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Q15788 (NCOA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor coactivator 1

Short name=NCoA-1
EC=2.3.1.48
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 names
Name:NCOA1
Synonyms:BHLHE74, SRC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1441 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.8 Ref.11 Ref.12 Ref.13 Ref.16 Ref.25

Catalytic activity

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

Subunit structure

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. Ref.1 Ref.8 Ref.12 Ref.15 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34

Subcellular location

Nucleus By similarity.

Tissue specificity

Widely expressed. Ref.2 Ref.10

Domain

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

Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL motifs 3, 4 and 5 are essential for the association with nuclear receptors. LXXLL motif 7, which is not present in isoform 2, increases the affinity for steroid receptors in vitro.

Post-translational modification

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. Ref.24

Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites. Ref.24

Involvement in disease

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.

Sequence similarities

Belongs to the SRC/p160 nuclear receptor coactivator family.

Contains 1 bHLH (basic helix-loop-helix) domain.

Contains 1 PAS (PER-ARNT-SIM) domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainRepeat
   Molecular functionActivator
Acyltransferase
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

estrous cycle phase

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

histone H4 acetylation

Inferred from electronic annotation. Source: Ensembl

hypothalamus development

Inferred from electronic annotation. Source: Ensembl

labyrinthine layer morphogenesis

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

male mating behavior

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of female receptivity

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15919756. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter by galactose

Inferred from direct assay PubMed 10207113. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.27. Source: UniProtKB

regulation of cellular response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from direct assay Ref.11. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from direct assay PubMed 17363140. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA polymerase II regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription coactivator activity

Non-traceable author statement PubMed 15774904. Source: BHF-UCL

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction Ref.22. Source: UniProtKB

histone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ligand-dependent nuclear receptor binding

Inferred from physical interaction PubMed 18798693. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay PubMed 15919756. Source: UniProtKB

nuclear hormone receptor binding

Inferred from direct assay PubMed 10207113. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction Ref.26. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12578355Ref.26Ref.27PubMed 17254542Ref.33PubMed 21454491. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Inferred from direct assay PubMed 10207113. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15788-1)

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.
Isoform 2 (identifier: Q15788-2)

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.
Isoform 3 (identifier: Q15788-3)

Also known as: SRC-1 (-Q);

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.32
Chain2 – 14411440Nuclear receptor coactivator 1
PRO_0000094400

Regions

Domain23 – 8058bHLH
Domain109 – 18072PAS
Region361 – 567207Interaction with STAT3
Region781 – 988208Interaction with CREBBP
Motif46 – 505LXXLL motif 1
Motif112 – 1165LXXLL motif 2
Motif633 – 6375LXXLL motif 3
Motif690 – 6945LXXLL motif 4
Motif749 – 7535LXXLL motif 5
Motif913 – 9175LXXLL motif 6
Motif1435 – 14395LXXLL motif 7
Compositional bias389 – 682294Ser-rich
Compositional bias1053 – 113886Gln-rich

Sites

Site867 – 8682Breakpoint for translocation to form PAX3-NCOA1 oncogene

Amino acid modifications

Modified residue21N-acetylserine Ref.32
Modified residue221Phosphoserine By similarity
Modified residue3721Phosphoserine Ref.17
Modified residue3951Phosphoserine Ref.17 Ref.35
Modified residue5171Phosphoserine Ref.17
Modified residue5691Phosphoserine Ref.17
Modified residue6981Phosphoserine By similarity
Modified residue10331Phosphoserine Ref.17
Modified residue11791Phosphothreonine Ref.17
Modified residue11851Phosphoserine Ref.17
Cross-link732Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.24
Cross-link774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.24

Natural variations

Alternative sequence13851Missing in isoform 3.
VSP_011738
Alternative sequence1386 – 144156QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2.
VSP_011739
Natural variant4571Q → K. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049015 [ dbSNP | Ensembl ].
VAR_019768
Natural variant4661N → K. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049016 [ dbSNP | Ensembl ].
VAR_019769
Natural variant4741S → P. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049018 [ dbSNP | Ensembl ].
VAR_019770
Natural variant5911I → T. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049020 [ dbSNP | Ensembl ].
VAR_019771
Natural variant6851E → A. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049021 [ dbSNP | Ensembl ].
VAR_019772
Natural variant7941P → A. Ref.8
Corresponds to variant rs1049025 [ dbSNP | Ensembl ].
VAR_019773
Natural variant9991S → F. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049032 [ dbSNP | Ensembl ].
VAR_019774
Natural variant11541M → T. Ref.1 Ref.3 Ref.8
Corresponds to variant rs1049038 [ dbSNP | Ensembl ].
VAR_019775
Natural variant12381V → I. Ref.4
Corresponds to variant rs56099330 [ dbSNP | Ensembl ].
VAR_038832
Natural variant12721P → S. Ref.4
Corresponds to variant rs1804645 [ dbSNP | Ensembl ].
VAR_034882

Experimental info

Mutagenesis636 – 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. Ref.2
Mutagenesis693 – 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. Ref.2
Mutagenesis7321K → R: Abolishes sumoylation; when associated with R-774. Ref.2 Ref.24
Mutagenesis752 – 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. Ref.2
Mutagenesis7741K → R: Abolishes sumoylation; when associated with R-732. Ref.2 Ref.24
Mutagenesis8001K → R: Does not affect sumoylation of the protein. Ref.2 Ref.24
Mutagenesis8461K → R: Does not affect sumoylation of the protein. Ref.2 Ref.24
Mutagenesis13781K → R: Does not affect sumoylation of the protein. Ref.2 Ref.24
Sequence conflict10351Missing in AAT47737. Ref.10
Sequence conflict13701Q → H in AAA64187. Ref.9
Sequence conflict13821D → G in AAT47737. Ref.10
Sequence conflict14351L → R in AAB50242. Ref.3

Secondary structure

....................... 1441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SRC-1A) (SRC1a) [UniParc].

Last modified September 11, 2007. Version 3.
Checksum: 25EF6F389489121E

FASTA1,441156,757
        10         20         30         40         50         60 
MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL 

        70         80         90        100        110        120 
SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL 

       130        140        150        160        170        180 
DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG 

       190        200        210        220        230        240 
VPWPQEATRR NSHTFNCRML IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ 

       250        260        270        280        290        300 
SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 

       310        320        330        340        350        360 
QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG 

       370        380        390        400        410        420 
IHIIDREHSG LSPQDDTNSG MSIPRVNPSV NPSISPAHGV ARSSTLPPSN SNMVSTRINR 

       430        440        450        460        470        480 
QQSSDLHSSS HSNSSNSQGS FGCSPGSQIV ANVALNQGQA SSQSSNPSLN LNNSPMEGTG 

       490        500        510        520        530        540 
ISLAQFMSPR RQVTSGLATR PRMPNNSFPP NISTLSSPVG MTSSACNNNN RSYSNIPVTS 

       550        560        570        580        590        600 
LQGMNEGPNN SVGFSASSPV LRQMSSQNSP SRLNIQPAKA ESKDNKEIAS ILNEMIQSDN 

       610        620        630        640        650        660 
SSSDGKPLDS GLLHNNDRLS DGDSKYSQTS HKLVQLLTTT AEQQLRHADI DTSCKDVLSC 

       670        680        690        700        710        720 
TGTSNSASAN SSGGSCPSSH SSLTERHKIL HRLLQEGSPS DITTLSVEPD KKDSASTSVS 

       730        740        750        760        770        780 
VTGQVQGNSS IKLELDASKK KESKDHQLLR YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ 

       790        800        810        820        830        840 
MDPCNTNPTP MTKPTPEEIK LEAQSQFTAD LDQFDQLLPT LEKAAQLPGL CETDRMDGAV 

       850        860        870        880        890        900 
TSVTIKSEIL PASLQSATAR PTSRLNRLPE LELEAIDNQF GQPGTGDQIP WTNNTVTAIN 

       910        920        930        940        950        960 
QSKSEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE LDRALGIDKL 

       970        980        990       1000       1010       1020 
VQGGGLDVLS ERFPPQQATP PLIMEERPNL YSQPYSSPSP TANLPSPFQG MVRQKPSLGT 

      1030       1040       1050       1060       1070       1080 
MPVQVTPPRG AFSPGMGMQP RQTLNRPPAA PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF 

      1090       1100       1110       1120       1130       1140 
AATAPVGINM RSGMQQQITP QPPLNAQMLA QRQRELYSQQ HRQRQLIQQQ RAMLMRQQSF 

      1150       1160       1170       1180       1190       1200 
GNNLPPSSGL PVQMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AANPEASLAN 

      1210       1220       1230       1240       1250       1260 
RNSMVSRGMT GNIGGQFGTG INPQMQQNVF QYPGAGMVPQ GEANFAPSLS PGSSMVPMPI 

      1270       1280       1290       1300       1310       1320 
PPPQSSLLQQ TPPASGYQSP DMKAWQQGAI GNNNVFSQAV QNQPTPAQPG VYNNMSITVS 

      1330       1340       1350       1360       1370       1380 
MAGGNTNVQN MNPMMAQMQM SSLQMPGMNT VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE 

      1390       1400       1410       1420       1430       1440 
ADGTQQVQQV QVFADVQCTV NLVGGDPYLN QPGPLGTQKP TSGPQTPQAQ QKSLLQQLLT 


E 

« Hide

Isoform 2 (SRC-1E) (SRC1e) [UniParc].

Checksum: DACE967B31AC6B69
Show »

FASTA1,399152,385
Isoform 3 (SRC-1 (-Q)) [UniParc].

Checksum: 4E3FFED7088CDBF8
Show »

FASTA1,440156,628

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Steroid receptor coactivator-1 is a histone acetyltransferase."
Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J., Mizzen C.A., McKenna N.J., Onate S.A., Tsai S.Y., Tsai M.-J., O'Malley B.W.
Nature 389:194-198(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A HISTONE ACETYLTRANSFERASE, INTERACTION WITH PCAF.
[13]"Steroid receptor induction of gene transcription: a two-step model."
Jenster G., Spencer T.E., Burcin M.M., Tsai S.Y., Tsai M.-J., O'Malley B.W.
Proc. Natl. Acad. Sci. U.S.A. 94:7879-7884(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
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]"JAB1 interacts with both the progesterone receptor and SRC-1."
Chauchereau A., Georgiakaki M., Perrin-Wolff M., Milgrom E., Loosfelt H.
J. Biol. Chem. 275:8540-8548(2000) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1712.1. [Q15788-1]
CCDS1713.1. [Q15788-2]
CCDS42660.1. [Q15788-3]
PIRA57620.
PC4363.
PC4364.
RefSeqNP_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]
UniGeneHs.596314.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ15788.
SMRQ15788. Positions 29-367, 920-974.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114200. 72 interactions.
DIPDIP-30877N.
IntActQ15788. 24 interactions.
MINTMINT-153305.

Chemistry

BindingDBQ15788.
ChEMBLCHEMBL1615387.

PTM databases

PhosphoSiteQ15788.

Polymorphism databases

DMDM158518533.

Proteomic databases

MaxQBQ15788.
PaxDbQ15788.
PRIDEQ15788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288599; 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]
GeneID8648.
KEGGhsa:8648.
UCSCuc002rfj.3. human. [Q15788-2]
uc002rfk.3. human. [Q15788-1]
uc002rfl.3. human. [Q15788-3]

Organism-specific databases

CTD8648.
GeneCardsGC02P024719.
HGNCHGNC:7668. NCOA1.
HPACAB019402.
MIM602691. gene.
neXtProtNX_Q15788.
PharmGKBPA31470.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315556.
HOVERGENHBG052583.
InParanoidQ15788.
KOK09101.
OMAQITPQPP.
OrthoDBEOG789C9C.
PhylomeDBQ15788.
TreeFamTF332652.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.
SignaLinkQ15788.

Gene expression databases

ArrayExpressQ15788.
BgeeQ15788.
GenevestigatorQ15788.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProIPR011598. 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]
PANTHERPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF1. PTHR10684:SF1. 1 hit.
PfamPF07469. DUF1518. 2 hits.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
PIRSFPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
SMARTSM00353. HLH. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCOA1. human.
EvolutionaryTraceQ15788.
GeneWikiNuclear_receptor_coactivator_1.
GenomeRNAi8648.
NextBio32423.
PROQ15788.
SOURCESearch...

Entry information

Entry nameNCOA1_HUMAN
AccessionPrimary (citable) accession number: Q15788
Secondary accession number(s): O00150 expand/collapse secondary AC list , O43792, O43793, Q13071, Q13420, Q2T9G5, Q53SX3, Q6GVI5, Q7KYV3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM