SP130_MOUSE
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 03-AUG-2022, entry version 135.
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.ENSMUSP00000136842; -.
DR iPTMnet; Q8BIH0; -.
DR PhosphoSitePlus; Q8BIH0; -.
DR EPD; Q8BIH0; -.
DR jPOST; Q8BIH0; -.
DR MaxQB; Q8BIH0; -.
DR PaxDb; Q8BIH0; -.
DR PeptideAtlas; Q8BIH0; -.
DR PRIDE; Q8BIH0; -.
DR ProteomicsDB; 257286; -. [Q8BIH0-1]
DR ProteomicsDB; 257287; -. [Q8BIH0-2]
DR ProteomicsDB; 257288; -. [Q8BIH0-3]
DR Antibodypedia; 33473; 163 antibodies from 25 providers.
DR Ensembl; ENSMUST00000235017; ENSMUSP00000157127; ENSMUSG00000024260. [Q8BIH0-1]
DR GeneID; 269003; -.
DR KEGG; mmu:269003; -.
DR UCSC; uc008eib.1; mouse. [Q8BIH0-1]
DR UCSC; uc008eie.1; mouse. [Q8BIH0-2]
DR CTD; 79595; -.
DR MGI; MGI:1919782; Sap130.
DR VEuPathDB; HostDB:ENSMUSG00000024260; -.
DR eggNOG; ENOG502QQ6P; Eukaryota.
DR GeneTree; ENSGT00440000037733; -.
DR InParanoid; Q8BIH0; -.
DR OrthoDB; 242848at2759; -.
DR PhylomeDB; Q8BIH0; -.
DR BioGRID-ORCS; 269003; 19 hits in 77 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 226 other tissues.
DR ExpressionAtlas; Q8BIH0; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
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: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 InterPro; IPR024137; His_deAcase_cplx_SAP130.
DR InterPro; IPR031963; SAP130_C.
DR PANTHER; PTHR13497; PTHR13497; 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
