SAP30_MOUSE
ID SAP30_MOUSE Reviewed; 220 AA.
AC O88574; A2RSE9; Q99JB9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Histone deacetylase complex subunit SAP30;
DE AltName: Full=30 kDa Sin3-associated polypeptide;
DE AltName: Full=Sin3 corepressor complex subunit SAP30;
DE AltName: Full=Sin3-associated polypeptide p30;
GN Name=Sap30 {ECO:0000312|MGI:MGI:1929129};
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:AAC26007.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH NCOR1; SIN3A;
RP SIN3B; HDAC1; HDAC2 AND RBBP4.
RX PubMed=9702189; DOI=10.1016/s1097-2765(00)80111-2;
RA Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G.,
RA Ayer D.E., Eisenman R.N.;
RT "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-
RT mediated repression by specific transcription factors.";
RL Mol. Cell 2:33-42(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Thymus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5] {ECO:0000312|EMBL:CAC24848.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-220.
RC STRAIN=C57BL/6N {ECO:0000312|EMBL:CAC24848.1};
RC TISSUE=Liver {ECO:0000312|EMBL:CAC24848.1};
RX PubMed=11087671; DOI=10.1006/geno.2000.6358;
RA Dron M., Tartare X., Guillo F., Haik S., Barbin G., Maury C., Tovey M.,
RA Dandoy-Dron F.;
RT "Mouse scrapie responsive gene 1 (Scrg1): genomic organization, physical
RT linkage to sap30, genetic mapping on chromosome 8, and expression in
RT neuronal primary cell cultures.";
RL Genomics 70:140-149(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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 expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH SAMSN1.
RX PubMed=20478393; DOI=10.1016/j.biocel.2010.05.004;
RA Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A.,
RA Schmitz I., Beer-Hammer S.;
RT "SLy2 targets the nuclear SAP30/HDAC1 complex.";
RL Int. J. Biochem. Cell Biol. 42:1472-1481(2010).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH SIN3A; SINHCAF; HDAC1; RBBP4; OGT AND
RP TET1.
RX PubMed=28554894; DOI=10.15252/embj.201696307;
RA Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B., Das S.,
RA Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T., Jammula S.,
RA Hokamp K., O'Connor D.P., Pasini D., Cagney G., Bracken A.P.;
RT "Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells
RT required for self-renewal.";
RL EMBO J. 36:2216-2232(2017).
CC -!- FUNCTION: Involved in the functional recruitment of the Sin3-histone
CC deacetylase complex (HDAC) to a specific subset of N-CoR corepressor
CC complexes. Capable of transcription repression by N-CoR. Active in
CC deacetylating core histone octamers (when in a complex) but inactive in
CC deacetylating nucleosomal histones. {ECO:0000250|UniProtKB:O75446,
CC ECO:0000269|PubMed:9702189}.
CC -!- SUBUNIT: Component of the histone deacetylase complex that includes at
CC least SIN3A, HDAC1 and HDAC2 (PubMed:9702189). Found in a complex
CC composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1
CC (PubMed:28554894). Interacts with HDAC1 (PubMed:9702189). Interacts
CC with SIN3A, SIN3B, HDAC2, RBBP4 and NCOR1 (PubMed:9702189). Interacts
CC directly with SAMSN1 (PubMed:20478393). Interacts with HCFC1 (By
CC similarity). Interacts with SAP30BP (By similarity).
CC {ECO:0000250|UniProtKB:O75446, ECO:0000269|PubMed:20478393,
CC ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:9702189}.
CC -!- INTERACTION:
CC O88574; Q60974: Ncor1; NbExp=3; IntAct=EBI-593511, EBI-349004;
CC O88574; Q60520: Sin3a; NbExp=6; IntAct=EBI-593511, EBI-349034;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the SAP30 family. {ECO:0000305}.
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DR EMBL; AF075136; AAC26007.1; -; mRNA.
DR EMBL; AK010928; BAB27273.1; -; mRNA.
DR EMBL; AK088745; BAC40543.1; -; mRNA.
DR EMBL; CH466569; EDL28616.1; -; Genomic_DNA.
DR EMBL; BC132081; AAI32082.1; -; mRNA.
DR EMBL; BC132087; AAI32088.1; -; mRNA.
DR EMBL; AJ251216; CAC24848.1; -; Genomic_DNA.
DR CCDS; CCDS22316.1; -.
DR RefSeq; NP_068560.1; NM_021788.2.
DR PDB; 2LD7; NMR; -; A=130-220.
DR PDBsum; 2LD7; -.
DR AlphaFoldDB; O88574; -.
DR BMRB; O88574; -.
DR SMR; O88574; -.
DR BioGRID; 208559; 7.
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; O88574; -.
DR IntAct; O88574; 7.
DR MINT; O88574; -.
DR STRING; 10090.ENSMUSP00000034022; -.
DR iPTMnet; O88574; -.
DR PhosphoSitePlus; O88574; -.
DR EPD; O88574; -.
DR MaxQB; O88574; -.
DR PaxDb; O88574; -.
DR PeptideAtlas; O88574; -.
DR PRIDE; O88574; -.
DR ProteomicsDB; 256833; -.
DR Antibodypedia; 17174; 186 antibodies from 28 providers.
DR DNASU; 60406; -.
DR Ensembl; ENSMUST00000034022; ENSMUSP00000034022; ENSMUSG00000031609.
DR GeneID; 60406; -.
DR KEGG; mmu:60406; -.
DR UCSC; uc009lsu.2; mouse.
DR CTD; 8819; -.
DR MGI; MGI:1929129; Sap30.
DR VEuPathDB; HostDB:ENSMUSG00000031609; -.
DR eggNOG; ENOG502QWFH; Eukaryota.
DR GeneTree; ENSGT00390000006633; -.
DR HOGENOM; CLU_097961_0_0_1; -.
DR InParanoid; O88574; -.
DR OMA; MNGFAPE; -.
DR OrthoDB; 1520155at2759; -.
DR PhylomeDB; O88574; -.
DR TreeFam; TF324135; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR BioGRID-ORCS; 60406; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Sap30; mouse.
DR EvolutionaryTrace; O88574; -.
DR PRO; PR:O88574; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O88574; protein.
DR Bgee; ENSMUSG00000031609; Expressed in animal zygote and 252 other tissues.
DR Genevisible; O88574; MM.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016580; C:Sin3 complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0052472; P:modulation by host of symbiont transcription; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR Gene3D; 6.10.160.20; -; 1.
DR IDEAL; IID50061; -.
DR InterPro; IPR024145; His_deAcase_SAP30/SAP30L.
DR InterPro; IPR038291; SAP30_C_sf.
DR InterPro; IPR025718; SAP30_Sin3-bd.
DR InterPro; IPR025717; SAP30_zn-finger.
DR PANTHER; PTHR13286; PTHR13286; 1.
DR Pfam; PF13867; SAP30_Sin3_bdg; 1.
DR Pfam; PF13866; zf-SAP30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..220
FT /note="Histone deacetylase complex subunit SAP30"
FT /id="PRO_0000097583"
FT ZN_FING 67..115
FT /note="Atypical"
FT REGION 1..129
FT /note="Interaction with NCOR1"
FT /evidence="ECO:0000269|PubMed:9702189"
FT REGION 123..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..220
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000269|PubMed:9702189"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75446"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2LD7"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:2LD7"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:2LD7"
SQ SEQUENCE 220 AA; 23231 MW; A9D4CBDAB97BBD8C CRC64;
MNGFTPEEMS RGGDAAAAVA AVVAAAAAAA SAGNGNAAGG GAEVPGAGAV SASGPPGAAG
PGPGQLCCLR EDGERCGRAA GNASFSKRIQ KSISQKKVKI ELDKSARHLY ICDYHKNLIQ
SVRNRRKRKG SDDDGGDSPV QDIDTPEVDL YQLQVNTLRR YKRHFKLPTR PGLNKAQLVE
IVGCHFKSIP VNEKDTLTCF IYSVRNDKNK SDLKADSGVH
