacts with USP17L2; the interaction is direct (By
CC similarity). Interacts with FOXK2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- INTERACTION:
CC Q8BR65; Q60520: Sin3a; NbExp=4; IntAct=EBI-591431, EBI-349034;
CC Q8BR65; Q62141: Sin3b; NbExp=5; IntAct=EBI-591431, EBI-591450;
CC Q8BR65; Q8BR65: Suds3; NbExp=3; IntAct=EBI-591431, EBI-591431;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- TISSUE SPECIFICITY: Expressed in all newborn tissues tested, including
CC brain, kidney and liver. {ECO:0000269|PubMed:11909966}.
CC -!- DOMAIN: The C-terminus is involved in transcriptional repression by
CC HDAC-independent mechanisms. {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- PTM: Polyubiquitinated. 'Lys-63'-polyubiquitinated SUDS3 positively
CC regulates histone deacetylation. Regulated through deubiquitination by
CC USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains (By
CC similarity). {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- SIMILARITY: Belongs to the SDS3 family. {ECO:0000305}.
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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 PDB; 2N2H; NMR; -; A=205-228.
DR PDB; 4ZQA; X-ray; 1.65 A; A=90-172.
DR PDB; 7SXI; NMR; -; A=250-326.
DR PDBsum; 2N2H; -.
DR PDBsum; 4ZQA; -.
DR PDBsum; 7SXI; -.
DR AlphaFoldDB; Q8BR65; -.
DR SMR; Q8BR65; -.
DR BioGRID; 215053; 14.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR CORUM; Q8BR65; -.
DR IntAct; Q8BR65; 2.
DR STRING; 10090.ENSMUSP00000130535; -.
DR iPTMnet; Q8BR65; -.
DR PhosphoSitePlus; Q8BR65; -.
DR EPD; Q8BR65; -.
DR jPOST; Q8BR65; -.
DR MaxQB; Q8BR65; -.
DR PaxDb; Q8BR65; -.
DR PeptideAtlas; Q8BR65; -.
DR PRIDE; Q8BR65; -.
DR ProteomicsDB; 255507; -.
DR Antibodypedia; 31389; 110 antibodies from 20 providers.
DR DNASU; 71954; -.
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 VEuPathDB; HostDB:ENSMUSG00000066900; -.
DR eggNOG; KOG4466; Eukaryota.
DR GeneTree; ENSGT00910000144281; -.
DR HOGENOM; CLU_050862_0_1_1; -.
DR InParanoid; Q8BR65; -.
DR OMA; IGTEAIW; -.
DR OrthoDB; 1456563at2759; -.
DR PhylomeDB; Q8BR65; -.
DR TreeFam; TF323740; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 71954; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Suds3; mouse.
DR PRO; PR:Q8BR65; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BR65; protein.
DR Bgee; ENSMUSG00000066900; Expressed in spermatid and 264 other tissues.
DR ExpressionAtlas; Q8BR65; baseline and differential.
DR Genevisible; Q8BR65; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004407; F:histone deacetylase activity; 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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR InterPro; IPR013907; Sds3.
DR PANTHER; PTHR21964; PTHR21964; 1.
DR Pfam; PF08598; Sds3; 1.
DR SMART; SM01401; Sds3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Chromatin regulator; Coiled coil;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CHAIN 2..328
FT /note="Sin3 histone deacetylase corepressor complex
FT component SDS3"
FT /id="PRO_0000097653"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..170
FT /note="Mediates interaction with USP17L2"
FT /evidence="ECO:0000250"
FT REGION 188..226
FT /note="Sin3 interaction domain (SID)"
FT REGION 226..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..171
FT /evidence="ECO:0000255"
FT COMPBIAS 35..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CONFLICT 142
FT /note="K -> N (in Ref. 2; BAC31608)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="R -> W (in Ref. 1; AAM22676)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..328
FT /note="SAA -> KFLTYRD (in Ref. 3; AAH62176)"
FT /evidence="ECO:0000305"
FT HELIX 90..170
FT /evidence="ECO:0007829|PDB:4ZQA"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:2N2H"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:7SXI"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:7SXI"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:7SXI"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:7SXI"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7SXI"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:7SXI"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:7SXI"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:7SXI"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:7SXI"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:7SXI"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:7SXI"
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
