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Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC RAP250) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (PRIP) (Thyroid hormone receptor-binding protein)

 NCOA6_HUMAN             Reviewed;        2063 AA.
Q14686; A6NLF1; B2RMN5; E1P5P7; Q9NTZ9; Q9UH74; Q9UK86;
12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
22-NOV-2017, entry version 162.
RecName: Full=Nuclear receptor coactivator 6;
AltName: Full=Activating signal cointegrator 2;
Short=ASC-2;
AltName: Full=Amplified in breast cancer protein 3;
AltName: Full=Cancer-amplified transcriptional coactivator ASC-2;
AltName: Full=Nuclear receptor coactivator RAP250;
Short=NRC RAP250;
AltName: Full=Nuclear receptor-activating protein, 250 kDa;
AltName: Full=Peroxisome proliferator-activated receptor-interacting protein;
Short=PPAR-interacting protein;
Short=PRIP;
AltName: Full=Thyroid hormone receptor-binding protein;
Name=NCOA6; Synonyms=AIB3, KIAA0181, RAP250, TRBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CREBBP; NCOA1; GTF2A;
TBP; RXRA; ESR1; RARA AND THRA, AND VARIANT SER-955.
PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y.,
Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D.,
Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional
coactivator essential for ligand-dependent transactivation by nuclear
receptors in vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, INTERACTION WITH CREBBP;
RXRA; ESR1; NR3C1; RARA; VDR AND THRA, AND VARIANT SER-955.
PubMed=10866662; DOI=10.1128/MCB.20.14.5048-5063.2000;
Mahajan M.A., Samuels H.H.;
"A new family of nuclear receptor coregulators that integrates nuclear
receptor signaling through CBP.";
Mol. Cell. Biol. 20:5048-5063(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PPARA; PPARG; ESR1; ESR2
AND THR, AND VARIANT SER-955.
TISSUE=Testis;
PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
"Cloning and characterization of RAP250, a nuclear receptor
coactivator.";
J. Biol. Chem. 275:5308-5317(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY PRKDC, INTERACTION WITH
THR; RAR; EP300 AND CRSP3, AND VARIANT SER-955.
TISSUE=Lymphocyte;
PubMed=10823961; DOI=10.1073/pnas.97.11.6212;
Ko L., Cardona G.R., Chin W.W.;
"Thyroid hormone receptor-binding protein, an LXXLL motif-containing
protein, functions as a general coactivator.";
Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-955.
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[6]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
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.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH NCOA6IP.
PubMed=11517327; DOI=10.1073/pnas.181347498;
Zhu Y.-J., Qi C., Cao W.-Q., Yeldandi A.V., Rao M.S., Reddy J.K.;
"Cloning and characterization of PIMT, a protein with a
methyltransferase domain, which interacts with and enhances nuclear
receptor coactivator PRIP function.";
Proc. Natl. Acad. Sci. U.S.A. 98:10380-10385(2001).
[11]
INTERACTION WITH RBM14.
PubMed=11443112; DOI=10.1074/jbc.M101517200;
Iwasaki T., Chin W.W., Ko L.;
"Identification and characterization of RRM-containing coactivator
activator (CoAA) as TRBP-interacting protein, and its splice variant
as a coactivator modulator (CoAM).";
J. Biol. Chem. 276:33375-33383(2001).
[12]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[13]
INTERACTION WITH ZNF335.
PubMed=12215545; DOI=10.1128/MCB.22.19.6883-6894.2002;
Mahajan M.A., Murray A., Samuels H.H.;
"NRC-interacting factor 1 is a novel cotransducer that interacts with
and regulates the activity of the nuclear hormone receptor coactivator
NRC.";
Mol. Cell. Biol. 22:6883-6894(2002).
[14]
IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
TISSUE=Cervix carcinoma;
PubMed=12482968; DOI=10.1128/MCB.23.1.140-149.2003;
Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J.,
Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G.,
Azorsa D.O., Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C.,
Lee J.W.;
"Activating signal cointegrator 2 belongs to a novel steady-state
complex that contains a subset of trithorax group proteins.";
Mol. Cell. Biol. 23:140-149(2003).
[15]
MUTAGENESIS OF 883-THR--GLU-894, AND PHOSPHORYLATION AT SER-884.
PubMed=11773444; DOI=10.1210/mend.16.1.0755;
Ko L., Cardona G.R., Iwasaki T., Bramlett K.S., Burris T.P.,
Chin W.W.;
"Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines
selectivity for ERs and TRs.";
Mol. Endocrinol. 16:128-140(2002).
[16]
IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
PubMed=17021013; DOI=10.1073/pnas.0607313103;
Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y.,
Lee S.K., Roeder R.G., Lee J.W.;
"Coactivator as a target gene specificity determinant for histone H3
lysine 4 methyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006).
[17]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MLL2/3
COMPLEX.
PubMed=17500065; DOI=10.1074/jbc.M701574200;
Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
methyltransferase complex.";
J. Biol. Chem. 282:20395-20406(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2018, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-95, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
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).
[21]
VARIANTS [LARGE SCALE ANALYSIS] SER-1060 AND ARG-1191.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
receptors and stimulates the transcriptional activities in a
hormone-dependent fashion. Coactivates expression in an
agonist- and AF2-dependent manner. Involved in the coactivation of
different nuclear receptors, such as for steroids (GR and ERs),
retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR)
and prostanoids (PPARs). Probably functions as a general
coactivator, rather than just a nuclear receptor coactivator. May
also be involved in the coactivation of the NF-kappa-B pathway.
May coactivate expression via a remodeling of chromatin and its
interaction with histone acetyltransferase proteins.
-!- SUBUNIT: Monomer and homodimer. Interacts with RBM39 (By
similarity). Interacts in vitro with the basal transcription
factors GTF2A and TBP, suggesting an autonomous transactivation
function. Interacts with NCOA1, CRSP3, RBM14, the histone
acetyltransferases EP300 and CREBBP, and with the
methyltransferases NCOA6IP and PRMT2/HRMT1L1. Component of the
MLL2/3 complex (also named ASCOM complex), at least composed of
KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A,
PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with
ZNF335; may enhance ligand-dependent transcriptional activation by
nuclear hormone receptors. {ECO:0000250,
ECO:0000269|PubMed:10567404, ECO:0000269|PubMed:10681503,
ECO:0000269|PubMed:10823961, ECO:0000269|PubMed:10866662,
ECO:0000269|PubMed:11443112, ECO:0000269|PubMed:11517327,
ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12215545,
ECO:0000269|PubMed:12482968, ECO:0000269|PubMed:17021013,
ECO:0000269|PubMed:17500065}.
-!- INTERACTION:
P10275:AR; NbExp=2; IntAct=EBI-78670, EBI-608057;
Q9UBL3:ASH2L; NbExp=13; IntAct=EBI-78670, EBI-540797;
Q92793:CREBBP; NbExp=2; IntAct=EBI-78670, EBI-81215;
Q9UMN6:KMT2B; NbExp=5; IntAct=EBI-78670, EBI-765774;
Q8NEZ4:KMT2C; NbExp=7; IntAct=EBI-78670, EBI-1042997;
P06400:RB1; NbExp=3; IntAct=EBI-78670, EBI-491274;
Q12888:TP53BP1; NbExp=3; IntAct=EBI-78670, EBI-396540;
Q12888-1:TP53BP1; NbExp=3; IntAct=EBI-78670, EBI-8022649;
P61964:WDR5; NbExp=7; IntAct=EBI-78670, EBI-540834;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain,
prostate, testis and ovary; weakly expressed in lung, thymus and
small intestine.
-!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Only
motif 1 is essential for the association with nuclear receptors,
while adjacent Ser-884 displays selectivity for nuclear receptors.
-!- PTM: Phosphorylated by PRKDC.
-!- PTM: Phosphorylation on Ser-884 leads to a strong decrease in
binding to ESR1 and ESR2. {ECO:0000269|PubMed:10823961,
ECO:0000269|PubMed:11773444}.
-!- MISCELLANEOUS: Frequently amplified or overexpressed in colon,
breast and lung cancers.
-!- SEQUENCE CAUTION:
Sequence=AAF16403.1; Type=Frameshift; Positions=88; Evidence={ECO:0000305};
Sequence=BAA11498.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF177388; AAF13595.1; -; mRNA.
EMBL; AF208227; AAF16403.1; ALT_FRAME; mRNA.
EMBL; AF245115; AAF78480.1; -; mRNA.
EMBL; AF128458; AAF37003.1; -; mRNA.
EMBL; AF171667; AAF71829.1; -; mRNA.
EMBL; D80003; BAA11498.2; ALT_INIT; mRNA.
EMBL; AL109824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW76254.1; -; Genomic_DNA.
EMBL; CH471077; EAW76255.1; -; Genomic_DNA.
EMBL; BC136272; AAI36273.1; -; mRNA.
CCDS; CCDS13241.1; -.
RefSeq; NP_001229468.1; NM_001242539.2.
RefSeq; NP_001305169.1; NM_001318240.1.
RefSeq; NP_054790.2; NM_014071.4.
UniGene; Hs.368971; -.
UniGene; Hs.736403; -.
ProteinModelPortal; Q14686; -.
SMR; Q14686; -.
BioGrid; 116691; 81.
CORUM; Q14686; -.
DIP; DIP-30934N; -.
IntAct; Q14686; 40.
MINT; MINT-1194462; -.
STRING; 9606.ENSP00000351894; -.
iPTMnet; Q14686; -.
PhosphoSitePlus; Q14686; -.
BioMuta; NCOA6; -.
DMDM; 116242672; -.
EPD; Q14686; -.
MaxQB; Q14686; -.
PaxDb; Q14686; -.
PeptideAtlas; Q14686; -.
PRIDE; Q14686; -.
Ensembl; ENST00000359003; ENSP00000351894; ENSG00000198646.
Ensembl; ENST00000374796; ENSP00000363929; ENSG00000198646.
GeneID; 23054; -.
KEGG; hsa:23054; -.
UCSC; uc002xav.3; human.
CTD; 23054; -.
DisGeNET; 23054; -.
EuPathDB; HostDB:ENSG00000198646.13; -.
GeneCards; NCOA6; -.
H-InvDB; HIX0015752; -.
HGNC; HGNC:15936; NCOA6.
HPA; HPA004198; -.
HPA; HPA050211; -.
MIM; 605299; gene.
neXtProt; NX_Q14686; -.
OpenTargets; ENSG00000198646; -.
PharmGKB; PA31475; -.
eggNOG; ENOG410IK20; Eukaryota.
eggNOG; ENOG410XW4F; LUCA.
GeneTree; ENSGT00730000111114; -.
HOVERGEN; HBG052586; -.
InParanoid; Q14686; -.
KO; K14971; -.
OMA; GMPKRLP; -.
OrthoDB; EOG091G00CR; -.
PhylomeDB; Q14686; -.
TreeFam; TF332639; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
ChiTaRS; NCOA6; human.
GeneWiki; NCOA6; -.
GenomeRNAi; 23054; -.
PRO; PR:Q14686; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000198646; -.
CleanEx; HS_NCOA6; -.
ExpressionAtlas; Q14686; baseline and differential.
Genevisible; Q14686; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; TAS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; TAS:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IPI:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; TAS:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0007420; P:brain development; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0006310; P:DNA recombination; NAS:UniProtKB.
GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; NAS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0009725; P:response to hormone; TAS:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR026638; NCOA6.
InterPro; IPR032715; NCOA6_nucleic_acid-bd.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR15690; PTHR15690; 2.
Pfam; PF13820; Nucleic_acid_bd; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation.
CHAIN 1 2063 Nuclear receptor coactivator 6.
/FTId=PRO_0000094413.
REGION 1 1310 NCOA1-binding region.
REGION 1 1057 CREBBP-binding region.
REGION 1 928 TBP/GTF2A-binding region.
REGION 773 927 NCOA6IP-binding region.
REGION 1641 2063 EP300/CRSP3-binding region.
MOTIF 887 891 LXXLL motif 1.
MOTIF 1491 1495 LXXLL motif 2.
COMPBIAS 227 1041 Gln-rich.
COMPBIAS 372 377 Poly-Pro.
COMPBIAS 913 918 Poly-Lys.
MOD_RES 95 95 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 884 884 Phosphoserine; by MAPK; in vitro.
{ECO:0000269|PubMed:11773444}.
MOD_RES 1047 1047 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9JL19}.
MOD_RES 1058 1058 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9JL19}.
MOD_RES 1096 1096 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9JL19}.
MOD_RES 1321 1321 Phosphothreonine.
{ECO:0000269|PubMed:10823961}.
MOD_RES 1819 1819 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JL19}.
MOD_RES 1822 1822 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JL19}.
MOD_RES 2018 2018 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 512 512 P -> L (in dbSNP:rs6060031).
/FTId=VAR_027874.
VARIANT 955 955 N -> S (in dbSNP:rs17092079).
{ECO:0000269|PubMed:10567404,
ECO:0000269|PubMed:10681503,
ECO:0000269|PubMed:10823961,
ECO:0000269|PubMed:10866662,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_027875.
VARIANT 1060 1060 P -> S (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036551.
VARIANT 1191 1191 S -> R (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036552.
VARIANT 1995 1995 I -> V (in dbSNP:rs6060022).
/FTId=VAR_027876.
MUTAGEN 883 894 TSPLLVNLLQSD->ENPLLVNLLQFI: Reduced
binding to THRB, RXRA, ESR2 and ESR1.
{ECO:0000269|PubMed:11773444}.
MUTAGEN 883 894 TSPLLVNLLQSD->NLPLLVNLLQHT: Reduced
binding to THRB, RXRA, ESR2 and ESR1.
{ECO:0000269|PubMed:11773444}.
MUTAGEN 883 894 TSPLLVNLLQSD->VNPLLVNLLQFI: Reduced
binding to THRB, RXRA, ESR2 and ESR1.
{ECO:0000269|PubMed:11773444}.
MUTAGEN 883 884 TS->SY: Strong increase in binding to
THRB, RXRA and ESR2, but dramatic
decrease in binding to ESR1.
MUTAGEN 884 894 SPLLVNLLQSD->NPLLVNLLQLL: Reduced binding
to THRB, RXRA, ESR2 and ESR1.
SEQUENCE 2063 AA; 219145 MW; 73219502F5138427 CRC64;
MVLDDLPNLE DIYTSLCSST MEDSEMDFDS GLEDDDTKSD SILEDSTIFV AFKGNIDDKD
FKWKLDAILK NVPNLLHMES SKLKVQKVEP WNSVRVTFNI PREAAERLRI LAQSNNQQLR
DLGILSVQIE GEGAINLALA QNRSQDVRMN GPMGAGNSVR MEAGFPMASG PGIIRMNNPA
TVMIPPGGNV SSSMMAPGPN PELQPRTPRP ASQSDAMDPL LSGLHIQQQS HPSGSLAPPH
HPMQPVSVNR QMNPANFPQL QQQQQQQQQQ QQQQQQQQQQ QQQQQLQARP PQQHQQQQPQ
GIRPQFTAPT QVPVPPGWNQ LPSGALQPPP AQGSLGTMTA NQGWKKAPLP GPMQQQLQAR
PSLATVQTPS HPPPPYPFGS QQASQAHTNF PQMSNPGQFT APQMKSLQGG PSRVPTPLQQ
PHLTNKSPAS SPSSFQQGSP ASSPTVNQTQ QQMGPRPPQN NPLPQGFQQP VSSPGRNPMV
QQGNVPPNFM VMQQQPPNQG PQSLHPGLGG MPKRLPPGFS AGQANPNFMQ GQVPSTTATT
PGNSGAPQLQ ANQNVQHAGG QGAGPPQNQM QVSHGPPNMM QPSLMGIHGN MNNQQAGTSG
VPQVNLSNMQ GQPQQGPPSQ LMGMHQQIVP SQGQMVQQQG TLNPQNPMIL SRAQLMPQGQ
MMVNPPSQNL GPSPQRMTPP KQMLSQQGPQ MMAPHNQMMG PQGQVLLQQN PMIEQIMTNQ
MQGNKQQFNT QNQSNVMPGP AQIMRGPTPN MQGNMVQFTG QMSGQMLPQQ GPVNNSPSQV
MGIQGQVLRP PGPSPHMAQQ HGDPATTANN DVSLSQMMPD VSIQQTNMVP PHVQAMQGNS
ASGNHFSGHG MSFNAPFSGA PNGNQMSCGQ NPGFPVNKDV TLTSPLLVNL LQSDISAGHF
GVNNKQNNTN ANKPKKKKPP RKKKNSQQDL NTPDTRPAGL EEADQPPLPG EQGINLDNSG
PKLPEFSNRP PGYPSQPVEQ RPLQQMPPQL MQHVAPPPQP PQQQPQPQLP QQQQPPPPSQ
PQSQQQQQQQ QQMMMMLMMQ QDPKSVRLPV SQNVHPPRGP LNPDSQRMPM QQSGSVPVMV
SLQGPASVPP SPDKQRMPMP VNTPLGSNSR KMVYQESPQN PSSSPLAEMA SLPEASGSEA
PSVPGGPNNM PSHVVLPQNQ LMMTGPKPGP SPLSATQGAT PQQPPVNSLP SSHGHHFPNV
AAPTQTSRPK TPNRASPRPY YPQTPNNRPP STEPSEISLS PERLNASIAG LFPPQINIPL
PPRPNLNRGF DQQGLNPTTL KAIGQAPSNL TMNPSNFATP QTHKLDSVVV NSGKQSNSGA
TKRASPSNSR RSSPGSSRKT TPSPGRQNSK APKLTLASQT NAALLQNVEL PRNVLVSPTP
LANPPVPGSF PNNSGLNPQN STVSVAAVGG VVEDNKESLN VPQDSDCQNS QSRKEQVNIE
LKAVPAQEVK MVVPEDQSKK DGQPSDPNKL PSVEENKNLV SPAMREAPTS LSQLLDNSGA
PNVTIKPPGL TDLEVTPPVV SGEDLKKASV IPTLQDLSSS KEPSNSLNLP HSNELCSSLV
HPELSEVSSN VAPSIPPVMS RPVSSSSIST PLPPNQITVF VTSNPITTSA NTSAALPTHL
QSALMSTVVT MPNAGSKVMV SEGQSAAQSN ARPQFITPVF INSSSIIQVM KGSQPSTIPA
APLTTNSGLM PPSVAVVGPL HIPQNIKFSS APVPPNALSS SPAPNIQTGR PLVLSSRATP
VQLPSPPCTS SPVVPSHPPV QQVKELNPDE ASPQVNTSAD QNTLPSSQST TMVSPLLTNS
PGSSGNRRSP VSSSKGKGKV DKIGQILLTK ACKKVTGSLE KGEEQYGADG ETEGQGLDTT
APGLMGTEQL STELDSKTPT PPAPTLLKMT SSPVGPGTAS AGPSLPGGAL PTSVRSIVTT
LVPSELISAV PTTKSNHGGI ASESLAGGLV EEKVGSHPEL LPSIAPSQNL VSKETSTTAL
QASVARPELE VNAAIVSGQS SEPKEIVEKS KIPGRRNSRT EEPTVASESV ENGHRKRSSR
PASASSSTKD ITSAVQSKRR KSK


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