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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
  • signal transducer activity Source: InterPro

GO - Biological processi

  • cellular response to hormone stimulus Source: GO_Central
  • 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
ProteomesiUP000002494 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 1082›1082Nuclear receptor coactivator 3PRO_0000094408Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei251 – 2511PhosphoserineBy similarity
Modified residuei316 – 3161N6-acetyllysine; by CREBBPBy similarity
Modified residuei319 – 3191N6-acetyllysine; by CREBBPBy similarity
Modified residuei320 – 3201N6-acetyllysine; by CREBBPBy similarity
Modified residuei387 – 3871N6-acetyllysineBy similarity
Modified residuei427 – 4271PhosphoserineBy similarity
Modified residuei551 – 5511PhosphoserineBy similarity
Modified residuei554 – 5541PhosphoserineBy similarity

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

PhosphoSiteiQ9EPU2.

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).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059144.

Structurei

3D structure databases

ProteinModelPortaliQ9EPU2.
SMRiQ9EPU2. Positions 734-780.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni712 – 78271Interaction with CREBBPBy similarityAdd
BLAST
Regioni786 – 962177AcetyltransferaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi385 – 3895LXXLL motif 1
Motifi437 – 4415LXXLL motif 2
Motifi723 – 7275LXXLL motif 3

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi136 – 371236Ser-richAdd
BLAST
Compositional biasi773 – 936164Gln-richAdd
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) (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG315556.
HOGENOMiHOG000230947.
HOVERGENiHBG052583.
InParanoidiQ9EPU2.
PhylomeDBiQ9EPU2.

Family and domain databases

Gene3Di4.10.630.10. 2 hits.
InterProiIPR010011. DUF1518.
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.
PF08815. Nuc_rec_co-act. 1 hit.
PF08832. SRC-1. 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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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.
SMRiQ9EPU2. Positions 734-780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059144.

PTM databases

PhosphoSiteiQ9EPU2.

Proteomic databases

PaxDbiQ9EPU2.
PRIDEiQ9EPU2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:620109. rat.

Organism-specific databases

RGDi620109. Ncoa3.

Phylogenomic databases

eggNOGiNOG315556.
HOGENOMiHOG000230947.
HOVERGENiHBG052583.
InParanoidiQ9EPU2.
PhylomeDBiQ9EPU2.

Miscellaneous databases

PROiQ9EPU2.

Family and domain databases

Gene3Di4.10.630.10. 2 hits.
InterProiIPR010011. DUF1518.
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.
PF08815. Nuc_rec_co-act. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
SSF69125. SSF69125. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Expression of estrogen receptor coactivators in the rat uterus."
    Nephew K.P., Ray S., Hlaing M., Ahluwalia A., Wu S.D., Long X., Hyder S.M., Bigsby R.M.
    Biol. Reprod. 63:361-367(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.

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: June 24, 2015
This is version 104 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

External Data

Dasty 3

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 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.