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Q9Y6Q9

- NCOA3_HUMAN

UniProt

Q9Y6Q9 - NCOA3_HUMAN

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Protein
Nuclear receptor coactivator 3
Gene
NCOA3, AIB1, BHLHE42, RAC3, TRAM1
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. 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 activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].1 Publication

Enzyme regulationi

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.

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. chromatin binding Source: Ensembl
  3. histone acetyltransferase activity Source: UniProtKB
  4. ligand-dependent nuclear receptor binding Source: UniProtKB
  5. ligand-dependent nuclear receptor transcription coactivator activity Source: InterPro
  6. nuclear hormone receptor binding Source: UniProtKB
  7. protein N-terminus binding Source: UniProtKB
  8. protein binding Source: UniProtKB
  9. signal transducer activity Source: InterPro
  10. thyroid hormone receptor binding Source: UniProtKB
  11. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. developmental growth Source: Ensembl
  3. histone acetylation Source: GOC
  4. labyrinthine layer morphogenesis Source: Ensembl
  5. mammary gland branching involved in thelarche Source: Ensembl
  6. multicellular organism growth Source: Ensembl
  7. positive regulation of gene expression Source: UniProtKB
  8. positive regulation of keratinocyte differentiation Source: UniProtKB
  9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. positive regulation of transcription, DNA-templated Source: UniProtKB
  11. receptor transactivation Source: UniProtKB
  12. regulation of RNA biosynthetic process Source: UniProtKB
  13. transcription, DNA-templated Source: UniProtKB-KW
  14. vagina development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ9Y6Q9.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor coactivator 3 (EC:2.3.1.48)
Short name:
NCoA-3
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 namesi
Name:NCOA3
Synonyms:AIB1, BHLHE42, RAC3, TRAM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:7670. NCOA3.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi616 – 6161K → Q: Strongly reduces acetylation by CREBBP. 1 Publication
Mutagenesisi619 – 6202KK → QQ: Abolishes acetylation by CREBBP.
Mutagenesisi647 – 6471K → Q: Does not affect acetylation by CREBBP. 1 Publication
Mutagenesisi681 – 6811K → Q: Does not affect acetylation by CREBBP. 1 Publication
Mutagenesisi687 – 6871K → Q: Does not affect acetylation by CREBBP. 1 Publication
Mutagenesisi700 – 7001K → Q: Does not affect acetylation by CREBBP. 1 Publication
Mutagenesisi708 – 7081K → Q: Does not affect acetylation by CREBBP. 1 Publication

Organism-specific databases

PharmGKBiPA31472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 14241423Nuclear receptor coactivator 3
PRO_0000094406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei214 – 2141Phosphoserine2 Publications
Modified residuei551 – 5511Phosphoserine1 Publication
Modified residuei601 – 6011Phosphoserine; by CK11 Publication
Modified residuei616 – 6161N6-acetyllysine; by CREBBP1 Publication
Modified residuei619 – 6191N6-acetyllysine; by CREBBP1 Publication
Modified residuei620 – 6201N6-acetyllysine; by CREBBP1 Publication
Modified residuei687 – 6871N6-acetyllysine1 Publication
Modified residuei728 – 7281Phosphoserine1 Publication
Modified residuei857 – 8571Phosphoserine4 Publications
Modified residuei860 – 8601Phosphoserine By similarity
Modified residuei867 – 8671Phosphoserine2 Publications

Post-translational modificationi

Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function.1 Publication
Methylated by CARM1 By similarity.
Phosphorylated by IKK complex. Regulated its function. Phosphorylation at Ser-601 by CK1 promotes coactivator function.2 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y6Q9.
PaxDbiQ9Y6Q9.
PRIDEiQ9Y6Q9.

PTM databases

PhosphoSiteiQ9Y6Q9.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9Y6Q9.
BgeeiQ9Y6Q9.
CleanExiHS_NCOA3.
HS_RAC3.
HS_TRAM1.
GenevestigatoriQ9Y6Q9.

Organism-specific databases

HPAiCAB009800.
HPA024210.

Interactioni

Subunit structurei

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 NPAS2.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX17Q928412EBI-81196,EBI-746012
EP300Q094722EBI-81196,EBI-447295
ESR1P033722EBI-81196,EBI-78473
IKBKBO149203EBI-81196,EBI-81266
PSMB9P280653EBI-81196,EBI-603300
PSME3P612895EBI-81196,EBI-355546
PTENP604842EBI-81196,EBI-696162
SPOPO437916EBI-81196,EBI-743549
VdrP482812EBI-81196,EBI-346797From a different organism.

Protein-protein interaction databases

BioGridi113841. 99 interactions.
DIPiDIP-30876N.
IntActiQ9Y6Q9. 43 interactions.
MINTiMINT-231818.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi619 – 6268
Helixi736 – 7438
Helixi1049 – 106012
Helixi1069 – 10757
Helixi1078 – 10847
Helixi1086 – 10883

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KBHNMR-A1045-1091[»]
3L3XX-ray1.55B618-629[»]
3L3ZX-ray2.00B735-746[»]
DisProtiDP00343.
ProteinModelPortaliQ9Y6Q9.
SMRiQ9Y6Q9. Positions 34-367, 1045-1091.

Miscellaneous databases

EvolutionaryTraceiQ9Y6Q9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 8258bHLH
Add
BLAST
Domaini110 – 18071PAS
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1023 – 109371Interaction with CREBBP
Add
BLAST
Regioni1097 – 1304208Acetyltransferase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi685 – 6895LXXLL motif 1
Motifi738 – 7425LXXLL motif 2
Motifi1057 – 10615LXXLL motif 3

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi505 – 671167Ser-rich
Add
BLAST
Compositional biasi976 – 9805Poly-Gln
Compositional biasi1248 – 127831Poly-Gln
Add
BLAST
Compositional biasi1392 – 141726Met-rich
Add
BLAST

Domaini

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).

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG315556.
HOVERGENiHBG052583.
InParanoidiQ9Y6Q9.
KOiK11256.
OMAiDGNIVFV.
OrthoDBiEOG72JWFB.
PhylomeDBiQ9Y6Q9.
TreeFamiTF332652.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProiIPR011598. 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]
PANTHERiPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF3. PTHR10684:SF3. 1 hit.
PfamiPF07469. DUF1518. 1 hit.
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 (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9Y6Q9-1) [UniParc]FASTAAdd to Basket

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

MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE     50
LISANLSDID NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV 100
SSTGQGVIDK DSLGPLLLQA LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE 150
DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG VSWTNETQRQ KSHTFNCRML 200
MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE DLQSCMICVA 250
RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC 300
IQRFFSLNDG QSWSQKRHYQ EAYLNGHAET PVYRFSLADG TIVTAQTKSK 350
LFRNPVTNDR HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG 400
MSMSPNQGLQ MPSSRAYGLA DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS 450
PSSYQNNNYG LNMSSPPHGS PGLAPNQQNI MISPRNRGSP KIASHQFSPV 500
AGVHSPMASS GNTGNHSFSS SSLSALQAIS EGVGTSLLST LSSPGPKLDN 550
SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR DHLSDKESKE 600
SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS 650
VSVTSPSGVS SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK 700
ITAEATGKDT SSITSCGDGN VVKQEQLSPK KKENNALLRY LLDRDDPSDA 750
LSKELQPQVE GVDNKMSQCT SSTIPSSSQE KDPKIKTETS EEGSGDLDNL 800
DAILGDLTSS DFYNNSISSN GSHLGTKQQV FQGTNSLGLK SSQSVQSIRP 850
PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR MMDSQENYGS 900
SMGGPNRNVT VTQTPSSGDW GLPNSKAGRM EPMNSNSMGR PGGDYNTSLP 950
RPALGGSIPT LPLRSNSIPG ARPVLQQQQQ MLQMRPGEIP MGMGANPYGQ 1000
AAASNQLGSW PDGMLSMEQV SHGTQNRPLL RNSLDDLVGP PSNLEGQSDE 1050
RALLDQLHTL LSNTDATGLE EIDRALGIPE LVNQGQALEP KQDAFQGQEA 1100
AVMMDQKAGL YGQTYPAQGP PMQGGFHLQG QSPSFNSMMN QMNQQGNFPL 1150
QGMHPRANIM RPRTNTPKQL RMQLQQRLQG QQFLNQSRQA LELKMENPTA 1200
GGAAVMRPMM QPQVSSQQGF LNAQMVAQRS RELLSHHFRQ QRVAMMMQQQ 1250
QQQQQQQQQQ QQQQQQQQQQ QQQQQQTQAF SPPPNVTASP SMDGLLAGPT 1300
MPQAPPQQFP YQPNYGMGQQ PDPAFGRVSS PPNAMMSSRM GPSQNPMMQH 1350
PQAASIYQSS EMKGWPSGNL ARNSSFSQQQ FAHQGNPAVY SMVHMNGSSG 1400
HMGQMNMNPM PMSGMPMGPD QKYC 1424
Length:1,424
Mass (Da):155,293
Last modified:November 1, 1999 - v1
Checksum:i732CDF0423161679
GO
Isoform 2 (identifier: Q9Y6Q9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     903-917: Missing.

Show »
Length:1,409
Mass (Da):153,797
Checksum:i04B4DF09150BD916
GO
Isoform 3 (identifier: Q9Y6Q9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: E → EVTSDGIFSPT
     903-917: Missing.
     1214-1217: Missing.

Show »
Length:1,415
Mass (Da):154,400
Checksum:i4A162AB05BA34062
GO
Isoform 4 (identifier: Q9Y6Q9-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,350
Mass (Da):147,499
Checksum:iF75584B329A892C4
GO
Isoform 5 (identifier: Q9Y6Q9-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,420
Mass (Da):154,892
Checksum:i654343CEA0855C60
GO

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti218 – 2181R → C.1 Publication
Corresponds to variant rs6094752 [ dbSNP | Ensembl ].
VAR_053527
Natural varianti220 – 2201R → I.1 Publication
VAR_060695
Natural varianti369 – 3691L → F.
Corresponds to variant rs6094756 [ dbSNP | Ensembl ].
VAR_053528
Natural varianti460 – 4601G → R.
Corresponds to variant rs1052765 [ dbSNP | Ensembl ].
VAR_013831
Natural varianti556 – 5561I → V.1 Publication
Corresponds to variant rs72645272 [ dbSNP | Ensembl ].
VAR_060696
Natural varianti559 – 5591P → S.1 Publication
Corresponds to variant rs2230781 [ dbSNP | Ensembl ].
VAR_013832
Natural varianti586 – 5861Q → H.1 Publication
Corresponds to variant rs2230782 [ dbSNP | Ensembl ].
VAR_013833
Natural varianti777 – 7771S → A.1 Publication
Corresponds to variant rs2230783 [ dbSNP | Ensembl ].
VAR_053529
Natural varianti1247 – 12471M → K.1 Publication
VAR_060697
Natural varianti1247 – 12471M → L.1 Publication
VAR_060698
Natural varianti1248 – 12503Missing.
VAR_013834

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei321 – 3211E → EVTSDGIFSPT in isoform 3 and isoform 4.
VSP_003405
Alternative sequencei837 – 90165Missing in isoform 4.
VSP_003406Add
BLAST
Alternative sequencei903 – 91715Missing in isoform 2, isoform 3 and isoform 4.
VSP_003407Add
BLAST
Alternative sequencei1214 – 12174Missing in isoform 3, isoform 4 and isoform 5.
VSP_003408

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1322DG → EA in AAC51663. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13406.1. [Q9Y6Q9-5]
CCDS13407.1. [Q9Y6Q9-1]
CCDS54472.1. [Q9Y6Q9-3]
PIRiT03851.
RefSeqiNP_001167559.1. NM_001174088.1. [Q9Y6Q9-3]
NP_006525.2. NM_006534.3. [Q9Y6Q9-5]
NP_858045.1. NM_181659.2. [Q9Y6Q9-1]
UniGeneiHs.592142.

Genome annotation databases

EnsembliENST00000371997; ENSP00000361065; ENSG00000124151. [Q9Y6Q9-3]
ENST00000371998; ENSP00000361066; ENSG00000124151. [Q9Y6Q9-1]
ENST00000372004; ENSP00000361073; ENSG00000124151. [Q9Y6Q9-5]
GeneIDi8202.
KEGGihsa:8202.
UCSCiuc002xtk.3. human. [Q9Y6Q9-1]
uc002xtl.3. human. [Q9Y6Q9-5]
uc010ght.2. human. [Q9Y6Q9-3]

Polymorphism databases

DMDMi23396777.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13406.1. [Q9Y6Q9-5 ]
CCDS13407.1. [Q9Y6Q9-1 ]
CCDS54472.1. [Q9Y6Q9-3 ]
PIRi T03851.
RefSeqi NP_001167559.1. NM_001174088.1. [Q9Y6Q9-3 ]
NP_006525.2. NM_006534.3. [Q9Y6Q9-5 ]
NP_858045.1. NM_181659.2. [Q9Y6Q9-1 ]
UniGenei Hs.592142.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KBH NMR - A 1045-1091 [» ]
3L3X X-ray 1.55 B 618-629 [» ]
3L3Z X-ray 2.00 B 735-746 [» ]
DisProti DP00343.
ProteinModelPortali Q9Y6Q9.
SMRi Q9Y6Q9. Positions 34-367, 1045-1091.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113841. 99 interactions.
DIPi DIP-30876N.
IntActi Q9Y6Q9. 43 interactions.
MINTi MINT-231818.

Chemistry

BindingDBi Q9Y6Q9.
ChEMBLi CHEMBL2095161.

PTM databases

PhosphoSitei Q9Y6Q9.

Polymorphism databases

DMDMi 23396777.

Proteomic databases

MaxQBi Q9Y6Q9.
PaxDbi Q9Y6Q9.
PRIDEi Q9Y6Q9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371997 ; ENSP00000361065 ; ENSG00000124151 . [Q9Y6Q9-3 ]
ENST00000371998 ; ENSP00000361066 ; ENSG00000124151 . [Q9Y6Q9-1 ]
ENST00000372004 ; ENSP00000361073 ; ENSG00000124151 . [Q9Y6Q9-5 ]
GeneIDi 8202.
KEGGi hsa:8202.
UCSCi uc002xtk.3. human. [Q9Y6Q9-1 ]
uc002xtl.3. human. [Q9Y6Q9-5 ]
uc010ght.2. human. [Q9Y6Q9-3 ]

Organism-specific databases

CTDi 8202.
GeneCardsi GC20P046130.
HGNCi HGNC:7670. NCOA3.
HPAi CAB009800.
HPA024210.
MIMi 601937. gene.
neXtProti NX_Q9Y6Q9.
PharmGKBi PA31472.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG315556.
HOVERGENi HBG052583.
InParanoidi Q9Y6Q9.
KOi K11256.
OMAi DGNIVFV.
OrthoDBi EOG72JWFB.
PhylomeDBi Q9Y6Q9.
TreeFami TF332652.

Enzyme and pathway databases

Reactomei REACT_116145. PPARA activates gene expression.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki Q9Y6Q9.

Miscellaneous databases

ChiTaRSi NCOA3. human.
EvolutionaryTracei Q9Y6Q9.
GeneWikii Nuclear_receptor_coactivator_3.
GenomeRNAii 8202.
NextBioi 30907.
PROi Q9Y6Q9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y6Q9.
Bgeei Q9Y6Q9.
CleanExi HS_NCOA3.
HS_RAC3.
HS_TRAM1.
Genevestigatori Q9Y6Q9.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProi IPR011598. 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 ]
PANTHERi PTHR10684. PTHR10684. 1 hit.
PTHR10684:SF3. PTHR10684:SF3. 1 hit.
Pfami PF07469. DUF1518. 1 hit.
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. "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. 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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNCOA3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6Q9
Secondary accession number(s): A4LAZ5
, Q0VF45, Q5JYD9, Q5JYE0, Q9BR49, Q9UPC9, Q9UPG4, Q9UPG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 159 of the entry and version 1 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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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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