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Q9Y6Q9

- NCOA3_HUMAN

UniProt

Q9Y6Q9 - NCOA3_HUMAN

Protein

Nuclear receptor coactivator 3

Gene

NCOA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit.

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

    Enzyme regulationi

    Coactivator activity on nuclear receptors and NF-kappa-B pathways is enhanced by various hormones, and the TNF cytokine, respectively. TNF stimulation probably enhances phosphorylation, which in turn activates coactivator function. In contrast, acetylation by CREBBP apparently suppresses coactivation of target genes by disrupting its association with nuclear receptors. Binds to CSNK1D.

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. chromatin binding Source: Ensembl
    3. histone acetyltransferase activity Source: UniProtKB
    4. ligand-dependent nuclear receptor binding Source: UniProtKB
    5. ligand-dependent nuclear receptor transcription coactivator activity Source: InterPro
    6. nuclear hormone receptor binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein N-terminus binding Source: UniProtKB
    9. signal transducer activity Source: InterPro
    10. thyroid hormone receptor binding Source: UniProtKB
    11. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. developmental growth Source: Ensembl
    3. histone acetylation Source: GOC
    4. labyrinthine layer morphogenesis Source: Ensembl
    5. mammary gland branching involved in thelarche Source: Ensembl
    6. multicellular organism growth Source: Ensembl
    7. positive regulation of gene expression Source: UniProtKB
    8. positive regulation of keratinocyte differentiation Source: UniProtKB
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    11. receptor transactivation Source: UniProtKB
    12. regulation of RNA biosynthetic process Source: UniProtKB
    13. transcription, DNA-templated Source: UniProtKB-KW
    14. vagina development Source: Ensembl

    Keywords - Molecular functioni

    Activator, Acyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiQ9Y6Q9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor coactivator 3 (EC:2.3.1.48)
    Short name:
    NCoA-3
    Alternative name(s):
    ACTR
    Amplified in breast cancer 1 protein
    Short name:
    AIB-1
    CBP-interacting protein
    Short name:
    pCIP
    Class E basic helix-loop-helix protein 42
    Short name:
    bHLHe42
    Receptor-associated coactivator 3
    Short name:
    RAC-3
    Steroid receptor coactivator protein 3
    Short name:
    SRC-3
    Thyroid hormone receptor activator molecule 1
    Short name:
    TRAM-1
    Gene namesi
    Name:NCOA3
    Synonyms:AIB1, BHLHE42, RAC3, TRAM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:7670. NCOA3.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi616 – 6161K → Q: Strongly reduces acetylation by CREBBP. 1 Publication
    Mutagenesisi619 – 6202KK → QQ: Abolishes acetylation by CREBBP.
    Mutagenesisi647 – 6471K → Q: Does not affect acetylation by CREBBP. 1 Publication
    Mutagenesisi681 – 6811K → Q: Does not affect acetylation by CREBBP. 1 Publication
    Mutagenesisi687 – 6871K → Q: Does not affect acetylation by CREBBP. 1 Publication
    Mutagenesisi700 – 7001K → Q: Does not affect acetylation by CREBBP. 1 Publication
    Mutagenesisi708 – 7081K → Q: Does not affect acetylation by CREBBP. 1 Publication

    Organism-specific databases

    PharmGKBiPA31472.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 14241423Nuclear receptor coactivator 3PRO_0000094406Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei214 – 2141Phosphoserine3 Publications
    Modified residuei551 – 5511Phosphoserine2 Publications
    Modified residuei601 – 6011Phosphoserine; by CK12 Publications
    Modified residuei616 – 6161N6-acetyllysine; by CREBBP1 Publication
    Modified residuei619 – 6191N6-acetyllysine; by CREBBP1 Publication
    Modified residuei620 – 6201N6-acetyllysine; by CREBBP1 Publication
    Modified residuei687 – 6871N6-acetyllysine1 Publication
    Modified residuei728 – 7281Phosphoserine2 Publications
    Modified residuei857 – 8571Phosphoserine5 Publications
    Modified residuei860 – 8601PhosphoserineBy similarity
    Modified residuei867 – 8671Phosphoserine3 Publications

    Post-translational modificationi

    Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function.3 Publications
    Methylated by CARM1.By similarity
    Phosphorylated by IKK complex. Regulated its function. Phosphorylation at Ser-601 by CK1 promotes coactivator function.6 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y6Q9.
    PaxDbiQ9Y6Q9.
    PRIDEiQ9Y6Q9.

    PTM databases

    PhosphoSiteiQ9Y6Q9.

    Expressioni

    Tissue specificityi

    Widely expressed. High expression in heart, skeletal muscle, pancreas and placenta. Low expression in brain, and very low in lung, liver and kidney.

    Gene expression databases

    ArrayExpressiQ9Y6Q9.
    BgeeiQ9Y6Q9.
    CleanExiHS_NCOA3.
    HS_RAC3.
    HS_TRAM1.
    GenevestigatoriQ9Y6Q9.

    Organism-specific databases

    HPAiCAB009800.
    HPA024210.

    Interactioni

    Subunit structurei

    Interacts with CARM1 By similarity. Present in a complex containing NCOA2, IKKA, IKKB, IKBKG and the histone acetyltransferase protein CREBBP. Interacts with CASP8AP2, NR3C1 and PCAF. Interacts with ATAD2 and this interaction is enhanced by estradiol. Found in a complex containing NCOA3, AR and MAK. Interacts with DDX5. Interacts with PSMB9. Interacts with NPAS2.By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX17Q928412EBI-81196,EBI-746012
    EP300Q094722EBI-81196,EBI-447295
    ESR1P033722EBI-81196,EBI-78473
    IKBKBO149203EBI-81196,EBI-81266
    PSMB9P280653EBI-81196,EBI-603300
    PSME3P612895EBI-81196,EBI-355546
    PTENP604842EBI-81196,EBI-696162
    SPOPO437916EBI-81196,EBI-743549
    VdrP482812EBI-81196,EBI-346797From a different organism.

    Protein-protein interaction databases

    BioGridi113841. 99 interactions.
    DIPiDIP-30876N.
    IntActiQ9Y6Q9. 43 interactions.
    MINTiMINT-231818.

    Structurei

    Secondary structure

    1
    1424
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi619 – 6268
    Helixi736 – 7438
    Helixi1049 – 106012
    Helixi1069 – 10757
    Helixi1078 – 10847
    Helixi1086 – 10883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KBHNMR-A1045-1091[»]
    3L3XX-ray1.55B618-629[»]
    3L3ZX-ray2.00B735-746[»]
    DisProtiDP00343.
    ProteinModelPortaliQ9Y6Q9.
    SMRiQ9Y6Q9. Positions 34-367, 1045-1091.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6Q9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 8258bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini110 – 18071PASPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1023 – 109371Interaction with CREBBPAdd
    BLAST
    Regioni1097 – 1304208AcetyltransferaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi685 – 6895LXXLL motif 1
    Motifi738 – 7425LXXLL motif 2
    Motifi1057 – 10615LXXLL motif 3

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi505 – 671167Ser-richAdd
    BLAST
    Compositional biasi976 – 9805Poly-Gln
    Compositional biasi1248 – 127831Poly-GlnAdd
    BLAST
    Compositional biasi1392 – 141726Met-richAdd
    BLAST

    Domaini

    Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and 2 are essential for the association with nuclear receptors, and constitute the RID domain (Receptor-interacting domain).

    Sequence similaritiesi

    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
    Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG315556.
    HOVERGENiHBG052583.
    InParanoidiQ9Y6Q9.
    KOiK11256.
    OMAiDGNIVFV.
    OrthoDBiEOG72JWFB.
    PhylomeDBiQ9Y6Q9.
    TreeFamiTF332652.

    Family and domain databases

    Gene3Di4.10.280.10. 1 hit.
    4.10.630.10. 2 hits.
    InterProiIPR011598. bHLH_dom.
    IPR010011. DUF1518.
    IPR028818. NCOA3.
    IPR009110. Nuc_rcpt_coact.
    IPR014920. Nuc_rcpt_coact_Ncoa-typ.
    IPR017426. Nuclear_rcpt_coactivator.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    IPR014935. SRC-1.
    IPR008955. Src1_rcpt_coact.
    [Graphical view]
    PANTHERiPTHR10684. PTHR10684. 1 hit.
    PTHR10684:SF3. PTHR10684:SF3. 1 hit.
    PfamiPF07469. DUF1518. 1 hit.
    PF08815. Nuc_rec_co-act. 1 hit.
    PF00989. PAS. 1 hit.
    PF08832. SRC-1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
    SMARTiSM00353. HLH. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    SSF69125. SSF69125. 1 hit.
    PROSITEiPS50888. BHLH. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9Y6Q9-1) [UniParc]FASTAAdd to Basket

    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

    MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE     50
    LISANLSDID NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV 100
    SSTGQGVIDK DSLGPLLLQA LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE 150
    DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG VSWTNETQRQ KSHTFNCRML 200
    MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE DLQSCMICVA 250
    RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC 300
    IQRFFSLNDG QSWSQKRHYQ EAYLNGHAET PVYRFSLADG TIVTAQTKSK 350
    LFRNPVTNDR HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG 400
    MSMSPNQGLQ MPSSRAYGLA DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS 450
    PSSYQNNNYG LNMSSPPHGS PGLAPNQQNI MISPRNRGSP KIASHQFSPV 500
    AGVHSPMASS GNTGNHSFSS SSLSALQAIS EGVGTSLLST LSSPGPKLDN 550
    SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR DHLSDKESKE 600
    SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS 650
    VSVTSPSGVS SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK 700
    ITAEATGKDT SSITSCGDGN VVKQEQLSPK KKENNALLRY LLDRDDPSDA 750
    LSKELQPQVE GVDNKMSQCT SSTIPSSSQE KDPKIKTETS EEGSGDLDNL 800
    DAILGDLTSS DFYNNSISSN GSHLGTKQQV FQGTNSLGLK SSQSVQSIRP 850
    PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR MMDSQENYGS 900
    SMGGPNRNVT VTQTPSSGDW GLPNSKAGRM EPMNSNSMGR PGGDYNTSLP 950
    RPALGGSIPT LPLRSNSIPG ARPVLQQQQQ MLQMRPGEIP MGMGANPYGQ 1000
    AAASNQLGSW PDGMLSMEQV SHGTQNRPLL RNSLDDLVGP PSNLEGQSDE 1050
    RALLDQLHTL LSNTDATGLE EIDRALGIPE LVNQGQALEP KQDAFQGQEA 1100
    AVMMDQKAGL YGQTYPAQGP PMQGGFHLQG QSPSFNSMMN QMNQQGNFPL 1150
    QGMHPRANIM RPRTNTPKQL RMQLQQRLQG QQFLNQSRQA LELKMENPTA 1200
    GGAAVMRPMM QPQVSSQQGF LNAQMVAQRS RELLSHHFRQ QRVAMMMQQQ 1250
    QQQQQQQQQQ QQQQQQQQQQ QQQQQQTQAF SPPPNVTASP SMDGLLAGPT 1300
    MPQAPPQQFP YQPNYGMGQQ PDPAFGRVSS PPNAMMSSRM GPSQNPMMQH 1350
    PQAASIYQSS EMKGWPSGNL ARNSSFSQQQ FAHQGNPAVY SMVHMNGSSG 1400
    HMGQMNMNPM PMSGMPMGPD QKYC 1424
    Length:1,424
    Mass (Da):155,293
    Last modified:November 1, 1999 - v1
    Checksum:i732CDF0423161679
    GO
    Isoform 2 (identifier: Q9Y6Q9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         903-917: Missing.

    Show »
    Length:1,409
    Mass (Da):153,797
    Checksum:i04B4DF09150BD916
    GO
    Isoform 3 (identifier: Q9Y6Q9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         321-321: E → EVTSDGIFSPT
         903-917: Missing.
         1214-1217: Missing.

    Show »
    Length:1,415
    Mass (Da):154,400
    Checksum:i4A162AB05BA34062
    GO
    Isoform 4 (identifier: Q9Y6Q9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         321-321: E → EVTSDGIFSPT
         837-901: Missing.
         903-917: Missing.
         1214-1217: Missing.

    Show »
    Length:1,350
    Mass (Da):147,499
    Checksum:iF75584B329A892C4
    GO
    Isoform 5 (identifier: Q9Y6Q9-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1214-1217: Missing.

    Show »
    Length:1,420
    Mass (Da):154,892
    Checksum:i654343CEA0855C60
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1322DG → EA in AAC51663. (PubMed:9238002)Curated

    Polymorphismi

    The length of the poly-Gln region is polymorphic in the normal population.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti218 – 2181R → C.1 Publication
    Corresponds to variant rs6094752 [ dbSNP | Ensembl ].
    VAR_053527
    Natural varianti220 – 2201R → I.1 Publication
    VAR_060695
    Natural varianti369 – 3691L → F.
    Corresponds to variant rs6094756 [ dbSNP | Ensembl ].
    VAR_053528
    Natural varianti460 – 4601G → R.
    Corresponds to variant rs1052765 [ dbSNP | Ensembl ].
    VAR_013831
    Natural varianti556 – 5561I → V.1 Publication
    Corresponds to variant rs72645272 [ dbSNP | Ensembl ].
    VAR_060696
    Natural varianti559 – 5591P → S.1 Publication
    Corresponds to variant rs2230781 [ dbSNP | Ensembl ].
    VAR_013832
    Natural varianti586 – 5861Q → H.1 Publication
    Corresponds to variant rs2230782 [ dbSNP | Ensembl ].
    VAR_013833
    Natural varianti777 – 7771S → A.1 Publication
    Corresponds to variant rs2230783 [ dbSNP | Ensembl ].
    VAR_053529
    Natural varianti1247 – 12471M → K.1 Publication
    VAR_060697
    Natural varianti1247 – 12471M → L.1 Publication
    VAR_060698
    Natural varianti1248 – 12503Missing.2 Publications
    VAR_013834

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei321 – 3211E → EVTSDGIFSPT in isoform 3 and isoform 4. 1 PublicationVSP_003405
    Alternative sequencei837 – 90165Missing in isoform 4. 1 PublicationVSP_003406Add
    BLAST
    Alternative sequencei903 – 91715Missing in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_003407Add
    BLAST
    Alternative sequencei1214 – 12174Missing in isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_003408

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF016031 mRNA. Translation: AAC51849.1.
    AF036892 mRNA. Translation: AAB92368.1.
    AF012108 mRNA. Translation: AAC51677.1.
    AF010227 mRNA. Translation: AAC51663.1.
    EF488684 Genomic DNA. Translation: ABO43042.1.
    AL034418 Genomic DNA. Translation: CAB40662.1.
    AL034418 Genomic DNA. Translation: CAC17693.1.
    AL034418 Genomic DNA. Translation: CAI42141.1.
    CH471077 Genomic DNA. Translation: EAW75698.1.
    CH471077 Genomic DNA. Translation: EAW75702.1.
    BC119001 mRNA. Translation: AAI19002.1.
    CCDSiCCDS13406.1. [Q9Y6Q9-5]
    CCDS13407.1. [Q9Y6Q9-1]
    CCDS54472.1. [Q9Y6Q9-3]
    PIRiT03851.
    RefSeqiNP_001167559.1. NM_001174088.1. [Q9Y6Q9-3]
    NP_006525.2. NM_006534.3. [Q9Y6Q9-5]
    NP_858045.1. NM_181659.2. [Q9Y6Q9-1]
    UniGeneiHs.592142.

    Genome annotation databases

    EnsembliENST00000371997; ENSP00000361065; ENSG00000124151. [Q9Y6Q9-3]
    ENST00000371998; ENSP00000361066; ENSG00000124151. [Q9Y6Q9-1]
    ENST00000372004; ENSP00000361073; ENSG00000124151. [Q9Y6Q9-5]
    GeneIDi8202.
    KEGGihsa:8202.
    UCSCiuc002xtk.3. human. [Q9Y6Q9-1]
    uc002xtl.3. human. [Q9Y6Q9-5]
    uc010ght.2. human. [Q9Y6Q9-3]

    Polymorphism databases

    DMDMi23396777.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF016031 mRNA. Translation: AAC51849.1 .
    AF036892 mRNA. Translation: AAB92368.1 .
    AF012108 mRNA. Translation: AAC51677.1 .
    AF010227 mRNA. Translation: AAC51663.1 .
    EF488684 Genomic DNA. Translation: ABO43042.1 .
    AL034418 Genomic DNA. Translation: CAB40662.1 .
    AL034418 Genomic DNA. Translation: CAC17693.1 .
    AL034418 Genomic DNA. Translation: CAI42141.1 .
    CH471077 Genomic DNA. Translation: EAW75698.1 .
    CH471077 Genomic DNA. Translation: EAW75702.1 .
    BC119001 mRNA. Translation: AAI19002.1 .
    CCDSi CCDS13406.1. [Q9Y6Q9-5 ]
    CCDS13407.1. [Q9Y6Q9-1 ]
    CCDS54472.1. [Q9Y6Q9-3 ]
    PIRi T03851.
    RefSeqi NP_001167559.1. NM_001174088.1. [Q9Y6Q9-3 ]
    NP_006525.2. NM_006534.3. [Q9Y6Q9-5 ]
    NP_858045.1. NM_181659.2. [Q9Y6Q9-1 ]
    UniGenei Hs.592142.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KBH NMR - A 1045-1091 [» ]
    3L3X X-ray 1.55 B 618-629 [» ]
    3L3Z X-ray 2.00 B 735-746 [» ]
    DisProti DP00343.
    ProteinModelPortali Q9Y6Q9.
    SMRi Q9Y6Q9. Positions 34-367, 1045-1091.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113841. 99 interactions.
    DIPi DIP-30876N.
    IntActi Q9Y6Q9. 43 interactions.
    MINTi MINT-231818.

    Chemistry

    BindingDBi Q9Y6Q9.
    ChEMBLi CHEMBL2095161.

    PTM databases

    PhosphoSitei Q9Y6Q9.

    Polymorphism databases

    DMDMi 23396777.

    Proteomic databases

    MaxQBi Q9Y6Q9.
    PaxDbi Q9Y6Q9.
    PRIDEi Q9Y6Q9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371997 ; ENSP00000361065 ; ENSG00000124151 . [Q9Y6Q9-3 ]
    ENST00000371998 ; ENSP00000361066 ; ENSG00000124151 . [Q9Y6Q9-1 ]
    ENST00000372004 ; ENSP00000361073 ; ENSG00000124151 . [Q9Y6Q9-5 ]
    GeneIDi 8202.
    KEGGi hsa:8202.
    UCSCi uc002xtk.3. human. [Q9Y6Q9-1 ]
    uc002xtl.3. human. [Q9Y6Q9-5 ]
    uc010ght.2. human. [Q9Y6Q9-3 ]

    Organism-specific databases

    CTDi 8202.
    GeneCardsi GC20P046130.
    HGNCi HGNC:7670. NCOA3.
    HPAi CAB009800.
    HPA024210.
    MIMi 601937. gene.
    neXtProti NX_Q9Y6Q9.
    PharmGKBi PA31472.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG315556.
    HOVERGENi HBG052583.
    InParanoidi Q9Y6Q9.
    KOi K11256.
    OMAi DGNIVFV.
    OrthoDBi EOG72JWFB.
    PhylomeDBi Q9Y6Q9.
    TreeFami TF332652.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki Q9Y6Q9.

    Miscellaneous databases

    ChiTaRSi NCOA3. human.
    EvolutionaryTracei Q9Y6Q9.
    GeneWikii Nuclear_receptor_coactivator_3.
    GenomeRNAii 8202.
    NextBioi 30907.
    PROi Q9Y6Q9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6Q9.
    Bgeei Q9Y6Q9.
    CleanExi HS_NCOA3.
    HS_RAC3.
    HS_TRAM1.
    Genevestigatori Q9Y6Q9.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    4.10.630.10. 2 hits.
    InterProi IPR011598. bHLH_dom.
    IPR010011. DUF1518.
    IPR028818. NCOA3.
    IPR009110. Nuc_rcpt_coact.
    IPR014920. Nuc_rcpt_coact_Ncoa-typ.
    IPR017426. Nuclear_rcpt_coactivator.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    IPR014935. SRC-1.
    IPR008955. Src1_rcpt_coact.
    [Graphical view ]
    PANTHERi PTHR10684. PTHR10684. 1 hit.
    PTHR10684:SF3. PTHR10684:SF3. 1 hit.
    Pfami PF07469. DUF1518. 1 hit.
    PF08815. Nuc_rec_co-act. 1 hit.
    PF00989. PAS. 1 hit.
    PF08832. SRC-1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038181. Nuclear_receptor_coactivator. 1 hit.
    SMARTi SM00353. HLH. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    SSF69125. SSF69125. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1."
      Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.
      J. Biol. Chem. 272:27629-27634(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CREBBP; PCAF; RARA; RXRA; THRA AND ESR.
      Tissue: Pituitary.
    2. "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300."
      Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M.
      Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ENZYME ACTIVITY, VARIANT 1248-GLN--GLN-1250 DEL.
      Tissue: Leukemia.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH ESR.
      Tissue: Lung.
    4. "RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2."
      Li H., Gomes P.J., Chen J.D.
      Proc. Natl. Acad. Sci. U.S.A. 94:8479-8484(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH VDR; RARA; PPARA; RXRA; THRA AND ESR, VARIANT 1248-GLN--GLN-1250 DEL.
      Tissue: Brain.
    5. NIEHS SNPs program
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-218; ILE-220; VAL-556; SER-559; HIS-586; ALA-777; LEU-1247 AND LYS-1247.
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 5).
    9. "Polymorphic exonic CAG microsatellites in the gene amplified in breast cancer (AIB1 gene)."
      Shirazi S.K., Bober M.A., Coetzee G.A.
      Clin. Genet. 54:102-103(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM OF POLY-GLN REGION.
    10. "Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase."
      Chen H., Lin R.J., Xie W., Wilpitz D., Evans R.M.
      Cell 98:675-686(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-616; LYS-619 AND LYS-620 BY CREBBP, MUTAGENESIS OF LYS-616; 619-LYS-LYS-620; LYS-647; LYS-681; LYS-687; LYS-700 AND LYS-708.
    11. Cited for: INTERACTION WITH NFKB1.
    12. "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA."
      Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.
      EMBO J. 20:1341-1352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX5.
    13. "Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase."
      Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
      Mol. Cell. Biol. 22:3549-3561(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; IKKA; IKKB AND IKBKG, PHOSPHORYLATION.
    14. "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
      Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
      Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR3C1.
    15. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
      Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
      J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NPAS2.
    16. "FLASH interacts with p160 coactivator subtypes and differentially suppresses transcriptional activity of steroid hormone receptors."
      Kino T., Ichijo T., Chrousos G.P.
      J. Steroid Biochem. Mol. Biol. 92:357-363(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CASP8AP2.
    17. "Male germ cell-associated kinase, a male-specific kinase regulated by androgen, is a coactivator of androgen receptor in prostate cancer cells."
      Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M., Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.
      Cancer Res. 66:8439-8447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    18. "The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription."
      Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R., Sun X., Shang Y.
      EMBO J. 25:4223-4233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMB9.
    19. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification."
      Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.
      Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATAD2.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-551; SER-728 AND SER-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "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].
    23. "CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an estrogen-dependent manner and regulates ERalpha-AIB1 interactions."
      Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.
      Nucleic Acids Res. 37:3110-3123(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-601 BY CSNK1D/CK1, INTERACTION WITH CSNK1D.
    24. "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-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "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-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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-214; SER-857 AND SER-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNCOA3_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6Q9
    Secondary accession number(s): A4LAZ5
    , Q0VF45, Q5JYD9, Q5JYE0, Q9BR49, Q9UPC9, Q9UPG4, Q9UPG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 160 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

    Miscellaneous

    NCOA3 is frequently amplified or overexpressed in breast and ovarian cancers.

    Keywords - Technical termi

    3D-structure, 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
    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