LCOR_HUMAN
ID LCOR_HUMAN Reviewed; 433 AA.
AC Q96JN0; D3DR47; Q5VW16; Q7Z723; Q86T32; Q86T33; Q8N3L6; Q8N655; Q9H945;
AC Q9Y457;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ligand-dependent corepressor;
DE Short=LCoR;
DE AltName: Full=Mblk1-related protein 2;
GN Name=LCOR {ECO:0000312|HGNC:HGNC:29503};
GN Synonyms=C10orf12 {ECO:0000312|HGNC:HGNC:29503},
GN KIAA1795 {ECO:0000312|EMBL:BAB47424.1}, MLR2;
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=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Bone marrow, Brain, and Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lung, and Pancreas;
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 [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [7]
RP FUNCTION, INTERACTION WITH CTBP1; ESR1; ESR2; HDAC3 AND HDAC6, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF 56-LEU-LEU-57, AND TISSUE SPECIFICITY.
RX PubMed=12535528; DOI=10.1016/s1097-2765(03)00014-5;
RA Fernandes I., Bastien Y., Wai T., Nygard K., Lin R., Cormier O., Lee H.S.,
RA Eng F., Bertos N.R., Pelletier N., Mader S., Han V.K.M., Yang X.-J.,
RA White J.H.;
RT "Ligand-dependent nuclear receptor corepressor LCoR functions by histone
RT deacetylase-dependent and -independent mechanisms.";
RL Mol. Cell 11:139-150(2003).
RN [8]
RP IDENTIFICATION IN A COREPRESSOR COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12700765; DOI=10.1038/nature01550;
RA Shi Y., Sawada J., Sui G., Affar E.B., Whetstine J.R., Lan F., Ogawa H.,
RA Luke M.P.-S., Nakatani Y., Shi Y.;
RT "Coordinated histone modifications mediated by a CtBP co-repressor
RT complex.";
RL Nature 422:735-738(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1077 (ISOFORM 3), AND
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-249,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792; SER-1048 AND SER-1274
RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583 (ISOFORM 3), AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-249,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583 AND SER-605 (ISOFORM 3),
RP AND 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 [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-1214 AND LYS-1219 (ISOFORM 3),
RP AND 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254 AND LYS-414, SUMOYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-345; LYS-391; LYS-543 AND LYS-976 (ISOFORM
RP 3), AND 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).
RN [18]
RP STRUCTURE BY NMR OF 343-405.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the HTH domain of human LCOR protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May act as transcription activator that binds DNA elements
CC with the sequence 5'-CCCTATCGATCGATCTCTACCT-3' (By similarity).
CC Repressor of ligand-dependent transcription activation by target
CC nuclear receptors. Repressor of ligand-dependent transcription
CC activation by ESR1, ESR2, NR3C1, PGR, RARA, RARB, RARG, RXRA and VDR.
CC {ECO:0000250, ECO:0000269|PubMed:12535528}.
CC -!- SUBUNIT: Interacts with ESR1 and ESR2 in the presence of estradiol.
CC Interacts with CTBP1, HDAC3 and HDAC6. Component of a large corepressor
CC complex that contains about 20 proteins, including CTBP1, CTBP2, HDAC1
CC and HDAC2. {ECO:0000269|PubMed:12535528, ECO:0000269|PubMed:12700765}.
CC -!- INTERACTION:
CC Q96JN0; Q13363: CTBP1; NbExp=8; IntAct=EBI-746045, EBI-908846;
CC Q96JN0; P56545: CTBP2; NbExp=5; IntAct=EBI-746045, EBI-741533;
CC Q96JN0; P56545-3: CTBP2; NbExp=3; IntAct=EBI-746045, EBI-10171902;
CC Q96JN0; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-746045, EBI-10174566;
CC Q96JN0; Q08379: GOLGA2; NbExp=3; IntAct=EBI-746045, EBI-618309;
CC Q96JN0; Q13077: TRAF1; NbExp=3; IntAct=EBI-746045, EBI-359224;
CC Q96JN0-2; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-10961483, EBI-517623;
CC Q96JN0-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10961483, EBI-739624;
CC Q96JN0-2; Q92753-1: RORB; NbExp=3; IntAct=EBI-10961483, EBI-18560266;
CC Q96JN0-2; Q13077: TRAF1; NbExp=3; IntAct=EBI-10961483, EBI-359224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320,
CC ECO:0000269|PubMed:12535528}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96JN0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JN0-2; Sequence=VSP_018585, VSP_018586;
CC Name=3;
CC IsoId=Q96JN0-3; Sequence=VSP_058760;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12535528}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24315.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB47424.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB058698; BAB47424.1; ALT_INIT; mRNA.
DR EMBL; AL834245; CAD38921.2; -; mRNA.
DR EMBL; AL832106; CAD91159.1; -; mRNA.
DR EMBL; AL832044; CAD91160.1; -; mRNA.
DR EMBL; AL049938; CAB43214.1; -; mRNA.
DR EMBL; AL442123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49963.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49965.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49966.1; -; Genomic_DNA.
DR EMBL; BC024315; AAH24315.1; ALT_INIT; mRNA.
DR EMBL; BC053359; AAH53359.1; -; mRNA.
DR EMBL; AK023084; BAB14396.1; ALT_INIT; mRNA.
DR CCDS; CCDS53561.1; -. [Q96JN0-2]
DR CCDS; CCDS7451.1; -. [Q96JN0-1]
DR CCDS; CCDS86132.1; -. [Q96JN0-3]
DR PIR; T08672; T08672.
DR RefSeq; NP_001164236.1; NM_001170765.1. [Q96JN0-1]
DR RefSeq; NP_001164237.1; NM_001170766.1. [Q96JN0-2]
DR RefSeq; NP_001333445.1; NM_001346516.1. [Q96JN0-3]
DR RefSeq; NP_115816.2; NM_032440.3. [Q96JN0-1]
DR RefSeq; XP_016872275.1; XM_017016786.1.
DR RefSeq; XP_016872276.1; XM_017016787.1.
DR RefSeq; XP_016872277.1; XM_017016788.1.
DR PDB; 2COB; NMR; -; A=343-405.
DR PDB; 6V3X; X-ray; 1.70 A; B=98-103.
DR PDB; 6V3Y; X-ray; 1.63 A; B=5-9.
DR PDBsum; 2COB; -.
DR PDBsum; 6V3X; -.
DR PDBsum; 6V3Y; -.
DR AlphaFoldDB; Q96JN0; -.
DR SMR; Q96JN0; -.
DR BioGRID; 117579; 53.
DR BioGRID; 124093; 79.
DR CORUM; Q96JN0; -.
DR ELM; Q96JN0; -.
DR IntAct; Q96JN0; 86.
DR MINT; Q96JN0; -.
DR STRING; 9606.ENSP00000360138; -.
DR GlyGen; Q96JN0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96JN0; -.
DR PhosphoSitePlus; Q96JN0; -.
DR BioMuta; LCOR; -.
DR DMDM; 68565212; -.
DR EPD; Q96JN0; -.
DR jPOST; Q96JN0; -.
DR MassIVE; Q96JN0; -.
DR MaxQB; Q96JN0; -.
DR PaxDb; Q96JN0; -.
DR PeptideAtlas; Q96JN0; -.
DR PRIDE; Q96JN0; -.
DR ProteomicsDB; 72131; -.
DR ProteomicsDB; 76989; -. [Q96JN0-1]
DR ProteomicsDB; 76990; -. [Q96JN0-2]
DR Antibodypedia; 30781; 231 antibodies from 25 providers.
DR DNASU; 26148; -.
DR DNASU; 84458; -.
DR Ensembl; ENST00000356016.7; ENSP00000348298.2; ENSG00000196233.14. [Q96JN0-1]
DR Ensembl; ENST00000371097.8; ENSP00000360138.3; ENSG00000196233.14. [Q96JN0-1]
DR Ensembl; ENST00000371103.8; ENSP00000360144.3; ENSG00000196233.14. [Q96JN0-1]
DR Ensembl; ENST00000421806.4; ENSP00000490116.2; ENSG00000196233.14. [Q96JN0-3]
DR Ensembl; ENST00000540664.6; ENSP00000443431.1; ENSG00000196233.14. [Q96JN0-2]
DR Ensembl; ENST00000675471.1; ENSP00000502633.1; ENSG00000196233.14. [Q96JN0-1]
DR Ensembl; ENST00000675537.1; ENSP00000501560.1; ENSG00000196233.14. [Q96JN0-1]
DR Ensembl; ENST00000675971.1; ENSP00000501639.1; ENSG00000196233.14. [Q96JN0-1]
DR GeneID; 84458; -.
DR KEGG; hsa:84458; -.
DR MANE-Select; ENST00000421806.4; ENSP00000490116.2; NM_001346516.2; NP_001333445.1. [Q96JN0-3]
DR UCSC; uc001kmr.4; human. [Q96JN0-1]
DR CTD; 84458; -.
DR DisGeNET; 84458; -.
DR GeneCards; LCOR; -.
DR HGNC; HGNC:29503; LCOR.
DR HPA; ENSG00000196233; Low tissue specificity.
DR MIM; 607698; gene.
DR neXtProt; NX_Q96JN0; -.
DR OpenTargets; ENSG00000196233; -.
DR PharmGKB; PA145148487; -.
DR VEuPathDB; HostDB:ENSG00000196233; -.
DR eggNOG; KOG4565; Eukaryota.
DR GeneTree; ENSGT00940000154965; -.
DR HOGENOM; CLU_040042_0_0_1; -.
DR InParanoid; Q96JN0; -.
DR OMA; IYVQSKM; -.
DR OrthoDB; 134164at2759; -.
DR PhylomeDB; Q96JN0; -.
DR TreeFam; TF319589; -.
DR TreeFam; TF332137; -.
DR PathwayCommons; Q96JN0; -.
DR SignaLink; Q96JN0; -.
DR BioGRID-ORCS; 84458; 25 hits in 1108 CRISPR screens.
DR EvolutionaryTrace; Q96JN0; -.
DR GeneWiki; LCOR; -.
DR GenomeRNAi; 84458; -.
DR Pharos; Q96JN0; Tbio.
DR PRO; PR:Q96JN0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96JN0; protein.
DR Bgee; ENSG00000196233; Expressed in secondary oocyte and 189 other tissues.
DR ExpressionAtlas; Q96JN0; baseline and differential.
DR Genevisible; Q96JN0; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:ARUK-UCL.
DR GO; GO:1990226; F:histone methyltransferase binding; IPI:ARUK-UCL.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:ARUK-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:ARUK-UCL.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ARUK-UCL.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007889; HTH_Psq.
DR Pfam; PF05225; HTH_psq; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50960; HTH_PSQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..433
FT /note="Ligand-dependent corepressor"
FT /id="PRO_0000236807"
FT DOMAIN 340..392
FT /note="HTH psq-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT DNA_BIND 368..388
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 53..57
FT /note="Interaction with nuclear receptors"
FT MOTIF 339..345
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 66..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 112..433
FT /note="RPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEEL
FT LSRNQLSTAASLGPSGLQNHGQHLILSREASWAKPHYEFNLSRMKFRGNGALSNISDLP
FT FLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMG
FT SQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPR
FT KKRGRYRQYNSEILEEAISVVMSGKMSVSKAQSIYGIPHSTLEYKVKERLGTLKNPPKK
FT KMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE -> ENSTEAKAVDSNNQSKSPLEK
FT FMVKLCTHHQKQFIRVLNDLYTESQPGTEDLQPSDSGAMDVSTCNAGCAQLSTKHKEKD
FT ALCLDMKSSASVDLFVDSSDSHSPLHLTEQTPKKPPPEINPVDGRENALTVVQKDSSEL
FT PTTKSNSINSSSVDSFTPGYLTASNCSSVNFHHIPKILEGQTTGQEQDTNVNICEDGKD
FT HMQSSALVESLITVKMAAENSEEGNTCIIPQRNLFKALSEEAWNSGFMGNSSRTADKEN
FT TLQCPKTPLRQDLEANEQDARPKQENHLHSLGRNKVGYHLHPSDKGQFDHSKDGWLGPG
FT PMPAVHKAANGHSRTKMISTSIKTARKSKRASGLRINDYDNQCDVVYISQPITECHFEN
FT QKSILSSRKTARKSTRGYFFNGDCCELPTVRTLARNLHSQEKASCSALASEAVFTPKQT
FT LTIPAPRHTVDVQLPREDNPEEPSKEITSHEEGGGDVSPRKEPQEPEVCPTKIKPNLSS
FT SPRSEETTASSLVWPLPAHLPEEDLPEGGSTVSAPTASGMSSPEHNQPPVALLDTEEMS
FT VPQDCHLLPSTESFSGGVSEDVISRPHSPPEIVSREESPQCSENQSSPMGLEPPMSLGK
FT AEDNQSISAEVESGDTQELNVDPLLKESSTFTDENPSETEESEAAGGIGKLEGEDGDVK
FT CLSEKDTYDTSIDSLEENLDKKKKGKKFPEASDRCLRSQLSDSSSADRCLRNQSSDSSS
FT ACLEIKVPKNPSAKRSKKEGHPGGTTPKGLLPDSFHTETLEDTEKPSVNERPSEKDAEQ
FT EGEGGGIITRQTLKNMLDKEVKELRGEIFPSRDPITTAGQPLPGERLEIYVQSKMDEKN
FT AHIPSESIACKRDPEQAKEEPGHIPTQHVEEAVNEVDNENTQQKDDESDAPCSSLGLSS
FT SGSGDAARAPKSVPRPKRLTSSTYNLRHAHSLGSLDASKVTSEKEAAQVNPIMPKENGA
FT SESGDPLDEDDVDTVVDEQPKFMEWCAEEENQELIANFNAQYMKVQKGWIQLEKEGQPT
FT PRARNKSDKLKEIWKSKKRSRKCRSSLESQKCSPVQMLFMTNFKLSNVCKWFLETTETR
FT SLVIVKKLNTRLPGDVPPVKHPLQKYAPSSLYPSSLQAERLKKHLKKFPGATPAKNNWK
FT MQKLWAKFRENPDQVEPEDGSDVSPGPNSEDSIEEVKEDRNSHPPANLPTPASTRILRK
FT YSNIRGKLRAQQRLIKNEKMECPDALAVESKPSRKSVCINPLMSPKLALQVDADGFPVK
FT PKSTEGMKGRKGKQVSEILPKAEVQSKRKRTEGSSPPDSKNKGPTVKASKEKHADGATK
FT TPAAKRPAARDRSSQPPKKTSLKENKVKIPKKSAGKSCPPSRKEKENTNKRPSQSIASE
FT TLTKPAKQKGAGESSSRPQKATNRKQSSGKTRARPSTKTPESSAAQRKRKLKAKLDCSH
FT SKRRRLDAK (in isoform 3)"
FT /id="VSP_058760"
FT VAR_SEQ 405..406
FT /note="RS -> SG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018585"
FT VAR_SEQ 407..433
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018586"
FT MUTAGEN 56..57
FT /note="LL->AA: Loss of estradiol-dependent interaction with
FT ESR1 and ESR2."
FT /evidence="ECO:0000269|PubMed:12535528"
FT CONFLICT 6
FT /note="Q -> P (in Ref. 2; CAD91159)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="S -> P (in Ref. 2; CAD38921)"
FT /evidence="ECO:0000305"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:2COB"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:2COB"
FT HELIX 379..389
FT /evidence="ECO:0007829|PDB:2COB"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:2COB"
FT MOD_RES Q96JN0-3:583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES Q96JN0-3:605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES Q96JN0-3:792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q96JN0-3:1048
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q96JN0-3:1077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q96JN0-3:1214
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q96JN0-3:1219
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q96JN0-3:1274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK Q96JN0-3:345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q96JN0-3:391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q96JN0-3:543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK Q96JN0-3:976
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT Q96JN0-3:922
FT /note="E -> G (in Ref. 6; BAB14396)"
FT /evidence="ECO:0000305"
FT CONFLICT Q96JN0-3:1209
FT /note="D -> G (in Ref. 6; BAB14396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 47007 MW; 5F934FE687417740 CRC64;
MQRMIQQFAA EYTSKNSSTQ DPSQPNSTKN QSLPKASPVT TSPTAATTQN PVLSKLLMAD
QDSPLDLTVR KSQSEPSEQD GVLDLSTKKS PCAGSTSLSH SPGCSSTQGN GRPGRPSQYR
PDGLRSGDGV PPRSLQDGTR EGFGHSTSLK VPLARSLQIS EELLSRNQLS TAASLGPSGL
QNHGQHLILS REASWAKPHY EFNLSRMKFR GNGALSNISD LPFLAENSAF PKMALQAKQD
GKKDVSHSSP VDLKIPQVRG MDLSWESRTG DQYSYSSLVM GSQTESALSK KLRAILPKQS
RKSMLDAGPD SWGSDAEQST SGQPYPTSDQ EGDPGSKQPR KKRGRYRQYN SEILEEAISV
VMSGKMSVSK AQSIYGIPHS TLEYKVKERL GTLKNPPKKK MKLMRSEGPD VSVKIELDPQ
GEAAQSANES KNE
