NCOA5_HUMAN
ID NCOA5_HUMAN Reviewed; 579 AA.
AC Q9HCD5; B2RTV9; E1P5R0; Q6HA99; Q9H1F2; Q9H2T2; Q9H4Y9;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nuclear receptor coactivator 5;
DE Short=NCoA-5;
DE AltName: Full=Coactivator independent of AF-2;
DE Short=CIA;
GN Name=NCOA5; Synonyms=KIAA1637;
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 ESR1; ESR2 AND NR1D2, AND
RP MUTAGENESIS OF ILE-342 AND 348-LEU-LEU-349.
RC TISSUE=Fetal kidney;
RX PubMed=11113208; DOI=10.1128/mcb.21.1.343-353.2001;
RA Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.;
RT "CIA, a novel estrogen receptor coactivator with a bifunctional nuclear
RT receptor interacting determinant.";
RL Mol. Cell. Biol. 21:343-353(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 86-91 AND 280-292,
RP FUNCTION, AND INTERACTION WITH HTATIP2.
RX PubMed=15073177; DOI=10.1074/jbc.m401809200;
RA Jiang C., Ito M., Piening V., Bruck K., Roeder R.G., Xiao H.;
RT "TIP30 interacts with an estrogen receptor alpha-interacting coactivator
RT CIA and regulates c-myc transcription.";
RL J. Biol. Chem. 279:27781-27789(2004).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-579.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND
RP PPP1CA, AND INTERACTION WITH YLPM1.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N.,
RA Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside
RT kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-3; SER-9; SER-29; SER-34; SER-378 AND SER-381, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-9; SER-126 AND SER-381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-21; SER-24; SER-29;
RP SER-34; SER-96; SER-116; SER-126; SER-143; SER-151; THR-274; SER-378;
RP THR-379 AND SER-381, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP 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 [18]
RP STRUCTURE BY NMR OF 197-313.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of anticodon binding domain from nuclear receptor
RT coactivator 5 (human KIAA1637 protein).";
RL Submitted (JUL-2004) to the PDB data bank.
CC -!- FUNCTION: Nuclear receptor coregulator that can have both coactivator
CC and corepressor functions. Interacts with nuclear receptors for
CC steroids (ESR1 and ESR2) independently of the steroid binding domain
CC (AF-2) of the ESR receptors, and with the orphan nuclear receptor
CC NR1D2. Involved in the coactivation of nuclear steroid receptors (ER)
CC as well as the corepression of MYC in response to 17-beta-estradiol
CC (E2). {ECO:0000269|PubMed:15073177}.
CC -!- SUBUNIT: Binds HTATIP2/TIP30. Interacts with YLPM1. Forms a complex
CC with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and PPP1CA.
CC {ECO:0000269|PubMed:11113208, ECO:0000269|PubMed:15073177,
CC ECO:0000269|PubMed:17890166}.
CC -!- INTERACTION:
CC Q9HCD5; Q60674: Nr1d2; Xeno; NbExp=2; IntAct=EBI-2863498, EBI-5326205;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LxxLL) motif that is
CC essential for the association with nuclear receptors.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG36793.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF230533; AAG36793.1; ALT_INIT; mRNA.
DR EMBL; AF470686; AAO33457.1; -; mRNA.
DR EMBL; AL035662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75765.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75769.1; -; Genomic_DNA.
DR EMBL; BC140836; AAI40837.1; -; mRNA.
DR EMBL; BC151133; AAI51134.1; -; mRNA.
DR EMBL; AB046857; BAB13463.1; -; mRNA.
DR CCDS; CCDS13392.1; -.
DR RefSeq; NP_066018.1; NM_020967.2.
DR PDB; 1V95; NMR; -; A=197-313.
DR PDB; 2J7X; X-ray; 2.10 A; B=338-354.
DR PDB; 2J7Y; X-ray; 1.80 A; B=338-354.
DR PDB; 4ZI1; X-ray; 2.10 A; B=341-352.
DR PDBsum; 1V95; -.
DR PDBsum; 2J7X; -.
DR PDBsum; 2J7Y; -.
DR PDBsum; 4ZI1; -.
DR AlphaFoldDB; Q9HCD5; -.
DR BMRB; Q9HCD5; -.
DR SMR; Q9HCD5; -.
DR BioGRID; 121747; 111.
DR IntAct; Q9HCD5; 42.
DR MINT; Q9HCD5; -.
DR STRING; 9606.ENSP00000290231; -.
DR DrugBank; DB07702; 17alpha-Estriol.
DR GlyGen; Q9HCD5; 15 sites, 2 O-linked glycans (15 sites).
DR iPTMnet; Q9HCD5; -.
DR MetOSite; Q9HCD5; -.
DR PhosphoSitePlus; Q9HCD5; -.
DR BioMuta; NCOA5; -.
DR DMDM; 28380083; -.
DR EPD; Q9HCD5; -.
DR jPOST; Q9HCD5; -.
DR MassIVE; Q9HCD5; -.
DR MaxQB; Q9HCD5; -.
DR PaxDb; Q9HCD5; -.
DR PeptideAtlas; Q9HCD5; -.
DR PRIDE; Q9HCD5; -.
DR ProteomicsDB; 81676; -.
DR Antibodypedia; 27960; 148 antibodies from 24 providers.
DR DNASU; 57727; -.
DR Ensembl; ENST00000290231.11; ENSP00000290231.6; ENSG00000124160.12.
DR GeneID; 57727; -.
DR KEGG; hsa:57727; -.
DR MANE-Select; ENST00000290231.11; ENSP00000290231.6; NM_020967.3; NP_066018.1.
DR UCSC; uc002xre.4; human.
DR CTD; 57727; -.
DR DisGeNET; 57727; -.
DR GeneCards; NCOA5; -.
DR HGNC; HGNC:15909; NCOA5.
DR HPA; ENSG00000124160; Low tissue specificity.
DR neXtProt; NX_Q9HCD5; -.
DR OpenTargets; ENSG00000124160; -.
DR PharmGKB; PA31474; -.
DR VEuPathDB; HostDB:ENSG00000124160; -.
DR eggNOG; KOG0845; Eukaryota.
DR GeneTree; ENSGT00530000064134; -.
DR HOGENOM; CLU_030807_1_1_1; -.
DR InParanoid; Q9HCD5; -.
DR OMA; ERRNMNK; -.
DR OrthoDB; 994112at2759; -.
DR PhylomeDB; Q9HCD5; -.
DR TreeFam; TF324704; -.
DR PathwayCommons; Q9HCD5; -.
DR SignaLink; Q9HCD5; -.
DR BioGRID-ORCS; 57727; 49 hits in 1086 CRISPR screens.
DR ChiTaRS; NCOA5; human.
DR EvolutionaryTrace; Q9HCD5; -.
DR GeneWiki; NCOA5; -.
DR GenomeRNAi; 57727; -.
DR Pharos; Q9HCD5; Tbio.
DR PRO; PR:Q9HCD5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9HCD5; protein.
DR Bgee; ENSG00000124160; Expressed in oviduct epithelium and 156 other tissues.
DR ExpressionAtlas; Q9HCD5; baseline and differential.
DR Genevisible; Q9HCD5; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; NAS:ARUK-UCL.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; NAS:ARUK-UCL.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..579
FT /note="Nuclear receptor coactivator 5"
FT /id="PRO_0000094411"
FT REGION 1..158
FT /note="Transcription repression"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..579
FT /note="Transcription activation"
FT REGION 560..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 345..349
FT /note="LXXLL motif"
FT COMPBIAS 16..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 326
FT /note="E -> G (in dbSNP:rs11549557)"
FT /id="VAR_053530"
FT MUTAGEN 342
FT /note="I->A: Abolishes E2-inducible strong interaction with
FT ESR1, but not basal interaction."
FT /evidence="ECO:0000269|PubMed:11113208"
FT MUTAGEN 348..349
FT /note="LL->AA: Abolishes interaction with ESR1."
FT /evidence="ECO:0000269|PubMed:11113208"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:1V95"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1V95"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:1V95"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1V95"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1V95"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:1V95"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:1V95"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:1V95"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1V95"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1V95"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:1V95"
FT HELIX 283..302
FT /evidence="ECO:0007829|PDB:1V95"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1V95"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:2J7Y"
SQ SEQUENCE 579 AA; 65536 MW; D2ADCCEBEE566A91 CRC64;
MNTAPSRPSP TRRDPYGFGD SRDSRRDRSP IRGSPRREPR DGRNGRDARD SRDIRDPRDL
RDHRHSRDLR DHRDSRSVRD VRDVRDLRDF RDLRDSRDFR DQRDPMYDRY RDMRDSRDPM
YRREGSYDRY LRMDDYCRRK DDSYFDRYRD SFDGRGPPGP ESQSRAKERL KREERRREEL
YRQYFEEIQR RFDAERPVDC SVIVVNKQTK DYAESVGRKV RDLGMVVDLI FLNTEVSLSQ
ALEDVSRGGS PFAIVITQQH QIHRSCTVNI MFGTPQEHRN MPQADAMVLV ARNYERYKNE
CREKEREEIA RQAAKMADEA ILQERERGGP EEGVRGGHPP AIQSLINLLA DNRYLTAEET
DKIINYLRER KERLMRSSTD SLPGPISRQP LGATSGASLK TQPSSQPLQS GQVLPSATPT
PSAPPTSQQE LQAKILSLFN SGTVTANSSS ASPSVAAGNT PNQNFSTAAN SQPQQRSQAS
GNQPPSILGQ GGSAQNMGPR PGAPSQGLFG QPSSRLAPAS NMTSQRPVSS TGINFDNPSV
QKALDTLIQS GPALSHLVSQ TTAQMGQPQA PMGSYQRHY
