BCOR_HUMAN
ID BCOR_HUMAN Reviewed; 1755 AA.
AC Q6W2J9; D3DWB3; D3DWB4; Q29RF6; Q6P4B6; Q7Z2K7; Q8TEB4; Q96DB3; Q9H232;
AC Q9H233; Q9HCJ7; Q9NXF2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=BCL-6 corepressor;
DE Short=BCoR;
GN Name=BCOR; Synonyms=KIAA1575;
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 [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH
RP BCL6; HDAC1; HDAC3 AND HDAC5, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Frontal cortex;
RX PubMed=10898795;
RA Huynh K.D., Fischle W., Verdin E., Bardwell V.J.;
RT "BCoR, a novel corepressor involved in BCL-6 repression.";
RL Genes Dev. 14:1810-1823(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT MCOPS2
RP LEU-85.
RX PubMed=15004558; DOI=10.1038/ng1321;
RA Ng D., Thakker N., Corcoran C.M., Donnai D., Perveen R., Schneider A.,
RA Hadley D.W., Tifft C., Zhang L., Wilkie A.O., van der Smagt J.J.,
RA Gorlin R.J., Burgess S.M., Bardwell V.J., Black G.C.M., Biesecker L.G.;
RT "Oculofaciocardiodental and Lenz microphthalmia syndromes result from
RT distinct classes of mutations in BCOR.";
RL Nat. Genet. 36:411-416(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
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 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1395-1755 (ISOFORM 1).
RC TISSUE=Liver, Lymph, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1755 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1328-1755.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP INTERACTION WITH PCGF1 AND KDM2B, AND IDENTIFICATION IN A COMPLEX WITH
RP RYBP; PCGF1; RING1; RNF2; KDM2B AND SKP1.
RX PubMed=16943429; DOI=10.1128/mcb.00630-06;
RA Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.;
RT "Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex
RT that is recruited to BCL6 targets.";
RL Mol. Cell. Biol. 26:6880-6889(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND SER-1410, 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 [10]
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 [11]
RP FUNCTION.
RX PubMed=19578371; DOI=10.1038/ncb1913;
RA Fan Z., Yamaza T., Lee J.S., Yu J., Wang S., Fan G., Shi S., Wang C.-Y.;
RT "BCOR regulates mesenchymal stem cell function by epigenetic mechanisms.";
RL Nat. Cell Biol. 11:1002-1009(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1139, AND IDENTIFICATION BY
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-392, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-340; SER-365;
RP SER-367 AND SER-423, 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, 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 [17]
RP FUNCTION AS COREPRESSOR, INTERACTION WITH BCL6, AND IDENTIFICATION IN A
RP COMPLEX WITH BCL6 AND SMRT.
RX PubMed=23911289; DOI=10.1016/j.celrep.2013.06.016;
RA Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D.,
RA Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M.,
RA Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W.,
RA Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.;
RT "A hybrid mechanism of action for BCL6 in B cells defined by formation of
RT functionally distinct complexes at enhancers and promoters.";
RL Cell Rep. 4:578-588(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-1139; SER-1290 AND
RP SER-1410, 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PCGF1.
RX PubMed=26687479; DOI=10.1038/srep18388;
RA Oliviero G., Munawar N., Watson A., Streubel G., Manning G., Bardwell V.,
RA Bracken A.P., Cagney G.;
RT "The variant Polycomb Repressor Complex 1 component PCGF1 interacts with a
RT pluripotency sub-network that includes DPPA4, a regulator of
RT embryogenesis.";
RL Sci. Rep. 5:18388-18388(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-786; LYS-872; LYS-1256 AND
RP LYS-1413, 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 [21]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1634-1748 IN COMPLEX WITH PCGF1,
RP INTERACTION WITH PCGF1, AND MUTAGENESIS OF LEU-1706.
RX PubMed=23523425; DOI=10.1016/j.str.2013.02.013;
RA Junco S.E., Wang R., Gaipa J.C., Taylor A.B., Schirf V., Gearhart M.D.,
RA Bardwell V.J., Demeler B., Hart P.J., Kim C.A.;
RT "Structure of the polycomb group protein PCGF1 in complex with BCOR reveals
RT basis for binding selectivity of PCGF homologs.";
RL Structure 21:665-671(2013).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 498-514 IN COMPLEX WITH BCL6,
RP FUNCTION, AND MUTAGENESIS OF SER-507; SER-508; TRP-509 AND VAL-511.
RX PubMed=18280243; DOI=10.1016/j.molcel.2007.12.026;
RA Ghetu A.F., Corcoran C.M., Cerchietti L., Bardwell V.J., Melnick A.,
RA Prive G.G.;
RT "Structure of a BCOR corepressor peptide in complex with the BCL6 BTB
RT domain dimer.";
RL Mol. Cell 29:384-391(2008).
CC -!- FUNCTION: Transcriptional corepressor. May specifically inhibit gene
CC expression when recruited to promoter regions by sequence-specific DNA-
CC binding proteins such as BCL6 and MLLT3. This repression may be
CC mediated at least in part by histone deacetylase activities which can
CC associate with this corepressor. Involved in the repression of TFAP2A;
CC impairs binding of BCL6 and KDM2B to TFAP2A promoter regions. Via
CC repression of TFAP2A acts as a negative regulator of osteo-dentiogenic
CC capacity in adult stem cells; the function implies inhibition of
CC methylation on histone H3 'Lys-4' (H3K4me3) and 'Lys-36' (H3K36me2).
CC {ECO:0000269|PubMed:10898795, ECO:0000269|PubMed:15004558,
CC ECO:0000269|PubMed:18280243, ECO:0000269|PubMed:19578371,
CC ECO:0000269|PubMed:23911289}.
CC -!- SUBUNIT: Interacts with BCL6; the interaction is direct
CC (PubMed:10898795). Forms ternary complexes with BCL6 and SMRT/NCOR2 on
CC selected target genes promoters; potently repress expression
CC (PubMed:23911289, PubMed:18280243). Can interact with HDAC1, HDAC3 and
CC HDAC5 (PubMed:10898795). Interacts with PCGF1; the interaction is
CC direct (PubMed:16943429, PubMed:23523425, PubMed:26687479). Interacts
CC with KDM2B. Component of an approximately 800 kDa repressive BCOR
CC complex at least composed of BCOR, RYBP, PCGF1, RING1, RNF2/RING2,
CC KDM2B and SKP1 (PubMed:16943429). Interacts with CPNE4 (via VWFA
CC domain) (By similarity). Isoform 1 may interact with MLLT3/AF9 (By
CC similarity). {ECO:0000250|UniProtKB:Q8CGN4,
CC ECO:0000269|PubMed:10898795, ECO:0000269|PubMed:16943429,
CC ECO:0000269|PubMed:18280243, ECO:0000269|PubMed:23523425,
CC ECO:0000269|PubMed:23911289, ECO:0000269|PubMed:26687479}.
CC -!- INTERACTION:
CC Q6W2J9; Q9HC52: CBX8; NbExp=9; IntAct=EBI-950027, EBI-712912;
CC Q6W2J9; Q8NHM5: KDM2B; NbExp=5; IntAct=EBI-950027, EBI-3955564;
CC Q6W2J9; Q9BSM1: PCGF1; NbExp=13; IntAct=EBI-950027, EBI-749901;
CC Q6W2J9; Q93009: USP7; NbExp=3; IntAct=EBI-950027, EBI-302474;
CC Q6W2J9-1; P42568: MLLT3; NbExp=2; IntAct=EBI-16028932, EBI-716132;
CC Q6W2J9-1; Q9BSM1-1: PCGF1; NbExp=7; IntAct=EBI-16028932, EBI-16041863;
CC Q6W2J9-4; P41227: NAA10; NbExp=3; IntAct=EBI-10208579, EBI-747693;
CC Q6W2J9-4; Q3KNV8: PCGF3; NbExp=3; IntAct=EBI-10208579, EBI-2339807;
CC Q6W2J9-4; Q86SE9: PCGF5; NbExp=3; IntAct=EBI-10208579, EBI-2827999;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10898795}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long;
CC IsoId=Q6W2J9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6W2J9-2; Sequence=VSP_012557;
CC Name=3; Synonyms=Short;
CC IsoId=Q6W2J9-3; Sequence=VSP_012554, VSP_012556;
CC Name=4;
CC IsoId=Q6W2J9-4; Sequence=VSP_012555, VSP_012557;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10898795}.
CC -!- DISEASE: Microphthalmia, syndromic, 2 (MCOPS2) [MIM:300166]: A very
CC rare multiple congenital anomaly syndrome characterized by eye
CC anomalies (congenital cataract, microphthalmia, or secondary glaucoma),
CC facial abnormalities (long narrow face, high nasal bridge, pointed nose
CC with cartilages separated at the tip, cleft palate, or submucous cleft
CC palate), cardiac anomalies (atrial septal defect, ventricular septal
CC defect, or floppy mitral valve) and dental abnormalities (canine
CC radiculomegaly, delayed dentition, oligodontia, persistent primary
CC teeth, or variable root length). Microphthalmia is a disorder of eye
CC formation, ranging from small size of a single eye to complete
CC bilateral absence of ocular tissues (anophthalmia). In many cases,
CC microphthalmia/anophthalmia occurs in association with syndromes that
CC include non-ocular abnormalities. {ECO:0000269|PubMed:15004558}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the BCOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63536.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Presence of complementary strand sequence in the clone.; Evidence={ECO:0000305};
CC Sequence=BAA91061.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAB13401.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB85037.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF317391; AAG41429.1; -; mRNA.
DR EMBL; AF317392; AAG41430.1; -; mRNA.
DR EMBL; AY316592; AAR08265.1; -; mRNA.
DR EMBL; AB046795; BAB13401.2; ALT_INIT; mRNA.
DR EMBL; CH471141; EAW59425.1; -; Genomic_DNA.
DR EMBL; CH471141; EAW59427.1; -; Genomic_DNA.
DR EMBL; CH471141; EAW59428.1; -; Genomic_DNA.
DR EMBL; CH471141; EAW59430.1; -; Genomic_DNA.
DR EMBL; BC009675; AAH09675.2; -; mRNA.
DR EMBL; BC063536; AAH63536.1; ALT_SEQ; mRNA.
DR EMBL; BC114220; AAI14221.1; -; mRNA.
DR EMBL; AK000292; BAA91061.1; ALT_SEQ; mRNA.
DR EMBL; AK074286; BAB85037.1; ALT_FRAME; mRNA.
DR CCDS; CCDS14250.1; -. [Q6W2J9-2]
DR CCDS; CCDS48092.1; -. [Q6W2J9-4]
DR CCDS; CCDS48093.1; -. [Q6W2J9-1]
DR RefSeq; NP_001116855.1; NM_001123383.1. [Q6W2J9-2]
DR RefSeq; NP_001116856.1; NM_001123384.1. [Q6W2J9-4]
DR RefSeq; NP_001116857.1; NM_001123385.1. [Q6W2J9-1]
DR RefSeq; NP_060215.4; NM_017745.5. [Q6W2J9-2]
DR RefSeq; XP_005272673.1; XM_005272616.1. [Q6W2J9-1]
DR RefSeq; XP_005272675.1; XM_005272618.3. [Q6W2J9-1]
DR RefSeq; XP_005272677.1; XM_005272620.3. [Q6W2J9-4]
DR RefSeq; XP_006724599.1; XM_006724536.3. [Q6W2J9-1]
DR RefSeq; XP_011542231.1; XM_011543929.2. [Q6W2J9-1]
DR RefSeq; XP_011542232.1; XM_011543930.1. [Q6W2J9-1]
DR RefSeq; XP_011542233.1; XM_011543931.2. [Q6W2J9-1]
DR RefSeq; XP_016885104.1; XM_017029615.1. [Q6W2J9-2]
DR PDB; 2N1L; NMR; -; A=1634-1748.
DR PDB; 3BIM; X-ray; 2.60 A; I/J/K/L/M/N/O/P=498-514.
DR PDB; 4HPL; X-ray; 2.00 A; A=1634-1748.
DR PDB; 6B7G; NMR; -; B=1176-1207.
DR PDBsum; 2N1L; -.
DR PDBsum; 3BIM; -.
DR PDBsum; 4HPL; -.
DR PDBsum; 6B7G; -.
DR AlphaFoldDB; Q6W2J9; -.
DR SMR; Q6W2J9; -.
DR BioGRID; 120228; 270.
DR CORUM; Q6W2J9; -.
DR DIP; DIP-50009N; -.
DR IntAct; Q6W2J9; 136.
DR MINT; Q6W2J9; -.
DR STRING; 9606.ENSP00000367705; -.
DR GlyGen; Q6W2J9; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q6W2J9; -.
DR PhosphoSitePlus; Q6W2J9; -.
DR BioMuta; BCOR; -.
DR EPD; Q6W2J9; -.
DR jPOST; Q6W2J9; -.
DR MassIVE; Q6W2J9; -.
DR MaxQB; Q6W2J9; -.
DR PaxDb; Q6W2J9; -.
DR PeptideAtlas; Q6W2J9; -.
DR PRIDE; Q6W2J9; -.
DR ProteomicsDB; 67737; -. [Q6W2J9-1]
DR ProteomicsDB; 67738; -. [Q6W2J9-2]
DR ProteomicsDB; 67739; -. [Q6W2J9-3]
DR ProteomicsDB; 67740; -. [Q6W2J9-4]
DR Antibodypedia; 24949; 302 antibodies from 34 providers.
DR DNASU; 54880; -.
DR Ensembl; ENST00000342274.8; ENSP00000345923.4; ENSG00000183337.18. [Q6W2J9-2]
DR Ensembl; ENST00000378444.9; ENSP00000367705.4; ENSG00000183337.18. [Q6W2J9-1]
DR Ensembl; ENST00000378455.8; ENSP00000367716.4; ENSG00000183337.18. [Q6W2J9-4]
DR Ensembl; ENST00000397354.7; ENSP00000380512.3; ENSG00000183337.18. [Q6W2J9-2]
DR Ensembl; ENST00000406200.4; ENSP00000384485.3; ENSG00000183337.18. [Q6W2J9-1]
DR Ensembl; ENST00000615339.2; ENSP00000483217.2; ENSG00000183337.18. [Q6W2J9-1]
DR Ensembl; ENST00000672922.2; ENSP00000499892.2; ENSG00000183337.18. [Q6W2J9-1]
DR Ensembl; ENST00000673391.1; ENSP00000500446.1; ENSG00000183337.18. [Q6W2J9-2]
DR Ensembl; ENST00000679513.1; ENSP00000505761.1; ENSG00000183337.18. [Q6W2J9-1]
DR Ensembl; ENST00000680831.1; ENSP00000505507.1; ENSG00000183337.18. [Q6W2J9-1]
DR GeneID; 54880; -.
DR KEGG; hsa:54880; -.
DR MANE-Select; ENST00000378444.9; ENSP00000367705.4; NM_001123385.2; NP_001116857.1.
DR UCSC; uc004dem.5; human. [Q6W2J9-1]
DR CTD; 54880; -.
DR DisGeNET; 54880; -.
DR GeneCards; BCOR; -.
DR HGNC; HGNC:20893; BCOR.
DR HPA; ENSG00000183337; Low tissue specificity.
DR MalaCards; BCOR; -.
DR MIM; 300166; phenotype.
DR MIM; 300485; gene.
DR neXtProt; NX_Q6W2J9; -.
DR OpenTargets; ENSG00000183337; -.
DR Orphanet; 520; Acute promyelocytic leukemia.
DR Orphanet; 457246; Clear cell sarcoma of kidney.
DR Orphanet; 568; Microphthalmia, Lenz type.
DR Orphanet; 2712; Oculofaciocardiodental syndrome.
DR PharmGKB; PA134921737; -.
DR VEuPathDB; HostDB:ENSG00000183337; -.
DR eggNOG; ENOG502RZ5N; Eukaryota.
DR GeneTree; ENSGT00940000153737; -.
DR HOGENOM; CLU_003863_0_0_1; -.
DR InParanoid; Q6W2J9; -.
DR OMA; CTEEKHP; -.
DR OrthoDB; 85469at2759; -.
DR PhylomeDB; Q6W2J9; -.
DR TreeFam; TF333317; -.
DR PathwayCommons; Q6W2J9; -.
DR SignaLink; Q6W2J9; -.
DR SIGNOR; Q6W2J9; -.
DR BioGRID-ORCS; 54880; 14 hits in 718 CRISPR screens.
DR ChiTaRS; BCOR; human.
DR EvolutionaryTrace; Q6W2J9; -.
DR GeneWiki; BCOR; -.
DR GenomeRNAi; 54880; -.
DR Pharos; Q6W2J9; Tbio.
DR PRO; PR:Q6W2J9; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q6W2J9; protein.
DR Bgee; ENSG00000183337; Expressed in buccal mucosa cell and 175 other tissues.
DR ExpressionAtlas; Q6W2J9; baseline and differential.
DR Genevisible; Q6W2J9; HS.
DR GO; GO:0140261; C:BCOR complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0000415; P:negative regulation of histone H3-K36 methylation; IMP:UniProtKB.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0070171; P:negative regulation of tooth mineralization; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IMP:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IMP:UniProtKB.
DR GO; GO:0065001; P:specification of axis polarity; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.10.260.40; -; 1.
DR IDEAL; IID00087; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR031628; BCOR.
DR InterPro; IPR032365; PUFD.
DR InterPro; IPR038227; PUFD_som_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF15808; BCOR; 1.
DR Pfam; PF16553; PUFD; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ANK repeat;
KW Chromatin regulator; Disease variant; Isopeptide bond; Microphthalmia;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1755
FT /note="BCL-6 corepressor"
FT /id="PRO_0000066978"
FT REPEAT 1462..1495
FT /note="ANK 1"
FT REPEAT 1496..1525
FT /note="ANK 2"
FT REPEAT 1529..1558
FT /note="ANK 3"
FT REGION 309..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..514
FT /note="Interaction with BCL6"
FT REGION 557..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1748
FT /note="Necessary and sufficient for interaction with PCGF1"
FT COMPBIAS 1071..1105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGN4"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGN4"
FT MOD_RES 1410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 786
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 872
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1000..1017
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012555"
FT VAR_SEQ 1000..1004
FT /note="MEGLQ -> VSPPT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10898795,
FT ECO:0000303|PubMed:10997877"
FT /id="VSP_012554"
FT VAR_SEQ 1005..1755
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10898795,
FT ECO:0000303|PubMed:10997877"
FT /id="VSP_012556"
FT VAR_SEQ 1168..1201
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10898795,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_012557"
FT VARIANT 85
FT /note="P -> L (in MCOPS2; dbSNP:rs121434618)"
FT /evidence="ECO:0000269|PubMed:15004558"
FT /id="VAR_020921"
FT MUTAGEN 507
FT /note="S->A: Abolishes interaction with BCL6 and inhibits
FT BCL6 corepression activity; when associated with A-509 and
FT A-511."
FT /evidence="ECO:0000269|PubMed:18280243"
FT MUTAGEN 508
FT /note="S->A: Diminishes interaction with BCL6."
FT /evidence="ECO:0000269|PubMed:18280243"
FT MUTAGEN 509
FT /note="W->A: Abolishes interaction with BCL6 and inhibits
FT BCL6 corepression activity; when associated with A-507 and
FT A-511."
FT /evidence="ECO:0000269|PubMed:18280243"
FT MUTAGEN 511
FT /note="V->A: Abolishes interaction with BCL6 and inhibits
FT BCL6 corepression activity; when associated with A-507 and
FT A-509."
FT /evidence="ECO:0000269|PubMed:18280243"
FT MUTAGEN 1706
FT /note="L->D,R: Slightly inhibits interaction with PCGF1."
FT /evidence="ECO:0000269|PubMed:23523425"
FT CONFLICT 406
FT /note="V -> A (in Ref. 6; BAB85037)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="Q -> L (in Ref. 6; BAB85037)"
FT /evidence="ECO:0000305"
FT CONFLICT 1459
FT /note="N -> S (in Ref. 6; BAA91061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1577
FT /note="K -> R (in Ref. 6; BAA91061)"
FT /evidence="ECO:0000305"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:3BIM"
FT STRAND 1190..1193
FT /evidence="ECO:0007829|PDB:6B7G"
FT STRAND 1195..1199
FT /evidence="ECO:0007829|PDB:6B7G"
FT TURN 1200..1202
FT /evidence="ECO:0007829|PDB:6B7G"
FT STRAND 1637..1644
FT /evidence="ECO:0007829|PDB:4HPL"
FT STRAND 1650..1653
FT /evidence="ECO:0007829|PDB:4HPL"
FT TURN 1656..1658
FT /evidence="ECO:0007829|PDB:4HPL"
FT STRAND 1660..1665
FT /evidence="ECO:0007829|PDB:4HPL"
FT HELIX 1666..1673
FT /evidence="ECO:0007829|PDB:4HPL"
FT HELIX 1677..1683
FT /evidence="ECO:0007829|PDB:4HPL"
FT STRAND 1689..1693
FT /evidence="ECO:0007829|PDB:4HPL"
FT HELIX 1694..1702
FT /evidence="ECO:0007829|PDB:4HPL"
FT HELIX 1705..1707
FT /evidence="ECO:0007829|PDB:4HPL"
FT HELIX 1710..1712
FT /evidence="ECO:0007829|PDB:4HPL"
FT TURN 1713..1715
FT /evidence="ECO:0007829|PDB:4HPL"
FT STRAND 1723..1728
FT /evidence="ECO:0007829|PDB:4HPL"
FT HELIX 1731..1736
FT /evidence="ECO:0007829|PDB:4HPL"
FT STRAND 1740..1744
FT /evidence="ECO:0007829|PDB:4HPL"
SQ SEQUENCE 1755 AA; 192189 MW; A80CFCD5618EE717 CRC64;
MLSATPLYGN VHSWMNSERV RMCGASEDRK ILVNDGDASK ARLELREENP LNHNVVDAST
AHRIDGLAAL SMDRTGLIRE GLRVPGNIVY SSLCGLGSEK GREAATSTLG GLGFSSERNP
EMQFKPNTPE TVEASAVSGK PPNGFSAIYK TPPGIQKSAV ATAEALGLDR PASDKQSPLN
INGASYLRLP WVNPYMEGAT PAIYPFLDSP NKYSLNMYKA LLPQQSYSLA QPLYSPVCTN
GERFLYLPPP HYVGPHIPSS LASPMRLSTP SASPAIPPLV HCADKSLPWK MGVSPGNPVD
SHAYPHIQNS KQPRVPSAKA VTSGLPGDTA LLLPPSPRPS PRVHLPTQPA ADTYSEFHKH
YARISTSPSV ALSKPYMTVS SEFPAARLSN GKYPKAPEGG EGAQPVPGHA RKTAVQDRKD
GSSPPLLEKQ TVTKDVTDKP LDLSSKVVDV DASKADHMKK MAPTVLVHSR AGSGLVLSGS
EIPKETLSPP GNGCAIYRSE IISTAPSSWV VPGPSPNEEN NGKSMSLKNK ALDWAIPQQR
SSSCPRMGGT DAVITNVSGS VSSAGRPASA SPAPNANADG TKTSRSSVET TPSVIQHVGQ
PPATPAKHSS STSSKGAKAS NPEPSFKANE NGLPPSSIFL SPNEAFRSPP IPYPRSYLPY
PAPEGIAVSP LSLHGKGPVY PHPVLLPNGS LFPGHLAPKP GLPYGLPTGR PEFVTYQDAL
GLGMVHPMLI PHTPIEITKE EKPERRSRSH ERARYEDPTL RNRFSEILET SSTKLHPDVP
TDKNLKPNPN WNQGKTVVKS DKLVYVDLLR EEPDAKTDTN VSKPSFAAES VGQSAEPPKP
SVEPALQQHR DFIALREELG RISDFHETYT FKQPVFTVSK DSVLAGTNKE NLGLPVSTPF
LEPPLGSDGP AVTFGKTQED PKPFCVGSAP PSVDVTPTYT KDGADEAESN DGKVLKPKPS
KLAKRIANSA GYVGDRFKCV TTELYADSSQ LSREQRALQM EGLQEDSILC LPAAYCERAM
MRFSELEMKE REGGHPATKD SEMCKFSPAD WERLKGNQDK KPKSVTLEEA IAEQNESERC
EYSVGNKHRD PFEAPEDKDL PVEKYFVERQ PVSEPPADQV ASDMPHSPTL RVDRKRKVSG
DSSHTETTAE EVPEDPLLKA KRRRVSKDDW PEREMTNSSS NHLEDPHYSE LTNLKVCIEL
TGLHPKKQRH LLHLRERWEQ QVSAADGKPG RQSRKEVTQA TQPEAIPQGT NITEEKPGRK
RAEAKGNRSW SEESLKPSDN EQGLPVFSGS PPMKSLSSTS AGGKKQAQPS CAPASRPPAK
QQKIKENQKT DVLCADEEED CQAASLLQKY TDNSEKPSGK RLCKTKHLIP QESRRGLPLT
GEYYVENADG KVTVRRFRKR PEPSSDYDLS PAKQEPKPFD RLQQLLPASQ STQLPCSSSP
QETTQSRPMP PEARRLIVNK NAGETLLQRA ARLGYEEVVL YCLENKICDV NHRDNAGYCA
LHEACARGWL NIVRHLLEYG ADVNCSAQDG TRPLHDAVEN DHLEIVRLLL SYGADPTLAT
YSGRTIMKMT HSELMEKFLT DYLNDLQGRN DDDASGTWDF YGSSVCEPDD ESGYDVLANP
PGPEDQDDDD DAYSDVFEFE FSETPLLPCY NIQVSVAQGP RNWLLLSDVL KKLKMSSRIF
RCNFPNVEIV TIAEAEFYRQ VSASLLFSCS KDLEAFNPES KELLDLVEFT NEIQTLLGSS
VEWLHPSDLA SDNYW
