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Q15788

- NCOA1_HUMAN

UniProt

Q15788 - NCOA1_HUMAN

Protein

Nuclear receptor coactivator 1

Gene

NCOA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (11 Sep 2007)
      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 3.7 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei867 – 8682Breakpoint for translocation to form PAX3-NCOA1 oncogene

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. chromatin binding Source: Ensembl
    3. enzyme binding Source: UniProtKB
    4. histone acetyltransferase activity Source: UniProtKB-EC
    5. ligand-dependent nuclear receptor binding Source: UniProtKB
    6. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    7. nuclear hormone receptor binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein N-terminus binding Source: UniProtKB
    10. RNA polymerase II regulatory region DNA binding Source: Ensembl
    11. RNA polymerase II transcription coactivator activity Source: BHF-UCL
    12. signal transducer activity Source: InterPro
    13. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Activator, Acyltransferase, Transferase

    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.
    SignaLinkiQ15788.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor coactivator 1 (EC:2.3.1.48)
    Short name:
    NCoA-1
    Alternative name(s):
    Class E basic helix-loop-helix protein 74
    Short name:
    bHLHe74
    Protein Hin-2
    RIP160
    Renal carcinoma antigen NY-REN-52
    Steroid receptor coactivator 1
    Short name:
    SRC-1
    Gene namesi
    Name:NCOA1
    Synonyms:BHLHE74, SRC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7668. NCOA1.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving NCOA1 is a cause of rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with PAX3 generates the NCOA1-PAX3 oncogene consisting of the N-terminus part of PAX3 and the C-terminus part of NCOA1. The fusion protein acts as a transcriptional activator. Rhabdomyosarcoma is the most common soft tissue carcinoma in childhood, representing 5-8% of all malignancies in children.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi636 – 6372LL → AA: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-693; A-694; A-752 and A-753. 1 Publication
    Mutagenesisi693 – 6942LL → AA: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-636; A-637; A-752 and A-753. 1 Publication
    Mutagenesisi732 – 7321K → R: Abolishes sumoylation; when associated with R-774. 2 Publications
    Mutagenesisi752 – 7532LL → AA: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-636; A-637; A-693 and A-694. 1 Publication
    Mutagenesisi774 – 7741K → R: Abolishes sumoylation; when associated with R-732. 2 Publications
    Mutagenesisi800 – 8001K → R: Does not affect sumoylation of the protein. 2 Publications
    Mutagenesisi846 – 8461K → R: Does not affect sumoylation of the protein. 2 Publications
    Mutagenesisi1378 – 13781K → R: Does not affect sumoylation of the protein. 2 Publications

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA31470.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 14411440Nuclear receptor coactivator 1PRO_0000094400Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei22 – 221PhosphoserineBy similarity
    Modified residuei372 – 3721Phosphoserine1 Publication
    Modified residuei395 – 3951Phosphoserine2 Publications
    Modified residuei517 – 5171Phosphoserine1 Publication
    Modified residuei569 – 5691Phosphoserine1 Publication
    Modified residuei698 – 6981PhosphoserineBy similarity
    Cross-linki732 – 732Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki774 – 774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei1033 – 10331Phosphoserine1 Publication
    Modified residuei1179 – 11791Phosphothreonine1 Publication
    Modified residuei1185 – 11851Phosphoserine1 Publication

    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.1 Publication
    Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15788.
    PaxDbiQ15788.
    PRIDEiQ15788.

    PTM databases

    PhosphoSiteiQ15788.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ15788.
    BgeeiQ15788.
    GenevestigatoriQ15788.

    Organism-specific databases

    HPAiCAB019402.

    Interactioni

    Subunit structurei

    Interacts with the methyltransferase CARM1 By similarity. 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 the histone acetyltransferases EP300 and CREBBP. Interacts with PCAF, COPS5, NR3C1 and TTLL5/STAMP. 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.By similarity22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Asxl1P595982EBI-455189,EBI-5743705From a different organism.
    ESR1P0337210EBI-455189,EBI-78473
    Esr1P197852EBI-455189,EBI-346765From a different organism.
    KANK2Q63ZY34EBI-455189,EBI-2556193
    Nfkb1P257992EBI-455189,EBI-643958From a different organism.
    NR1H3Q1313314EBI-455189,EBI-781356
    Nr3c1P065362EBI-455189,EBI-1187143From a different organism.
    PAGR1Q9BTK64EBI-455189,EBI-2372223
    PSMB9P280653EBI-455189,EBI-603300
    RARAP102763EBI-455189,EBI-413374
    RXRAP197935EBI-455189,EBI-78598

    Protein-protein interaction databases

    BioGridi114200. 72 interactions.
    DIPiDIP-30877N.
    IntActiQ15788. 24 interactions.
    MINTiMINT-153305.

    Structurei

    Secondary structure

    1
    1441
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi632 – 6387
    Helixi683 – 6864
    Helixi688 – 6958
    Helixi747 – 7548
    Turni924 – 9263
    Helixi929 – 94113
    Helixi945 – 9473
    Helixi952 – 9543
    Turni958 – 9625
    Beta strandi964 – 9663
    Helixi1434 – 14407

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FM6X-ray2.10B/E/V/Y676-700[»]
    1FM9X-ray2.10B/E676-700[»]
    1K4WX-ray1.90B686-700[»]
    1K74X-ray2.30B/E676-700[»]
    1K7LX-ray2.50B/D/F/H680-700[»]
    1KV6X-ray2.70C/D686-700[»]
    1N4HX-ray2.10B686-700[»]
    1NQ7X-ray1.50B687-696[»]
    1NRLX-ray2.00C/D676-700[»]
    1P8DX-ray2.80C/D676-700[»]
    1PZLX-ray2.10B687-700[»]
    1RDTX-ray2.40B676-700[»]
    1TFCX-ray2.40C/D686-700[»]
    1U3RX-ray2.21C/D630-640[»]
    1U3SX-ray2.50C/D630-640[»]
    1X76X-ray2.20C/D630-640[»]
    1X78X-ray2.30C/D630-640[»]
    1X7BX-ray2.30C/D630-640[»]
    1X7JX-ray2.30C/D630-640[»]
    1XIUX-ray2.50E/F686-700[»]
    1XV9X-ray2.70E/F/G/H685-697[»]
    1XVPX-ray2.60E/F/G/H685-697[»]
    1YY4X-ray2.70C/D630-640[»]
    1YYEX-ray2.03C/D630-640[»]
    1ZAFX-ray2.20C/D630-640[»]
    2A3IX-ray1.95B1430-1441[»]
    2C52NMR-B920-970[»]
    2FVJX-ray1.99B628-640[»]
    2GTKX-ray2.10B631-640[»]
    2HBHX-ray2.65B686-700[»]
    2HC4X-ray2.20B686-700[»]
    2HCDX-ray2.60B686-700[»]
    2HFPX-ray2.00B680-700[»]
    2NPAX-ray2.30B/D683-697[»]
    2NV7X-ray2.10C/D631-640[»]
    2P54X-ray1.79B686-696[»]
    2PRGX-ray2.30C623-710[»]
    3BEJX-ray1.90E/F676-700[»]
    3BQDX-ray2.50B1429-1441[»]
    3CTBX-ray2.00A/B678-700[»]
    3CWDX-ray2.40C/D685-700[»]
    3DCTX-ray2.50B741-761[»]
    3DCUX-ray2.95B741-761[»]
    3DR1X-ray2.70B686-700[»]
    3ET1X-ray2.50P/Q681-696[»]
    3ET3X-ray1.95P680-695[»]
    3FEIX-ray2.40Z744-756[»]
    3FEJX-ray2.01B628-640[»]
    3FURX-ray2.30H629-640[»]
    3FXVX-ray2.26B744-756[»]
    3G8IX-ray2.20Z744-756[»]
    3G9EX-ray2.30B628-640[»]
    3GYTX-ray2.40B1429-1441[»]
    3GYUX-ray2.40B1429-1441[»]
    3H0AX-ray2.10B/E629-640[»]
    3HC5X-ray2.60B741-761[»]
    3HC6X-ray3.20B741-761[»]
    3HVLX-ray2.10A/B678-700[»]
    3IPQX-ray2.00B676-700[»]
    3IPSX-ray2.26C/D676-700[»]
    3IPUX-ray2.40C/D676-700[»]
    3KMRX-ray1.80C686-698[»]
    3LMPX-ray1.90C686-700[»]
    3OKHX-ray2.50B744-757[»]
    3OKIX-ray2.00B/D744-757[»]
    3OLFX-ray1.90B/D744-757[»]
    3OLLX-ray1.50C/D683-701[»]
    3OLSX-ray2.20C/D683-701[»]
    3OMKX-ray1.90B/D744-757[»]
    3OMMX-ray2.10B/D744-757[»]
    3OMOX-ray2.21C/D683-701[»]
    3OMPX-ray2.05C/D683-701[»]
    3OMQX-ray1.97C/D683-701[»]
    3OOFX-ray2.29B/D744-757[»]
    3OOKX-ray2.29B/D744-757[»]
    3P88X-ray2.95B745-755[»]
    3P89X-ray2.30B745-755[»]
    3QT0X-ray2.50C685-700[»]
    3RUTX-ray3.00B745-755[»]
    3RUUX-ray2.50B745-755[»]
    3RVFX-ray3.10B741-761[»]
    3S9SX-ray2.55B685-697[»]
    3T03X-ray2.10C/D683-700[»]
    3UU7X-ray2.20F/G686-698[»]
    3UUAX-ray2.05F/G686-698[»]
    3UUDX-ray1.60C/D686-698[»]
    3V9YX-ray2.10B686-700[»]
    3VN2X-ray2.18C685-700[»]
    4DK7X-ray2.45B/D745-756[»]
    4DK8X-ray2.75B/D745-756[»]
    4DM6X-ray1.90E/F676-700[»]
    4DM8X-ray2.30C/D676-700[»]
    4DQMX-ray2.75B/D1432-1441[»]
    4F9MX-ray1.90C686-700[»]
    4FGYX-ray2.84B686-696[»]
    4G1DX-ray2.90B686-700[»]
    4G1YX-ray2.85B686-700[»]
    4G1ZX-ray2.50B686-700[»]
    4G20X-ray2.90B686-700[»]
    4G21X-ray2.90B686-700[»]
    4G2HX-ray2.50B686-700[»]
    4HEEX-ray2.50Y676-700[»]
    4J5XX-ray2.80A/B/C/D678-700[»]
    4JYGX-ray2.35F/G686-698[»]
    4JYHX-ray2.60C/G686-698[»]
    4JYIX-ray1.90F/G686-698[»]
    ProteinModelPortaliQ15788.
    SMRiQ15788. Positions 29-367, 920-974.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15788.

    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 – 567207Interaction with STAT3Add
    BLAST
    Regioni781 – 988208Interaction with CREBBPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi46 – 505LXXLL motif 1
    Motifi112 – 1165LXXLL motif 2
    Motifi633 – 6375LXXLL motif 3
    Motifi690 – 6945LXXLL motif 4
    Motifi749 – 7535LXXLL motif 5
    Motifi913 – 9175LXXLL motif 6
    Motifi1435 – 14395LXXLL motif 7

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi389 – 682294Ser-richAdd
    BLAST
    Compositional biasi1053 – 113886Gln-richAdd
    BLAST

    Domaini

    The C-terminal (1107-1441) part mediates the histone acetyltransferase (HAT) activity.

    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.
    InParanoidiQ15788.
    KOiK09101.
    OMAiQITPQPP.
    OrthoDBiEOG789C9C.
    PhylomeDBiQ15788.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15788-1) [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
    IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ SCLICIARRL 250
    PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 300
    QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ 350
    SPDMQPFIMG IHIIDREHSG LSPQDDTNSG MSIPRVNPSV NPSISPAHGV 400
    ARSSTLPPSN SNMVSTRINR QQSSDLHSSS HSNSSNSQGS FGCSPGSQIV 450
    ANVALNQGQA SSQSSNPSLN LNNSPMEGTG ISLAQFMSPR RQVTSGLATR 500
    PRMPNNSFPP NISTLSSPVG MTSSACNNNN RSYSNIPVTS LQGMNEGPNN 550
    SVGFSASSPV LRQMSSQNSP SRLNIQPAKA ESKDNKEIAS ILNEMIQSDN 600
    SSSDGKPLDS GLLHNNDRLS DGDSKYSQTS HKLVQLLTTT AEQQLRHADI 650
    DTSCKDVLSC TGTSNSASAN SSGGSCPSSH SSLTERHKIL HRLLQEGSPS 700
    DITTLSVEPD KKDSASTSVS VTGQVQGNSS IKLELDASKK KESKDHQLLR 750
    YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ MDPCNTNPTP MTKPTPEEIK 800
    LEAQSQFTAD LDQFDQLLPT LEKAAQLPGL CETDRMDGAV TSVTIKSEIL 850
    PASLQSATAR PTSRLNRLPE LELEAIDNQF GQPGTGDQIP WTNNTVTAIN 900
    QSKSEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE 950
    LDRALGIDKL VQGGGLDVLS ERFPPQQATP PLIMEERPNL YSQPYSSPSP 1000
    TANLPSPFQG MVRQKPSLGT MPVQVTPPRG AFSPGMGMQP RQTLNRPPAA 1050
    PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF AATAPVGINM RSGMQQQITP 1100
    QPPLNAQMLA QRQRELYSQQ HRQRQLIQQQ RAMLMRQQSF GNNLPPSSGL 1150
    PVQMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AANPEASLAN 1200
    RNSMVSRGMT GNIGGQFGTG INPQMQQNVF QYPGAGMVPQ GEANFAPSLS 1250
    PGSSMVPMPI PPPQSSLLQQ TPPASGYQSP DMKAWQQGAI GNNNVFSQAV 1300
    QNQPTPAQPG VYNNMSITVS MAGGNTNVQN MNPMMAQMQM SSLQMPGMNT 1350
    VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE ADGTQQVQQV QVFADVQCTV 1400
    NLVGGDPYLN QPGPLGTQKP TSGPQTPQAQ QKSLLQQLLT E 1441
    Length:1,441
    Mass (Da):156,757
    Last modified:September 11, 2007 - v3
    Checksum:i25EF6F389489121E
    GO
    Isoform 2 (identifier: Q15788-2) [UniParc]FASTAAdd to Basket

    Also known as: SRC-1E, SRC1e

    The sequence of this isoform differs from the canonical sequence as follows:
         1386-1441: QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE → DKKTEEFFSVVTTD

    Note: Major form. Contains a domain at its C-terminus (1241-1399) that is able to mediate transactivation.

    Show »
    Length:1,399
    Mass (Da):152,385
    Checksum:iDACE967B31AC6B69
    GO
    Isoform 3 (identifier: Q15788-3) [UniParc]FASTAAdd to Basket

    Also known as: SRC-1 (-Q)

    The sequence of this isoform differs from the canonical sequence as follows:
         1385-1385: Missing.

    Show »
    Length:1,440
    Mass (Da):156,628
    Checksum:i4E3FFED7088CDBF8
    GO

    Sequence cautioni

    The sequence AAA64187.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAC50305.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1035 – 10351Missing in AAT47737. (PubMed:15313887)Curated
    Sequence conflicti1370 – 13701Q → H in AAA64187. (PubMed:11831720)Curated
    Sequence conflicti1382 – 13821D → G in AAT47737. (PubMed:15313887)Curated
    Sequence conflicti1435 – 14351L → R in AAB50242. (PubMed:9575154)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti457 – 4571Q → K.3 Publications
    Corresponds to variant rs1049015 [ dbSNP | Ensembl ].
    VAR_019768
    Natural varianti466 – 4661N → K.3 Publications
    Corresponds to variant rs1049016 [ dbSNP | Ensembl ].
    VAR_019769
    Natural varianti474 – 4741S → P.3 Publications
    Corresponds to variant rs1049018 [ dbSNP | Ensembl ].
    VAR_019770
    Natural varianti591 – 5911I → T.3 Publications
    Corresponds to variant rs1049020 [ dbSNP | Ensembl ].
    VAR_019771
    Natural varianti685 – 6851E → A.3 Publications
    Corresponds to variant rs1049021 [ dbSNP | Ensembl ].
    VAR_019772
    Natural varianti794 – 7941P → A.1 Publication
    Corresponds to variant rs1049025 [ dbSNP | Ensembl ].
    VAR_019773
    Natural varianti999 – 9991S → F.3 Publications
    Corresponds to variant rs1049032 [ dbSNP | Ensembl ].
    VAR_019774
    Natural varianti1154 – 11541M → T.3 Publications
    Corresponds to variant rs1049038 [ dbSNP | Ensembl ].
    VAR_019775
    Natural varianti1238 – 12381V → I.1 Publication
    Corresponds to variant rs56099330 [ dbSNP | Ensembl ].
    VAR_038832
    Natural varianti1272 – 12721P → S.1 Publication
    Corresponds to variant rs1804645 [ dbSNP | Ensembl ].
    VAR_034882

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1385 – 13851Missing in isoform 3. 1 PublicationVSP_011738
    Alternative sequencei1386 – 144156QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2. 4 PublicationsVSP_011739Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59302 mRNA. Translation: AAC50631.1.
    AJ000881 mRNA. Translation: CAA04371.1.
    AJ000882 mRNA. Translation: CAA04372.1.
    U90661 mRNA. Translation: AAB50242.1.
    EF660499 Genomic DNA. Translation: ABS29266.1.
    AC013459 Genomic DNA. Translation: AAX93184.1.
    AC093798 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00746.1.
    BC111533 mRNA. Translation: AAI11534.1.
    BC111534 mRNA. Translation: AAI11535.1.
    U40396 mRNA. Translation: AAC50305.1. Different initiation.
    U19179 mRNA. Translation: AAA64187.1. Different initiation.
    AY633656 mRNA. Translation: AAT47737.1.
    CCDSiCCDS1712.1. [Q15788-1]
    CCDS1713.1. [Q15788-2]
    CCDS42660.1. [Q15788-3]
    PIRiA57620.
    PC4363.
    PC4364.
    RefSeqiNP_003734.3. NM_003743.4. [Q15788-1]
    NP_671756.1. NM_147223.2. [Q15788-2]
    NP_671766.1. NM_147233.2. [Q15788-3]
    XP_005264682.1. XM_005264625.1. [Q15788-1]
    XP_005264683.1. XM_005264626.1. [Q15788-3]
    XP_005264684.1. XM_005264627.1. [Q15788-2]
    XP_005264685.1. XM_005264628.1. [Q15788-2]
    UniGeneiHs.596314.

    Genome annotation databases

    EnsembliENST00000288599; ENSP00000288599; ENSG00000084676. [Q15788-2]
    ENST00000348332; ENSP00000320940; ENSG00000084676. [Q15788-1]
    ENST00000395856; ENSP00000379197; ENSG00000084676. [Q15788-3]
    ENST00000405141; ENSP00000385097; ENSG00000084676. [Q15788-2]
    ENST00000406961; ENSP00000385216; ENSG00000084676. [Q15788-1]
    GeneIDi8648.
    KEGGihsa:8648.
    UCSCiuc002rfj.3. human. [Q15788-2]
    uc002rfk.3. human. [Q15788-1]
    uc002rfl.3. human. [Q15788-3]

    Polymorphism databases

    DMDMi158518533.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59302 mRNA. Translation: AAC50631.1 .
    AJ000881 mRNA. Translation: CAA04371.1 .
    AJ000882 mRNA. Translation: CAA04372.1 .
    U90661 mRNA. Translation: AAB50242.1 .
    EF660499 Genomic DNA. Translation: ABS29266.1 .
    AC013459 Genomic DNA. Translation: AAX93184.1 .
    AC093798 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00746.1 .
    BC111533 mRNA. Translation: AAI11534.1 .
    BC111534 mRNA. Translation: AAI11535.1 .
    U40396 mRNA. Translation: AAC50305.1 . Different initiation.
    U19179 mRNA. Translation: AAA64187.1 . Different initiation.
    AY633656 mRNA. Translation: AAT47737.1 .
    CCDSi CCDS1712.1. [Q15788-1 ]
    CCDS1713.1. [Q15788-2 ]
    CCDS42660.1. [Q15788-3 ]
    PIRi A57620.
    PC4363.
    PC4364.
    RefSeqi NP_003734.3. NM_003743.4. [Q15788-1 ]
    NP_671756.1. NM_147223.2. [Q15788-2 ]
    NP_671766.1. NM_147233.2. [Q15788-3 ]
    XP_005264682.1. XM_005264625.1. [Q15788-1 ]
    XP_005264683.1. XM_005264626.1. [Q15788-3 ]
    XP_005264684.1. XM_005264627.1. [Q15788-2 ]
    XP_005264685.1. XM_005264628.1. [Q15788-2 ]
    UniGenei Hs.596314.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FM6 X-ray 2.10 B/E/V/Y 676-700 [» ]
    1FM9 X-ray 2.10 B/E 676-700 [» ]
    1K4W X-ray 1.90 B 686-700 [» ]
    1K74 X-ray 2.30 B/E 676-700 [» ]
    1K7L X-ray 2.50 B/D/F/H 680-700 [» ]
    1KV6 X-ray 2.70 C/D 686-700 [» ]
    1N4H X-ray 2.10 B 686-700 [» ]
    1NQ7 X-ray 1.50 B 687-696 [» ]
    1NRL X-ray 2.00 C/D 676-700 [» ]
    1P8D X-ray 2.80 C/D 676-700 [» ]
    1PZL X-ray 2.10 B 687-700 [» ]
    1RDT X-ray 2.40 B 676-700 [» ]
    1TFC X-ray 2.40 C/D 686-700 [» ]
    1U3R X-ray 2.21 C/D 630-640 [» ]
    1U3S X-ray 2.50 C/D 630-640 [» ]
    1X76 X-ray 2.20 C/D 630-640 [» ]
    1X78 X-ray 2.30 C/D 630-640 [» ]
    1X7B X-ray 2.30 C/D 630-640 [» ]
    1X7J X-ray 2.30 C/D 630-640 [» ]
    1XIU X-ray 2.50 E/F 686-700 [» ]
    1XV9 X-ray 2.70 E/F/G/H 685-697 [» ]
    1XVP X-ray 2.60 E/F/G/H 685-697 [» ]
    1YY4 X-ray 2.70 C/D 630-640 [» ]
    1YYE X-ray 2.03 C/D 630-640 [» ]
    1ZAF X-ray 2.20 C/D 630-640 [» ]
    2A3I X-ray 1.95 B 1430-1441 [» ]
    2C52 NMR - B 920-970 [» ]
    2FVJ X-ray 1.99 B 628-640 [» ]
    2GTK X-ray 2.10 B 631-640 [» ]
    2HBH X-ray 2.65 B 686-700 [» ]
    2HC4 X-ray 2.20 B 686-700 [» ]
    2HCD X-ray 2.60 B 686-700 [» ]
    2HFP X-ray 2.00 B 680-700 [» ]
    2NPA X-ray 2.30 B/D 683-697 [» ]
    2NV7 X-ray 2.10 C/D 631-640 [» ]
    2P54 X-ray 1.79 B 686-696 [» ]
    2PRG X-ray 2.30 C 623-710 [» ]
    3BEJ X-ray 1.90 E/F 676-700 [» ]
    3BQD X-ray 2.50 B 1429-1441 [» ]
    3CTB X-ray 2.00 A/B 678-700 [» ]
    3CWD X-ray 2.40 C/D 685-700 [» ]
    3DCT X-ray 2.50 B 741-761 [» ]
    3DCU X-ray 2.95 B 741-761 [» ]
    3DR1 X-ray 2.70 B 686-700 [» ]
    3ET1 X-ray 2.50 P/Q 681-696 [» ]
    3ET3 X-ray 1.95 P 680-695 [» ]
    3FEI X-ray 2.40 Z 744-756 [» ]
    3FEJ X-ray 2.01 B 628-640 [» ]
    3FUR X-ray 2.30 H 629-640 [» ]
    3FXV X-ray 2.26 B 744-756 [» ]
    3G8I X-ray 2.20 Z 744-756 [» ]
    3G9E X-ray 2.30 B 628-640 [» ]
    3GYT X-ray 2.40 B 1429-1441 [» ]
    3GYU X-ray 2.40 B 1429-1441 [» ]
    3H0A X-ray 2.10 B/E 629-640 [» ]
    3HC5 X-ray 2.60 B 741-761 [» ]
    3HC6 X-ray 3.20 B 741-761 [» ]
    3HVL X-ray 2.10 A/B 678-700 [» ]
    3IPQ X-ray 2.00 B 676-700 [» ]
    3IPS X-ray 2.26 C/D 676-700 [» ]
    3IPU X-ray 2.40 C/D 676-700 [» ]
    3KMR X-ray 1.80 C 686-698 [» ]
    3LMP X-ray 1.90 C 686-700 [» ]
    3OKH X-ray 2.50 B 744-757 [» ]
    3OKI X-ray 2.00 B/D 744-757 [» ]
    3OLF X-ray 1.90 B/D 744-757 [» ]
    3OLL X-ray 1.50 C/D 683-701 [» ]
    3OLS X-ray 2.20 C/D 683-701 [» ]
    3OMK X-ray 1.90 B/D 744-757 [» ]
    3OMM X-ray 2.10 B/D 744-757 [» ]
    3OMO X-ray 2.21 C/D 683-701 [» ]
    3OMP X-ray 2.05 C/D 683-701 [» ]
    3OMQ X-ray 1.97 C/D 683-701 [» ]
    3OOF X-ray 2.29 B/D 744-757 [» ]
    3OOK X-ray 2.29 B/D 744-757 [» ]
    3P88 X-ray 2.95 B 745-755 [» ]
    3P89 X-ray 2.30 B 745-755 [» ]
    3QT0 X-ray 2.50 C 685-700 [» ]
    3RUT X-ray 3.00 B 745-755 [» ]
    3RUU X-ray 2.50 B 745-755 [» ]
    3RVF X-ray 3.10 B 741-761 [» ]
    3S9S X-ray 2.55 B 685-697 [» ]
    3T03 X-ray 2.10 C/D 683-700 [» ]
    3UU7 X-ray 2.20 F/G 686-698 [» ]
    3UUA X-ray 2.05 F/G 686-698 [» ]
    3UUD X-ray 1.60 C/D 686-698 [» ]
    3V9Y X-ray 2.10 B 686-700 [» ]
    3VN2 X-ray 2.18 C 685-700 [» ]
    4DK7 X-ray 2.45 B/D 745-756 [» ]
    4DK8 X-ray 2.75 B/D 745-756 [» ]
    4DM6 X-ray 1.90 E/F 676-700 [» ]
    4DM8 X-ray 2.30 C/D 676-700 [» ]
    4DQM X-ray 2.75 B/D 1432-1441 [» ]
    4F9M X-ray 1.90 C 686-700 [» ]
    4FGY X-ray 2.84 B 686-696 [» ]
    4G1D X-ray 2.90 B 686-700 [» ]
    4G1Y X-ray 2.85 B 686-700 [» ]
    4G1Z X-ray 2.50 B 686-700 [» ]
    4G20 X-ray 2.90 B 686-700 [» ]
    4G21 X-ray 2.90 B 686-700 [» ]
    4G2H X-ray 2.50 B 686-700 [» ]
    4HEE X-ray 2.50 Y 676-700 [» ]
    4J5X X-ray 2.80 A/B/C/D 678-700 [» ]
    4JYG X-ray 2.35 F/G 686-698 [» ]
    4JYH X-ray 2.60 C/G 686-698 [» ]
    4JYI X-ray 1.90 F/G 686-698 [» ]
    ProteinModelPortali Q15788.
    SMRi Q15788. Positions 29-367, 920-974.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114200. 72 interactions.
    DIPi DIP-30877N.
    IntActi Q15788. 24 interactions.
    MINTi MINT-153305.

    Chemistry

    BindingDBi Q15788.
    ChEMBLi CHEMBL1615387.

    PTM databases

    PhosphoSitei Q15788.

    Polymorphism databases

    DMDMi 158518533.

    Proteomic databases

    MaxQBi Q15788.
    PaxDbi Q15788.
    PRIDEi Q15788.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288599 ; ENSP00000288599 ; ENSG00000084676 . [Q15788-2 ]
    ENST00000348332 ; ENSP00000320940 ; ENSG00000084676 . [Q15788-1 ]
    ENST00000395856 ; ENSP00000379197 ; ENSG00000084676 . [Q15788-3 ]
    ENST00000405141 ; ENSP00000385097 ; ENSG00000084676 . [Q15788-2 ]
    ENST00000406961 ; ENSP00000385216 ; ENSG00000084676 . [Q15788-1 ]
    GeneIDi 8648.
    KEGGi hsa:8648.
    UCSCi uc002rfj.3. human. [Q15788-2 ]
    uc002rfk.3. human. [Q15788-1 ]
    uc002rfl.3. human. [Q15788-3 ]

    Organism-specific databases

    CTDi 8648.
    GeneCardsi GC02P024719.
    HGNCi HGNC:7668. NCOA1.
    HPAi CAB019402.
    MIMi 602691. gene.
    neXtProti NX_Q15788.
    PharmGKBi PA31470.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG315556.
    HOVERGENi HBG052583.
    InParanoidi Q15788.
    KOi K09101.
    OMAi QITPQPP.
    OrthoDBi EOG789C9C.
    PhylomeDBi Q15788.
    TreeFami TF332652.

    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.
    SignaLinki Q15788.

    Miscellaneous databases

    ChiTaRSi NCOA1. human.
    EvolutionaryTracei Q15788.
    GeneWikii Nuclear_receptor_coactivator_1.
    GenomeRNAii 8648.
    NextBioi 32423.
    PROi Q15788.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15788.
    Bgeei Q15788.
    Genevestigatori Q15788.

    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. "Molecular cloning and properties of a full-length putative thyroid hormone receptor coactivator."
      Takeshita A., Yen P.M., Misiti S., Cardona G.R., Liu Y., Chin W.W.
      Endocrinology 137:3594-3597(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH GTF2B, VARIANTS LYS-457; LYS-466; PRO-474; THR-591; ALA-685; PHE-999 AND THR-1154.
    2. "Isoforms of steroid receptor coactivator 1 differ in their ability to potentiate transcription by the oestrogen receptor."
      Kalkhoven E., Valentine J.E., Heery D.M., Parker M.G.
      EMBO J. 17:232-243(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF 636-LEU-LEU-637; 693-LEU-LEU-694 AND 752-LEU-LEU-753.
    3. "The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors."
      Onate S.A., Boonyaratanakornkit V., Spencer T.E., Tsai S.Y., Tsai M.-J., Edwards D.P., O'Malley B.W.
      J. Biol. Chem. 273:12101-12108(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LYS-457; LYS-466; PRO-474; THR-591; ALA-685; PHE-999 AND THR-1154.
      Tissue: Heart muscle and Skeletal muscle.
    4. SeattleSNPs variation discovery resource
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-1238 AND SER-1272.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1 AND 2).
    8. "Sequence and characterization of a coactivator for the steroid hormone receptor superfamily."
      Onate S.A., Tsai S.Y., Tsai M.-J., O'Malley B.W.
      Science 270:1354-1357(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 363-1441 (ISOFORM 1), FUNCTION, INTERACTION WITH ESR1; RXRA; GCCR; PGR AND THRA, VARIANTS LYS-457; LYS-466; PRO-474; THR-591; ALA-685; ALA-794; PHE-999 AND THR-1154.
    9. "Analysis of human immunodeficiency virus type 1 promoter insertion in vivo."
      Raineri I., Soler M., Senn H.-P.
      Virology 208:359-364(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 865-1441 (ISOFORM 2).
    10. "Gene expression signatures identify rhabdomyosarcoma subtypes and detect a novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1."
      Wachtel M., Dettling M., Koscielniak E., Stegmaier S., Treuner J., Simon-Klingenstein K., Buehlmann P., Niggli F.K., Schaefer B.W.
      Cancer Res. 64:5539-5545(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 868-1441 (ISOFORM 2), CHROMOSOMAL TRANSLOCATION WITH PAX3, TISSUE SPECIFICITY.
    11. "A splicing variant of steroid receptor coactivator-1 (SRC-1E): the major isoform of SRC-1 to mediate thyroid hormone action."
      Hayashi Y., Ohmori S., Ito T., Seo H.
      Biochem. Biophys. Res. Commun. 236:83-87(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING.
    12. Cited for: FUNCTION AS A HISTONE ACETYLTRANSFERASE, INTERACTION WITH PCAF.
    13. Cited for: FUNCTION.
    14. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    15. "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: INTERACTION WITH NCOA6.
    16. "Steroid receptor coactivator-1 (SRC-1) enhances ligand-dependent and receptor-dependent cell-free transcription of chromatin."
      Liu Z., Wong J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
      Proc. Natl. Acad. Sci. U.S.A. 96:9485-9490(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Phosphorylation of steroid receptor coactivator-1. Identification of the phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway."
      Rowan B.G., Weigel N.L., O'Malley B.W.
      J. Biol. Chem. 275:4475-4483(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-372; SER-395; SER-517; SER-569; SER-1033; THR-1179 AND SER-1185.
    18. Cited for: INTERACTION WITH COPS5.
    19. "Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha."
      Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H., Poellinger L.
      Mol. Cell. Biol. 20:402-415(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA2.
    20. "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.
    21. "Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a."
      Giraud S., Bienvenu F., Avril S., Gascan H., Heery D.M., Coqueret O.
      J. Biol. Chem. 277:8004-8011(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAT3.
    22. "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.
    23. "An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1."
      Litterst C.M., Pfitzner E.
      J. Biol. Chem. 277:36052-36060(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAT6.
    24. "Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1."
      Chauchereau A., Amazit L., Quesne M., Guiochon-Mantel A., Milgrom E.
      J. Biol. Chem. 278:12335-12343(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-732 AND LYS-774, UBIQUITINATION, MUTAGENESIS OF LYS-732; LYS-774; LYS-800; LYS-846 AND LYS-1378.
    25. "NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the FDL motif in the alpha-helical region of the STAT5 transactivation domain."
      Litterst C.M., Kliem S., Marilley D., Pfitzner E.
      J. Biol. Chem. 278:45340-45351(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH STAT5A AND STAT5B.
    26. "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.
    27. "The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors."
      Verma S., Ismail A., Gao X., Fu G., Li X., O'Malley B.W., Nawaz Z.
      Mol. Cell. Biol. 24:8716-8726(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2L3.
    28. "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.
    29. "Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor."
      Cho Y.S., Kim E.J., Park U.H., Sin H.S., Um S.J.
      J. Biol. Chem. 281:17588-17598(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASXL1.
    30. "STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression."
      He Y., Simons S.S. Jr.
      Mol. Cell. Biol. 27:1467-1485(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTLL5.
      Tissue: Testis.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    32. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    33. "The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."
      Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., Makishima M.
      Mol. Pharmacol. 76:1360-1369(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RXRA.
    34. "Protein arginine methyltransferase 6 regulates multiple aspects of gene expression."
      Harrison M.J., Tang Y.H., Dowhan D.H.
      Nucleic Acids Res. 38:2201-2216(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT6.
    35. "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-395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    36. "Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma."
      Nolte R.T., Wisely G.B., Westin S., Cobb J.E., Lambert M.H., Kurokawa R., Rosenfeld M.G., Willson T.M., Glass C.K., Milburn M.V.
      Nature 395:137-143(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 623-710 IN COMPLEX WITH PPARG.
    37. "Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors."
      Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B., Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D., Moore J.T., Willson T.M.
      Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 687-696 IN COMPLEX WITH PPARA.
    38. "Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3."
      Greschik H., Wurtz J.-M., Sanglier S., Bourguet W., van Dorsselaer A., Moras D., Renaud J.-P.
      Mol. Cell 9:303-313(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 686-700 IN COMPLEX WITH ESRRG.
    39. "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 795-808 OF STAT6.

    Entry informationi

    Entry nameiNCOA1_HUMAN
    AccessioniPrimary (citable) accession number: Q15788
    Secondary accession number(s): O00150
    , O43792, O43793, Q13071, Q13420, Q2T9G5, Q53SX3, Q6GVI5, Q7KYV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 134 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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