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Protein

Nuclear receptor coactivator 1

Gene

NCOA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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].

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • chromatin binding Source: Ensembl
  • enzyme binding Source: UniProtKB
  • histone acetyltransferase activity Source: UniProtKB-EC
  • ligand-dependent nuclear receptor binding Source: UniProtKB
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • RNA polymerase II regulatory region DNA binding Source: Ensembl
  • RNA polymerase II transcription coactivator activity Source: BHF-UCL
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-159418. Recycling of bile acids and salts.
R-HSA-192105. Synthesis of bile acids and bile salts.
R-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-HSA-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-HSA-211976. Endogenous sterols.
R-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-3214847. HATs acetylate histones.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-HSA-400253. Circadian Clock.
SignaLinkiQ15788.
SIGNORiQ15788.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:7668. NCOA1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • neuron projection Source: Ensembl
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
Complete GO annotation...

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. 1 Publication
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. 1 Publication
Mutagenesisi800 – 8001K → R: Does not affect sumoylation of the protein. 1 Publication
Mutagenesisi846 – 8461K → R: Does not affect sumoylation of the protein. 1 Publication
Mutagenesisi1378 – 13781K → R: Does not affect sumoylation of the protein. 1 Publication

Sites

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

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA31470.

Chemistry

ChEMBLiCHEMBL2095162.
GuidetoPHARMACOLOGYi2693.

Polymorphism and mutation databases

BioMutaiNCOA1.
DMDMi158518533.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 14411440Nuclear receptor coactivator 1PRO_0000094400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei22 – 221PhosphoserineCombined sources
Modified residuei372 – 3721PhosphoserineCombined sources1 Publication
Modified residuei395 – 3951PhosphoserineCombined sources1 Publication
Modified residuei517 – 5171Phosphoserine1 Publication
Modified residuei558 – 5581PhosphoserineBy similarity
Modified residuei569 – 5691Phosphoserine1 Publication
Modified residuei698 – 6981PhosphoserineCombined sources
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
Modified residuei1372 – 13721PhosphoserineCombined sources

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

EPDiQ15788.
MaxQBiQ15788.
PaxDbiQ15788.
PeptideAtlasiQ15788.
PRIDEiQ15788.

PTM databases

iPTMnetiQ15788.
PhosphoSiteiQ15788.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiENSG00000084676.
ExpressionAtlasiQ15788. baseline and differential.
GenevisibleiQ15788. HS.

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. Interacts with TRIP4. Interacts with NR4A3 (By similarity).By similarity23 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.
NR1H3Q1313315EBI-455189,EBI-781356
NR1H4Q96RI14EBI-455189,EBI-1250177
Nr3c1P065362EBI-455189,EBI-1187143From a different organism.
PAGR1Q9BTK64EBI-455189,EBI-2372223
PSMB9P280653EBI-455189,EBI-603300
RARAP102763EBI-455189,EBI-413374
RORCP514492EBI-455189,EBI-3908771
RXRAP197935EBI-455189,EBI-78598

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • ligand-dependent nuclear receptor binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114200. 108 interactions.
DIPiDIP-30877N.
IntActiQ15788. 27 interactions.
MINTiMINT-153305.
STRINGi9606.ENSP00000320940.

Chemistry

BindingDBiQ15788.

Structurei

Secondary structure

1
1441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi632 – 6387Combined sources
Helixi684 – 6863Combined sources
Helixi688 – 6958Combined sources
Helixi747 – 7548Combined sources
Turni924 – 9263Combined sources
Helixi929 – 94113Combined sources
Helixi945 – 9473Combined sources
Helixi952 – 9543Combined sources
Turni958 – 9625Combined sources
Beta strandi964 – 9663Combined sources
Helixi1434 – 14407Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4MG5X-ray2.05C/D686-698[»]
4MG6X-ray2.10C/D686-698[»]
4MG7X-ray2.15C/D686-698[»]
4MG8X-ray1.85C/D686-698[»]
4MG9X-ray2.00F/G686-698[»]
4MGAX-ray1.80C/D686-698[»]
4MGBX-ray1.85C/D686-698[»]
4MGCX-ray2.15F/G686-698[»]
4MGDX-ray1.90F/G686-698[»]
4RUJX-ray2.35B686-700[»]
4RUPX-ray2.75B686-700[»]
4TUZX-ray1.90F/G686-698[»]
4TV1X-ray1.85C/D686-698[»]
4UDAX-ray2.03B1427-1441[»]
4UDBX-ray2.36B1427-1441[»]
4Y29X-ray1.98B1432-1441[»]
5A86X-ray2.25C/D682-698[»]
5AVIX-ray2.70B/D676-700[»]
5AVLX-ray2.80B676-700[»]
5E7VX-ray2.40B686-700[»]
5HJSX-ray1.72C/D676-700[»]
ProteinModelPortaliQ15788.
SMRiQ15788. Positions 259-367, 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

eggNOGiENOG410IQ5S. Eukaryota.
ENOG410XPF9. LUCA.
GeneTreeiENSGT00530000063109.
HOVERGENiHBG052583.
InParanoidiQ15788.
KOiK09101.
OMAiQITPQPP.
OrthoDBiEOG091G00US.
PhylomeDBiQ15788.
TreeFamiTF332652.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProiIPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR009110. Nuc_rcpt_coact.
IPR014920. Nuc_rcpt_coact_Ncoa-typ.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR014935. SRC-1.
IPR008955. Src1_rcpt_coact.
[Graphical view]
PfamiPF07469. DUF1518. 2 hits.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
SMARTiSM01151. DUF1518. 2 hits.
SM00353. 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. AlignAdd to basket

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

        10         20         30         40         50
MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL
60 70 80 90 100
SANISDIDSL SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS
110 120 130 140 150
SSSQGVIEKE SLGPLLLEAL DGFFFVVNCE GRIVFVSENV TSYLGYNQEE
160 170 180 190 200
LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG VPWPQEATRR NSHTFNCRML
210 220 230 240 250
IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ SCLICIARRL
260 270 280 290 300
PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF
310 320 330 340 350
QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ
360 370 380 390 400
SPDMQPFIMG IHIIDREHSG LSPQDDTNSG MSIPRVNPSV NPSISPAHGV
410 420 430 440 450
ARSSTLPPSN SNMVSTRINR QQSSDLHSSS HSNSSNSQGS FGCSPGSQIV
460 470 480 490 500
ANVALNQGQA SSQSSNPSLN LNNSPMEGTG ISLAQFMSPR RQVTSGLATR
510 520 530 540 550
PRMPNNSFPP NISTLSSPVG MTSSACNNNN RSYSNIPVTS LQGMNEGPNN
560 570 580 590 600
SVGFSASSPV LRQMSSQNSP SRLNIQPAKA ESKDNKEIAS ILNEMIQSDN
610 620 630 640 650
SSSDGKPLDS GLLHNNDRLS DGDSKYSQTS HKLVQLLTTT AEQQLRHADI
660 670 680 690 700
DTSCKDVLSC TGTSNSASAN SSGGSCPSSH SSLTERHKIL HRLLQEGSPS
710 720 730 740 750
DITTLSVEPD KKDSASTSVS VTGQVQGNSS IKLELDASKK KESKDHQLLR
760 770 780 790 800
YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ MDPCNTNPTP MTKPTPEEIK
810 820 830 840 850
LEAQSQFTAD LDQFDQLLPT LEKAAQLPGL CETDRMDGAV TSVTIKSEIL
860 870 880 890 900
PASLQSATAR PTSRLNRLPE LELEAIDNQF GQPGTGDQIP WTNNTVTAIN
910 920 930 940 950
QSKSEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE
960 970 980 990 1000
LDRALGIDKL VQGGGLDVLS ERFPPQQATP PLIMEERPNL YSQPYSSPSP
1010 1020 1030 1040 1050
TANLPSPFQG MVRQKPSLGT MPVQVTPPRG AFSPGMGMQP RQTLNRPPAA
1060 1070 1080 1090 1100
PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF AATAPVGINM RSGMQQQITP
1110 1120 1130 1140 1150
QPPLNAQMLA QRQRELYSQQ HRQRQLIQQQ RAMLMRQQSF GNNLPPSSGL
1160 1170 1180 1190 1200
PVQMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AANPEASLAN
1210 1220 1230 1240 1250
RNSMVSRGMT GNIGGQFGTG INPQMQQNVF QYPGAGMVPQ GEANFAPSLS
1260 1270 1280 1290 1300
PGSSMVPMPI PPPQSSLLQQ TPPASGYQSP DMKAWQQGAI GNNNVFSQAV
1310 1320 1330 1340 1350
QNQPTPAQPG VYNNMSITVS MAGGNTNVQN MNPMMAQMQM SSLQMPGMNT
1360 1370 1380 1390 1400
VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE ADGTQQVQQV QVFADVQCTV
1410 1420 1430 1440
NLVGGDPYLN QPGPLGTQKP TSGPQTPQAQ QKSLLQQLLT E
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAC50305 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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_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.4. human. [Q15788-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005264685.1. XM_005264628.1. [Q15788-2]
UniGeneiHs.596314.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4MG5X-ray2.05C/D686-698[»]
4MG6X-ray2.10C/D686-698[»]
4MG7X-ray2.15C/D686-698[»]
4MG8X-ray1.85C/D686-698[»]
4MG9X-ray2.00F/G686-698[»]
4MGAX-ray1.80C/D686-698[»]
4MGBX-ray1.85C/D686-698[»]
4MGCX-ray2.15F/G686-698[»]
4MGDX-ray1.90F/G686-698[»]
4RUJX-ray2.35B686-700[»]
4RUPX-ray2.75B686-700[»]
4TUZX-ray1.90F/G686-698[»]
4TV1X-ray1.85C/D686-698[»]
4UDAX-ray2.03B1427-1441[»]
4UDBX-ray2.36B1427-1441[»]
4Y29X-ray1.98B1432-1441[»]
5A86X-ray2.25C/D682-698[»]
5AVIX-ray2.70B/D676-700[»]
5AVLX-ray2.80B676-700[»]
5E7VX-ray2.40B686-700[»]
5HJSX-ray1.72C/D676-700[»]
ProteinModelPortaliQ15788.
SMRiQ15788. Positions 259-367, 920-974.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114200. 108 interactions.
DIPiDIP-30877N.
IntActiQ15788. 27 interactions.
MINTiMINT-153305.
STRINGi9606.ENSP00000320940.

Chemistry

BindingDBiQ15788.
ChEMBLiCHEMBL2095162.
GuidetoPHARMACOLOGYi2693.

PTM databases

iPTMnetiQ15788.
PhosphoSiteiQ15788.

Polymorphism and mutation databases

BioMutaiNCOA1.
DMDMi158518533.

Proteomic databases

EPDiQ15788.
MaxQBiQ15788.
PaxDbiQ15788.
PeptideAtlasiQ15788.
PRIDEiQ15788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.4. human. [Q15788-1]

Organism-specific databases

CTDi8648.
GeneCardsiNCOA1.
HGNCiHGNC:7668. NCOA1.
HPAiCAB019402.
MIMi602691. gene.
neXtProtiNX_Q15788.
PharmGKBiPA31470.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQ5S. Eukaryota.
ENOG410XPF9. LUCA.
GeneTreeiENSGT00530000063109.
HOVERGENiHBG052583.
InParanoidiQ15788.
KOiK09101.
OMAiQITPQPP.
OrthoDBiEOG091G00US.
PhylomeDBiQ15788.
TreeFamiTF332652.

Enzyme and pathway databases

ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-159418. Recycling of bile acids and salts.
R-HSA-192105. Synthesis of bile acids and bile salts.
R-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-HSA-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-HSA-211976. Endogenous sterols.
R-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-3214847. HATs acetylate histones.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-HSA-400253. Circadian Clock.
SignaLinkiQ15788.
SIGNORiQ15788.

Miscellaneous databases

ChiTaRSiNCOA1. human.
EvolutionaryTraceiQ15788.
GeneWikiiNuclear_receptor_coactivator_1.
GenomeRNAii8648.
PROiQ15788.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000084676.
ExpressionAtlasiQ15788. baseline and differential.
GenevisibleiQ15788. HS.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProiIPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR009110. Nuc_rcpt_coact.
IPR014920. Nuc_rcpt_coact_Ncoa-typ.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR014935. SRC-1.
IPR008955. Src1_rcpt_coact.
[Graphical view]
PfamiPF07469. DUF1518. 2 hits.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
SMARTiSM01151. DUF1518. 2 hits.
SM00353. 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]
ProtoNetiSearch...

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: September 7, 2016
This is version 156 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.