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Q14686

- NCOA6_HUMAN

UniProt

Q14686 - NCOA6_HUMAN

Protein

Nuclear receptor coactivator 6

Gene

NCOA6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Coactivates expression in an agonist- and AF2-dependent manner. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ERs), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Probably functions as a general coactivator, rather than just a nuclear receptor coactivator. May also be involved in the coactivation of the NF-kappa-B pathway. May coactivate expression via a remodeling of chromatin and its interaction with histone acetyltransferase proteins.

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. enzyme binding Source: UniProtKB
    3. estrogen receptor binding Source: UniProtKB
    4. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. retinoid X receptor binding Source: UniProtKB
    7. thyroid hormone receptor binding Source: UniProtKB
    8. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. brain development Source: UniProtKB
    2. cellular lipid metabolic process Source: Reactome
    3. cellular response to DNA damage stimulus Source: MGI
    4. DNA recombination Source: UniProtKB
    5. DNA repair Source: UniProtKB
    6. DNA replication Source: UniProtKB
    7. DNA-templated transcription, initiation Source: UniProtKB
    8. glucocorticoid receptor signaling pathway Source: UniProtKB
    9. heart development Source: UniProtKB
    10. intracellular estrogen receptor signaling pathway Source: UniProtKB
    11. labyrinthine layer blood vessel development Source: Ensembl
    12. myeloid cell differentiation Source: UniProtKB
    13. positive regulation of transcription, DNA-templated Source: UniProtKB
    14. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    15. response to hormone Source: UniProtKB
    16. small molecule metabolic process Source: Reactome
    17. transcription initiation from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor coactivator 6
    Alternative name(s):
    Activating signal cointegrator 2
    Short name:
    ASC-2
    Amplified in breast cancer protein 3
    Cancer-amplified transcriptional coactivator ASC-2
    Nuclear receptor coactivator RAP250
    Short name:
    NRC RAP250
    Nuclear receptor-activating protein, 250 kDa
    Peroxisome proliferator-activated receptor-interacting protein
    Short name:
    PPAR-interacting protein
    Short name:
    PRIP
    Thyroid hormone receptor-binding protein
    Gene namesi
    Name:NCOA6
    Synonyms:AIB3, KIAA0181, RAP250, TRBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15936. NCOA6.

    Subcellular locationi

    GO - Cellular componenti

    1. histone methyltransferase complex Source: MGI
    2. intracellular membrane-bounded organelle Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. transcription factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi883 – 89412TSPLL…LLQSD → ENPLLVNLLQFI: Reduced binding to THRB, RXRA, ESR2 and ESR1. 1 PublicationAdd
    BLAST
    Mutagenesisi883 – 89412TSPLL…LLQSD → NLPLLVNLLQHT: Reduced binding to THRB, RXRA, ESR2 and ESR1. 1 PublicationAdd
    BLAST
    Mutagenesisi883 – 89412TSPLL…LLQSD → VNPLLVNLLQFI: Reduced binding to THRB, RXRA, ESR2 and ESR1. 1 PublicationAdd
    BLAST
    Mutagenesisi883 – 8842TS → SY: Strong increase in binding to THRB, RXRA and ESR2, but dramatic decrease in binding to ESR1. 1 Publication
    Mutagenesisi884 – 89411SPLLVNLLQSD → NPLLVNLLQLL: Reduced binding to THRB, RXRA, ESR2 and ESR1. 1 PublicationAdd
    BLAST

    Organism-specific databases

    PharmGKBiPA31475.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20632063Nuclear receptor coactivator 6PRO_0000094413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei884 – 8841Phosphoserine; by MAPK; in vitro2 Publications
    Modified residuei1321 – 13211Phosphothreonine1 Publication
    Modified residuei1819 – 18191N6-acetyllysineBy similarity
    Modified residuei1822 – 18221N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated by PRKDC.
    Phosphorylation on Ser-884 leads to a strong decrease in binding to ESR1 and ESR2.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14686.
    PaxDbiQ14686.
    PRIDEiQ14686.

    PTM databases

    PhosphoSiteiQ14686.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in brain, prostate, testis and ovary; weakly expressed in lung, thymus and small intestine.

    Gene expression databases

    BgeeiQ14686.
    CleanExiHS_NCOA6.
    GenevestigatoriQ14686.

    Organism-specific databases

    HPAiHPA004198.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts with RBM39 By similarity. Interacts in vitro with the basal transcription factors GTF2A and TBP, suggesting an autonomous transactivation function. Interacts with NCOA1, CRSP3, RBM14, the histone acetyltransferases EP300 and CREBBP, and with the methyltransferases NCOA6IP and PRMT2/HRMT1L1. Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with ZNF335; may enhance ligand-dependent transcriptional activation by nuclear hormone receptors.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102752EBI-78670,EBI-608057
    ASH2LQ9UBL37EBI-78670,EBI-540797
    CREBBPQ927932EBI-78670,EBI-81215
    KMT2CQ8NEZ45EBI-78670,EBI-1042997
    KMT2DO146866EBI-78670,EBI-996065
    RB1P064003EBI-78670,EBI-491274
    WDR5P619642EBI-78670,EBI-540834

    Protein-protein interaction databases

    BioGridi116691. 78 interactions.
    DIPiDIP-30934N.
    IntActiQ14686. 31 interactions.
    MINTiMINT-1194462.
    STRINGi9606.ENSP00000351894.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14686.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 13101310NCOA1-binding regionAdd
    BLAST
    Regioni1 – 10571057CREBBP-binding regionAdd
    BLAST
    Regioni1 – 928928TBP/GTF2A-binding regionAdd
    BLAST
    Regioni773 – 927155NCOA6IP-binding regionAdd
    BLAST
    Regioni1641 – 2063423EP300/CRSP3-binding regionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi887 – 8915LXXLL motif 1
    Motifi1491 – 14955LXXLL motif 2

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi227 – 1041815Gln-richAdd
    BLAST
    Compositional biasi372 – 3776Poly-Pro
    Compositional biasi913 – 9186Poly-Lys

    Domaini

    Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Only motif 1 is essential for the association with nuclear receptors, while adjacent Ser-884 displays selectivity for nuclear receptors.

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG052586.
    InParanoidiQ14686.
    KOiK14971.
    OMAiNARPQFI.
    OrthoDBiEOG7W9RSX.
    PhylomeDBiQ14686.
    TreeFamiTF332639.

    Family and domain databases

    InterProiIPR026638. NCOA6.
    [Graphical view]
    PANTHERiPTHR15690. PTHR15690. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q14686-1 [UniParc]FASTAAdd to Basket

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    MVLDDLPNLE DIYTSLCSST MEDSEMDFDS GLEDDDTKSD SILEDSTIFV     50
    AFKGNIDDKD FKWKLDAILK NVPNLLHMES SKLKVQKVEP WNSVRVTFNI 100
    PREAAERLRI LAQSNNQQLR DLGILSVQIE GEGAINLALA QNRSQDVRMN 150
    GPMGAGNSVR MEAGFPMASG PGIIRMNNPA TVMIPPGGNV SSSMMAPGPN 200
    PELQPRTPRP ASQSDAMDPL LSGLHIQQQS HPSGSLAPPH HPMQPVSVNR 250
    QMNPANFPQL QQQQQQQQQQ QQQQQQQQQQ QQQQQLQARP PQQHQQQQPQ 300
    GIRPQFTAPT QVPVPPGWNQ LPSGALQPPP AQGSLGTMTA NQGWKKAPLP 350
    GPMQQQLQAR PSLATVQTPS HPPPPYPFGS QQASQAHTNF PQMSNPGQFT 400
    APQMKSLQGG PSRVPTPLQQ PHLTNKSPAS SPSSFQQGSP ASSPTVNQTQ 450
    QQMGPRPPQN NPLPQGFQQP VSSPGRNPMV QQGNVPPNFM VMQQQPPNQG 500
    PQSLHPGLGG MPKRLPPGFS AGQANPNFMQ GQVPSTTATT PGNSGAPQLQ 550
    ANQNVQHAGG QGAGPPQNQM QVSHGPPNMM QPSLMGIHGN MNNQQAGTSG 600
    VPQVNLSNMQ GQPQQGPPSQ LMGMHQQIVP SQGQMVQQQG TLNPQNPMIL 650
    SRAQLMPQGQ MMVNPPSQNL GPSPQRMTPP KQMLSQQGPQ MMAPHNQMMG 700
    PQGQVLLQQN PMIEQIMTNQ MQGNKQQFNT QNQSNVMPGP AQIMRGPTPN 750
    MQGNMVQFTG QMSGQMLPQQ GPVNNSPSQV MGIQGQVLRP PGPSPHMAQQ 800
    HGDPATTANN DVSLSQMMPD VSIQQTNMVP PHVQAMQGNS ASGNHFSGHG 850
    MSFNAPFSGA PNGNQMSCGQ NPGFPVNKDV TLTSPLLVNL LQSDISAGHF 900
    GVNNKQNNTN ANKPKKKKPP RKKKNSQQDL NTPDTRPAGL EEADQPPLPG 950
    EQGINLDNSG PKLPEFSNRP PGYPSQPVEQ RPLQQMPPQL MQHVAPPPQP 1000
    PQQQPQPQLP QQQQPPPPSQ PQSQQQQQQQ QQMMMMLMMQ QDPKSVRLPV 1050
    SQNVHPPRGP LNPDSQRMPM QQSGSVPVMV SLQGPASVPP SPDKQRMPMP 1100
    VNTPLGSNSR KMVYQESPQN PSSSPLAEMA SLPEASGSEA PSVPGGPNNM 1150
    PSHVVLPQNQ LMMTGPKPGP SPLSATQGAT PQQPPVNSLP SSHGHHFPNV 1200
    AAPTQTSRPK TPNRASPRPY YPQTPNNRPP STEPSEISLS PERLNASIAG 1250
    LFPPQINIPL PPRPNLNRGF DQQGLNPTTL KAIGQAPSNL TMNPSNFATP 1300
    QTHKLDSVVV NSGKQSNSGA TKRASPSNSR RSSPGSSRKT TPSPGRQNSK 1350
    APKLTLASQT NAALLQNVEL PRNVLVSPTP LANPPVPGSF PNNSGLNPQN 1400
    STVSVAAVGG VVEDNKESLN VPQDSDCQNS QSRKEQVNIE LKAVPAQEVK 1450
    MVVPEDQSKK DGQPSDPNKL PSVEENKNLV SPAMREAPTS LSQLLDNSGA 1500
    PNVTIKPPGL TDLEVTPPVV SGEDLKKASV IPTLQDLSSS KEPSNSLNLP 1550
    HSNELCSSLV HPELSEVSSN VAPSIPPVMS RPVSSSSIST PLPPNQITVF 1600
    VTSNPITTSA NTSAALPTHL QSALMSTVVT MPNAGSKVMV SEGQSAAQSN 1650
    ARPQFITPVF INSSSIIQVM KGSQPSTIPA APLTTNSGLM PPSVAVVGPL 1700
    HIPQNIKFSS APVPPNALSS SPAPNIQTGR PLVLSSRATP VQLPSPPCTS 1750
    SPVVPSHPPV QQVKELNPDE ASPQVNTSAD QNTLPSSQST TMVSPLLTNS 1800
    PGSSGNRRSP VSSSKGKGKV DKIGQILLTK ACKKVTGSLE KGEEQYGADG 1850
    ETEGQGLDTT APGLMGTEQL STELDSKTPT PPAPTLLKMT SSPVGPGTAS 1900
    AGPSLPGGAL PTSVRSIVTT LVPSELISAV PTTKSNHGGI ASESLAGGLV 1950
    EEKVGSHPEL LPSIAPSQNL VSKETSTTAL QASVARPELE VNAAIVSGQS 2000
    SEPKEIVEKS KIPGRRNSRT EEPTVASESV ENGHRKRSSR PASASSSTKD 2050
    ITSAVQSKRR KSK 2063
    Length:2,063
    Mass (Da):219,145
    Last modified:October 17, 2006 - v3
    Checksum:i73219502F5138427
    GO

    Sequence cautioni

    The sequence AAF16403.1 differs from that shown. Reason: Frameshift at position 88.
    The sequence BAA11498.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti512 – 5121P → L.
    Corresponds to variant rs6060031 [ dbSNP | Ensembl ].
    VAR_027874
    Natural varianti955 – 9551N → S.5 Publications
    Corresponds to variant rs17092079 [ dbSNP | Ensembl ].
    VAR_027875
    Natural varianti1060 – 10601P → S in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036551
    Natural varianti1191 – 11911S → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036552
    Natural varianti1995 – 19951I → V.
    Corresponds to variant rs6060022 [ dbSNP | Ensembl ].
    VAR_027876

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177388 mRNA. Translation: AAF13595.1.
    AF208227 mRNA. Translation: AAF16403.1. Frameshift.
    AF245115 mRNA. Translation: AAF78480.1.
    AF128458 mRNA. Translation: AAF37003.1.
    AF171667 mRNA. Translation: AAF71829.1.
    D80003 mRNA. Translation: BAA11498.2. Different initiation.
    AL109824 Genomic DNA. Translation: CAB92721.2.
    CH471077 Genomic DNA. Translation: EAW76254.1.
    CH471077 Genomic DNA. Translation: EAW76255.1.
    BC136272 mRNA. Translation: AAI36273.1.
    CCDSiCCDS13241.1.
    RefSeqiNP_001229468.1. NM_001242539.1.
    NP_054790.2. NM_014071.3.
    XP_005260405.1. XM_005260348.2.
    UniGeneiHs.368971.
    Hs.736403.

    Genome annotation databases

    EnsembliENST00000359003; ENSP00000351894; ENSG00000198646.
    ENST00000374796; ENSP00000363929; ENSG00000198646.
    GeneIDi23054.
    KEGGihsa:23054.
    UCSCiuc002xav.3. human.

    Polymorphism databases

    DMDMi116242672.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177388 mRNA. Translation: AAF13595.1 .
    AF208227 mRNA. Translation: AAF16403.1 . Frameshift.
    AF245115 mRNA. Translation: AAF78480.1 .
    AF128458 mRNA. Translation: AAF37003.1 .
    AF171667 mRNA. Translation: AAF71829.1 .
    D80003 mRNA. Translation: BAA11498.2 . Different initiation.
    AL109824 Genomic DNA. Translation: CAB92721.2 .
    CH471077 Genomic DNA. Translation: EAW76254.1 .
    CH471077 Genomic DNA. Translation: EAW76255.1 .
    BC136272 mRNA. Translation: AAI36273.1 .
    CCDSi CCDS13241.1.
    RefSeqi NP_001229468.1. NM_001242539.1.
    NP_054790.2. NM_014071.3.
    XP_005260405.1. XM_005260348.2.
    UniGenei Hs.368971.
    Hs.736403.

    3D structure databases

    ProteinModelPortali Q14686.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116691. 78 interactions.
    DIPi DIP-30934N.
    IntActi Q14686. 31 interactions.
    MINTi MINT-1194462.
    STRINGi 9606.ENSP00000351894.

    PTM databases

    PhosphoSitei Q14686.

    Polymorphism databases

    DMDMi 116242672.

    Proteomic databases

    MaxQBi Q14686.
    PaxDbi Q14686.
    PRIDEi Q14686.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359003 ; ENSP00000351894 ; ENSG00000198646 .
    ENST00000374796 ; ENSP00000363929 ; ENSG00000198646 .
    GeneIDi 23054.
    KEGGi hsa:23054.
    UCSCi uc002xav.3. human.

    Organism-specific databases

    CTDi 23054.
    GeneCardsi GC20M033302.
    H-InvDB HIX0015752.
    HGNCi HGNC:15936. NCOA6.
    HPAi HPA004198.
    MIMi 605299. gene.
    neXtProti NX_Q14686.
    PharmGKBi PA31475.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG052586.
    InParanoidi Q14686.
    KOi K14971.
    OMAi NARPQFI.
    OrthoDBi EOG7W9RSX.
    PhylomeDBi Q14686.
    TreeFami TF332639.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Miscellaneous databases

    ChiTaRSi NCOA6. human.
    GeneWikii NCOA6.
    GenomeRNAii 23054.
    NextBioi 44111.
    PROi Q14686.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14686.
    CleanExi HS_NCOA6.
    Genevestigatori Q14686.

    Family and domain databases

    InterProi IPR026638. NCOA6.
    [Graphical view ]
    PANTHERi PTHR15690. PTHR15690. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."
      Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.
      J. Biol. Chem. 274:34283-34293(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CREBBP; NCOA1; GTF2A; TBP; RXRA; ESR1; RARA AND THRA, VARIANT SER-955.
    2. "A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP."
      Mahajan M.A., Samuels H.H.
      Mol. Cell. Biol. 20:5048-5063(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, INTERACTION WITH CREBBP; RXRA; ESR1; NR3C1; RARA; VDR AND THRA, VARIANT SER-955.
    3. "Cloning and characterization of RAP250, a nuclear receptor coactivator."
      Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.
      J. Biol. Chem. 275:5308-5317(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PPARA; PPARG; ESR1; ESR2 AND THR, VARIANT SER-955.
      Tissue: Testis.
    4. "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator."
      Ko L., Cardona G.R., Chin W.W.
      Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY PRKDC, INTERACTION WITH THR; RAR; EP300 AND CRSP3, VARIANT SER-955.
      Tissue: Lymphocyte.
    5. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-955.
      Tissue: Bone marrow.
    6. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    7. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Tissue: Cerebellum.
    10. "Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function."
      Zhu Y.-J., Qi C., Cao W.-Q., Yeldandi A.V., Rao M.S., Reddy J.K.
      Proc. Natl. Acad. Sci. U.S.A. 98:10380-10385(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA6IP.
    11. "Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM)."
      Iwasaki T., Chin W.W., Ko L.
      J. Biol. Chem. 276:33375-33383(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM14.
    12. "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
      Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
      J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT2.
    13. "NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC."
      Mahajan M.A., Murray A., Samuels H.H.
      Mol. Cell. Biol. 22:6883-6894(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF335.
    14. "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins."
      Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J., Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G., Azorsa D.O., Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., Lee J.W.
      Mol. Cell. Biol. 23:140-149(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
      Tissue: Cervix carcinoma.
    15. "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs."
      Ko L., Cardona G.R., Iwasaki T., Bramlett K.S., Burris T.P., Chin W.W.
      Mol. Endocrinol. 16:128-140(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 883-THR--GLU-894, PHOSPHORYLATION AT SER-884.
    16. "Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases."
      Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y., Lee S.K., Roeder R.G., Lee J.W.
      Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
    17. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
      Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
      J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
    18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-1060 AND ARG-1191.

    Entry informationi

    Entry nameiNCOA6_HUMAN
    AccessioniPrimary (citable) accession number: Q14686
    Secondary accession number(s): A6NLF1
    , B2RMN5, E1P5P7, Q9NTZ9, Q9UH74, Q9UK86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 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

    Miscellaneous

    Frequently amplified or overexpressed in colon, breast and lung cancers.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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

    External Data

    Dasty 3