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   27-MAR-2024, entry version 176.
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; 136.
DR   IntAct; Q9HCD5; 44.
DR   MINT; Q9HCD5; -.
DR   STRING; 9606.ENSP00000290231; -.
DR   DrugBank; DB07702; 17alpha-Estriol.
DR   GlyCosmos; Q9HCD5; 15 sites, 2 glycans.
DR   GlyGen; Q9HCD5; 19 sites, 2 O-linked glycans (19 sites).
DR   iPTMnet; Q9HCD5; -.
DR   MetOSite; Q9HCD5; -.
DR   PhosphoSitePlus; Q9HCD5; -.
DR   SwissPalm; Q9HCD5; -.
DR   BioMuta; NCOA5; -.
DR   DMDM; 28380083; -.
DR   EPD; Q9HCD5; -.
DR   jPOST; Q9HCD5; -.
DR   MassIVE; Q9HCD5; -.
DR   MaxQB; Q9HCD5; -.
DR   PaxDb; 9606-ENSP00000290231; -.
DR   PeptideAtlas; Q9HCD5; -.
DR   ProteomicsDB; 81676; -.
DR   Pumba; Q9HCD5; -.
DR   Antibodypedia; 27960; 175 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   AGR; HGNC:15909; -.
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; PMEEGVR; -.
DR   OrthoDB; 3061812at2759; -.
DR   PhylomeDB; Q9HCD5; -.
DR   TreeFam; TF324704; -.
DR   PathwayCommons; Q9HCD5; -.
DR   SignaLink; Q9HCD5; -.
DR   BioGRID-ORCS; 57727; 50 hits in 1165 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 158 other cell types or tissues.
DR   ExpressionAtlas; Q9HCD5; baseline and differential.
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; Anticodon-binding domain; 1.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   PANTHER; PTHR23295:SF3; NUCLEAR RECEPTOR COACTIVATOR 5; 1.
DR   PANTHER; PTHR23295; NUCLEAR RECEPTOR COACTIVATOR 5-RELATED; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   Genevisible; Q9HCD5; HS.
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
//