ID   SP130_MOUSE             Reviewed;        1057 AA.
AC   Q8BIH0; Q6NZP5; Q6P553; Q8BID9; Q9CSU1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Histone deacetylase complex subunit SAP130;
DE   AltName: Full=130 kDa Sin3-associated polypeptide;
DE   AltName: Full=Sin3-associated polypeptide p130;
GN   Name=Sap130;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Spinal ganglion;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; 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   [3]
RP   INTERACTION WITH CLEC4E.
RX   PubMed=18776906; DOI=10.1038/ni.1651;
RA   Yamasaki S., Ishikawa E., Sakuma M., Hara H., Ogata K., Saito T.;
RT   "Mincle is an ITAM-coupled activating receptor that senses damaged cells.";
RL   Nat. Immunol. 9:1179-1188(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 AND SER-884, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
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: Acts as a transcriptional repressor. May function in the
CC       assembly and/or enzymatic activity of the mSin3A corepressor complex or
CC       in mediating interactions between the complex and other regulatory
CC       complexes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a mSin3A corepressor complex that contains SIN3A,
CC       SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2 (By similarity).
CC       Interacts (released by dead or dying cells) with CLEC4E. {ECO:0000250,
CC       ECO:0000269|PubMed:18776906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BIH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BIH0-2; Sequence=VSP_024357;
CC       Name=3;
CC         IsoId=Q8BIH0-3; Sequence=VSP_024358, VSP_024359;
CC   -!- DOMAIN: The N-terminus may interact with a transcriptional coactivator.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The C-terminus may interact with HDAC-dependent and HDAC-
CC       independent corepressors. {ECO:0000250}.
CC   -!- PTM: Acetylated. {ECO:0000250}.
CC   -!- PTM: Sumoylated with SUMO1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SAP130 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH66030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK011978; BAB27953.1; -; mRNA.
DR   EMBL; AK053675; BAC35469.1; -; mRNA.
DR   EMBL; AK084078; BAC39113.1; -; mRNA.
DR   EMBL; BC063075; AAH63075.1; -; mRNA.
DR   EMBL; BC066030; AAH66030.1; ALT_INIT; mRNA.
DR   CCDS; CCDS89207.1; -. [Q8BIH0-1]
DR   RefSeq; NP_766553.1; NM_172965.2.
DR   RefSeq; XP_006526014.1; XM_006525951.2. [Q8BIH0-1]
DR   RefSeq; XP_006526015.1; XM_006525952.3. [Q8BIH0-1]
DR   RefSeq; XP_006526017.1; XM_006525954.3.
DR   AlphaFoldDB; Q8BIH0; -.
DR   SMR; Q8BIH0; -.
DR   BioGRID; 234593; 9.
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   IntAct; Q8BIH0; 1.
DR   MINT; Q8BIH0; -.
DR   STRING; 10090.ENSMUSP00000025109; -.
DR   GlyGen; Q8BIH0; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; Q8BIH0; -.
DR   PhosphoSitePlus; Q8BIH0; -.
DR   EPD; Q8BIH0; -.
DR   jPOST; Q8BIH0; -.
DR   MaxQB; Q8BIH0; -.
DR   PaxDb; 10090-ENSMUSP00000136842; -.
DR   PeptideAtlas; Q8BIH0; -.
DR   ProteomicsDB; 257286; -. [Q8BIH0-1]
DR   ProteomicsDB; 257287; -. [Q8BIH0-2]
DR   ProteomicsDB; 257288; -. [Q8BIH0-3]
DR   Pumba; Q8BIH0; -.
DR   Antibodypedia; 33473; 184 antibodies from 25 providers.
DR   Ensembl; ENSMUST00000235017.2; ENSMUSP00000157127.2; ENSMUSG00000024260.15. [Q8BIH0-1]
DR   GeneID; 269003; -.
DR   KEGG; mmu:269003; -.
DR   UCSC; uc008eib.1; mouse. [Q8BIH0-1]
DR   UCSC; uc008eie.1; mouse. [Q8BIH0-2]
DR   AGR; MGI:1919782; -.
DR   CTD; 79595; -.
DR   MGI; MGI:1919782; Sap130.
DR   VEuPathDB; HostDB:ENSMUSG00000024260; -.
DR   eggNOG; ENOG502QQ6P; Eukaryota.
DR   GeneTree; ENSGT00440000037733; -.
DR   InParanoid; Q8BIH0; -.
DR   OrthoDB; 5401347at2759; -.
DR   PhylomeDB; Q8BIH0; -.
DR   BioGRID-ORCS; 269003; 20 hits in 83 CRISPR screens.
DR   ChiTaRS; Sap130; mouse.
DR   PRO; PR:Q8BIH0; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q8BIH0; Protein.
DR   Bgee; ENSMUSG00000024260; Expressed in animal zygote and 229 other cell types or tissues.
DR   ExpressionAtlas; Q8BIH0; baseline and differential.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR   GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal.
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; ISO:MGI.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; NAS:ComplexPortal.
DR   GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal.
DR   InterPro; IPR024137; His_deAcase_cplx_SAP130.
DR   InterPro; IPR031963; SAP130_C.
DR   PANTHER; PTHR13497; HISTONE DEACETYLASE COMPLEX SUBUNIT SAP130; 1.
DR   PANTHER; PTHR13497:SF3; HISTONE DEACETYLASE COMPLEX SUBUNIT SAP130; 1.
DR   Pfam; PF16014; SAP130_C; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..1057
FT                   /note="Histone deacetylase complex subunit SAP130"
FT                   /id="PRO_0000283737"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..1057
FT                   /note="Interactions with SIN3A and HDAC1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..737
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         206
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0E3"
FT   MOD_RES         329
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0E3"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0E3"
FT   MOD_RES         864
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0E3"
FT   MOD_RES         865
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0E3"
FT   MOD_RES         884
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        794
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0E3"
FT   CROSSLNK        873
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0E3"
FT   CROSSLNK        878
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0E3"
FT   VAR_SEQ         1..178
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024357"
FT   VAR_SEQ         340..348
FT                   /note="KTIFSTGTP -> VRTVTPPEG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024358"
FT   VAR_SEQ         349..1057
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024359"
FT   CONFLICT        594
FT                   /note="Missing (in Ref. 1; BAC35469)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1057 AA;  111228 MW;  9D963F4CD53B971A CRC64;
     MSSQQFPRLG TPSPGLSQPP SQIASSGSAG LINQVATVND EAGRDADVGT REHVGPSSSL
     PPREEKQEPV VVRPYPQVQM LPAHHAVASA TPVAVTAPPA HLTPAVPLSF SEGLMKPPPK
     PTMPSRPIAP APPSTMSLPP KVPGQVTVTM ESSIPQASAI PVATISGQQG HPSNLHHIMT
     TNVQMSIIRS NAPGPPLHIG ASHLPRGAAA AAVMSSSKVT TVLRPTSQLP NAATAQPAVQ
     HLIHQPIQSR PPVTTSSTIP PAVVATVSAT RAQSPVITTT AAHAADSTLS RPTLSIQHPP
     SAAISIQRPA QSRDVTTRIT LPSHPALGTP KQQLHTMAQK TIFSTGTPVA AATVAPILAT
     NTLPSTTTAG SVSHTQAPTS TIVTMTMPSH SSHATAVTTS NIPVAKVVPQ QITHTSPRIQ
     PDYPPERSSL IPISGHRASP NPVAMETRND NRPSVPVQFQ YFLPTYPPSA YPLAAHTYTP
     ITSSVSTIRQ YPVSAQAPNS TITAQTGVGV ASTVHLNPMQ LMTVDASHAR HIQGIQPAPI
     STQGIQPAPI GTSGIQPAPI GTPGIHSAAP INTQGLQPAA MANQQPQPEG KTSAVVLADG
     ATIVANPISN PFSAAPAATT VVQTHSQSAS TNTPAQGSSP RPSILRKKPA TDGMAVRKTL
     LPPQPPDVAT PRVESSMRSA SGSPRPAGAK PKSEVHVSIA TPVTVSLETI SNQNAEQPTV
     AVPPTAQQPP PTIPSMIAAA SPPSQPAIAL STIPGAVPVT PPITTIAATP TLSAPVGGTP
     STVLGPPVPE IKVKEEAEPV DITRPVSTVP PLATNTVSPS LALLASNLSM PPSDLPPGAS
     PRKKPRKQQH VISTEEGDMM ETNSTDDEKS AAKSLLVKAE KRKSPPKEYI DEEGVRYVPV
     RPRPPITLLR HYRNPWKAAY HHFQRYSDVR VKEEKKAMLQ EIANQKGVSC RAQGWKVHLC
     AAQLLQLTNL EHDVYERLTN LQEGIIPKKK AATDDDLHRI NELIQGNMQR CKLVMDQISE
     ARDSMLKVLD HKDRVLKLLN KNGTVKKVSK LKRKEKV
//