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 09-DEC-2015, entry version 142. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CREBBP; NCOA1; GTF2A; RP TBP; 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., RA Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., RA Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.; RT "A nuclear factor ASC-2, as a cancer-amplified transcriptional RT coactivator essential for ligand-dependent transactivation by nuclear RT receptors in 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 RP AND 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 RT coactivator."; RL J. Biol. Chem. 275:5308-5317(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY PRKDC, INTERACTION WITH RP THR; 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. RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by RT analysis of 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT methyltransferase domain, which interacts with and enhances nuclear RT receptor coactivator PRIP 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 RT as a 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 RT coactivator 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 RT and regulates the activity of the nuclear hormone receptor coactivator RT 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., RA Azorsa D.O., Meltzer P.S., Suh P.-G., Song E.J., Lee K.-J., Lee Y.C., RA Lee J.W.; RT "Activating signal cointegrator 2 belongs to a novel steady-state RT complex 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/me.16.1.128; RA Ko L., Cardona G.R., Iwasaki T., Bramlett K.S., Burris T.P., RA 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., RA Lee S.K., Roeder R.G., Lee J.W.; RT "Coactivator as a target gene specificity determinant for histone H3 RT lysine 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 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] 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., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT 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 CC hormone-dependent fashion. Coactivates expression in an agonist- CC and AF2-dependent manner. Involved in the coactivation of CC different nuclear receptors, such as for steroids (GR and ERs), CC retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) CC and prostanoids (PPARs). Probably functions as a general CC coactivator, rather than just a nuclear receptor coactivator. May CC also be involved in the coactivation of the NF-kappa-B pathway. CC May coactivate expression via a remodeling of chromatin and its CC interaction with histone acetyltransferase proteins. CC -!- SUBUNIT: Monomer and homodimer. Interacts with RBM39 (By CC similarity). Interacts in vitro with the basal transcription CC factors GTF2A and TBP, suggesting an autonomous transactivation CC function. Interacts with NCOA1, CRSP3, RBM14, the histone CC acetyltransferases EP300 and CREBBP, and with the CC methyltransferases NCOA6IP and PRMT2/HRMT1L1. Component of the CC 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 CC ZNF335; may enhance ligand-dependent transcriptional activation by CC nuclear hormone receptors. {ECO:0000250, CC ECO:0000269|PubMed:10567404, ECO:0000269|PubMed:10681503, CC ECO:0000269|PubMed:10823961, ECO:0000269|PubMed:10866662, CC ECO:0000269|PubMed:11443112, ECO:0000269|PubMed:11517327, CC ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12215545, CC ECO:0000269|PubMed:12482968, ECO:0000269|PubMed:17021013, CC ECO:0000269|PubMed:17500065}. CC -!- INTERACTION: CC P10275:AR; NbExp=2; IntAct=EBI-78670, EBI-608057; CC Q9UBL3:ASH2L; NbExp=7; IntAct=EBI-78670, EBI-540797; CC Q92793:CREBBP; NbExp=2; IntAct=EBI-78670, EBI-81215; CC Q8NEZ4:KMT2C; NbExp=5; IntAct=EBI-78670, EBI-1042997; CC O14686:KMT2D; NbExp=6; IntAct=EBI-78670, EBI-996065; CC P06400:RB1; NbExp=3; IntAct=EBI-78670, EBI-491274; CC P61964:WDR5; NbExp=2; IntAct=EBI-78670, EBI-540834; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, CC prostate, testis and ovary; weakly expressed in lung, thymus and CC small intestine. CC -!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Only CC motif 1 is essential for the association with nuclear receptors, CC while adjacent Ser-884 displays selectivity for nuclear receptors. CC -!- PTM: Phosphorylated by PRKDC. CC -!- PTM: Phosphorylation on Ser-884 leads to a strong decrease in CC binding to ESR1 and ESR2. {ECO:0000269|PubMed:10823961, CC ECO:0000269|PubMed:11773444}. CC -!- MISCELLANEOUS: Frequently amplified or overexpressed in colon, CC breast and lung cancers. CC -!- SEQUENCE CAUTION: CC Sequence=AAF16403.1; Type=Frameshift; Positions=88; Evidence={ECO:0000305}; CC Sequence=BAA11498.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CAB92721.2; -; 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_001242539.1. DR RefSeq; NP_054790.2; NM_014071.3. DR RefSeq; XP_011527027.1; XM_011528725.1. DR UniGene; Hs.368971; -. DR UniGene; Hs.736403; -. DR ProteinModelPortal; Q14686; -. DR BioGrid; 116691; 80. DR DIP; DIP-30934N; -. DR IntAct; Q14686; 31. DR MINT; MINT-1194462; -. DR STRING; 9606.ENSP00000351894; -. DR PhosphoSite; Q14686; -. DR BioMuta; NCOA6; -. DR DMDM; 116242672; -. DR MaxQB; Q14686; -. DR PaxDb; Q14686; -. DR PRIDE; Q14686; -. DR Ensembl; ENST00000359003; ENSP00000351894; ENSG00000198646. DR Ensembl; ENST00000374796; ENSP00000363929; ENSG00000198646. DR GeneID; 23054; -. DR KEGG; hsa:23054; -. DR UCSC; uc002xav.3; human. DR CTD; 23054; -. DR GeneCards; NCOA6; -. DR H-InvDB; HIX0015752; -. DR HGNC; HGNC:15936; NCOA6. DR HPA; HPA004198; -. DR MIM; 605299; gene. DR neXtProt; NX_Q14686; -. DR PharmGKB; PA31475; -. DR eggNOG; ENOG410IK20; Eukaryota. DR eggNOG; ENOG410XW4F; LUCA. DR GeneTree; ENSGT00730000111114; -. DR HOVERGEN; HBG052586; -. DR InParanoid; Q14686; -. DR KO; K14971; -. DR OMA; PAMTGIP; -. DR OrthoDB; EOG7W9RSX; -. DR PhylomeDB; Q14686; -. DR TreeFam; TF332639; -. 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-2032785; YAP1- and WWTR1 (TAZ)-stimulated 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 Peroxisome proliferator-activated receptor alpha (PPARalpha). DR Reactome; R-HSA-400253; Circadian Clock. DR ChiTaRS; NCOA6; human. DR GeneWiki; NCOA6; -. DR GenomeRNAi; 23054; -. DR NextBio; 44111; -. DR PRO; PR:Q14686; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; Q14686; -. DR CleanEx; HS_NCOA6; -. DR ExpressionAtlas; Q14686; baseline and differential. DR Genevisible; Q14686; HS. DR GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription factor complex; TAS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0030331; F:estrogen receptor binding; TAS:UniProtKB. DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IPI:UniProtKB. DR GO; GO:0046965; F:retinoid X receptor binding; TAS:UniProtKB. DR GO; GO:0046966; F: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:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI. DR GO; GO:0006310; P:DNA recombination; NAS:UniProtKB. DR GO; GO:0006281; P:DNA repair; NAS:UniProtKB. DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB. DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; NAS:UniProtKB. DR GO; GO:0007507; P:heart development; ISS:UniProtKB. DR GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl. DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; NAS:UniProtKB. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl. DR GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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 GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:UniProtKB. DR InterPro; IPR026638; NCOA6. DR PANTHER; PTHR15690:SF0; PTHR15690:SF0; 2. PE 1: Evidence at protein level; KW Acetylation; Activator; Complete proteome; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Transcription; KW Transcription regulation. FT CHAIN 1 2063 Nuclear receptor coactivator 6. FT /FTId=PRO_0000094413. FT REGION 1 1310 NCOA1-binding region. FT REGION 1 1057 CREBBP-binding region. FT REGION 1 928 TBP/GTF2A-binding region. FT REGION 773 927 NCOA6IP-binding region. FT REGION 1641 2063 EP300/CRSP3-binding region. FT MOTIF 887 891 LXXLL motif 1. FT MOTIF 1491 1495 LXXLL motif 2. FT COMPBIAS 227 1041 Gln-rich. FT COMPBIAS 372 377 Poly-Pro. FT COMPBIAS 913 918 Poly-Lys. FT MOD_RES 884 884 Phosphoserine; by MAPK; in vitro. FT {ECO:0000269|PubMed:11773444}. FT MOD_RES 1321 1321 Phosphothreonine. FT {ECO:0000269|PubMed:10823961}. FT MOD_RES 1819 1819 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9JL19}. FT MOD_RES 1822 1822 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9JL19}. FT MOD_RES 2018 2018 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9JL19}. FT VARIANT 512 512 P -> L (in dbSNP:rs6060031). FT /FTId=VAR_027874. FT VARIANT 955 955 N -> S (in dbSNP:rs17092079). FT {ECO:0000269|PubMed:10567404, FT ECO:0000269|PubMed:10681503, FT ECO:0000269|PubMed:10823961, FT ECO:0000269|PubMed:10866662, FT ECO:0000269|PubMed:8724849}. FT /FTId=VAR_027875. FT VARIANT 1060 1060 P -> S (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036551. FT VARIANT 1191 1191 S -> R (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036552. FT VARIANT 1995 1995 I -> V (in dbSNP:rs6060022). FT /FTId=VAR_027876. FT MUTAGEN 883 894 TSPLLVNLLQSD->ENPLLVNLLQFI: Reduced FT binding to THRB, RXRA, ESR2 and ESR1. FT {ECO:0000269|PubMed:11773444}. FT MUTAGEN 883 894 TSPLLVNLLQSD->NLPLLVNLLQHT: Reduced FT binding to THRB, RXRA, ESR2 and ESR1. FT {ECO:0000269|PubMed:11773444}. FT MUTAGEN 883 894 TSPLLVNLLQSD->VNPLLVNLLQFI: Reduced FT binding to THRB, RXRA, ESR2 and ESR1. FT {ECO:0000269|PubMed:11773444}. FT MUTAGEN 883 884 TS->SY: Strong increase in binding to FT THRB, RXRA and ESR2, but dramatic FT decrease in binding to ESR1. FT MUTAGEN 884 894 SPLLVNLLQSD->NPLLVNLLQLL: Reduced binding FT to THRB, 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 //