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Q6W2J9 (BCOR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BCL-6 corepressor

Short name=BCoR
Gene names
Name:BCOR
Synonyms:KIAA1575
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1755 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional corepressor. May specifically inhibit gene expression when recruited to promoter regions by sequence-specific DNA-binding proteins such as BCL6 and MLLT3. This repression may be mediated at least in part by histone deacetylase activities which can associate with this corepressor. Involved in the repression of TFAP2A; impairs binding of BCL6 and KDM2B to TFAP2A promoter regions. Via repression of TFAP2A acts as a negative regulator of osteo-dentiogenic capacity in adult stem cells; the function implies inhibition of methylation on histone H3 'Lys-4' (H3K4me3) and 'Lys-36' (H3K36me2). Ref.1 Ref.2 Ref.11 Ref.17 Ref.19

Subunit structure

Interacts with BCL6; the interaction is direct. Forms ternary complexes with BCL6 and SMRT/NCOR2 on selected target genes promoters; potently repress expression. Can interact with HDAC1, HDAC3 and HDAC5. Interacts with PCGF1; the interaction is direct. Interacts with KDM2B. Component of an approximative 800 kDa repressive BCOR complex at least composed of BCOR, RYBP, PCGF1, RING1, RNF2/RING2, KDM2B and SKP1. Isoform 1 may interact with MLLT3/AF9. Ref.1 Ref.8 Ref.17 Ref.18

Subcellular location

Nucleus Ref.1.

Tissue specificity

Ubiquitously expressed. Ref.1

Involvement in disease

Microphthalmia, syndromic, 2 (MCOPS2) [MIM:300166]: A very rare multiple congenital anomaly syndrome characterized by eye anomalies (congenital cataract, microphthalmia, or secondary glaucoma), facial abnormalities (long narrow face, high nasal bridge, pointed nose with cartilages separated at the tip, cleft palate, or submucous cleft palate), cardiac anomalies (atrial septal defect, ventricular septal defect, or floppy mitral valve) and dental abnormalities (canine radiculomegaly, delayed dentition, oligodontia, persistent primary teeth, or variable root length). Microphthalmia is a disorder of eye formation, ranging from small size of a single eye to complete bilateral absence of ocular tissues (anophthalmia). In many cases, microphthalmia/anophthalmia occurs in association with syndromes that include non-ocular abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2

Sequence similarities

Belongs to the BCOR family.

Contains 3 ANK repeats.

Sequence caution

The sequence AAH63536.1 differs from that shown. Reason: Contaminating sequence. Presence of complementary strand sequence in the clone.

The sequence BAA91061.1 differs from that shown. Reason: Intron retention.

The sequence BAB13401.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB85037.1 differs from that shown. Reason: Frameshift at position 1353.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Microphthalmia
   DomainANK repeat
Repeat
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheart development

Inferred from mutant phenotype PubMed 17517692. Source: UniProtKB

histone H2A monoubiquitination

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of bone mineralization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of histone H3-K36 methylation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of histone H3-K4 methylation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of tooth mineralization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

odontogenesis

Inferred from mutant phenotype PubMed 17517692. Source: UniProtKB

palate development

Inferred from mutant phenotype PubMed 17517692. Source: UniProtKB

specification of axis polarity

Inferred from mutant phenotype PubMed 17517692. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionheat shock protein binding

Inferred from direct assay Ref.8. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction Ref.1. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.1. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.1. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from mutant phenotype Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KDM2BQ8NHM52EBI-950027,EBI-3955564
PCGF1Q9BSM16EBI-950027,EBI-749901

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6W2J9-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6W2J9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1168-1201: Missing.
Isoform 3 (identifier: Q6W2J9-3)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1000-1004: MEGLQ → VSPPT
     1005-1755: Missing.
Isoform 4 (identifier: Q6W2J9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1000-1017: Missing.
     1168-1201: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17551755BCL-6 corepressor
PRO_0000066978

Regions

Repeat1462 – 149534ANK 1
Repeat1496 – 152530ANK 2
Repeat1529 – 155830ANK 3
Region498 – 51417Interaction with BCL6
Region1634 – 1748115Necessary and sufficient for interaction with PCGF1
Compositional bias634 – 71178Pro-rich
Compositional bias1625 – 16317Poly-Asp

Amino acid modifications

Modified residue3361Phosphoserine Ref.14
Modified residue3401Phosphoserine Ref.14
Modified residue3651Phosphoserine Ref.14
Modified residue3671Phosphoserine Ref.14
Modified residue3921N6-acetyllysine Ref.13
Modified residue4231Phosphoserine Ref.9 Ref.14 Ref.16
Modified residue11391Phosphoserine Ref.12
Modified residue14101Phosphoserine Ref.9

Natural variations

Alternative sequence1000 – 101718Missing in isoform 4.
VSP_012555
Alternative sequence1000 – 10045MEGLQ → VSPPT in isoform 3.
VSP_012554
Alternative sequence1005 – 1755751Missing in isoform 3.
VSP_012556
Alternative sequence1168 – 120134Missing in isoform 2 and isoform 4.
VSP_012557
Natural variant851P → L in MCOPS2. Ref.2
Corresponds to variant rs28935183 [ dbSNP | Ensembl ].
VAR_020921

Experimental info

Mutagenesis5071S → A: Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-509 and A-511. Ref.19
Mutagenesis5081S → A: Diminishes interaction with BCL6. Ref.19
Mutagenesis5091W → A: Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-507 and A-511. Ref.19
Mutagenesis5111V → A: Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-507 and A-509. Ref.19
Mutagenesis17061L → D or R: Slightly inhibits interaction with PCGF1. Ref.18
Sequence conflict4061V → A in BAB85037. Ref.6
Sequence conflict5961Q → L in BAB85037. Ref.6
Sequence conflict14591N → S in BAA91061. Ref.6
Sequence conflict15771K → R in BAA91061. Ref.6

Secondary structure

............................ 1755
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A80CFCD5618EE717

FASTA1,755192,189
        10         20         30         40         50         60 
MLSATPLYGN VHSWMNSERV RMCGASEDRK ILVNDGDASK ARLELREENP LNHNVVDAST 

        70         80         90        100        110        120 
AHRIDGLAAL SMDRTGLIRE GLRVPGNIVY SSLCGLGSEK GREAATSTLG GLGFSSERNP 

       130        140        150        160        170        180 
EMQFKPNTPE TVEASAVSGK PPNGFSAIYK TPPGIQKSAV ATAEALGLDR PASDKQSPLN 

       190        200        210        220        230        240 
INGASYLRLP WVNPYMEGAT PAIYPFLDSP NKYSLNMYKA LLPQQSYSLA QPLYSPVCTN 

       250        260        270        280        290        300 
GERFLYLPPP HYVGPHIPSS LASPMRLSTP SASPAIPPLV HCADKSLPWK MGVSPGNPVD 

       310        320        330        340        350        360 
SHAYPHIQNS KQPRVPSAKA VTSGLPGDTA LLLPPSPRPS PRVHLPTQPA ADTYSEFHKH 

       370        380        390        400        410        420 
YARISTSPSV ALSKPYMTVS SEFPAARLSN GKYPKAPEGG EGAQPVPGHA RKTAVQDRKD 

       430        440        450        460        470        480 
GSSPPLLEKQ TVTKDVTDKP LDLSSKVVDV DASKADHMKK MAPTVLVHSR AGSGLVLSGS 

       490        500        510        520        530        540 
EIPKETLSPP GNGCAIYRSE IISTAPSSWV VPGPSPNEEN NGKSMSLKNK ALDWAIPQQR 

       550        560        570        580        590        600 
SSSCPRMGGT DAVITNVSGS VSSAGRPASA SPAPNANADG TKTSRSSVET TPSVIQHVGQ 

       610        620        630        640        650        660 
PPATPAKHSS STSSKGAKAS NPEPSFKANE NGLPPSSIFL SPNEAFRSPP IPYPRSYLPY 

       670        680        690        700        710        720 
PAPEGIAVSP LSLHGKGPVY PHPVLLPNGS LFPGHLAPKP GLPYGLPTGR PEFVTYQDAL 

       730        740        750        760        770        780 
GLGMVHPMLI PHTPIEITKE EKPERRSRSH ERARYEDPTL RNRFSEILET SSTKLHPDVP 

       790        800        810        820        830        840 
TDKNLKPNPN WNQGKTVVKS DKLVYVDLLR EEPDAKTDTN VSKPSFAAES VGQSAEPPKP 

       850        860        870        880        890        900 
SVEPALQQHR DFIALREELG RISDFHETYT FKQPVFTVSK DSVLAGTNKE NLGLPVSTPF 

       910        920        930        940        950        960 
LEPPLGSDGP AVTFGKTQED PKPFCVGSAP PSVDVTPTYT KDGADEAESN DGKVLKPKPS 

       970        980        990       1000       1010       1020 
KLAKRIANSA GYVGDRFKCV TTELYADSSQ LSREQRALQM EGLQEDSILC LPAAYCERAM 

      1030       1040       1050       1060       1070       1080 
MRFSELEMKE REGGHPATKD SEMCKFSPAD WERLKGNQDK KPKSVTLEEA IAEQNESERC 

      1090       1100       1110       1120       1130       1140 
EYSVGNKHRD PFEAPEDKDL PVEKYFVERQ PVSEPPADQV ASDMPHSPTL RVDRKRKVSG 

      1150       1160       1170       1180       1190       1200 
DSSHTETTAE EVPEDPLLKA KRRRVSKDDW PEREMTNSSS NHLEDPHYSE LTNLKVCIEL 

      1210       1220       1230       1240       1250       1260 
TGLHPKKQRH LLHLRERWEQ QVSAADGKPG RQSRKEVTQA TQPEAIPQGT NITEEKPGRK 

      1270       1280       1290       1300       1310       1320 
RAEAKGNRSW SEESLKPSDN EQGLPVFSGS PPMKSLSSTS AGGKKQAQPS CAPASRPPAK 

      1330       1340       1350       1360       1370       1380 
QQKIKENQKT DVLCADEEED CQAASLLQKY TDNSEKPSGK RLCKTKHLIP QESRRGLPLT 

      1390       1400       1410       1420       1430       1440 
GEYYVENADG KVTVRRFRKR PEPSSDYDLS PAKQEPKPFD RLQQLLPASQ STQLPCSSSP 

      1450       1460       1470       1480       1490       1500 
QETTQSRPMP PEARRLIVNK NAGETLLQRA ARLGYEEVVL YCLENKICDV NHRDNAGYCA 

      1510       1520       1530       1540       1550       1560 
LHEACARGWL NIVRHLLEYG ADVNCSAQDG TRPLHDAVEN DHLEIVRLLL SYGADPTLAT 

      1570       1580       1590       1600       1610       1620 
YSGRTIMKMT HSELMEKFLT DYLNDLQGRN DDDASGTWDF YGSSVCEPDD ESGYDVLANP 

      1630       1640       1650       1660       1670       1680 
PGPEDQDDDD DAYSDVFEFE FSETPLLPCY NIQVSVAQGP RNWLLLSDVL KKLKMSSRIF 

      1690       1700       1710       1720       1730       1740 
RCNFPNVEIV TIAEAEFYRQ VSASLLFSCS KDLEAFNPES KELLDLVEFT NEIQTLLGSS 

      1750 
VEWLHPSDLA SDNYW 

« Hide

Isoform 2 [UniParc].

Checksum: F22343D545DB67AB
Show »

FASTA1,721188,202
Isoform 3 (Short) [UniParc].

Checksum: 126BD762958CB9F4
Show »

FASTA1,004107,404
Isoform 4 [UniParc].

Checksum: 7433FBCE7238261F
Show »

FASTA1,703186,235

References

« Hide 'large scale' references
[1]"BCoR, a novel corepressor involved in BCL-6 repression."
Huynh K.D., Fischle W., Verdin E., Bardwell V.J.
Genes Dev. 14:1810-1823(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH BCL6; HDAC1; HDAC3 AND HDAC5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Frontal cortex.
[2]"Oculofaciocardiodental and Lenz microphthalmia syndromes result from distinct classes of mutations in BCOR."
Ng D., Thakker N., Corcoran C.M., Donnai D., Perveen R., Schneider A., Hadley D.W., Tifft C., Zhang L., Wilkie A.O., van der Smagt J.J., Gorlin R.J., Burgess S.M., Bardwell V.J., Black G.C.M., Biesecker L.G.
Nat. Genet. 36:411-416(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT MCOPS2 LEU-85.
[3]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1395-1755 (ISOFORM 1).
Tissue: Liver, Lymph and Uterus.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1755 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 1328-1755.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets."
Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.
Mol. Cell. Biol. 26:6880-6889(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCGF1 AND KDM2B, IDENTIFICATION IN A COMPLEX WITH RYBP; PCGF1; RING1; RNF2; KDM2B AND SKP1.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND SER-1410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"BCOR regulates mesenchymal stem cell function by epigenetic mechanisms."
Fan Z., Yamaza T., Lee J.S., Yu J., Wang S., Fan G., Shi S., Wang C.-Y.
Nat. Cell Biol. 11:1002-1009(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-340; SER-365; SER-367 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"A hybrid mechanism of action for BCL6 in B cells defined by formation of functionally distinct complexes at enhancers and promoters."
Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D., Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M., Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W., Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.
Cell Rep. 4:578-588(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS COREPRESSOR, INTERACTION WITH BCL6, IDENTIFICATION IN A COMPLEX WITH BCL6 AND SMRT.
[18]"Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs."
Junco S.E., Wang R., Gaipa J.C., Taylor A.B., Schirf V., Gearhart M.D., Bardwell V.J., Demeler B., Hart P.J., Kim C.A.
Structure 21:665-671(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1634-1748 IN COMPLEX WITH PCGF1, INTERACTION WITH PCGF1, MUTAGENESIS OF LEU-1706.
[19]"Structure of a BCOR corepressor peptide in complex with the BCL6 BTB domain dimer."
Ghetu A.F., Corcoran C.M., Cerchietti L., Bardwell V.J., Melnick A., Prive G.G.
Mol. Cell 29:384-391(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 498-514 IN COMPLEX WITH BCL6, FUNCTION, MUTAGENESIS OF SER-507; SER-508; TRP-509 AND VAL-511.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF317391 mRNA. Translation: AAG41429.1.
AF317392 mRNA. Translation: AAG41430.1.
AY316592 mRNA. Translation: AAR08265.1.
AB046795 mRNA. Translation: BAB13401.2. Different initiation.
CH471141 Genomic DNA. Translation: EAW59425.1.
CH471141 Genomic DNA. Translation: EAW59427.1.
CH471141 Genomic DNA. Translation: EAW59428.1.
CH471141 Genomic DNA. Translation: EAW59430.1.
BC009675 mRNA. Translation: AAH09675.2.
BC063536 mRNA. Translation: AAH63536.1. Sequence problems.
BC114220 mRNA. Translation: AAI14221.1.
AK000292 mRNA. Translation: BAA91061.1. Sequence problems.
AK074286 mRNA. Translation: BAB85037.1. Frameshift.
RefSeqNP_001116855.1. NM_001123383.1.
NP_001116856.1. NM_001123384.1.
NP_001116857.1. NM_001123385.1.
NP_060215.4. NM_017745.5.
XP_005272673.1. XM_005272616.1.
XP_005272674.1. XM_005272617.2.
XP_005272675.1. XM_005272618.1.
XP_005272677.1. XM_005272620.2.
UniGeneHs.659681.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BIMX-ray2.60I/J/K/L/M/N/O/P498-514[»]
4HPLX-ray2.00A1634-1748[»]
ProteinModelPortalQ6W2J9.
SMRQ6W2J9. Positions 1463-1618, 1636-1748.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120228. 24 interactions.
DIPDIP-50009N.
IntActQ6W2J9. 8 interactions.
MINTMINT-2817388.

PTM databases

PhosphoSiteQ6W2J9.

Proteomic databases

PaxDbQ6W2J9.
PRIDEQ6W2J9.

Protocols and materials databases

DNASU54880.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342274; ENSP00000345923; ENSG00000183337. [Q6W2J9-2]
ENST00000378444; ENSP00000367705; ENSG00000183337. [Q6W2J9-1]
ENST00000378455; ENSP00000367716; ENSG00000183337. [Q6W2J9-4]
ENST00000397354; ENSP00000380512; ENSG00000183337. [Q6W2J9-2]
GeneID54880.
KEGGhsa:54880.
UCSCuc004dem.4. human. [Q6W2J9-2]
uc004den.4. human. [Q6W2J9-1]
uc004deo.4. human. [Q6W2J9-4]
uc004deq.4. human. [Q6W2J9-3]

Organism-specific databases

CTD54880.
GeneCardsGC0XM039909.
HGNCHGNC:20893. BCOR.
MIM300166. phenotype.
300485. gene.
neXtProtNX_Q6W2J9.
Orphanet568. Microphthalmia, Lenz type.
2712. Oculofaciocardiodental syndrome.
PharmGKBPA134921737.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG050682.
InParanoidQ6W2J9.
OMASSCPRMG.
PhylomeDBQ6W2J9.
TreeFamTF333317.

Gene expression databases

ArrayExpressQ6W2J9.
BgeeQ6W2J9.
GenevestigatorQ6W2J9.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBCOR. human.
EvolutionaryTraceQ6W2J9.
GeneWikiBCOR.
GenomeRNAi54880.
NextBio57837.
PROQ6W2J9.
SOURCESearch...

Entry information

Entry nameBCOR_HUMAN
AccessionPrimary (citable) accession number: Q6W2J9
Secondary accession number(s): D3DWB3 expand/collapse secondary AC list , D3DWB4, Q29RF6, Q6P4B6, Q7Z2K7, Q8TEB4, Q96DB3, Q9H232, Q9H233, Q9HCJ7, Q9NXF2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM