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P70365

- NCOA1_MOUSE

UniProt

P70365 - NCOA1_MOUSE

Protein

Nuclear receptor coactivator 1

Gene

Ncoa1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (11 Oct 2004)
      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. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3.4 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. DNA binding Source: MGI
    3. histone acetyltransferase activity Source: UniProtKB-EC
    4. ligand-dependent nuclear receptor transcription coactivator activity Source: Ensembl
    5. protein binding Source: MGI
    6. RNA polymerase II regulatory region DNA binding Source: Ensembl
    7. signal transducer activity Source: InterPro
    8. transcription coactivator activity Source: UniProtKB
    9. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to hormone stimulus Source: Ensembl
    2. cerebellum development Source: Ensembl
    3. cerebral cortex development Source: Ensembl
    4. estrous cycle phase Source: Ensembl
    5. hippocampus development Source: Ensembl
    6. histone H4 acetylation Source: UniProtKB
    7. hypothalamus development Source: Ensembl
    8. labyrinthine layer morphogenesis Source: MGI
    9. lactation Source: Ensembl
    10. male gonad development Source: Ensembl
    11. male mating behavior Source: Ensembl
    12. positive regulation of apoptotic process Source: UniProtKB
    13. positive regulation of female receptivity Source: Ensembl
    14. positive regulation of neuron differentiation Source: UniProtKB
    15. positive regulation of transcription, DNA-templated Source: UniProtKB
    16. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    17. positive regulation of transcription from RNA polymerase II promoter by galactose Source: UniProtKB
    18. regulation of cellular response to drug Source: UniProtKB
    19. regulation of RNA biosynthetic process Source: UniProtKB
    20. response to estradiol Source: Ensembl
    21. response to progesterone Source: Ensembl
    22. response to retinoic acid Source: Ensembl
    23. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Acyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_118837. Rora activates circadian gene expression.
    REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor coactivator 1 (EC:2.3.1.48)
    Short name:
    NCoA-1
    Alternative name(s):
    Nuclear receptor coactivator protein 1
    Short name:
    mNRC-1
    Steroid receptor coactivator 1
    Short name:
    SRC-1
    Gene namesi
    Name:Ncoa1
    Synonyms:Src1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1276523. Ncoa1.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. neuron projection Source: Ensembl
    3. nuclear chromatin Source: Ensembl
    4. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice show partial hormone resistance: target organs such as uterus, prostate, testis and mammary gland exhibiting decreased growth and development in response to steroid hormones. Moreover, such mice are prone to obesity due to reduced energy expenditure.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi695 – 6984HRLL → AAAA: Abolishes the interactions with estrogen and retinoid-acids receptors. 1 Publication
    Mutagenesisi756 – 7594RYLL → AAAA: Abolishes the interactions with estrogen and retinoid-acids receptors. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 14471446Nuclear receptor coactivator 1PRO_0000094401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei22 – 221Phosphoserine1 Publication
    Modified residuei372 – 3721Phosphoserine1 Publication
    Modified residuei395 – 3951PhosphoserineBy similarity
    Modified residuei518 – 5181PhosphoserineBy similarity
    Modified residuei570 – 5701PhosphoserineBy similarity
    Modified residuei702 – 7021Phosphoserine1 Publication
    Cross-linki738 – 738Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki780 – 780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei1039 – 10391PhosphoserineBy similarity
    Modified residuei1185 – 11851PhosphothreonineBy similarity
    Modified residuei1191 – 11911PhosphoserineBy similarity

    Post-translational modificationi

    Sumoylated; sumoylation increases its interaction with PGR and prolongs its retention in the nucleus. It does not prevent its ubiquitination and does not exert a clear effect on the stability of the protein By similarity.By similarity
    Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP70365.
    PRIDEiP70365.

    PTM databases

    PhosphoSiteiP70365.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Gene expression databases

    BgeeiP70365.
    CleanExiMM_NCOA1.
    GenevestigatoriP70365.

    Interactioni

    Subunit structurei

    Interacts with NCOA6 and NCOA2. Interacts with the FDL motif of STAT5A and STAT5B. Interacts with the LXXLL motif of STAT6. Interacts with STAT3 following IL-6 stimulation. Interacts with the basal transcription factor GTF2B. Interacts with COPS5, NR3C1, PCAF and TTLL5/STAMP. Interacts with the histone acetyltransferases EP300 and CREBBP, and the methyltransferase CARM1. Interacts with PSMB9. Interacts with UBE2L3; they functionally interact to regulate progesterone receptor transcriptional activity. Interacts with PRMT2 and DDX5. Interacts with ASXL1. Interacts with PRMT6. Interacts (via LXXLL 1, 2 and 3 motifs) with RORC (via AF-2 motif). Interacts in a ligand-dependent fashion with RXRA.5 Publications

    Protein-protein interaction databases

    BioGridi201707. 14 interactions.
    MINTiMINT-1530933.

    Structurei

    Secondary structure

    1
    1447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi261 – 2666
    Beta strandi272 – 2765
    Helixi278 – 2814
    Helixi288 – 29912
    Helixi309 – 32012
    Beta strandi321 – 3244
    Beta strandi328 – 3314
    Beta strandi337 – 34711
    Beta strandi357 – 3659
    Turni687 – 6904
    Helixi693 – 6997

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OJ5X-ray2.20A257-385[»]
    2O9IX-ray2.80C/D686-700[»]
    4DMAX-ray2.30E/F690-704[»]
    ProteinModelPortaliP70365.
    SMRiP70365. Positions 29-367, 926-980.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP70365.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 8058bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini109 – 18072PASPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni361 – 568208Interaction with STAT3Add
    BLAST
    Regioni787 – 994208Interaction with CREBBPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi46 – 505LXXLL motif 1
    Motifi112 – 1165LXXLL motif 2
    Motifi637 – 6415LXXLL motif 3
    Motifi694 – 6985LXXLL motif 4
    Motifi755 – 7595LXXLL motif 5
    Motifi919 – 9235LXXLL motif 6
    Motifi1441 – 14455LXXLL motif 7

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi389 – 686298Ser-richAdd
    BLAST
    Compositional biasi1059 – 114486Gln-richAdd
    BLAST

    Domaini

    The C-terminal (1113-1447) part mediates the histone acetyltransferase (HAT) activity.By similarity

    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.
    GeneTreeiENSGT00530000063109.
    HOGENOMiHOG000230947.
    HOVERGENiHBG052583.
    InParanoidiP70365.
    KOiK09101.
    OMAiQITPQPP.
    OrthoDBiEOG789C9C.
    PhylomeDBiP70365.
    TreeFamiTF332652.

    Family and domain databases

    Gene3Di4.10.280.10. 1 hit.
    4.10.630.10. 2 hits.
    InterProiIPR011598. bHLH_dom.
    IPR010011. DUF1518.
    IPR028819. NCOA1.
    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:SF1. PTHR10684:SF1. 1 hit.
    PfamiPF07469. DUF1518. 2 hits.
    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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P70365-1) [UniParc]FASTAAdd to Basket

    Also known as: SRC-1A, SRC1a

    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

    MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL     50
    SANISDIDSL SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS 100
    SSSQGVIEKE SLGPLLLEAL DGFFFVVNCE GRIVFVSENV TSYLGYNQEE 150
    LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG VPWPQEATRR NSHTFNCRML 200
    IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ SCLICIARRL 250
    PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 300
    QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ 350
    SPDMQPFIMG IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV 400
    TRSSTLPPSN NNMVSARVNR QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI 450
    VANVALNQGQ AGSQSSNPSL NLNNSPMEGT GIALSQFMSP RRQANSGLAT 500
    RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT SLQGMNEGPN 550
    NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD 600
    NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR 650
    HADIDTSCKD VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE 700
    GSPSDITTLS VEPEKKDSVP ASTAVSVSGQ SQGSASIKLE LDAAKKKESK 750
    DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK VEKKEQMDPC NTNPTPMTKP 800
    APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD RMDGAVTGVS 850
    IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN 900
    TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD 950
    ETELAELDRA LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP 1000
    YSSPSPTAGL SGPFQGMVRQ KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL 1050
    NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ AILNQFAANA PVGMNMRSGM 1100
    QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML MRHQSFGNNI 1150
    PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP 1200
    EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT 1250
    FAPSLSPGSS MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN 1300
    VFSQAVQSQP APAQPGVYNN MSITVSMAGG NANIQNMNPM MGQMQMSSLQ 1350
    MPGMNTVCSE QMNDPALRHT GLYCNQLSST DLLKTDADGN QQVQQVQVFA 1400
    DVQCTVNLVG GDPYLNQPGP LGTQKPTSGP QTPQAQQKSL LQQLLTE 1447
    Length:1,447
    Mass (Da):157,016
    Last modified:October 11, 2004 - v2
    Checksum:i65C08AFFCF14241D
    GO
    Isoform 2 (identifier: P70365-2) [UniParc]FASTAAdd to Basket

    Also known as: SRC-1E, SRC1e

    The sequence of this isoform differs from the canonical sequence as follows:
         1392-1447: QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE → DKKTEEFFSVVTTD

    Show »
    Length:1,405
    Mass (Da):152,644
    Checksum:i92088DAE1A6A7F77
    GO
    Isoform 3 (identifier: P70365-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1392-1447: QVQQVQVFAD...KSLLQQLLTE → VSKKDNPSAELADSITLDTWRTSHGIC

    Note: No experimental confirmation available.

    Show »
    Length:1,418
    Mass (Da):153,943
    Checksum:i2AE9E75D49E5D1DC
    GO
    Isoform 4 (identifier: P70365-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1300-1376: NVFSQAVQSQ...LRHTGLYCNQ → KWKRKHSEHESNDGPDANELSADARDEYCVL
         1377-1447: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,330
    Mass (Da):144,762
    Checksum:iD7787C36638B2D94
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451E → G in AAB01228. (PubMed:8616895)Curated
    Sequence conflicti223 – 2231C → R in AAB06177. (PubMed:9041124)Curated
    Sequence conflicti234 – 2341E → G in AAB06177. (PubMed:9041124)Curated
    Sequence conflicti237 – 2371E → K in AAH80866. (PubMed:15489334)Curated
    Sequence conflicti465 – 4662SS → TT in AAB01228. (PubMed:8616895)Curated
    Sequence conflicti699 – 6991Q → P in AAB06177. (PubMed:9041124)Curated
    Sequence conflicti1115 – 11151L → M in BAC29244. (PubMed:16141072)Curated
    Sequence conflicti1130 – 11301R → K in AAB01228. (PubMed:8616895)Curated
    Sequence conflicti1137 – 11382RA → KP in AAB01228. (PubMed:8616895)Curated
    Sequence conflicti1142 – 11421R → K in AAB01228. (PubMed:8616895)Curated
    Sequence conflicti1162 – 11621T → D in AAB01228. (PubMed:8616895)Curated
    Sequence conflicti1164 – 11641R → S in AAB06177. (PubMed:9041124)Curated
    Sequence conflicti1166 – 11661P → L in AAB01228. (PubMed:8616895)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1300 – 137677NVFSQ…LYCNQ → KWKRKHSEHESNDGPDANEL SADARDEYCVL in isoform 4. 1 PublicationVSP_027855Add
    BLAST
    Alternative sequencei1377 – 144771Missing in isoform 4. 1 PublicationVSP_027856Add
    BLAST
    Alternative sequencei1392 – 144756QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2. 3 PublicationsVSP_011740Add
    BLAST
    Alternative sequencei1392 – 144756QVQQV…QLLTE → VSKKDNPSAELADSITLDTW RTSHGIC in isoform 3. 1 PublicationVSP_011741Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U56920 mRNA. Translation: AAB01228.1.
    U64606 mRNA. Translation: AAB06177.1.
    U64828 mRNA. Translation: AAB38841.1.
    AK035922 mRNA. Translation: BAC29244.1.
    BC068177 mRNA. Translation: AAH68177.1.
    BC080866 mRNA. Translation: AAH80866.1.
    CCDSiCCDS25789.1. [P70365-2]
    RefSeqiNP_035011.1. NM_010881.2. [P70365-2]
    XP_006515068.1. XM_006515005.1. [P70365-1]
    XP_006515069.1. XM_006515006.1. [P70365-1]
    XP_006515070.1. XM_006515007.1. [P70365-1]
    XP_006515072.1. XM_006515009.1. [P70365-2]
    UniGeneiMm.301039.

    Genome annotation databases

    EnsembliENSMUST00000085814; ENSMUSP00000082971; ENSMUSG00000020647. [P70365-2]
    GeneIDi17977.
    KEGGimmu:17977.
    UCSCiuc007mxr.2. mouse. [P70365-1]
    uc007mxs.2. mouse. [P70365-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U56920 mRNA. Translation: AAB01228.1 .
    U64606 mRNA. Translation: AAB06177.1 .
    U64828 mRNA. Translation: AAB38841.1 .
    AK035922 mRNA. Translation: BAC29244.1 .
    BC068177 mRNA. Translation: AAH68177.1 .
    BC080866 mRNA. Translation: AAH80866.1 .
    CCDSi CCDS25789.1. [P70365-2 ]
    RefSeqi NP_035011.1. NM_010881.2. [P70365-2 ]
    XP_006515068.1. XM_006515005.1. [P70365-1 ]
    XP_006515069.1. XM_006515006.1. [P70365-1 ]
    XP_006515070.1. XM_006515007.1. [P70365-1 ]
    XP_006515072.1. XM_006515009.1. [P70365-2 ]
    UniGenei Mm.301039.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OJ5 X-ray 2.20 A 257-385 [» ]
    2O9I X-ray 2.80 C/D 686-700 [» ]
    4DMA X-ray 2.30 E/F 690-704 [» ]
    ProteinModelPortali P70365.
    SMRi P70365. Positions 29-367, 926-980.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201707. 14 interactions.
    MINTi MINT-1530933.

    PTM databases

    PhosphoSitei P70365.

    Proteomic databases

    PaxDbi P70365.
    PRIDEi P70365.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000085814 ; ENSMUSP00000082971 ; ENSMUSG00000020647 . [P70365-2 ]
    GeneIDi 17977.
    KEGGi mmu:17977.
    UCSCi uc007mxr.2. mouse. [P70365-1 ]
    uc007mxs.2. mouse. [P70365-2 ]

    Organism-specific databases

    CTDi 8648.
    MGIi MGI:1276523. Ncoa1.

    Phylogenomic databases

    eggNOGi NOG315556.
    GeneTreei ENSGT00530000063109.
    HOGENOMi HOG000230947.
    HOVERGENi HBG052583.
    InParanoidi P70365.
    KOi K09101.
    OMAi QITPQPP.
    OrthoDBi EOG789C9C.
    PhylomeDBi P70365.
    TreeFami TF332652.

    Enzyme and pathway databases

    Reactomei REACT_118837. Rora activates circadian gene expression.
    REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    ChiTaRSi NCOA1. mouse.
    EvolutionaryTracei P70365.
    NextBioi 292937.
    PROi P70365.
    SOURCEi Search...

    Gene expression databases

    Bgeei P70365.
    CleanExi MM_NCOA1.
    Genevestigatori P70365.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    4.10.630.10. 2 hits.
    InterProi IPR011598. bHLH_dom.
    IPR010011. DUF1518.
    IPR028819. NCOA1.
    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:SF1. PTHR10684:SF1. 1 hit.
    Pfami PF07469. DUF1518. 2 hits.
    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. "A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors."
      Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.-C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G.
      Cell 85:403-414(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH EP300 AND CREBBP.
    2. "Cloning and identification of mouse steroid receptor coactivator-1 (mSRC-1), as a coactivator of peroxisome proliferator-activated receptor gamma."
      Zhu Y., Qi C., Calandra C., Rao M.S., Reddy J.K.
      Gene Expr. 6:185-195(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The nuclear hormone receptor coactivator SRC-1 is a specific target of p300."
      Yao T.-P., Ku G., Zhou N., Scully R., Livingston D.M.
      Proc. Natl. Acad. Sci. U.S.A. 93:10626-10631(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EP300 AND RAR.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    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] (ISOFORMS 2 AND 4).
      Strain: C57BL/6.
      Tissue: Brain and Eye.
    6. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 21-33, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    7. "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
      Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
      Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE OF LXXLL MOTIFS, TISSUE SPECIFICITY, MUTAGENESIS OF 695-HIS--LEU-698 AND 756-ARG--LEU-759.
    8. "Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene."
      Xu J., Qiu Y., DeMayo F.J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
      Science 279:1922-1925(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    9. "Regulation of transcription by a protein methyltransferase."
      Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T., Aswad D.W., Stallcup M.R.
      Science 284:2174-2177(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARM1.
    10. "SRC-1 and TIF2 control energy balance between white and brown adipose tissues."
      Picard F., Gehin M., Annicotte J.-S., Rocchi S., Champy M.-F., O'Malley B.W., Chambon P., Auwerx J.
      Cell 111:931-941(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "RORgammat recruits steroid receptor coactivators to ensure thymocyte survival."
      Xie H., Sadim M.S., Sun Z.
      J. Immunol. 175:3800-3809(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS COACTIVATOR, INTERACTION WITH RORC.
    12. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-372 AND SER-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain."
      Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C., Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E., Becker S.
      J. Mol. Biol. 336:319-329(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-385 IN COMPLEX WITH STAT6.

    Entry informationi

    Entry nameiNCOA1_MOUSE
    AccessioniPrimary (citable) accession number: P70365
    Secondary accession number(s): P70366
    , Q61202, Q66JL7, Q8CBI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3