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Q15788

- NCOA1_HUMAN

UniProt

Q15788 - NCOA1_HUMAN

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Protein

Nuclear receptor coactivator 1

Gene
NCOA1, BHLHE74, SRC1
Organism
Homo sapiens (Human)
Status
Reviewed - 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].

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
Complete GO annotation...

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 By similarity

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. neuron projection Source: Ensembl
  3. nuclear chromatin Source: BHF-UCL
  4. 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. 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 – 221Phosphoserine By similarity
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei395 – 3951Phosphoserine2 Publications
Modified residuei517 – 5171Phosphoserine1 Publication
Modified residuei569 – 5691Phosphoserine1 Publication
Modified residuei698 – 6981Phosphoserine By similarity
Cross-linki732 – 732Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki774 – 774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
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.18 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.

Miscellaneous databases

EvolutionaryTraceiQ15788.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 8058bHLHAdd
BLAST
Domaini109 – 18072PASAdd
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

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.

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. VSP_011738
Alternative sequencei1386 – 144156QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2. VSP_011739Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1035 – 10351Missing in AAT47737. 1 Publication
Sequence conflicti1370 – 13701Q → H in AAA64187. 1 Publication
Sequence conflicti1382 – 13821D → G in AAT47737. 1 Publication
Sequence conflicti1435 – 14351L → R in AAB50242. 1 Publication

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]
ENST00000538539; ENSP00000444039; ENSG00000084676. [Q15788-2]
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 ]
ENST00000538539 ; ENSP00000444039 ; ENSG00000084676 . [Q15788-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 133 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

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