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RCOR3_MOUSE
ID   RCOR3_MOUSE             Reviewed;         451 AA.
AC   Q6PGA0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=REST corepressor 3;
GN   Name=Rcor3;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Adrenal gland;
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] OF 38-451 (ISOFORM 1).
RC   TISSUE=Mammary tumor;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-227, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, 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   [4]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-401 AND ARG-413, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May act as a component of a corepressor complex that
CC       represses transcription. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC       ECO:0000255|PROSITE-ProRule:PRU00624}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PGA0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PGA0-2; Sequence=VSP_017463, VSP_017464;
CC   -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57141.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AK135612; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK135612; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC057141; AAH57141.2; ALT_INIT; mRNA.
DR   CCDS; CCDS69995.1; -. [Q6PGA0-1]
DR   CCDS; CCDS69996.1; -. [Q6PGA0-2]
DR   RefSeq; NP_001277207.1; NM_001290278.1. [Q6PGA0-2]
DR   RefSeq; NP_659063.3; NM_144814.3. [Q6PGA0-1]
DR   AlphaFoldDB; Q6PGA0; -.
DR   SMR; Q6PGA0; -.
DR   BioGRID; 229560; 2.
DR   IntAct; Q6PGA0; 1.
DR   STRING; 10090.ENSMUSP00000073004; -.
DR   iPTMnet; Q6PGA0; -.
DR   PhosphoSitePlus; Q6PGA0; -.
DR   EPD; Q6PGA0; -.
DR   MaxQB; Q6PGA0; -.
DR   PaxDb; Q6PGA0; -.
DR   PRIDE; Q6PGA0; -.
DR   ProteomicsDB; 300327; -. [Q6PGA0-1]
DR   ProteomicsDB; 300328; -. [Q6PGA0-2]
DR   Antibodypedia; 2380; 113 antibodies from 20 providers.
DR   DNASU; 214742; -.
DR   Ensembl; ENSMUST00000073279; ENSMUSP00000073004; ENSMUSG00000037395. [Q6PGA0-1]
DR   Ensembl; ENSMUST00000110849; ENSMUSP00000106473; ENSMUSG00000037395. [Q6PGA0-2]
DR   GeneID; 214742; -.
DR   KEGG; mmu:214742; -.
DR   UCSC; uc007edh.2; mouse. [Q6PGA0-1]
DR   UCSC; uc007edi.2; mouse. [Q6PGA0-2]
DR   CTD; 55758; -.
DR   MGI; MGI:2441920; Rcor3.
DR   VEuPathDB; HostDB:ENSMUSG00000037395; -.
DR   eggNOG; KOG1194; Eukaryota.
DR   GeneTree; ENSGT00940000154196; -.
DR   InParanoid; Q6PGA0; -.
DR   PhylomeDB; Q6PGA0; -.
DR   TreeFam; TF106450; -.
DR   BioGRID-ORCS; 214742; 3 hits in 55 CRISPR screens.
DR   ChiTaRS; Rcor3; mouse.
DR   PRO; PR:Q6PGA0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q6PGA0; protein.
DR   Bgee; ENSMUSG00000037395; Expressed in spermatocyte and 69 other tissues.
DR   ExpressionAtlas; Q6PGA0; baseline and differential.
DR   Genevisible; Q6PGA0; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IPI:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   Pfam; PF01448; ELM2; 1.
DR   SMART; SM01189; ELM2; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..451
FT                   /note="REST corepressor 3"
FT                   /id="PRO_0000226782"
FT   DOMAIN          55..139
FT                   /note="ELM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT   DOMAIN          140..191
FT                   /note="SANT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          293..329
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        222..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..386
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..421
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         401
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         413
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2K3"
FT   CROSSLNK        249
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2K3"
FT   VAR_SEQ         338..434
FT                   /note="AQTPQAPRTLGPSPPAPSSTPTPTVPIATLNQPPPLLRPTLPAAPALHRQPP
FT                   PLQQQARFIQPRPTLNQPPPPLIRPANSMPPRLNPRPVLTTVGGQ -> SNQKINARWT
FT                   TEEQLLAVQGTDPTGSSDSGSITSCPIIHSNTNSPHCHSEPASTTSSSNTACRPCSSPT
FT                   TSSTPAAGSVHPAPANSQSASSTSHSPC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017463"
FT   VAR_SEQ         435..451
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017464"
SQ   SEQUENCE   451 AA;  49779 MW;  FE0A068325A06C82 CRC64;
     MPGMMEKGPE LLGKSRSANG GAKSPAGGGG SSANGGLHFS EPESGCSSDD EHGDVGMRVG
     AEYQARIPEF DPGATKYTDK DNGGMLVWSP YHSIPDAKLD EYIAIAKEKH GYNVEQALGM
     LFWHKHNIEK SLADLPNFTP FPDEWTVEDK VLFEQAFSFH GKSFHRIQQM LPDKTIASLV
     KYYYSWKKTR SRTSLMDRQA RKLANRHNQG DSDDDVEEAH PMDGNDSDYD PKKEAKREGN
     ADQPVQTSKI GLGRREYQSL QHRHHSQRSK CRPPKGMYLT QEDVVAVSCS PNAANTILRQ
     LDMELISLKR QVQNAKQVNS ALKQKMEGGI EEFKPPEAQT PQAPRTLGPS PPAPSSTPTP
     TVPIATLNQP PPLLRPTLPA APALHRQPPP LQQQARFIQP RPTLNQPPPP LIRPANSMPP
     RLNPRPVLTT VGGQQPPSLI GIQTDSQPSL H
 
 
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