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Protein

Nuclear receptor coactivator 3

Gene

Ncoa3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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, probably 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 (By similarity).By similarity

Catalytic activityi

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

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 (By similarity).By similarity

GO - Molecular functioni

  • androgen receptor binding Source: RGD
  • estrogen receptor binding Source: RGD
  • histone acetyltransferase activity Source: UniProtKB-EC
  • ligand-dependent nuclear receptor binding Source: GO_Central
  • ligand-dependent nuclear receptor transcription coactivator activity Source: RGD
  • peroxisome proliferator activated receptor binding Source: RGD
  • protein complex binding Source: RGD
  • RNA polymerase II regulatory region DNA binding Source: RGD

GO - Biological processi

  • male gonad development Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • positive regulation of cell growth Source: RGD
  • positive regulation of intracellular estrogen receptor signaling pathway Source: RGD
  • positive regulation of intracellular steroid hormone receptor signaling pathway Source: RGD
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor coactivator 3 (EC:2.3.1.48)
Short name:
NCoA-3
Alternative name(s):
Amplified in breast cancer-1 protein homolog
Short name:
AIB-1
Gene namesi
Name:Ncoa3
Synonyms:Aib1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620109. Ncoa3.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • Golgi apparatus Source: RGD
  • nucleus Source: RGD
  • perinuclear region of cytoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000094408‹1 – 1082Nuclear receptor coactivator 3Add BLAST›1082

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei251PhosphoserineBy similarity1
Modified residuei269PhosphoserineBy similarity1
Modified residuei316N6-acetyllysine; by CREBBPBy similarity1
Modified residuei319N6-acetyllysine; by CREBBPBy similarity1
Modified residuei320N6-acetyllysine; by CREBBPBy similarity1
Modified residuei387N6-acetyllysineBy similarity1
Modified residuei394PhosphoserineBy similarity1
Modified residuei427PhosphoserineBy similarity1
Modified residuei551PhosphoserineBy similarity1
Modified residuei554PhosphoserineBy similarity1
Modified residuei722PhosphoserineBy similarity1
Modified residuei860Asymmetric dimethylarginineBy similarity1
Modified residuei866Asymmetric dimethylarginineBy similarity1
Modified residuei877Asymmetric dimethylarginineBy similarity1
Modified residuei988PhosphoserineBy similarity1

Post-translational modificationi

Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function (By similarity).By similarity
Methylated by CARM1.By similarity
Phosphorylated by IKK complex. Regulated its function (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ9EPU2.
PRIDEiQ9EPU2.

PTM databases

iPTMnetiQ9EPU2.
PhosphoSitePlusiQ9EPU2.

Expressioni

Tissue specificityi

Expressed constitutively in uterus.1 Publication

Interactioni

Subunit structurei

Present in a complex containing NCOA2, IKKA, IKKB, IKBKG and the histone acetyltransferase protein CREBBP. Interacts with PCAF and CARM1. Interacts with CASP8AP2 and NR3C1 (By similarity). Interacts with ATAD2 and this interaction is enhanced by estradiol (By similarity). Interacts with PSMB9. Binds to CSNK1D (By similarity). Found in a complex containing NCOA3, AR and MAK. Interacts with DDX5. Interacts with NPAS2 (By similarity). Interacts with NR4A3 (By similarity).By similarity

GO - Molecular functioni

  • androgen receptor binding Source: RGD
  • estrogen receptor binding Source: RGD
  • ligand-dependent nuclear receptor binding Source: GO_Central
  • peroxisome proliferator activated receptor binding Source: RGD
  • protein complex binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059144.

Structurei

3D structure databases

ProteinModelPortaliQ9EPU2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni712 – 782Interaction with CREBBPBy similarityAdd BLAST71
Regioni786 – 962AcetyltransferaseAdd BLAST177

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi385 – 389LXXLL motif 15
Motifi437 – 441LXXLL motif 25
Motifi723 – 727LXXLL motif 35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi136 – 371Ser-richAdd BLAST236
Compositional biasi773 – 936Gln-richAdd BLAST164

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) (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3561. Eukaryota.
ENOG410XRJI. LUCA.
HOGENOMiHOG000230947.
HOVERGENiHBG052583.
InParanoidiQ9EPU2.
PhylomeDBiQ9EPU2.

Family and domain databases

Gene3Di4.10.630.10. 2 hits.
InterProiIPR010011. DUF1518.
IPR032565. DUF4927.
IPR028818. NCOA3.
IPR009110. Nuc_rcpt_coact.
IPR014920. Nuc_rcpt_coact_Ncoa-typ.
IPR017426. Nuclear_rcpt_coactivator.
IPR000014. PAS.
IPR014935. SRC-1.
IPR008955. Src1_rcpt_coact.
[Graphical view]
PANTHERiPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF3. PTHR10684:SF3. 1 hit.
PfamiPF07469. DUF1518. 1 hit.
PF16279. DUF4927. 1 hit.
PF08815. Nuc_rec_co-act. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
SMARTiSM01151. DUF1518. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
SSF69125. SSF69125. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q9EPU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
IIRRCIQRFF SLNDGQSWSQ KRHYQEAYIH GHAETPVYRF SLADGTIVSA
60 70 80 90 100
QTKSKLFRNP VTNDRHGFVS THFLQREQNG CRPNPILQDK GIRPPAAGCG
110 120 130 140 150
MSLSPSQSVQ MLGSRTYGVA DPSNTGQMAG ARYGASSSVA SLTPGQSLQS
160 170 180 190 200
PSSYQSNSYG LNMSSPPHGS PGLGPNQQNI MISPRNRGSP KMASHQFSPA
210 220 230 240 250
AGVHSPMGSS GNTGSHSFSS SSLSALQAIS EGVGTSLLST LSSPGPKLDN
260 270 280 290 300
SPNMNINQPS KASSQDSKSP LGLYCEQNPV ESSVCPSNSR DPPVTKENKE
310 320 330 340 350
NSGEASETPR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSNCKDSS
360 370 380 390 400
ISVTSPSGVS SSTSGAVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK
410 420 430 440 450
ITAEATGKDT SSTASGGEGS VXQEQLSPXK KENNALLRYL LDRDDPSDVL
460 470 480 490 500
AKELQPQADG GDSKLSQCSC XTNPSSGQEK DPKIKTEEVS GDLDNLDAIL
510 520 530 540 550
GDLTSSDFYN SPTNGSHPGA KQQMFAGPSS LGLRSPQPVQ SVRPPYNRAL
560 570 580 590 600
SLDSPVSVGS VPPVKNVSAF PVLPKQPILA GNPRMMDSQE NYGANMGGPN
610 620 630 640 650
RNVPVNPTSS SGDWGLANSR ASRMEPLASS PLGRAGGDYS AALPRPALGS
660 670 680 690 700
SGPTLPLRSN RLPGARPTLM LQMRAGEVPM GMGVSPYSPA VPSNQPGSWP
710 720 730 740 750
EGMLSMEQGP HGAQNRPLLR NSLDELLGPP SNPEGQSDER ALLDQLHTLL
760 770 780 790 800
SNTDATGLEE IDRALGIPEL VSQGQALESK QDVFQGQEAA VMMDQKAALY
810 820 830 840 850
GQTYPAQGPP LQGGFHLQGQ SPSLNSMMSQ ISQQGSFPLQ GLHPRASMVR
860 870 880 890 900
PRTNTPKQLR MQLQQRLQGQ QFLNQSRQAL EMKMESPTGA AVMRPMLQSQ
910 920 930 940 950
QAFFNAQMAA QQKRELMNHH LQQQRMAMMM SQPQPQAFSP PPNVTASPSM
960 970 980 990 1000
DGVLAGSAMP QAPPQQFPYA TNYGMGQPPE PAFGRGSSPP SAMMSSRMGP
1010 1020 1030 1040 1050
SQNAMVQHPQ TAPMYQSSEM KGWPSGNLAR NGSFPQQQFA PQANPAAYNM
1060 1070 1080
VHMNSSGSHL GQMTMTPMPM SGMPMGPDQK YC
Length:1,082
Mass (Da):115,134
Last modified:March 1, 2001 - v1
Checksum:iBA35D946CBC8C080
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322224 mRNA. Translation: AAG42837.1.
UniGeneiRn.20691.

Genome annotation databases

UCSCiRGD:620109. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322224 mRNA. Translation: AAG42837.1.
UniGeneiRn.20691.

3D structure databases

ProteinModelPortaliQ9EPU2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059144.

PTM databases

iPTMnetiQ9EPU2.
PhosphoSitePlusiQ9EPU2.

Proteomic databases

PaxDbiQ9EPU2.
PRIDEiQ9EPU2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:620109. rat.

Organism-specific databases

RGDi620109. Ncoa3.

Phylogenomic databases

eggNOGiKOG3561. Eukaryota.
ENOG410XRJI. LUCA.
HOGENOMiHOG000230947.
HOVERGENiHBG052583.
InParanoidiQ9EPU2.
PhylomeDBiQ9EPU2.

Family and domain databases

Gene3Di4.10.630.10. 2 hits.
InterProiIPR010011. DUF1518.
IPR032565. DUF4927.
IPR028818. NCOA3.
IPR009110. Nuc_rcpt_coact.
IPR014920. Nuc_rcpt_coact_Ncoa-typ.
IPR017426. Nuclear_rcpt_coactivator.
IPR000014. PAS.
IPR014935. SRC-1.
IPR008955. Src1_rcpt_coact.
[Graphical view]
PANTHERiPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF3. PTHR10684:SF3. 1 hit.
PfamiPF07469. DUF1518. 1 hit.
PF16279. DUF4927. 1 hit.
PF08815. Nuc_rec_co-act. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
SMARTiSM01151. DUF1518. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
SSF69125. SSF69125. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNCOA3_RAT
AccessioniPrimary (citable) accession number: Q9EPU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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