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Nuclear receptor coactivator 2 (NCoA-2) (Glucocorticoid receptor-interacting protein 1) (GRIP-1) (Steroid receptor coactivator 2) (SRC-2) (Transcriptional intermediary factor 2)

 NCOA2_MOUSE             Reviewed;        1462 AA.
Q61026; E9QMH9; O09001; P97759;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 177.
RecName: Full=Nuclear receptor coactivator 2;
Short=NCoA-2;
AltName: Full=Glucocorticoid receptor-interacting protein 1;
Short=GRIP-1;
AltName: Full=Steroid receptor coactivator 2;
Short=SRC-2;
AltName: Full=Transcriptional intermediary factor 2;
Name=Ncoa2; Synonyms=Grip1, Src2, Tif2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NR3C2.
STRAIN=ICR; TISSUE=Brain;
PubMed=9111344; DOI=10.1128/MCB.17.5.2735;
Hong H., Kohli K., Garabedian M.J., Stallcup M.R.;
"GRIP1, a transcriptional coactivator for the AF-2 transactivation
domain of steroid, thyroid, retinoid, and vitamin D receptors.";
Mol. Cell. Biol. 17:2735-2744(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9192892; DOI=10.1038/42652;
Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K.,
Rosenfeld M.G.;
"The transcriptional co-activator p/CIP binds CBP and mediates
nuclear-receptor function.";
Nature 387:677-684(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 322-1119.
STRAIN=ICR; TISSUE=Embryo;
PubMed=8643509; DOI=10.1073/pnas.93.10.4948;
Hong H., Kohli K., Trivedi A., Johnson D.L., Stallcup M.R.;
"GRIP1, a novel mouse protein that serves as a transcriptional
coactivator in yeast for the hormone binding domains of steroid
receptors.";
Proc. Natl. Acad. Sci. U.S.A. 93:4948-4952(1996).
[5]
INTERACTION WITH CARM1.
PubMed=10381882; DOI=10.1126/science.284.5423.2174;
Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T.,
Aswad D.W., Stallcup M.R.;
"Regulation of transcription by a protein methyltransferase.";
Science 284:2174-2177(1999).
[6]
FUNCTION.
PubMed=12507421; DOI=10.1016/S0092-8674(02)01169-8;
Picard F., Gehin M., Annicotte J.-S., Rocchi S., Champy M.-F.,
O'Malley B.W., Chambon P., Auwerx J.;
"SRC-1 and TIF2 control energy balance between white and brown adipose
tissues.";
Cell 111:931-941(2002).
[7]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH EP300 AND NCOA2.
PubMed=11997499; DOI=10.1128/MCB.22.11.3621-3632.2002;
Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.;
"Synergy among nuclear receptor coactivators: selective requirement
for protein methyltransferase and acetyltransferase activities.";
Mol. Cell. Biol. 22:3621-3632(2002).
[8]
INTERACTION WITH CASP8AP2.
PubMed=12477726; DOI=10.1074/jbc.M209234200;
Kino T., Chrousos G.P.;
"Tumor necrosis factor alpha receptor- and Fas-associated FLASH
inhibit transcriptional activity of the glucocorticoid receptor by
binding to and interfering with its interaction with p160 type nuclear
receptor coactivators.";
J. Biol. Chem. 278:3023-3029(2003).
[9]
INTERACTION WITH NR4A3.
PubMed=12709428; DOI=10.1074/jbc.M300088200;
Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.;
"The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans-
activation, coactivator recruitment, and activation by the purine
anti-metabolite 6-mercaptopurine.";
J. Biol. Chem. 278:24776-24790(2003).
[10]
FUNCTION AS COACTIVATOR, INTERACTION WITH RORC, DOMAIN, AND
MUTAGENESIS OF 644-L-L-645; 689-L--L-694; 744-L--L-749.
PubMed=16148126; DOI=10.4049/jimmunol.175.6.3800;
Xie H., Sadim M.S., Sun Z.;
"RORgammat recruits steroid receptor coactivators to ensure thymocyte
survival.";
J. Immunol. 175:3800-3809(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
FUNCTION IN GLUCOSE METABOLISM REGULATION, INTERACTION WITH RORA, AND
DISRUPTION PHENOTYPE.
PubMed=19039140; DOI=10.1126/science.1164847;
Chopra A.R., Louet J.F., Saha P., An J., Demayo F., Xu J., York B.,
Karpen S., Finegold M., Moore D., Chan L., Newgard C.B.,
O'Malley B.W.;
"Absence of the SRC-2 coactivator results in a glycogenopathy
resembling Von Gierke's disease.";
Science 322:1395-1399(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493; SER-699 AND
SER-771, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487; SER-565 AND
SER-699, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
INTERACTS WITH RORA AND RORC.
PubMed=21499262; DOI=10.1038/nature10075;
Solt L.A., Kumar N., Nuhant P., Wang Y., Lauer J.L., Liu J.,
Istrate M.A., Kamenecka T.M., Roush W.R., Vidovic D., Schuerer S.C.,
Xu J., Wagoner G., Drew P.D., Griffin P.R., Burris T.P.;
"Suppression of TH17 differentiation and autoimmunity by a synthetic
ROR ligand.";
Nature 472:491-494(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-640; LYS-780 AND
LYS-785, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[18]
FUNCTION, INDUCTION, AND INTERACTION WITH CLOCK AND ARNTL.
PubMed=24529706; DOI=10.1016/j.celrep.2014.01.027;
Stashi E., Lanz R.B., Mao J., Michailidis G., Zhu B., Kettner N.M.,
Putluri N., Reineke E.L., Reineke L.C., Dasgupta S., Dean A.,
Stevenson C.R., Sivasubramanian N., Sreekumar A., Demayo F., York B.,
Fu L., O'Malley B.W.;
"SRC-2 is an essential coactivator for orchestrating metabolism and
circadian rhythm.";
Cell Rep. 6:633-645(2014).
[19]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-338; ARG-864; ARG-874;
ARG-1173; ARG-1177; ARG-1190; ARG-1203; ARG-1221 AND ARG-1240, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: 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 (PubMed:24529706).
{ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:12507421,
ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:19039140,
ECO:0000269|PubMed:24529706}.
-!- SUBUNIT: 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 (PubMed:12709428). {ECO:0000269|PubMed:10381882,
ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:12477726,
ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:16148126,
ECO:0000269|PubMed:19039140, ECO:0000269|PubMed:24529706,
ECO:0000269|PubMed:9111344}.
-!- INTERACTION:
Q4FZB7-1:KMT5B (xeno); NbExp=4; IntAct=EBI-688662, EBI-15746366;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- INDUCTION: Expressed in a circadian manner in the liver, brown
adipose tissue (BAT), white adipose tissue (WAT), heart, skeletal
muscle and suprachiasmatic nucleus (SCN) of the brain. Shows a
higher expression during the light phase compared with the dark
phase. {ECO:0000269|PubMed:24529706}.
-!- DOMAIN: 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
(PubMed:16148126). {ECO:0000269|PubMed:16148126}.
-!- DOMAIN: The LLXXLXXXL motif is involved in transcriptional
coactivation and CREBBP/CBP binding. {ECO:0000250}.
-!- DOMAIN: Contains 2 C-terminal transcription activation domains
(AD1 and AD2) that can function independently. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Animals show a glycogenopathy resembling to
Von Gierke's disease with impaired growth, fasting hypoglycemia,
and an increase in concentrations of triglycerides, cholesterol,
free fatty acids, ketone bodies, uric acid and lactic acid in the
plasma during fating. They also have increased liver glycogen
stores and hepatic steatosis. {ECO:0000269|PubMed:19039140}.
-!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB61575.1; Type=Frameshift; Positions=251, 256, 302, 321, 959, 964, 983; Evidence={ECO:0000305};
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EMBL; U39060; AAC53151.1; -; mRNA.
EMBL; AF000582; AAB61575.1; ALT_FRAME; mRNA.
EMBL; AC091248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS35515.1; -.
PIR; T30193; T30193.
PIR; T42639; T42639.
RefSeq; NP_032704.2; NM_008678.3.
RefSeq; XP_006495528.1; XM_006495465.3.
UniGene; Mm.2537; -.
PDB; 1L2I; X-ray; 1.95 A; C/D=686-698.
PDB; 1OSV; X-ray; 2.50 A; C/D/E=741-752.
PDB; 1WM0; X-ray; 2.90 A; Y=684-697.
PDB; 2Q6J; X-ray; 2.70 A; C/D=686-698.
PDB; 2QA6; X-ray; 2.60 A; C/D=686-698.
PDB; 2QA8; X-ray; 1.85 A; C/D=686-698.
PDB; 2QAB; X-ray; 1.89 A; C/D=686-698.
PDB; 2QGT; X-ray; 2.15 A; C/D=686-698.
PDB; 2QGW; X-ray; 2.39 A; C/D=686-698.
PDB; 2QH6; X-ray; 2.70 A; C/D=686-698.
PDB; 2QPY; X-ray; 2.50 A; B=744-753.
PDB; 2QR9; X-ray; 2.00 A; C/D=686-698.
PDB; 2QSE; X-ray; 1.85 A; C/D=686-698.
PDB; 2QXM; X-ray; 2.30 A; C/D=686-698.
PDB; 2QZO; X-ray; 1.72 A; C/D=686-698.
PDB; 3MNE; X-ray; 1.96 A; B=740-752.
PDB; 3MNO; X-ray; 1.55 A; B=740-752.
PDB; 3MNP; X-ray; 1.50 A; B=740-752.
PDBsum; 1L2I; -.
PDBsum; 1OSV; -.
PDBsum; 1WM0; -.
PDBsum; 2Q6J; -.
PDBsum; 2QA6; -.
PDBsum; 2QA8; -.
PDBsum; 2QAB; -.
PDBsum; 2QGT; -.
PDBsum; 2QGW; -.
PDBsum; 2QH6; -.
PDBsum; 2QPY; -.
PDBsum; 2QR9; -.
PDBsum; 2QSE; -.
PDBsum; 2QXM; -.
PDBsum; 2QZO; -.
PDBsum; 3MNE; -.
PDBsum; 3MNO; -.
PDBsum; 3MNP; -.
ProteinModelPortal; Q61026; -.
SMR; Q61026; -.
BioGrid; 201708; 13.
DIP; DIP-5979N; -.
IntAct; Q61026; 8.
MINT; MINT-236676; -.
STRING; 10090.ENSMUSP00000006037; -.
iPTMnet; Q61026; -.
PhosphoSitePlus; Q61026; -.
EPD; Q61026; -.
MaxQB; Q61026; -.
PaxDb; Q61026; -.
PRIDE; Q61026; -.
Ensembl; ENSMUST00000006037; ENSMUSP00000006037; ENSMUSG00000005886.
GeneID; 17978; -.
KEGG; mmu:17978; -.
UCSC; uc007aim.2; mouse.
CTD; 10499; -.
MGI; MGI:1276533; Ncoa2.
eggNOG; ENOG410IQ5S; Eukaryota.
eggNOG; ENOG410XPF9; LUCA.
GeneTree; ENSGT00530000063109; -.
HOGENOM; HOG000230947; -.
HOVERGEN; HBG052583; -.
InParanoid; Q61026; -.
KO; K11255; -.
OMA; PSDMNGW; -.
OrthoDB; EOG091G00US; -.
TreeFam; TF332652; -.
Reactome; R-MMU-159418; Recycling of bile acids and salts.
Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-MMU-211976; Endogenous sterols.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
EvolutionaryTrace; Q61026; -.
PRO; PR:Q61026; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000005886; -.
CleanEx; MM_GRIP1; -.
CleanEx; MM_NCOA2; -.
ExpressionAtlas; Q61026; baseline and differential.
Genevisible; Q61026; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; ISO:MGI.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:MGI.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0005102; F:receptor binding; IDA:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0030375; F:thyroid hormone receptor coactivator activity; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IDA:MGI.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; IBA:GO_Central.
GO; GO:0045475; P:locomotor rhythm; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 1.
Gene3D; 1.10.287.1070; -; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR010011; DUF1518.
InterPro; IPR032565; DUF4927.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR028822; NCOA2.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
InterPro; IPR017426; Nuclear_rcpt_coactivator.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
InterPro; IPR014935; SRC/p160_LXXLL.
PANTHER; PTHR10684; PTHR10684; 1.
PANTHER; PTHR10684:SF2; PTHR10684:SF2; 1.
Pfam; PF07469; DUF1518; 1.
Pfam; PF16279; DUF4927; 1.
Pfam; PF08815; Nuc_rec_co-act; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF08832; SRC-1; 1.
PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
SMART; SM01151; DUF1518; 1.
SMART; SM00353; HLH; 1.
SMART; SM00091; PAS; 1.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
SUPFAM; SSF69125; SSF69125; 1.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Biological rhythms;
Complete proteome; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q15596}.
CHAIN 2 1462 Nuclear receptor coactivator 2.
/FTId=PRO_0000094403.
DOMAIN 26 83 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 119 183 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
REGION 691 743 CASP8AP2-binding.
REGION 730 1121 Interaction with ARNTL.
{ECO:0000269|PubMed:24529706}.
MOTIF 641 645 LXXLL motif 1.
MOTIF 690 694 LXXLL motif 2.
MOTIF 745 749 LXXLL motif 3.
MOTIF 878 882 LXXLL motif 4.
MOTIF 1079 1087 LLXXLXXXL motif.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q15596}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:Q15596}.
MOD_RES 338 338 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 487 487 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000250|UniProtKB:Q15596}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000250|UniProtKB:Q15596}.
MOD_RES 565 565 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 636 636 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 640 640 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000250|UniProtKB:Q15596}.
MOD_RES 699 699 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000250|UniProtKB:Q15596}.
MOD_RES 771 771 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 780 780 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 785 785 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 864 864 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 874 874 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1173 1173 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1177 1177 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1190 1190 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1196 1196 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q15596}.
MOD_RES 1203 1203 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1221 1221 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1240 1240 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1259 1259 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q15596}.
MOD_RES 1264 1264 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q15596}.
CROSSLNK 239 239 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15596}.
CROSSLNK 648 648 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15596}.
CROSSLNK 705 705 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15596}.
CROSSLNK 731 731 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15596}.
CROSSLNK 785 785 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q15596}.
CROSSLNK 1452 1452 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q15596}.
MUTAGEN 644 645 LL->AA: Abolishes interaction with RORC;
when associated with 689-A--A-694 and
744-A--A-749.
{ECO:0000269|PubMed:16148126}.
MUTAGEN 689 694 ILHRLL->AAHRAA: Abolishes interaction
with RORC; when associated with 644-A-A-
645 and 744-A--A-749.
{ECO:0000269|PubMed:16148126}.
MUTAGEN 744 749 LLRYLL->AARAA: Abolishes interaction with
RORC; when associated with 644-A-A-645
and 689-A--A-694.
{ECO:0000269|PubMed:16148126}.
CONFLICT 51 51 E -> D (in Ref. 1; AAC53151).
{ECO:0000305}.
CONFLICT 140 141 SE -> FR (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 194 194 S -> T (in Ref. 1; AAC53151).
{ECO:0000305}.
CONFLICT 256 256 V -> I (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 286 286 S -> T (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 420 420 G -> S (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 512 512 S -> N (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 594 594 E -> K (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 607 608 EE -> KK (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 864 864 R -> C (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 869 869 T -> S (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 884 884 N -> Y (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 972 972 M -> K (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 980 980 M -> K (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 991 991 R -> G (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 996 996 P -> L (in Ref. 2; AAB61575).
{ECO:0000305}.
CONFLICT 1407 1407 G -> C (in Ref. 1; AAC53151).
{ECO:0000305}.
CONFLICT 1446 1446 P -> L (in Ref. 2; AAB61575).
{ECO:0000305}.
HELIX 689 694 {ECO:0000244|PDB:2QZO}.
HELIX 743 749 {ECO:0000244|PDB:3MNP}.
SEQUENCE 1462 AA; 158466 MW; 619462FF1ACC6067 CRC64;
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRSTEKRNRE QENKYIEELA ELIFANFNDI
DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML
EALDGFFFVV NLEGSVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSM
VNGGSWSGEP PRRSSHTFNC RMLVKPLPDS EEEGHDSQEA HQKYEAMQCF AVSQPKSIKE
EGEDLQSCLI CVARRVPMKE RPTLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV
RRCIQKFHTQ HEGESLSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT
TNEPQLVISL HMLHREQNVC VMNPDLTGQA MGKPLNPISS SSPAHQALCS GNPGQDMTLG
SNINFPMNGP KEQMGMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGMNPG
QASSVLSPRQ RMSPGVAGSP RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL
SEGHGVSLGS SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA
EASCHPEEQK GPNDSSMPQA ASGDRAEGHS RLHDSKGQTK LLQLLTTKSD QMEPSPLPSS
LSDTNKDSTG SLPGPGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKELSQESS
STAPGSEVTV KQEPASPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK
LIAMKTVKEE VSFEPSDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP TGSVDKQAII
NDLMQLTADS SPVPPAGAQK AALRMSQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG
PFPPIRNSSP YSVIPQPGMM GNQGMLGSQG NLGNNSTGMI GSSTSRPSMP SGEWAPQSPA
VRVTCAATTG AMNRPVQGGM IRNPTASIPM RANSQPGQRQ MLQSQVMNIG PSELEMNMGG
PQYNQQQAPP NQTAPWPESI LPIDQASFAS QNRQPFGSSP DDLLCPHPAA ESPSDEGALL
DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDAEQFSSQ ESSIMLEQKP PVFPQQYASQ
AQMAQGGYNP MQDPNFHTMG QRPNYTTLRM QPRPGLRPTG IVQNQPNQLR LQLQHRLQAQ
QNRQPLMNQI SSVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMQQQVQQRT
LMMRGQGLNV TPSMVAPAGL PAAMSNPRIP QANAQQFPFP PNYGISQQPD PGFTGATTPQ
SPLMSPRMAH TQSPMMQQSQ ANPAYQPTSD MNGWAQGSMG GNSMFSQQSP PHFGQQANTS
MYSNNMNISV SMATNTGGLS SMNQMTGQMS MTSVTSVPTS GLPSMGPEQV NDPALRGGNL
FPNQLPGMDM IKQEGDASRK YC


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