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RCOR3_HUMAN
ID   RCOR3_HUMAN             Reviewed;         495 AA.
AC   Q9P2K3; B3KYA2; B4DYY7; Q5VT47; Q7L9I5; Q8N5U3; Q9NV83;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=REST corepressor 3;
GN   Name=RCOR3; Synonyms=KIAA1343;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   TISSUE=Pericardium, Teratocarcinoma, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-42.
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]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-171 AND THR-376, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-445 AND ARG-457, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
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).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-193 AND LYS-285, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: May act as a component of a corepressor complex that
CC       represses transcription. {ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9P2K3; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-743428, EBI-10171570;
CC       Q9P2K3; Q01850: CDR2; NbExp=3; IntAct=EBI-743428, EBI-1181367;
CC       Q9P2K3; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-743428, EBI-747776;
CC       Q9P2K3; Q08379: GOLGA2; NbExp=3; IntAct=EBI-743428, EBI-618309;
CC       Q9P2K3; Q14687: GSE1; NbExp=9; IntAct=EBI-743428, EBI-372619;
CC       Q9P2K3; Q9UKT9: IKZF3; NbExp=4; IntAct=EBI-743428, EBI-747204;
CC       Q9P2K3; P19012: KRT15; NbExp=5; IntAct=EBI-743428, EBI-739566;
CC       Q9P2K3; Q15323: KRT31; NbExp=3; IntAct=EBI-743428, EBI-948001;
CC       Q9P2K3; Q6A162: KRT40; NbExp=3; IntAct=EBI-743428, EBI-10171697;
CC       Q9P2K3; Q86VQ0: LCA5; NbExp=3; IntAct=EBI-743428, EBI-6658186;
CC       Q9P2K3; Q9P127: LUZP4; NbExp=3; IntAct=EBI-743428, EBI-10198848;
CC       Q9P2K3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-743428, EBI-741037;
CC       Q9P2K3; P43360: MAGEA6; NbExp=3; IntAct=EBI-743428, EBI-1045155;
CC       Q9P2K3; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-743428, EBI-10172526;
CC       Q9P2K3; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-743428, EBI-2548751;
CC       Q9P2K3; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-743428, EBI-10172876;
CC       Q9P2K3; Q9Y2I6: NINL; NbExp=4; IntAct=EBI-743428, EBI-719716;
CC       Q9P2K3; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-743428, EBI-3957793;
CC       Q9P2K3; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-743428, EBI-1105213;
CC       Q9P2K3; Q12933: TRAF2; NbExp=4; IntAct=EBI-743428, EBI-355744;
CC       Q9P2K3; P14373: TRIM27; NbExp=3; IntAct=EBI-743428, EBI-719493;
CC       Q9P2K3; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-743428, EBI-5235829;
CC       Q9P2K3; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-743428, EBI-2130429;
CC       Q9P2K3; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-743428, EBI-744794;
CC       Q9P2K3; P40222: TXLNA; NbExp=3; IntAct=EBI-743428, EBI-359793;
CC       Q9P2K3-2; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-1504830, EBI-11743294;
CC       Q9P2K3-2; X5D778: ANKRD11; NbExp=3; IntAct=EBI-1504830, EBI-17183751;
CC       Q9P2K3-2; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-1504830, EBI-11519926;
CC       Q9P2K3-2; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-1504830, EBI-10193358;
CC       Q9P2K3-2; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-1504830, EBI-11524851;
CC       Q9P2K3-2; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-1504830, EBI-711501;
CC       Q9P2K3-2; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-1504830, EBI-10175300;
CC       Q9P2K3-2; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-1504830, EBI-11522539;
CC       Q9P2K3-2; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-1504830, EBI-2349927;
CC       Q9P2K3-2; Q8TBF8: FAM81A; NbExp=3; IntAct=EBI-1504830, EBI-11993062;
CC       Q9P2K3-2; P22607: FGFR3; NbExp=3; IntAct=EBI-1504830, EBI-348399;
CC       Q9P2K3-2; A1L4K1: FSD2; NbExp=3; IntAct=EBI-1504830, EBI-5661036;
CC       Q9P2K3-2; Q5VSY0: GKAP1; NbExp=3; IntAct=EBI-1504830, EBI-743722;
CC       Q9P2K3-2; O76003: GLRX3; NbExp=3; IntAct=EBI-1504830, EBI-374781;
CC       Q9P2K3-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1504830, EBI-618309;
CC       Q9P2K3-2; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-1504830, EBI-717919;
CC       Q9P2K3-2; Q14687: GSE1; NbExp=3; IntAct=EBI-1504830, EBI-372619;
CC       Q9P2K3-2; P06396: GSN; NbExp=3; IntAct=EBI-1504830, EBI-351506;
CC       Q9P2K3-2; Q68CZ6: HAUS3; NbExp=3; IntAct=EBI-1504830, EBI-2558217;
CC       Q9P2K3-2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-1504830, EBI-2549423;
CC       Q9P2K3-2; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-1504830, EBI-10961706;
CC       Q9P2K3-2; P01112: HRAS; NbExp=3; IntAct=EBI-1504830, EBI-350145;
CC       Q9P2K3-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-1504830, EBI-7116203;
CC       Q9P2K3-2; Q8NDH6-2: ICA1L; NbExp=3; IntAct=EBI-1504830, EBI-12141931;
CC       Q9P2K3-2; Q8WYH8: ING5; NbExp=3; IntAct=EBI-1504830, EBI-488533;
CC       Q9P2K3-2; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-1504830, EBI-18398632;
CC       Q9P2K3-2; O60341: KDM1A; NbExp=6; IntAct=EBI-1504830, EBI-710124;
CC       Q9P2K3-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1504830, EBI-10975473;
CC       Q9P2K3-2; P19012: KRT15; NbExp=3; IntAct=EBI-1504830, EBI-739566;
CC       Q9P2K3-2; P05783: KRT18; NbExp=3; IntAct=EBI-1504830, EBI-297888;
CC       Q9P2K3-2; P08727: KRT19; NbExp=3; IntAct=EBI-1504830, EBI-742756;
CC       Q9P2K3-2; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-1504830, EBI-2952736;
CC       Q9P2K3-2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1504830, EBI-3044087;
CC       Q9P2K3-2; Q15323: KRT31; NbExp=3; IntAct=EBI-1504830, EBI-948001;
CC       Q9P2K3-2; O95678: KRT75; NbExp=3; IntAct=EBI-1504830, EBI-2949715;
CC       Q9P2K3-2; Q86VQ0: LCA5; NbExp=3; IntAct=EBI-1504830, EBI-6658186;
CC       Q9P2K3-2; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-1504830, EBI-12039345;
CC       Q9P2K3-2; P43360: MAGEA6; NbExp=3; IntAct=EBI-1504830, EBI-1045155;
CC       Q9P2K3-2; P23508: MCC; NbExp=3; IntAct=EBI-1504830, EBI-307531;
CC       Q9P2K3-2; Q14696: MESD; NbExp=3; IntAct=EBI-1504830, EBI-6165891;
CC       Q9P2K3-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-1504830, EBI-10172526;
CC       Q9P2K3-2; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-1504830, EBI-11522433;
CC       Q9P2K3-2; P17568: NDUFB7; NbExp=3; IntAct=EBI-1504830, EBI-1246238;
CC       Q9P2K3-2; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-1504830, EBI-10172876;
CC       Q9P2K3-2; P07196: NEFL; NbExp=3; IntAct=EBI-1504830, EBI-475646;
CC       Q9P2K3-2; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-1504830, EBI-1042642;
CC       Q9P2K3-2; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-1504830, EBI-2339674;
CC       Q9P2K3-2; A0A0S2Z615: PHF21B; NbExp=3; IntAct=EBI-1504830, EBI-16434035;
CC       Q9P2K3-2; Q96EK2-3: PHF21B; NbExp=3; IntAct=EBI-1504830, EBI-16437793;
CC       Q9P2K3-2; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-1504830, EBI-357318;
CC       Q9P2K3-2; P60891: PRPS1; NbExp=3; IntAct=EBI-1504830, EBI-749195;
CC       Q9P2K3-2; Q9NZH5-2: PTTG2; NbExp=3; IntAct=EBI-1504830, EBI-17630019;
CC       Q9P2K3-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1504830, EBI-5235340;
CC       Q9P2K3-2; Q9H668: STN1; NbExp=3; IntAct=EBI-1504830, EBI-746930;
CC       Q9P2K3-2; Q13077: TRAF1; NbExp=3; IntAct=EBI-1504830, EBI-359224;
CC       Q9P2K3-2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-1504830, EBI-2130429;
CC       Q9P2K3-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1504830, EBI-739895;
CC       Q9P2K3-2; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-1504830, EBI-12227803;
CC       Q9P2K3-2; O76024: WFS1; NbExp=3; IntAct=EBI-1504830, EBI-720609;
CC       Q9P2K3-2; Q8NA42: ZNF383; NbExp=3; IntAct=EBI-1504830, EBI-20110775;
CC       Q9P2K3-2; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-1504830, EBI-4395732;
CC       Q9P2K3-2; Q9Y649; NbExp=3; IntAct=EBI-1504830, EBI-25900580;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC       ECO:0000255|PROSITE-ProRule:PRU00624}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9P2K3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P2K3-2; Sequence=VSP_017460, VSP_017461, VSP_017462;
CC       Name=3;
CC         IsoId=Q9P2K3-3; Sequence=VSP_017460;
CC       Name=4;
CC         IsoId=Q9P2K3-4; Sequence=VSP_017460, VSP_041465, VSP_041466;
CC   -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92581.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB037764; BAA92581.1; ALT_INIT; mRNA.
DR   EMBL; AK131312; BAG54764.1; -; mRNA.
DR   EMBL; AK302664; BAG63899.1; -; mRNA.
DR   EMBL; AK001738; BAA91872.1; -; mRNA.
DR   EMBL; AL590101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL611964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC031608; AAH31608.1; -; mRNA.
DR   CCDS; CCDS31016.1; -. [Q9P2K3-1]
DR   CCDS; CCDS44312.1; -. [Q9P2K3-3]
DR   CCDS; CCDS44313.1; -. [Q9P2K3-2]
DR   CCDS; CCDS44314.1; -. [Q9P2K3-4]
DR   RefSeq; NP_001129695.1; NM_001136223.1. [Q9P2K3-3]
DR   RefSeq; NP_001129696.2; NM_001136224.2. [Q9P2K3-2]
DR   RefSeq; NP_001129697.1; NM_001136225.1. [Q9P2K3-4]
DR   RefSeq; NP_060724.1; NM_018254.3. [Q9P2K3-1]
DR   PDB; 4CZZ; X-ray; 3.00 A; B=1-495.
DR   PDBsum; 4CZZ; -.
DR   AlphaFoldDB; Q9P2K3; -.
DR   SMR; Q9P2K3; -.
DR   BioGRID; 120876; 168.
DR   CORUM; Q9P2K3; -.
DR   IntAct; Q9P2K3; 133.
DR   MINT; Q9P2K3; -.
DR   STRING; 9606.ENSP00000413929; -.
DR   BindingDB; Q9P2K3; -.
DR   ChEMBL; CHEMBL4296112; -.
DR   ChEMBL; CHEMBL4296114; -.
DR   iPTMnet; Q9P2K3; -.
DR   PhosphoSitePlus; Q9P2K3; -.
DR   BioMuta; RCOR3; -.
DR   DMDM; 90103520; -.
DR   EPD; Q9P2K3; -.
DR   jPOST; Q9P2K3; -.
DR   MassIVE; Q9P2K3; -.
DR   MaxQB; Q9P2K3; -.
DR   PaxDb; Q9P2K3; -.
DR   PeptideAtlas; Q9P2K3; -.
DR   PRIDE; Q9P2K3; -.
DR   ProteomicsDB; 83829; -. [Q9P2K3-1]
DR   ProteomicsDB; 83830; -. [Q9P2K3-2]
DR   ProteomicsDB; 83831; -. [Q9P2K3-3]
DR   ProteomicsDB; 83832; -. [Q9P2K3-4]
DR   Antibodypedia; 2380; 113 antibodies from 20 providers.
DR   DNASU; 55758; -.
DR   Ensembl; ENST00000367005.8; ENSP00000355972.4; ENSG00000117625.14. [Q9P2K3-1]
DR   Ensembl; ENST00000367006.8; ENSP00000355973.4; ENSG00000117625.14. [Q9P2K3-2]
DR   Ensembl; ENST00000419091.7; ENSP00000413929.2; ENSG00000117625.14. [Q9P2K3-3]
DR   Ensembl; ENST00000452621.6; ENSP00000398558.2; ENSG00000117625.14. [Q9P2K3-4]
DR   GeneID; 55758; -.
DR   KEGG; hsa:55758; -.
DR   MANE-Select; ENST00000419091.7; ENSP00000413929.2; NM_001136223.3; NP_001129695.1. [Q9P2K3-3]
DR   UCSC; uc001hie.4; human. [Q9P2K3-1]
DR   CTD; 55758; -.
DR   DisGeNET; 55758; -.
DR   GeneCards; RCOR3; -.
DR   HGNC; HGNC:25594; RCOR3.
DR   HPA; ENSG00000117625; Low tissue specificity.
DR   neXtProt; NX_Q9P2K3; -.
DR   OpenTargets; ENSG00000117625; -.
DR   PharmGKB; PA134917623; -.
DR   VEuPathDB; HostDB:ENSG00000117625; -.
DR   eggNOG; KOG1194; Eukaryota.
DR   GeneTree; ENSGT00940000154196; -.
DR   HOGENOM; CLU_026741_1_0_1; -.
DR   InParanoid; Q9P2K3; -.
DR   OMA; XSNQKIN; -.
DR   OrthoDB; 641792at2759; -.
DR   PhylomeDB; Q9P2K3; -.
DR   TreeFam; TF106450; -.
DR   PathwayCommons; Q9P2K3; -.
DR   SignaLink; Q9P2K3; -.
DR   BioGRID-ORCS; 55758; 12 hits in 1101 CRISPR screens.
DR   ChiTaRS; RCOR3; human.
DR   GenomeRNAi; 55758; -.
DR   Pharos; Q9P2K3; Tdark.
DR   PRO; PR:Q9P2K3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9P2K3; protein.
DR   Bgee; ENSG00000117625; Expressed in sperm and 199 other tissues.
DR   ExpressionAtlas; Q9P2K3; baseline and differential.
DR   Genevisible; Q9P2K3; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
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   CDD; cd00167; SANT; 1.
DR   DisProt; DP02408; -. [Q9P2K3-3]
DR   IDEAL; IID00589; -.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   Pfam; PF01448; ELM2; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   SMART; SM01189; ELM2; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS51293; SANT; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Isopeptide bond;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..495
FT                   /note="REST corepressor 3"
FT                   /id="PRO_0000226781"
FT   DOMAIN          1..83
FT                   /note="ELM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT   DOMAIN          84..135
FT                   /note="SANT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   DOMAIN          285..336
FT                   /note="SANT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   REGION          147..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          237..273
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        166..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..430
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..465
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         171
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         376
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         445
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         457
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   CROSSLNK        20
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        193
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        285
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1
FT                   /note="M -> MPGMMEKGPELLGKNRSANGSAKSPAGGGGSGASSTNGGLHYSEPES
FT                   GCSSDDEHDVGM (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017460"
FT   VAR_SEQ         302..378
FT                   /note="VRKYGKDFQAIADVIGNKTVGQVKNFFVNYRRRFNLEEVLQEWEAEQGTQAS
FT                   NGDASTLGEETKSASNVPSGKSTDE -> TDPTGSSDTGSITSCPIIHSNTNSPYCHSE
FT                   PASTTSSSNTACCPGSSPAASSTPAAGSVHPAPANFKSASTTSYSPC (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017461"
FT   VAR_SEQ         379..495
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017462"
FT   VAR_SEQ         382..391
FT                   /note="AQTPQAPRTL -> VCLCMEFELI (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041465"
FT   VAR_SEQ         392..495
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041466"
FT   VARIANT         42
FT                   /note="K -> R (in dbSNP:rs17856928)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_025517"
FT   HELIX           225..232
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   STRAND          233..236
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   HELIX           237..269
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   TURN            270..272
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   HELIX           275..277
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   HELIX           292..305
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   HELIX           309..316
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   HELIX           322..331
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   TURN            332..336
FT                   /evidence="ECO:0007829|PDB:4CZZ"
FT   HELIX           337..345
FT                   /evidence="ECO:0007829|PDB:4CZZ"
SQ   SEQUENCE   495 AA;  55581 MW;  2673C9DDD3C176E4 CRC64;
     MRVGAEYQAR IPEFDPGATK YTDKDNGGML VWSPYHSIPD AKLDEYIAIA KEKHGYNVEQ
     ALGMLFWHKH NIEKSLADLP NFTPFPDEWT VEDKVLFEQA FSFHGKSFHR IQQMLPDKTI
     ASLVKYYYSW KKTRSRTSLM DRQARKLANR HNQGDSDDDV EETHPMDGND SDYDPKKEAK
     KEGNTEQPVQ TSKIGLGRRE YQSLQHRHHS QRSKCRPPKG MYLTQEDVVA VSCSPNAANT
     ILRQLDMELI SLKRQVQNAK QVNSALKQKM EGGIEEFKPP ESNQKINARW TTEEQLLAVQ
     GVRKYGKDFQ AIADVIGNKT VGQVKNFFVN YRRRFNLEEV LQEWEAEQGT QASNGDASTL
     GEETKSASNV PSGKSTDEEE EAQTPQAPRT LGPSPPAPSS TPTPTAPIAT LNQPPPLLRP
     TLPAAPALHR QPPPLQQQAR FIQPRPTLNQ PPPPLIRPAN SMPPRLNPRP VLSTVGGQQP
     PSLIGIQTDS QSSLH
 
 
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