Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6W2J9

- BCOR_HUMAN

UniProt

Q6W2J9 - BCOR_HUMAN

Protein

BCL-6 corepressor

Gene

BCOR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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).5 Publications

    GO - Molecular functioni

    1. heat shock protein binding Source: UniProtKB
    2. histone deacetylase binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. transcription corepressor activity Source: UniProtKB
    5. transcription factor binding Source: UniProtKB
    6. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. heart development Source: UniProtKB
    2. histone H2A monoubiquitination Source: UniProtKB
    3. negative regulation of bone mineralization Source: UniProtKB
    4. negative regulation of histone H3-K36 methylation Source: UniProtKB
    5. negative regulation of histone H3-K4 methylation Source: UniProtKB
    6. negative regulation of tooth mineralization Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. odontogenesis Source: UniProtKB
    10. palate development Source: UniProtKB
    11. specification of axis polarity Source: UniProtKB
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    BCL-6 corepressor
    Short name:
    BCoR
    Gene namesi
    Name:BCOR
    Synonyms:KIAA1575
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:20893. BCOR.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851P → L in MCOPS2. 1 Publication
    Corresponds to variant rs28935183 [ dbSNP | Ensembl ].
    VAR_020921

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi507 – 5071S → A: Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-509 and A-511. 1 Publication
    Mutagenesisi508 – 5081S → A: Diminishes interaction with BCL6. 1 Publication
    Mutagenesisi509 – 5091W → A: Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-507 and A-511. 1 Publication
    Mutagenesisi511 – 5111V → A: Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-507 and A-509. 1 Publication
    Mutagenesisi1706 – 17061L → D or R: Slightly inhibits interaction with PCGF1. 1 Publication

    Keywords - Diseasei

    Disease mutation, Microphthalmia

    Organism-specific databases

    MIMi300166. phenotype.
    Orphaneti568. Microphthalmia, Lenz type.
    2712. Oculofaciocardiodental syndrome.
    PharmGKBiPA134921737.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17551755BCL-6 corepressorPRO_0000066978Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei336 – 3361Phosphoserine1 Publication
    Modified residuei340 – 3401Phosphoserine1 Publication
    Modified residuei365 – 3651Phosphoserine1 Publication
    Modified residuei367 – 3671Phosphoserine1 Publication
    Modified residuei392 – 3921N6-acetyllysine1 Publication
    Modified residuei423 – 4231Phosphoserine3 Publications
    Modified residuei1139 – 11391Phosphoserine1 Publication
    Modified residuei1410 – 14101Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6W2J9.
    PaxDbiQ6W2J9.
    PRIDEiQ6W2J9.

    PTM databases

    PhosphoSiteiQ6W2J9.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ6W2J9.
    BgeeiQ6W2J9.
    GenevestigatoriQ6W2J9.

    Interactioni

    Subunit structurei

    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/AF9.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KDM2BQ8NHM52EBI-950027,EBI-3955564
    PCGF1Q9BSM16EBI-950027,EBI-749901

    Protein-protein interaction databases

    BioGridi120228. 25 interactions.
    DIPiDIP-50009N.
    IntActiQ6W2J9. 8 interactions.
    MINTiMINT-2817388.

    Structurei

    Secondary structure

    1
    1755
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi500 – 5034
    Beta strandi1637 – 16448
    Beta strandi1650 – 16534
    Turni1656 – 16583
    Beta strandi1660 – 16656
    Helixi1666 – 16738
    Helixi1677 – 16837
    Beta strandi1689 – 16935
    Helixi1694 – 17029
    Helixi1705 – 17073
    Helixi1710 – 17123
    Turni1713 – 17153
    Beta strandi1723 – 17286
    Helixi1731 – 17366
    Beta strandi1740 – 17445

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BIMX-ray2.60I/J/K/L/M/N/O/P498-514[»]
    4HPLX-ray2.00A1634-1748[»]
    ProteinModelPortaliQ6W2J9.
    SMRiQ6W2J9. Positions 1463-1579, 1636-1748.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6W2J9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1462 – 149534ANK 1Add
    BLAST
    Repeati1496 – 152530ANK 2Add
    BLAST
    Repeati1529 – 155830ANK 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni498 – 51417Interaction with BCL6Add
    BLAST
    Regioni1634 – 1748115Necessary and sufficient for interaction with PCGF1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi634 – 71178Pro-richAdd
    BLAST
    Compositional biasi1625 – 16317Poly-Asp

    Sequence similaritiesi

    Belongs to the BCOR family.Curated
    Contains 3 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOVERGENiHBG050682.
    InParanoidiQ6W2J9.
    OMAiSSCPRMG.
    PhylomeDBiQ6W2J9.
    TreeFamiTF333317.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    [Graphical view]
    PfamiPF12796. Ank_2. 1 hit.
    [Graphical view]
    SMARTiSM00248. ANK. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6W2J9-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLSATPLYGN VHSWMNSERV RMCGASEDRK ILVNDGDASK ARLELREENP     50
    LNHNVVDAST AHRIDGLAAL SMDRTGLIRE GLRVPGNIVY SSLCGLGSEK 100
    GREAATSTLG GLGFSSERNP EMQFKPNTPE TVEASAVSGK PPNGFSAIYK 150
    TPPGIQKSAV ATAEALGLDR PASDKQSPLN INGASYLRLP WVNPYMEGAT 200
    PAIYPFLDSP NKYSLNMYKA LLPQQSYSLA QPLYSPVCTN GERFLYLPPP 250
    HYVGPHIPSS LASPMRLSTP SASPAIPPLV HCADKSLPWK MGVSPGNPVD 300
    SHAYPHIQNS KQPRVPSAKA VTSGLPGDTA LLLPPSPRPS PRVHLPTQPA 350
    ADTYSEFHKH YARISTSPSV ALSKPYMTVS SEFPAARLSN GKYPKAPEGG 400
    EGAQPVPGHA RKTAVQDRKD GSSPPLLEKQ TVTKDVTDKP LDLSSKVVDV 450
    DASKADHMKK MAPTVLVHSR AGSGLVLSGS EIPKETLSPP GNGCAIYRSE 500
    IISTAPSSWV VPGPSPNEEN NGKSMSLKNK ALDWAIPQQR SSSCPRMGGT 550
    DAVITNVSGS VSSAGRPASA SPAPNANADG TKTSRSSVET TPSVIQHVGQ 600
    PPATPAKHSS STSSKGAKAS NPEPSFKANE NGLPPSSIFL SPNEAFRSPP 650
    IPYPRSYLPY PAPEGIAVSP LSLHGKGPVY PHPVLLPNGS LFPGHLAPKP 700
    GLPYGLPTGR PEFVTYQDAL GLGMVHPMLI PHTPIEITKE EKPERRSRSH 750
    ERARYEDPTL RNRFSEILET SSTKLHPDVP TDKNLKPNPN WNQGKTVVKS 800
    DKLVYVDLLR EEPDAKTDTN VSKPSFAAES VGQSAEPPKP SVEPALQQHR 850
    DFIALREELG RISDFHETYT FKQPVFTVSK DSVLAGTNKE NLGLPVSTPF 900
    LEPPLGSDGP AVTFGKTQED PKPFCVGSAP PSVDVTPTYT KDGADEAESN 950
    DGKVLKPKPS KLAKRIANSA GYVGDRFKCV TTELYADSSQ LSREQRALQM 1000
    EGLQEDSILC LPAAYCERAM MRFSELEMKE REGGHPATKD SEMCKFSPAD 1050
    WERLKGNQDK KPKSVTLEEA IAEQNESERC EYSVGNKHRD PFEAPEDKDL 1100
    PVEKYFVERQ PVSEPPADQV ASDMPHSPTL RVDRKRKVSG DSSHTETTAE 1150
    EVPEDPLLKA KRRRVSKDDW PEREMTNSSS NHLEDPHYSE LTNLKVCIEL 1200
    TGLHPKKQRH LLHLRERWEQ QVSAADGKPG RQSRKEVTQA TQPEAIPQGT 1250
    NITEEKPGRK RAEAKGNRSW SEESLKPSDN EQGLPVFSGS PPMKSLSSTS 1300
    AGGKKQAQPS CAPASRPPAK QQKIKENQKT DVLCADEEED CQAASLLQKY 1350
    TDNSEKPSGK RLCKTKHLIP QESRRGLPLT GEYYVENADG KVTVRRFRKR 1400
    PEPSSDYDLS PAKQEPKPFD RLQQLLPASQ STQLPCSSSP QETTQSRPMP 1450
    PEARRLIVNK NAGETLLQRA ARLGYEEVVL YCLENKICDV NHRDNAGYCA 1500
    LHEACARGWL NIVRHLLEYG ADVNCSAQDG TRPLHDAVEN DHLEIVRLLL 1550
    SYGADPTLAT YSGRTIMKMT HSELMEKFLT DYLNDLQGRN DDDASGTWDF 1600
    YGSSVCEPDD ESGYDVLANP PGPEDQDDDD DAYSDVFEFE FSETPLLPCY 1650
    NIQVSVAQGP RNWLLLSDVL KKLKMSSRIF RCNFPNVEIV TIAEAEFYRQ 1700
    VSASLLFSCS KDLEAFNPES KELLDLVEFT NEIQTLLGSS VEWLHPSDLA 1750
    SDNYW 1755
    Length:1,755
    Mass (Da):192,189
    Last modified:July 5, 2004 - v1
    Checksum:iA80CFCD5618EE717
    GO
    Isoform 2 (identifier: Q6W2J9-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,721
    Mass (Da):188,202
    Checksum:iF22343D545DB67AB
    GO
    Isoform 3 (identifier: Q6W2J9-3) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1000-1004: MEGLQ → VSPPT
         1005-1755: Missing.

    Show »
    Length:1,004
    Mass (Da):107,404
    Checksum:i126BD762958CB9F4
    GO
    Isoform 4 (identifier: Q6W2J9-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,703
    Mass (Da):186,235
    Checksum:i7433FBCE7238261F
    GO

    Sequence cautioni

    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 BAB85037.1 differs from that shown. Reason: Frameshift at position 1353.
    The sequence BAB13401.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti406 – 4061V → A in BAB85037. (PubMed:14702039)Curated
    Sequence conflicti596 – 5961Q → L in BAB85037. (PubMed:14702039)Curated
    Sequence conflicti1459 – 14591N → S in BAA91061. (PubMed:14702039)Curated
    Sequence conflicti1577 – 15771K → R in BAA91061. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851P → L in MCOPS2. 1 Publication
    Corresponds to variant rs28935183 [ dbSNP | Ensembl ].
    VAR_020921

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1000 – 101718Missing in isoform 4. 2 PublicationsVSP_012555Add
    BLAST
    Alternative sequencei1000 – 10045MEGLQ → VSPPT in isoform 3. 2 PublicationsVSP_012554
    Alternative sequencei1005 – 1755751Missing in isoform 3. 2 PublicationsVSP_012556Add
    BLAST
    Alternative sequencei1168 – 120134Missing in isoform 2 and isoform 4. 3 PublicationsVSP_012557Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14250.1. [Q6W2J9-2]
    CCDS48092.1. [Q6W2J9-4]
    CCDS48093.1. [Q6W2J9-1]
    RefSeqiNP_001116855.1. NM_001123383.1. [Q6W2J9-2]
    NP_001116856.1. NM_001123384.1. [Q6W2J9-4]
    NP_001116857.1. NM_001123385.1. [Q6W2J9-1]
    NP_060215.4. NM_017745.5. [Q6W2J9-2]
    XP_005272673.1. XM_005272616.1. [Q6W2J9-1]
    XP_005272674.1. XM_005272617.2. [Q6W2J9-1]
    XP_005272675.1. XM_005272618.1. [Q6W2J9-1]
    XP_005272677.1. XM_005272620.2. [Q6W2J9-4]
    XP_006724599.1. XM_006724536.1. [Q6W2J9-1]
    UniGeneiHs.659681.

    Genome annotation databases

    EnsembliENST00000342274; ENSP00000345923; ENSG00000183337. [Q6W2J9-2]
    ENST00000378444; ENSP00000367705; ENSG00000183337. [Q6W2J9-1]
    ENST00000378455; ENSP00000367716; ENSG00000183337. [Q6W2J9-4]
    ENST00000397354; ENSP00000380512; ENSG00000183337. [Q6W2J9-2]
    GeneIDi54880.
    KEGGihsa:54880.
    UCSCiuc004dem.4. human. [Q6W2J9-2]
    uc004den.4. human. [Q6W2J9-1]
    uc004deo.4. human. [Q6W2J9-4]
    uc004deq.4. human. [Q6W2J9-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS14250.1. [Q6W2J9-2 ]
    CCDS48092.1. [Q6W2J9-4 ]
    CCDS48093.1. [Q6W2J9-1 ]
    RefSeqi NP_001116855.1. NM_001123383.1. [Q6W2J9-2 ]
    NP_001116856.1. NM_001123384.1. [Q6W2J9-4 ]
    NP_001116857.1. NM_001123385.1. [Q6W2J9-1 ]
    NP_060215.4. NM_017745.5. [Q6W2J9-2 ]
    XP_005272673.1. XM_005272616.1. [Q6W2J9-1 ]
    XP_005272674.1. XM_005272617.2. [Q6W2J9-1 ]
    XP_005272675.1. XM_005272618.1. [Q6W2J9-1 ]
    XP_005272677.1. XM_005272620.2. [Q6W2J9-4 ]
    XP_006724599.1. XM_006724536.1. [Q6W2J9-1 ]
    UniGenei Hs.659681.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BIM X-ray 2.60 I/J/K/L/M/N/O/P 498-514 [» ]
    4HPL X-ray 2.00 A 1634-1748 [» ]
    ProteinModelPortali Q6W2J9.
    SMRi Q6W2J9. Positions 1463-1579, 1636-1748.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120228. 25 interactions.
    DIPi DIP-50009N.
    IntActi Q6W2J9. 8 interactions.
    MINTi MINT-2817388.

    PTM databases

    PhosphoSitei Q6W2J9.

    Proteomic databases

    MaxQBi Q6W2J9.
    PaxDbi Q6W2J9.
    PRIDEi Q6W2J9.

    Protocols and materials databases

    DNASUi 54880.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342274 ; ENSP00000345923 ; ENSG00000183337 . [Q6W2J9-2 ]
    ENST00000378444 ; ENSP00000367705 ; ENSG00000183337 . [Q6W2J9-1 ]
    ENST00000378455 ; ENSP00000367716 ; ENSG00000183337 . [Q6W2J9-4 ]
    ENST00000397354 ; ENSP00000380512 ; ENSG00000183337 . [Q6W2J9-2 ]
    GeneIDi 54880.
    KEGGi hsa:54880.
    UCSCi uc004dem.4. human. [Q6W2J9-2 ]
    uc004den.4. human. [Q6W2J9-1 ]
    uc004deo.4. human. [Q6W2J9-4 ]
    uc004deq.4. human. [Q6W2J9-3 ]

    Organism-specific databases

    CTDi 54880.
    GeneCardsi GC0XM039909.
    GeneReviewsi BCOR.
    HGNCi HGNC:20893. BCOR.
    MIMi 300166. phenotype.
    300485. gene.
    neXtProti NX_Q6W2J9.
    Orphaneti 568. Microphthalmia, Lenz type.
    2712. Oculofaciocardiodental syndrome.
    PharmGKBi PA134921737.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOVERGENi HBG050682.
    InParanoidi Q6W2J9.
    OMAi SSCPRMG.
    PhylomeDBi Q6W2J9.
    TreeFami TF333317.

    Miscellaneous databases

    ChiTaRSi BCOR. human.
    EvolutionaryTracei Q6W2J9.
    GeneWikii BCOR.
    GenomeRNAii 54880.
    NextBioi 57837.
    PROi Q6W2J9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6W2J9.
    Bgeei Q6W2J9.
    Genevestigatori Q6W2J9.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    [Graphical view ]
    Pfami PF12796. Ank_2. 1 hit.
    [Graphical view ]
    SMARTi SM00248. ANK. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiBCOR_HUMAN
    AccessioniPrimary (citable) accession number: Q6W2J9
    Secondary accession number(s): D3DWB3
    , D3DWB4, Q29RF6, Q6P4B6, Q7Z2K7, Q8TEB4, Q96DB3, Q9H232, Q9H233, Q9HCJ7, Q9NXF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3