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Protein

Nuclear receptor coactivator 2

Gene

Ncoa2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. Critical regulator of glucose metabolism regulation, acts as RORA coactivator to specifically modulate G6PC expression. Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the circadian clock by acting as a transcriptional coactivator for the CLOCK-ARNTL/BMAL1 heterodimer.By similarity

GO - Molecular functioni

  • DNA polymerase binding Source: RGD
  • estrogen receptor binding Source: RGD
  • glucocorticoid receptor binding Source: RGD
  • histone acetyltransferase activity Source: InterPro
  • ligand-dependent nuclear receptor binding Source: RGD
  • ligand-dependent nuclear receptor transcription coactivator activity Source: InterPro
  • PDZ domain binding Source: RGD
  • progesterone receptor binding Source: RGD
  • protein complex binding Source: RGD
  • retinoic acid receptor binding Source: RGD
  • retinoid X receptor binding Source: RGD
  • thyroid hormone receptor binding Source: RGD
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • cerebellum development Source: RGD
  • circadian regulation of gene expression Source: UniProtKB
  • male gonad development Source: RGD
  • positive regulation of female receptivity Source: RGD
  • positive regulation of glucocorticoid receptor signaling pathway 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

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor coactivator 2
Short name:
NCoA-2
Alternative name(s):
Transcriptional intermediary factor 2
Gene namesi
Name:Ncoa2
Synonyms:Tif2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620108. Ncoa2.

Subcellular locationi

GO - Cellular componenti

  • dendrite Source: RGD
  • dendritic spine Source: RGD
  • Golgi apparatus Source: RGD
  • microtubule Source: RGD
  • neuronal cell body Source: RGD
  • nucleus Source: RGD
  • postsynaptic density Source: RGD
  • presynaptic active zone Source: RGD
  • rough endoplasmic reticulum Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 14651464Nuclear receptor coactivator 2PRO_0000094404Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei396 – 3961PhosphoserineCombined sources
Modified residuei487 – 4871PhosphoserineBy similarity
Modified residuei493 – 4931PhosphoserineCombined sources
Modified residuei499 – 4991PhosphoserineCombined sources
Modified residuei554 – 5541PhosphoserineBy similarity
Modified residuei565 – 5651PhosphoserineBy similarity
Modified residuei636 – 6361N6-acetyllysineBy similarity
Modified residuei640 – 6401N6-acetyllysineBy similarity
Modified residuei699 – 6991PhosphoserineCombined sources
Modified residuei771 – 7711PhosphoserineBy similarity
Modified residuei780 – 7801N6-acetyllysineBy similarity
Modified residuei785 – 7851N6-acetyllysine; alternateBy similarity
Cross-linki785 – 785Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9WUI9.
PRIDEiQ9WUI9.

PTM databases

iPTMnetiQ9WUI9.
PhosphoSiteiQ9WUI9.

Interactioni

Subunit structurei

Present in a complex containing NCOA3, IKKA, IKKB, IKBKG and CREBBP. Interacts (via C-terminus) with CREBBP. Interacts with ESR1, HIF1A, NCOA1, APEX, NR3C1, NR3C2, CARM1, RARA, and RXRA. Present in a complex containing CARM1 and EP300/P300. Interacts with CASP8AP2 and TTLL5/STAMP. Interacts with PSMB9 and DDX5. Interacts (via LXXLL 1, 2 and 3 motifs) with RORA and RORC (via AF-2 motif). Interacts with RWDD3. Interacts with CLOCK and ARNTL/BMAL1. Interacts with NR4A3; potentiates the activity of the NR4A3 (By similarity).By similarity

GO - Molecular functioni

  • DNA polymerase binding Source: RGD
  • estrogen receptor binding Source: RGD
  • glucocorticoid receptor binding Source: RGD
  • ligand-dependent nuclear receptor binding Source: RGD
  • PDZ domain binding Source: RGD
  • progesterone receptor binding Source: RGD
  • protein complex binding Source: RGD
  • retinoic acid receptor binding Source: RGD
  • retinoid X receptor binding Source: RGD
  • thyroid hormone receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011026.

Structurei

Secondary structure

1
1465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi689 – 6957Combined sources
Helixi744 – 7485Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XLSX-ray2.96I/J/K/L/M/N/O/P740-756[»]
3HLVX-ray3.00C/D686-698[»]
3HM1X-ray2.33C/D686-698[»]
3L03X-ray1.90C/D686-698[»]
ProteinModelPortaliQ9WUI9.
SMRiQ9WUI9. Positions 1071-1115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WUI9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 8358bHLHPROSITE-ProRule annotationAdd
BLAST
Domaini119 – 18365PASPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni691 – 74353CASP8AP2-bindingAdd
BLAST
Regioni730 – 1121392Interaction with ARNTLBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi641 – 6455LXXLL motif 1
Motifi690 – 6945LXXLL motif 2
Motifi745 – 7495LXXLL motif 3
Motifi878 – 8825LXXLL motif 4
Motifi1079 – 10879LLXXLXXXL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1254 – 12607Poly-Gln

Domaini

Contains four Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL motifs are essential for the association with nuclear receptors and are, at least in part, functionally redundant (By similarity).By similarity
The LLXXLXXXL motif is involved in transcriptional coactivation and CREBBP/CBP binding.By similarity

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IQ5S. Eukaryota.
ENOG410XPF9. LUCA.
HOGENOMiHOG000230947.
HOVERGENiHBG052583.
InParanoidiQ9WUI9.
KOiK11255.
PhylomeDBiQ9WUI9.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProiIPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR032565. DUF4927.
IPR028822. NCOA2.
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. 2 hits.
PTHR10684:SF2. PTHR10684:SF2. 2 hits.
PfamiPF07469. DUF1518. 1 hit.
PF16279. DUF4927. 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.
SMARTiSM01151. DUF1518. 1 hit.
SM00353. 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]

Sequencei

Sequence statusi: Complete.

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

Q9WUI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRSTEKRNRE QENKYIEELA
60 70 80 90 100
ELIFANFNDI DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS
110 120 130 140 150
DVSSTGQGVI DKDALGPMML EALDGFFFVV NLEGNVVFVS ENVTQYLRYN
160 170 180 190 200
QEELMNKSVY SILHVGDHTE FVKNLLPKSM VNGGSWTGEP PRRNSHTFNC
210 220 230 240 250
RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE EGEDKQSCLI
260 270 280 290 300
CVARRVPMKE RPALPSSESF TTRQDLQGKI TFLDTSTMRD AMKPGWEDLV
310 320 330 340 350
RRCIQKFHTQ HEGESLSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ
360 370 380 390 400
TKSKLIRSQT TNEPQLVISI HMLHREQNVC VMNPDLTGQA MGKPLSPMSS
410 420 430 440 450
SSPARQAMCS GNPGQDVALG SNMNFPMNGP REQMSMPMGR FGGSGGMNHV
460 470 480 490 500
SGMQATTPQG SNYALKMNSP SQSSPGLNPG QPSSVLSPRH RMSPGVAGSP
510 520 530 540 550
RVPPSQFSPA GSLHSPAGVC SSTGNSHSYT NSSLNALQAL SEGHGVSLGP
560 570 580 590 600
SLASPDLKMG NSQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA
610 620 630 640 650
QASCHPEEQK RPNDSSMPQA ASEDRAEGHS RLHESKGQTK LLQLLTTKSD
660 670 680 690 700
QMEPSPLPSS LSDTNKDSTG SLPGPGSTHG TSLKEKHKIL HRLLQDSSSP
710 720 730 740 750
VDLAKLTAEA TGKELNQESS GTAPGSEVTV KQEPASPKKK ENALLRYLLD
760 770 780 790 800
KDDTKDIGLP EITPKLERLD SKTDPASNTK LIAMKTVKEE VSFEPSDQPG
810 820 830 840 850
SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP TGSVDKQAII NDLMQLTADS
860 870 880 890 900
SPVTPVGAQK AALRMSQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG
910 920 930 940 950
PFPPIRNSSP YSVIPQPGMM GNQGMLGSQG NLGNNSTGMI GSSTSRSSMP
960 970 980 990 1000
SGEWAPQSPA VRVTCAATTG AMNRPIQGGM IRNPTASIPM RANSQPGQRQ
1010 1020 1030 1040 1050
MLQPQVMNIG PSELEMNMGG PQYNQQQAPP NQTAPWPESI LPIDQASFGS
1060 1070 1080 1090 1100
QNRHPFGSSP DDLLCPHPAA ESPSDEGALL DQLYLALRNF DGLEEIDRAL
1110 1120 1130 1140 1150
GIPELVSQSQ AVDPEQFSSQ ESSMMLEQKP PVFPQQYASQ TQMAQGSYNP
1160 1170 1180 1190 1200
MQDPNFHTMG QRPNYTTLRM QPRPGLRPTG IVQNQPNQLR LQLQHRLQAQ
1210 1220 1230 1240 1250
QNRQPLMNQI SGVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR
1260 1270 1280 1290 1300
QMHQQQQVQQ RTLMMRGQGL NMTPSMVAPT GLPAAMSNPR IPQANAQQFP
1310 1320 1330 1340 1350
FPPNYGISQQ PDPGFTGATT PQSPLMSPRM AHTQSPMMQQ SQANPAYQPA
1360 1370 1380 1390 1400
SDINGWAQGS MGGNSMFSQQ SPPHFGQQAN TSMYNNNMNI NVSMATNTAG
1410 1420 1430 1440 1450
LSNMNQMTGQ MSMTSVTSVP TSGLSSMGPE QVNDPALRGS SLFTTNQLPG
1460
MDMIKQEGDG SRKYC
Length:1,465
Mass (Da):159,436
Last modified:November 1, 1999 - v1
Checksum:i36625B573EB0B39C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136943 mRNA. Translation: AAD24587.1.
RefSeqiNP_114010.1. NM_031822.1.
UniGeneiRn.49136.

Genome annotation databases

GeneIDi83724.
KEGGirno:83724.
UCSCiRGD:620108. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136943 mRNA. Translation: AAD24587.1.
RefSeqiNP_114010.1. NM_031822.1.
UniGeneiRn.49136.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XLSX-ray2.96I/J/K/L/M/N/O/P740-756[»]
3HLVX-ray3.00C/D686-698[»]
3HM1X-ray2.33C/D686-698[»]
3L03X-ray1.90C/D686-698[»]
ProteinModelPortaliQ9WUI9.
SMRiQ9WUI9. Positions 1071-1115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011026.

PTM databases

iPTMnetiQ9WUI9.
PhosphoSiteiQ9WUI9.

Proteomic databases

PaxDbiQ9WUI9.
PRIDEiQ9WUI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83724.
KEGGirno:83724.
UCSCiRGD:620108. rat.

Organism-specific databases

CTDi10499.
RGDi620108. Ncoa2.

Phylogenomic databases

eggNOGiENOG410IQ5S. Eukaryota.
ENOG410XPF9. LUCA.
HOGENOMiHOG000230947.
HOVERGENiHBG052583.
InParanoidiQ9WUI9.
KOiK11255.
PhylomeDBiQ9WUI9.

Miscellaneous databases

EvolutionaryTraceiQ9WUI9.
NextBioi616305.
PROiQ9WUI9.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProiIPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR032565. DUF4927.
IPR028822. NCOA2.
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. 2 hits.
PTHR10684:SF2. PTHR10684:SF2. 2 hits.
PfamiPF07469. DUF1518. 1 hit.
PF16279. DUF4927. 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.
SMARTiSM01151. DUF1518. 1 hit.
SM00353. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mechanistic principles in NR box-dependent interaction between nuclear hormone receptors and the coactivator TIF2."
    Leers J., Treuter E., Gustafsson J.-A.
    Mol. Cell. Biol. 18:6001-6013(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-493; SER-499 AND SER-699, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNCOA2_RAT
AccessioniPrimary (citable) accession number: Q9WUI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 125 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.