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Q9Y6Q9 (NCOA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. 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 3

Short name=NCoA-3
EC=2.3.1.48
Alternative name(s):
ACTR
Amplified in breast cancer 1 protein
Short name=AIB-1
CBP-interacting protein
Short name=pCIP
Class E basic helix-loop-helix protein 42
Short name=bHLHe42
Receptor-associated coactivator 3
Short name=RAC-3
Steroid receptor coactivator protein 3
Short name=SRC-3
Thyroid hormone receptor activator molecule 1
Short name=TRAM-1
Gene names
Name:NCOA3
Synonyms:AIB1, BHLHE42, RAC3, TRAM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1424 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. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit.

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.2

Enzyme regulation

Coactivator activity on nuclear receptors and NF-kappa-B pathways is enhanced by various hormones, and the TNF cytokine, respectively. TNF stimulation probably enhances phosphorylation, which in turn activates coactivator function. In contrast, acetylation by CREBBP apparently suppresses coactivation of target genes by disrupting its association with nuclear receptors. Binds to CSNK1D.

Subunit structure

Interacts with CARM1 By similarity. Present in a complex containing NCOA2, IKKA, IKKB, IKBKG and the histone acetyltransferase protein CREBBP. Interacts with CASP8AP2, NR3C1 and PCAF. Interacts with ATAD2 and this interaction is enhanced by estradiol. Found in a complex containing NCOA3, AR and MAK. Interacts with DDX5. Interacts with PSMB9. Interacts with NPAS2. Ref.1 Ref.3 Ref.4 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23

Subcellular location

Cytoplasm. Nucleus. Note: Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus.

Tissue specificity

Widely expressed. High expression in heart, skeletal muscle, pancreas and placenta. Low expression in brain, and very low in lung, liver and kidney.

Domain

Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and 2 are essential for the association with nuclear receptors, and constitute the RID domain (Receptor-interacting domain).

Post-translational modification

Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function. Ref.10

Methylated by CARM1 By similarity.

Phosphorylated by IKK complex. Regulated its function. Phosphorylation at Ser-601 by CK1 promotes coactivator function. Ref.13 Ref.23

Polymorphism

The length of the poly-Gln region is polymorphic in the normal population.

Miscellaneous

NCOA3 is frequently amplified or overexpressed in breast and ovarian cancers.

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.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionActivator
Acyltransferase
Transferase
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

developmental growth

Inferred from electronic annotation. Source: Ensembl

histone acetylation

Inferred from direct assay Ref.2. Source: GOC

labyrinthine layer morphogenesis

Inferred from electronic annotation. Source: Ensembl

mammary gland branching involved in thelarche

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

positive regulation of keratinocyte differentiation

Inferred from mutant phenotype PubMed 17082781PubMed 17223341. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

receptor transactivation

Traceable author statement PubMed 17223341. Source: UniProtKB

regulation of RNA biosynthetic process

Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

vagina development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17223341. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 17223341. Source: UniProtKB

   Molecular_functionandrogen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity

Inferred from direct assay Ref.2. Source: UniProtKB

ligand-dependent nuclear receptor binding

Inferred from physical interaction PubMed 18798693. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from electronic annotation. Source: InterPro

nuclear hormone receptor binding

Inferred from direct assay Ref.2. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11279242Ref.14Ref.15Ref.16PubMed 16456540. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

thyroid hormone receptor binding

Non-traceable author statement Ref.1. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.4Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9Y6Q9-1)

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: Q9Y6Q9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     903-917: Missing.
Isoform 3 (identifier: Q9Y6Q9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: E → EVTSDGIFSPT
     903-917: Missing.
     1214-1217: Missing.
Isoform 4 (identifier: Q9Y6Q9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: E → EVTSDGIFSPT
     837-901: Missing.
     903-917: Missing.
     1214-1217: Missing.
Isoform 5 (identifier: Q9Y6Q9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1214-1217: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.28
Chain2 – 14241423Nuclear receptor coactivator 3
PRO_0000094406

Regions

Domain25 – 8258bHLH
Domain110 – 18071PAS
Region1023 – 109371Interaction with CREBBP
Region1097 – 1304208Acetyltransferase
Motif685 – 6895LXXLL motif 1
Motif738 – 7425LXXLL motif 2
Motif1057 – 10615LXXLL motif 3
Compositional bias505 – 671167Ser-rich
Compositional bias976 – 9805Poly-Gln
Compositional bias1248 – 127831Poly-Gln
Compositional bias1392 – 141726Met-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.28
Modified residue2141Phosphoserine Ref.21 Ref.26
Modified residue5511Phosphoserine Ref.21
Modified residue6011Phosphoserine; by CK1 Ref.23
Modified residue6161N6-acetyllysine; by CREBBP Ref.10
Modified residue6191N6-acetyllysine; by CREBBP Ref.10
Modified residue6201N6-acetyllysine; by CREBBP Ref.10
Modified residue6871N6-acetyllysine Ref.25
Modified residue7281Phosphoserine Ref.21
Modified residue8571Phosphoserine Ref.19 Ref.21 Ref.24 Ref.26
Modified residue8601Phosphoserine By similarity
Modified residue8671Phosphoserine Ref.19 Ref.26

Natural variations

Alternative sequence3211E → EVTSDGIFSPT in isoform 3 and isoform 4.
VSP_003405
Alternative sequence837 – 90165Missing in isoform 4.
VSP_003406
Alternative sequence903 – 91715Missing in isoform 2, isoform 3 and isoform 4.
VSP_003407
Alternative sequence1214 – 12174Missing in isoform 3, isoform 4 and isoform 5.
VSP_003408
Natural variant2181R → C. Ref.5
Corresponds to variant rs6094752 [ dbSNP | Ensembl ].
VAR_053527
Natural variant2201R → I. Ref.5
VAR_060695
Natural variant3691L → F.
Corresponds to variant rs6094756 [ dbSNP | Ensembl ].
VAR_053528
Natural variant4601G → R.
Corresponds to variant rs1052765 [ dbSNP | Ensembl ].
VAR_013831
Natural variant5561I → V. Ref.5
Corresponds to variant rs72645272 [ dbSNP | Ensembl ].
VAR_060696
Natural variant5591P → S. Ref.5
Corresponds to variant rs2230781 [ dbSNP | Ensembl ].
VAR_013832
Natural variant5861Q → H. Ref.5
Corresponds to variant rs2230782 [ dbSNP | Ensembl ].
VAR_013833
Natural variant7771S → A. Ref.5
Corresponds to variant rs2230783 [ dbSNP | Ensembl ].
VAR_053529
Natural variant12471M → K. Ref.5
VAR_060697
Natural variant12471M → L. Ref.5
VAR_060698
Natural variant1248 – 12503Missing.
VAR_013834

Experimental info

Mutagenesis6161K → Q: Strongly reduces acetylation by CREBBP. Ref.10
Mutagenesis619 – 6202KK → QQ: Abolishes acetylation by CREBBP.
Mutagenesis6471K → Q: Does not affect acetylation by CREBBP. Ref.10
Mutagenesis6811K → Q: Does not affect acetylation by CREBBP. Ref.10
Mutagenesis6871K → Q: Does not affect acetylation by CREBBP. Ref.10
Mutagenesis7001K → Q: Does not affect acetylation by CREBBP. Ref.10
Mutagenesis7081K → Q: Does not affect acetylation by CREBBP. Ref.10
Sequence conflict131 – 1322DG → EA in AAC51663. Ref.4

Secondary structure

............. 1424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 732CDF0423161679

FASTA1,424155,293
        10         20         30         40         50         60 
MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE LISANLSDID 

        70         80         90        100        110        120 
NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV SSTGQGVIDK DSLGPLLLQA 

       130        140        150        160        170        180 
LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG 

       190        200        210        220        230        240 
VSWTNETQRQ KSHTFNCRML MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE 

       250        260        270        280        290        300 
DLQSCMICVA RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC 

       310        320        330        340        350        360 
IQRFFSLNDG QSWSQKRHYQ EAYLNGHAET PVYRFSLADG TIVTAQTKSK LFRNPVTNDR 

       370        380        390        400        410        420 
HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG MSMSPNQGLQ MPSSRAYGLA 

       430        440        450        460        470        480 
DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS PSSYQNNNYG LNMSSPPHGS PGLAPNQQNI 

       490        500        510        520        530        540 
MISPRNRGSP KIASHQFSPV AGVHSPMASS GNTGNHSFSS SSLSALQAIS EGVGTSLLST 

       550        560        570        580        590        600 
LSSPGPKLDN SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR DHLSDKESKE 

       610        620        630        640        650        660 
SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS VSVTSPSGVS 

       670        680        690        700        710        720 
SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT SSITSCGDGN 

       730        740        750        760        770        780 
VVKQEQLSPK KKENNALLRY LLDRDDPSDA LSKELQPQVE GVDNKMSQCT SSTIPSSSQE 

       790        800        810        820        830        840 
KDPKIKTETS EEGSGDLDNL DAILGDLTSS DFYNNSISSN GSHLGTKQQV FQGTNSLGLK 

       850        860        870        880        890        900 
SSQSVQSIRP PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR MMDSQENYGS 

       910        920        930        940        950        960 
SMGGPNRNVT VTQTPSSGDW GLPNSKAGRM EPMNSNSMGR PGGDYNTSLP RPALGGSIPT 

       970        980        990       1000       1010       1020 
LPLRSNSIPG ARPVLQQQQQ MLQMRPGEIP MGMGANPYGQ AAASNQLGSW PDGMLSMEQV 

      1030       1040       1050       1060       1070       1080 
SHGTQNRPLL RNSLDDLVGP PSNLEGQSDE RALLDQLHTL LSNTDATGLE EIDRALGIPE 

      1090       1100       1110       1120       1130       1140 
LVNQGQALEP KQDAFQGQEA AVMMDQKAGL YGQTYPAQGP PMQGGFHLQG QSPSFNSMMN 

      1150       1160       1170       1180       1190       1200 
QMNQQGNFPL QGMHPRANIM RPRTNTPKQL RMQLQQRLQG QQFLNQSRQA LELKMENPTA 

      1210       1220       1230       1240       1250       1260 
GGAAVMRPMM QPQVSSQQGF LNAQMVAQRS RELLSHHFRQ QRVAMMMQQQ QQQQQQQQQQ 

      1270       1280       1290       1300       1310       1320 
QQQQQQQQQQ QQQQQQTQAF SPPPNVTASP SMDGLLAGPT MPQAPPQQFP YQPNYGMGQQ 

      1330       1340       1350       1360       1370       1380 
PDPAFGRVSS PPNAMMSSRM GPSQNPMMQH PQAASIYQSS EMKGWPSGNL ARNSSFSQQQ 

      1390       1400       1410       1420 
FAHQGNPAVY SMVHMNGSSG HMGQMNMNPM PMSGMPMGPD QKYC 

« Hide

Isoform 2 [UniParc].

Checksum: 04B4DF09150BD916
Show »

FASTA1,409153,797
Isoform 3 [UniParc].

Checksum: 4A162AB05BA34062
Show »

FASTA1,415154,400
Isoform 4 [UniParc].

Checksum: F75584B329A892C4
Show »

FASTA1,350147,499
Isoform 5 [UniParc].

Checksum: 654343CEA0855C60
Show »

FASTA1,420154,892

References

« Hide 'large scale' references
[1]"TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1."
Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.
J. Biol. Chem. 272:27629-27634(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CREBBP; PCAF; RARA; RXRA; THRA AND ESR.
Tissue: Pituitary.
[2]"Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300."
Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M.
Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ENZYME ACTIVITY, VARIANT 1248-GLN--GLN-1250 DEL.
Tissue: Leukemia.
[3]"AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer."
Anzick S.L., Kononen J., Walker R.L., Azorsa D.O., Tanner M.M., Guan X.-Y., Sauter G., Kallioniemi O.-P., Trent J.M., Meltzer P.S.
Science 277:965-968(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH ESR.
Tissue: Lung.
[4]"RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2."
Li H., Gomes P.J., Chen J.D.
Proc. Natl. Acad. Sci. U.S.A. 94:8479-8484(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH VDR; RARA; PPARA; RXRA; THRA AND ESR, VARIANT 1248-GLN--GLN-1250 DEL.
Tissue: Brain.
[5]NIEHS SNPs program
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-218; ILE-220; VAL-556; SER-559; HIS-586; ALA-777; LEU-1247 AND LYS-1247.
[6]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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] (ISOFORM 5).
[9]"Polymorphic exonic CAG microsatellites in the gene amplified in breast cancer (AIB1 gene)."
Shirazi S.K., Bober M.A., Coetzee G.A.
Clin. Genet. 54:102-103(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM OF POLY-GLN REGION.
[10]"Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase."
Chen H., Lin R.J., Xie W., Wilpitz D., Evans R.M.
Cell 98:675-686(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-616; LYS-619 AND LYS-620 BY CREBBP, MUTAGENESIS OF LYS-616; 619-LYS-LYS-620; LYS-647; LYS-681; LYS-687; LYS-700 AND LYS-708.
[11]"RAC-3 is a NF-kappa B coactivator."
Werbajh S., Nojek I., Lanz R., Costas M.A.
FEBS Lett. 485:195-199(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFKB1.
[12]"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.
[13]"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase."
Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
Mol. Cell. Biol. 22:3549-3561(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; IKKA; IKKB AND IKBKG, PHOSPHORYLATION.
[14]"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.
[15]"Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPAS2.
[16]"FLASH interacts with p160 coactivator subtypes and differentially suppresses transcriptional activity of steroid hormone receptors."
Kino T., Ichijo T., Chrousos G.P.
J. Steroid Biochem. Mol. Biol. 92:357-363(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASP8AP2.
[17]"Male germ cell-associated kinase, a male-specific kinase regulated by androgen, is a coactivator of androgen receptor in prostate cancer cells."
Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M., Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.
Cancer Res. 66:8439-8447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[18]"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.
[19]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification."
Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.
Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATAD2.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-551; SER-728 AND SER-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an estrogen-dependent manner and regulates ERalpha-AIB1 interactions."
Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.
Nucleic Acids Res. 37:3110-3123(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-601 BY CSNK1D/CK1, INTERACTION WITH CSNK1D.
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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-214; SER-857 AND SER-867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF016031 mRNA. Translation: AAC51849.1.
AF036892 mRNA. Translation: AAB92368.1.
AF012108 mRNA. Translation: AAC51677.1.
AF010227 mRNA. Translation: AAC51663.1.
EF488684 Genomic DNA. Translation: ABO43042.1.
AL034418 Genomic DNA. Translation: CAB40662.1.
AL034418 Genomic DNA. Translation: CAC17693.1.
AL034418 Genomic DNA. Translation: CAI42141.1.
CH471077 Genomic DNA. Translation: EAW75698.1.
CH471077 Genomic DNA. Translation: EAW75702.1.
BC119001 mRNA. Translation: AAI19002.1.
CCDSCCDS13406.1. [Q9Y6Q9-5]
CCDS13407.1. [Q9Y6Q9-1]
CCDS54472.1. [Q9Y6Q9-3]
PIRT03851.
RefSeqNP_001167559.1. NM_001174088.1. [Q9Y6Q9-3]
NP_006525.2. NM_006534.3. [Q9Y6Q9-5]
NP_858045.1. NM_181659.2. [Q9Y6Q9-1]
UniGeneHs.592142.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KBHNMR-A1045-1091[»]
3L3XX-ray1.55B618-629[»]
3L3ZX-ray2.00B735-746[»]
DisProtDP00343.
ProteinModelPortalQ9Y6Q9.
SMRQ9Y6Q9. Positions 34-367, 1045-1091.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113841. 99 interactions.
DIPDIP-30876N.
IntActQ9Y6Q9. 43 interactions.
MINTMINT-231818.

Chemistry

BindingDBQ9Y6Q9.
ChEMBLCHEMBL2095161.

PTM databases

PhosphoSiteQ9Y6Q9.

Polymorphism databases

DMDM23396777.

Proteomic databases

MaxQBQ9Y6Q9.
PaxDbQ9Y6Q9.
PRIDEQ9Y6Q9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371997; ENSP00000361065; ENSG00000124151. [Q9Y6Q9-3]
ENST00000371998; ENSP00000361066; ENSG00000124151. [Q9Y6Q9-1]
ENST00000372004; ENSP00000361073; ENSG00000124151. [Q9Y6Q9-5]
GeneID8202.
KEGGhsa:8202.
UCSCuc002xtk.3. human. [Q9Y6Q9-1]
uc002xtl.3. human. [Q9Y6Q9-5]
uc010ght.2. human. [Q9Y6Q9-3]

Organism-specific databases

CTD8202.
GeneCardsGC20P046130.
HGNCHGNC:7670. NCOA3.
HPACAB009800.
HPA024210.
MIM601937. gene.
neXtProtNX_Q9Y6Q9.
PharmGKBPA31472.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315556.
HOVERGENHBG052583.
InParanoidQ9Y6Q9.
KOK11256.
OMADGNIVFV.
OrthoDBEOG72JWFB.
PhylomeDBQ9Y6Q9.
TreeFamTF332652.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkQ9Y6Q9.

Gene expression databases

ArrayExpressQ9Y6Q9.
BgeeQ9Y6Q9.
CleanExHS_NCOA3.
HS_RAC3.
HS_TRAM1.
GenevestigatorQ9Y6Q9.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProIPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR028818. NCOA3.
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:SF3. PTHR10684:SF3. 1 hit.
PfamPF07469. DUF1518. 1 hit.
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

ChiTaRSNCOA3. human.
EvolutionaryTraceQ9Y6Q9.
GeneWikiNuclear_receptor_coactivator_3.
GenomeRNAi8202.
NextBio30907.
PROQ9Y6Q9.
SOURCESearch...

Entry information

Entry nameNCOA3_HUMAN
AccessionPrimary (citable) accession number: Q9Y6Q9
Secondary accession number(s): A4LAZ5 expand/collapse secondary AC list , Q0VF45, Q5JYD9, Q5JYE0, Q9BR49, Q9UPC9, Q9UPG4, Q9UPG7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 158 of the entry and version 1 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 20

Human chromosome 20: entries, gene names and cross-references to MIM