NCOA6_HUMAN
ID NCOA6_HUMAN Reviewed; 2063 AA.
AC Q14686; A6NLF1; B2RMN5; E1P5P7; Q9NTZ9; Q9UH74; Q9UK86;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Nuclear receptor coactivator 6;
DE AltName: Full=Activating signal cointegrator 2;
DE Short=ASC-2;
DE AltName: Full=Amplified in breast cancer protein 3;
DE AltName: Full=Cancer-amplified transcriptional coactivator ASC-2;
DE AltName: Full=Nuclear receptor coactivator RAP250;
DE Short=NRC RAP250;
DE AltName: Full=Nuclear receptor-activating protein, 250 kDa;
DE AltName: Full=Peroxisome proliferator-activated receptor-interacting protein;
DE Short=PPAR-interacting protein;
DE Short=PRIP;
DE AltName: Full=Thyroid hormone receptor-binding protein;
GN Name=NCOA6; Synonyms=AIB3, KIAA0181, RAP250, TRBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CREBBP; NCOA1; GTF2A; TBP;
RP RXRA; ESR1; RARA AND THRA, AND VARIANT SER-955.
RX PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
RA Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K.,
RA Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H.,
RA Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
RT "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator
RT essential for ligand-dependent transactivation by nuclear receptors in
RT vivo.";
RL J. Biol. Chem. 274:34283-34293(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, INTERACTION WITH CREBBP;
RP RXRA; ESR1; NR3C1; RARA; VDR AND THRA, AND VARIANT SER-955.
RX PubMed=10866662; DOI=10.1128/mcb.20.14.5048-5063.2000;
RA Mahajan M.A., Samuels H.H.;
RT "A new family of nuclear receptor coregulators that integrates nuclear
RT receptor signaling through CBP.";
RL Mol. Cell. Biol. 20:5048-5063(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PPARA; PPARG; ESR1; ESR2 AND
RP THR, AND VARIANT SER-955.
RC TISSUE=Testis;
RX PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
RA Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
RT "Cloning and characterization of RAP250, a nuclear receptor coactivator.";
RL J. Biol. Chem. 275:5308-5317(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY PRKDC, INTERACTION WITH THR;
RP RAR; EP300 AND CRSP3, AND VARIANT SER-955.
RC TISSUE=Lymphocyte;
RX PubMed=10823961; DOI=10.1073/pnas.97.11.6212;
RA Ko L., Cardona G.R., Chin W.W.;
RT "Thyroid hormone receptor-binding protein, an LXXLL motif-containing
RT protein, functions as a general coactivator.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-955.
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [6]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH NCOA6IP.
RX PubMed=11517327; DOI=10.1073/pnas.181347498;
RA Zhu Y.-J., Qi C., Cao W.-Q., Yeldandi A.V., Rao M.S., Reddy J.K.;
RT "Cloning and characterization of PIMT, a protein with a methyltransferase
RT domain, which interacts with and enhances nuclear receptor coactivator PRIP
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10380-10385(2001).
RN [11]
RP INTERACTION WITH RBM14.
RX PubMed=11443112; DOI=10.1074/jbc.m101517200;
RA Iwasaki T., Chin W.W., Ko L.;
RT "Identification and characterization of RRM-containing coactivator
RT activator (CoAA) as TRBP-interacting protein, and its splice variant as a
RT coactivator modulator (CoAM).";
RL J. Biol. Chem. 276:33375-33383(2001).
RN [12]
RP INTERACTION WITH PRMT2.
RX PubMed=12039952; DOI=10.1074/jbc.m201053200;
RA Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
RT "Identification of protein arginine methyltransferase 2 as a coactivator
RT for estrogen receptor alpha.";
RL J. Biol. Chem. 277:28624-28630(2002).
RN [13]
RP INTERACTION WITH ZNF335.
RX PubMed=12215545; DOI=10.1128/mcb.22.19.6883-6894.2002;
RA Mahajan M.A., Murray A., Samuels H.H.;
RT "NRC-interacting factor 1 is a novel cotransducer that interacts with and
RT regulates the activity of the nuclear hormone receptor coactivator NRC.";
RL Mol. Cell. Biol. 22:6883-6894(2002).
RN [14]
RP IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
RC TISSUE=Cervix carcinoma;
RX PubMed=12482968; DOI=10.1128/mcb.23.1.140-149.2003;
RA Goo Y.-H., Sohn Y.C., Kim D.-H., Kim S.-W., Kang M.-J., Jung D.-J.,
RA Kwak E., Barlev N.A., Berger S.L., Chow V.T., Roeder R.G., Azorsa D.O.,
RA Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., Lee J.W.;
RT "Activating signal cointegrator 2 belongs to a novel steady-state complex
RT that contains a subset of trithorax group proteins.";
RL Mol. Cell. Biol. 23:140-149(2003).
RN [15]
RP MUTAGENESIS OF 883-THR--GLU-894, AND PHOSPHORYLATION AT SER-884.
RX PubMed=11773444; DOI=10.1210/mend.16.1.0755;
RA Ko L., Cardona G.R., Iwasaki T., Bramlett K.S., Burris T.P., Chin W.W.;
RT "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines
RT selectivity for ERs and TRs.";
RL Mol. Endocrinol. 16:128-140(2002).
RN [16]
RP IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
RX PubMed=17021013; DOI=10.1073/pnas.0607313103;
RA Lee S., Lee D.K., Dou Y., Lee J., Lee B., Kwak E., Kong Y.Y., Lee S.K.,
RA Roeder R.G., Lee J.W.;
RT "Coactivator as a target gene specificity determinant for histone H3 lysine
RT 4 methyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15392-15397(2006).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MLL2/3
RP COMPLEX.
RX PubMed=17500065; DOI=10.1074/jbc.m701574200;
RA Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
RA Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
RT "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:20395-20406(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2018, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-95, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [21]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-1060 AND ARG-1191.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
CC receptors and stimulates the transcriptional activities in a hormone-
CC dependent fashion. Coactivates expression in an agonist- and AF2-
CC dependent manner. Involved in the coactivation of different nuclear
CC receptors, such as for steroids (GR and ERs), retinoids (RARs and
CC RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs).
CC Probably functions as a general coactivator, rather than just a nuclear
CC receptor coactivator. May also be involved in the coactivation of the
CC NF-kappa-B pathway. May coactivate expression via a remodeling of
CC chromatin and its interaction with histone acetyltransferase proteins.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with RBM39 (By similarity).
CC Interacts in vitro with the basal transcription factors GTF2A and TBP,
CC suggesting an autonomous transactivation function. Interacts with
CC NCOA1, CRSP3, RBM14, the histone acetyltransferases EP300 and CREBBP,
CC and with the methyltransferases NCOA6IP and PRMT2/HRMT1L1. Component of
CC the MLL2/3 complex (also named ASCOM complex), at least composed of
CC KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A,
CC PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with ZNF335;
CC may enhance ligand-dependent transcriptional activation by nuclear
CC hormone receptors. {ECO:0000250, ECO:0000269|PubMed:10567404,
CC ECO:0000269|PubMed:10681503, ECO:0000269|PubMed:10823961,
CC ECO:0000269|PubMed:10866662, ECO:0000269|PubMed:11443112,
CC ECO:0000269|PubMed:11517327, ECO:0000269|PubMed:12039952,
CC ECO:0000269|PubMed:12215545, ECO:0000269|PubMed:12482968,
CC ECO:0000269|PubMed:17021013, ECO:0000269|PubMed:17500065}.
CC -!- INTERACTION:
CC Q14686; P10275: AR; NbExp=3; IntAct=EBI-78670, EBI-608057;
CC Q14686; Q9UBL3: ASH2L; NbExp=14; IntAct=EBI-78670, EBI-540797;
CC Q14686; Q92793: CREBBP; NbExp=2; IntAct=EBI-78670, EBI-81215;
CC Q14686; Q9UMN6: KMT2B; NbExp=5; IntAct=EBI-78670, EBI-765774;
CC Q14686; Q8NEZ4: KMT2C; NbExp=7; IntAct=EBI-78670, EBI-1042997;
CC Q14686; P46934: NEDD4; NbExp=2; IntAct=EBI-78670, EBI-726944;
CC Q14686; P06400: RB1; NbExp=3; IntAct=EBI-78670, EBI-491274;
CC Q14686; Q12888: TP53BP1; NbExp=3; IntAct=EBI-78670, EBI-396540;
CC Q14686; Q12888-1: TP53BP1; NbExp=3; IntAct=EBI-78670, EBI-8022649;
CC Q14686; P61964: WDR5; NbExp=9; IntAct=EBI-78670, EBI-540834;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, prostate,
CC testis and ovary; weakly expressed in lung, thymus and small intestine.
CC -!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Only motif 1
CC is essential for the association with nuclear receptors, while adjacent
CC Ser-884 displays selectivity for nuclear receptors.
CC -!- PTM: Phosphorylated by PRKDC.
CC -!- PTM: Phosphorylation on Ser-884 leads to a strong decrease in binding
CC to ESR1 and ESR2. {ECO:0000269|PubMed:10823961,
CC ECO:0000269|PubMed:11773444}.
CC -!- MISCELLANEOUS: Frequently amplified or overexpressed in colon, breast
CC and lung cancers.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF16403.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA11498.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF177388; AAF13595.1; -; mRNA.
DR EMBL; AF208227; AAF16403.1; ALT_FRAME; mRNA.
DR EMBL; AF245115; AAF78480.1; -; mRNA.
DR EMBL; AF128458; AAF37003.1; -; mRNA.
DR EMBL; AF171667; AAF71829.1; -; mRNA.
DR EMBL; D80003; BAA11498.2; ALT_INIT; mRNA.
DR EMBL; AL109824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76254.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76255.1; -; Genomic_DNA.
DR EMBL; BC136272; AAI36273.1; -; mRNA.
DR CCDS; CCDS13241.1; -.
DR RefSeq; NP_001229468.1; NM_001242539.2.
DR RefSeq; NP_001305169.1; NM_001318240.1.
DR RefSeq; NP_054790.2; NM_014071.4.
DR AlphaFoldDB; Q14686; -.
DR BioGRID; 116691; 117.
DR ComplexPortal; CPX-7091; Histone-lysine N-methyltransferase complex, KMT2C variant.
DR ComplexPortal; CPX-7104; Histone-lysine N-methyltransferase complex, KMT2D variant.
DR CORUM; Q14686; -.
DR DIP; DIP-30934N; -.
DR IntAct; Q14686; 56.
DR MINT; Q14686; -.
DR STRING; 9606.ENSP00000363929; -.
DR GlyGen; Q14686; 11 sites, 2 O-linked glycans (11 sites).
DR iPTMnet; Q14686; -.
DR PhosphoSitePlus; Q14686; -.
DR BioMuta; NCOA6; -.
DR DMDM; 116242672; -.
DR EPD; Q14686; -.
DR jPOST; Q14686; -.
DR MassIVE; Q14686; -.
DR MaxQB; Q14686; -.
DR PaxDb; Q14686; -.
DR PeptideAtlas; Q14686; -.
DR PRIDE; Q14686; -.
DR ProteomicsDB; 60120; -.
DR Antibodypedia; 1325; 99 antibodies from 23 providers.
DR DNASU; 23054; -.
DR Ensembl; ENST00000359003.7; ENSP00000351894.2; ENSG00000198646.14.
DR Ensembl; ENST00000374796.6; ENSP00000363929.2; ENSG00000198646.14.
DR GeneID; 23054; -.
DR KEGG; hsa:23054; -.
DR MANE-Select; ENST00000359003.7; ENSP00000351894.2; NM_014071.5; NP_054790.2.
DR UCSC; uc002xav.3; human.
DR CTD; 23054; -.
DR DisGeNET; 23054; -.
DR GeneCards; NCOA6; -.
DR HGNC; HGNC:15936; NCOA6.
DR HPA; ENSG00000198646; Low tissue specificity.
DR MIM; 605299; gene.
DR neXtProt; NX_Q14686; -.
DR OpenTargets; ENSG00000198646; -.
DR PharmGKB; PA31475; -.
DR VEuPathDB; HostDB:ENSG00000198646; -.
DR eggNOG; ENOG502QQMS; Eukaryota.
DR GeneTree; ENSGT00730000111114; -.
DR HOGENOM; CLU_001959_0_0_1; -.
DR InParanoid; Q14686; -.
DR OMA; EHSILEH; -.
DR OrthoDB; 35282at2759; -.
DR PhylomeDB; Q14686; -.
DR TreeFam; TF332639; -.
DR PathwayCommons; Q14686; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q14686; -.
DR SIGNOR; Q14686; -.
DR BioGRID-ORCS; 23054; 46 hits in 1086 CRISPR screens.
DR ChiTaRS; NCOA6; human.
DR GeneWiki; NCOA6; -.
DR GenomeRNAi; 23054; -.
DR Pharos; Q14686; Tbio.
DR PRO; PR:Q14686; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q14686; protein.
DR Bgee; ENSG00000198646; Expressed in secondary oocyte and 206 other tissues.
DR ExpressionAtlas; Q14686; baseline and differential.
DR Genevisible; Q14686; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0044666; C:MLL3/4 complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; TAS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IPI:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; TAS:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; IC:ComplexPortal.
DR GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0009725; P:response to hormone; TAS:UniProtKB.
DR InterPro; IPR026638; NCOA6.
DR InterPro; IPR032715; NCOA6_TRADD-N.
DR PANTHER; PTHR15690; PTHR15690; 2.
DR Pfam; PF13820; Nucleic_acid_bd; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..2063
FT /note="Nuclear receptor coactivator 6"
FT /id="PRO_0000094413"
FT REGION 1..1310
FT /note="NCOA1-binding region"
FT REGION 1..1057
FT /note="CREBBP-binding region"
FT REGION 1..928
FT /note="TBP/GTF2A-binding region"
FT REGION 184..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..927
FT /note="NCOA6IP-binding region"
FT REGION 789..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1641..2063
FT /note="EP300/CRSP3-binding region"
FT REGION 1738..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1837..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1995..2063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 887..891
FT /note="LXXLL motif 1"
FT MOTIF 1491..1495
FT /note="LXXLL motif 2"
FT COMPBIAS 184..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1767..1813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2039..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 884
FT /note="Phosphoserine; by MAPK; in vitro"
FT /evidence="ECO:0000269|PubMed:11773444"
FT MOD_RES 1047
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JL19"
FT MOD_RES 1058
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JL19"
FT MOD_RES 1096
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JL19"
FT MOD_RES 1819
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JL19"
FT MOD_RES 1822
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JL19"
FT MOD_RES 2018
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 512
FT /note="P -> L (in dbSNP:rs6060031)"
FT /id="VAR_027874"
FT VARIANT 955
FT /note="N -> S (in dbSNP:rs17092079)"
FT /evidence="ECO:0000269|PubMed:10567404,
FT ECO:0000269|PubMed:10681503, ECO:0000269|PubMed:10823961,
FT ECO:0000269|PubMed:10866662, ECO:0000269|PubMed:8724849"
FT /id="VAR_027875"
FT VARIANT 1060
FT /note="P -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036551"
FT VARIANT 1191
FT /note="S -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036552"
FT VARIANT 1995
FT /note="I -> V (in dbSNP:rs6060022)"
FT /id="VAR_027876"
FT MUTAGEN 883..894
FT /note="TSPLLVNLLQSD->ENPLLVNLLQFI: Reduced binding to THRB,
FT RXRA, ESR2 and ESR1."
FT /evidence="ECO:0000269|PubMed:11773444"
FT MUTAGEN 883..894
FT /note="TSPLLVNLLQSD->NLPLLVNLLQHT: Reduced binding to THRB,
FT RXRA, ESR2 and ESR1."
FT /evidence="ECO:0000269|PubMed:11773444"
FT MUTAGEN 883..894
FT /note="TSPLLVNLLQSD->VNPLLVNLLQFI: Reduced binding to THRB,
FT RXRA, ESR2 and ESR1."
FT /evidence="ECO:0000269|PubMed:11773444"
FT MUTAGEN 883..884
FT /note="TS->SY: Strong increase in binding to THRB, RXRA and
FT ESR2, but dramatic decrease in binding to ESR1."
FT MUTAGEN 884..894
FT /note="SPLLVNLLQSD->NPLLVNLLQLL: Reduced binding to THRB,
FT RXRA, ESR2 and ESR1."
SQ 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
