ID MED14_HUMAN Reviewed; 1454 AA. AC O60244; Q4KMR7; Q9UNB3; DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 24-JAN-2024, entry version 191. DE RecName: Full=Mediator of RNA polymerase II transcription subunit 14; DE AltName: Full=Activator-recruited cofactor 150 kDa component; DE Short=ARC150; DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 2; DE Short=CRSP complex subunit 2; DE AltName: Full=Mediator complex subunit 14; DE AltName: Full=RGR1 homolog; DE Short=hRGR1; DE AltName: Full=Thyroid hormone receptor-associated protein complex 170 kDa component; DE Short=Trap170; DE AltName: Full=Transcriptional coactivator CRSP150; DE AltName: Full=Vitamin D3 receptor-interacting protein complex 150 kDa component; DE Short=DRIP150; GN Name=MED14; GN Synonyms=ARC150, CRSP2, CXorf4, DRIP150, EXLM1, RGR1, TRAP170; 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 [GENOMIC DNA / MRNA]. RX PubMed=9598311; DOI=10.1006/geno.1998.5246; RA Yoshikawa H., Fujiyama A., Nakai K., Inazawa J., Matsubara K.; RT "Detection and isolation of a novel human gene located on Xp11.2-p11.4 that RT escapes X-inactivation using a two-dimensional DNA mapping method."; RL Genomics 49:237-246(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9989412; DOI=10.1038/17141; RA Ryu S., Zhou S., Ladurner A.G., Tjian R.; RT "The transcriptional cofactor complex CRSP is required for activity of the RT enhancer-binding protein Sp1."; RL Nature 397:446-450(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 250-263 AND 1106-1146, AND RP IDENTIFICATION IN ARC COMPLEX. RC TISSUE=Cervix carcinoma; RX PubMed=10235266; DOI=10.1038/19783; RA Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M., RA Erdjument-Bromage H., Tempst P., Freedman L.P.; RT "Ligand-dependent transcription activation by nuclear receptors requires RT the DRIP complex."; RL Nature 398:824-828(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND RP IDENTIFICATION IN THE SMCC COMPLEX. RX PubMed=10024883; DOI=10.1016/s1097-2765(00)80178-1; RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., RA Qin J., Roeder R.G.; RT "A novel human SRB/MED-containing cofactor complex, SMCC, involved in RT transcription regulation."; RL Mol. Cell 3:97-108(1999). RN [5] RP ERRATUM OF PUBMED:10024883. RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., RA Qin J., Roeder R.G.; RL Mol. Cell 3:541-541(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A FORM OF THE RP MEDIATOR COMPLEX. RX PubMed=9734358; DOI=10.1016/s1097-2765(00)80131-8; RA Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.; RT "NAT, a human complex containing Srb polypeptides that functions as a RT negative regulator of activated transcription."; RL Mol. Cell 2:213-222(1998). RN [8] RP PROTEIN SEQUENCE OF 4-13 AND 1256-1264, AND IDENTIFICATION IN ARC COMPLEX. RX PubMed=10235267; DOI=10.1038/19789; RA Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.; RT "Composite co-activator ARC mediates chromatin-directed transcriptional RT activation."; RL Nature 398:828-832(1999). RN [9] RP INTERACTION WITH AR. RX PubMed=12218053; DOI=10.1074/jbc.m206061200; RA Wang Q., Sharma D., Ren Y., Fondell J.D.; RT "A coregulatory role for the TRAP-mediator complex in androgen receptor- RT mediated gene expression."; RL J. Biol. Chem. 277:42852-42858(2002). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR RP COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2. RX PubMed=11867769; DOI=10.1073/pnas.261715899; RA Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.; RT "The TRAP/Mediator coactivator complex interacts directly with estrogen RT receptors alpha and beta through the TRAP220 subunit and directly enhances RT estrogen receptor function in vitro."; RL Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002). RN [11] RP INTERACTION WITH STAT2. RX PubMed=12509459; DOI=10.1128/mcb.23.2.620-628.2003; RA Lau J.F., Nusinzon I., Burakov D., Freedman L.P., Horvath C.M.; RT "Role of metazoan mediator proteins in interferon-responsive RT transcription."; RL Mol. Cell. Biol. 23:620-628(2003). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR RP COMPLEX. RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006; RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B., RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W., RA Conaway R.C.; RT "A set of consensus mammalian mediator subunits identified by RT multidimensional protein identification technology."; RL Mol. Cell 14:685-691(2004). RN [13] RP FUNCTION, AND INTERACTION WITH SREBF1. RX PubMed=15340088; DOI=10.1128/mcb.24.18.8288-8300.2004; RA Toth J.I., Datta S., Athanikar J.N., Freedman L.P., Osborne T.F.; RT "Selective coactivator interactions in gene activation by SREBP-1a and RT -1c."; RL Mol. Cell. Biol. 24:8288-8300(2004). RN [14] RP FUNCTION, AND INTERACTION WITH ESR1. RX PubMed=15625066; DOI=10.1074/jbc.m413184200; RA Lee J.E., Kim K., Sacchettini J.C., Smith C.V., Safe S.; RT "DRIP150 coactivation of estrogen receptor alpha in ZR-75 breast cancer RT cells is independent of LXXLL motifs."; RL J. Biol. Chem. 280:8819-8830(2005). RN [15] RP INTERACTION WITH MED1 AND MED10, IDENTIFICATION BY MASS SPECTROMETRY, RP IDENTIFICATION IN THE MEDIATOR COMPLEX, AND ASSOCIATION OF THE MEDIATOR RP COMPLEX WITH RNA POLYMERASE II. RX PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015; RA Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T., RA Roeder R.G.; RT "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation RT enriched in RNA polymerase II and is required for ER-mediated RT transcription."; RL Mol. Cell 19:89-100(2005). RN [16] RP FUNCTION, AND INTERACTION WITH MED1 AND MED10. RX PubMed=16595664; DOI=10.1074/jbc.m601983200; RA Baek H.J., Kang Y.K., Roeder R.G.; RT "Human Mediator enhances basal transcription by facilitating recruitment of RT transcription factor IIB during preinitiation complex assembly."; RL J. Biol. Chem. 281:15172-15181(2006). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1128; SER-1136 AND SER-1144, RP AND IDENTIFICATION BY 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617 AND SER-986, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1112; SER-1128 AND SER-1136, RP AND IDENTIFICATION BY 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1112; SER-1119; SER-1128 AND RP SER-1136, AND 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 [22] 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617; SER-1112; SER-1119; RP SER-1128; SER-1136 AND SER-1144, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [24] RP VARIANT [LARGE SCALE ANALYSIS] LEU-1325. 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: Component of the Mediator complex, a coactivator involved in CC the regulated transcription of nearly all RNA polymerase II-dependent CC genes. Mediator functions as a bridge to convey information from gene- CC specific regulatory proteins to the basal RNA polymerase II CC transcription machinery. Mediator is recruited to promoters by direct CC interactions with regulatory proteins and serves as a scaffold for the CC assembly of a functional preinitiation complex with RNA polymerase II CC and the general transcription factors. {ECO:0000269|PubMed:15340088, CC ECO:0000269|PubMed:15625066, ECO:0000269|PubMed:16595664}. CC -!- SUBUNIT: Interacts with GATA1 (By similarity). Component of the CC Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8, CC MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, CC MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, CC MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CC CCNC and CDK8 subunits form a distinct module termed the CDK8 module. CC Mediator containing the CDK8 module is less active than Mediator CC lacking this module in supporting transcriptional activation. CC Individual preparations of the Mediator complex lacking one or more CC distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC CC and TRAP. Interacts with AR, ESR1, SREBF1 and STAT2. {ECO:0000250, CC ECO:0000269|PubMed:10024883, ECO:0000269|PubMed:10235266, CC ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:11867769, CC ECO:0000269|PubMed:12218053, ECO:0000269|PubMed:12509459, CC ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15340088, CC ECO:0000269|PubMed:15625066, ECO:0000269|PubMed:15989967, CC ECO:0000269|PubMed:16595664, ECO:0000269|PubMed:9734358}. CC -!- INTERACTION: CC O60244; Q96RN5: MED15; NbExp=2; IntAct=EBI-394489, EBI-394506; CC O60244; Q9Y2X0: MED16; NbExp=2; IntAct=EBI-394489, EBI-394541; CC O60244; Q9ULK4: MED23; NbExp=4; IntAct=EBI-394489, EBI-311161; CC O60244; Q71SY5: MED25; NbExp=2; IntAct=EBI-394489, EBI-394558; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the Mediator complex subunit 14 family. CC {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; AB006651; BAA28626.1; -; mRNA. DR EMBL; AB006652; BAA28627.1; -; Genomic_DNA. DR EMBL; AF104256; AAD12725.1; -; mRNA. DR EMBL; AF304448; AAG22547.1; -; mRNA. DR EMBL; AF135802; AAD24360.1; -; mRNA. DR EMBL; BC098377; AAH98377.1; -; mRNA. DR EMBL; BC132672; AAI32673.1; -; mRNA. DR EMBL; BC132674; AAI32675.1; -; mRNA. DR CCDS; CCDS14254.1; -. DR RefSeq; NP_004220.2; NM_004229.3. DR PDB; 7EMF; EM; 3.50 A; N=1-1454. DR PDB; 7ENA; EM; 4.07 A; n=1-1454. DR PDB; 7ENC; EM; 4.13 A; n=1-1454. DR PDB; 7ENJ; EM; 4.40 A; N=1-1454. DR PDB; 7LBM; EM; 4.80 A; r=1-1454. DR PDB; 7NVR; EM; 4.50 A; l=1-1454. DR PDB; 8GXQ; EM; 5.04 A; n=1-1454. DR PDB; 8GXS; EM; 4.16 A; n=1-1454. DR PDBsum; 7EMF; -. DR PDBsum; 7ENA; -. DR PDBsum; 7ENC; -. DR PDBsum; 7ENJ; -. DR PDBsum; 7LBM; -. DR PDBsum; 7NVR; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR AlphaFoldDB; O60244; -. DR EMDB; EMD-12610; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-31191; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-31211; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR SMR; O60244; -. DR BioGRID; 114699; 173. DR ComplexPortal; CPX-3227; Core mediator complex. DR CORUM; O60244; -. DR DIP; DIP-31460N; -. DR IntAct; O60244; 66. DR MINT; O60244; -. DR STRING; 9606.ENSP00000323720; -. DR GlyGen; O60244; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O60244; -. DR MetOSite; O60244; -. DR PhosphoSitePlus; O60244; -. DR BioMuta; MED14; -. DR EPD; O60244; -. DR jPOST; O60244; -. DR MassIVE; O60244; -. DR MaxQB; O60244; -. DR PaxDb; 9606-ENSP00000323720; -. DR PeptideAtlas; O60244; -. DR ProteomicsDB; 49278; -. DR Pumba; O60244; -. DR Antibodypedia; 10773; 189 antibodies from 30 providers. DR DNASU; 9282; -. DR Ensembl; ENST00000324817.6; ENSP00000323720.1; ENSG00000180182.11. DR GeneID; 9282; -. DR KEGG; hsa:9282; -. DR MANE-Select; ENST00000324817.6; ENSP00000323720.1; NM_004229.4; NP_004220.2. DR UCSC; uc004dex.5; human. DR AGR; HGNC:2370; -. DR CTD; 9282; -. DR DisGeNET; 9282; -. DR GeneCards; MED14; -. DR HGNC; HGNC:2370; MED14. DR HPA; ENSG00000180182; Low tissue specificity. DR MIM; 300182; gene. DR neXtProt; NX_O60244; -. DR OpenTargets; ENSG00000180182; -. DR PharmGKB; PA26890; -. DR VEuPathDB; HostDB:ENSG00000180182; -. DR eggNOG; KOG1875; Eukaryota. DR GeneTree; ENSGT00390000001021; -. DR HOGENOM; CLU_001928_0_0_1; -. DR InParanoid; O60244; -. DR OMA; GFGRMLN; -. DR OrthoDB; 2873934at2759; -. DR PhylomeDB; O60244; -. DR TreeFam; TF314388; -. DR PathwayCommons; O60244; -. DR Reactome; R-HSA-1989781; PPARA activates gene expression. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation. DR SignaLink; O60244; -. DR SIGNOR; O60244; -. DR BioGRID-ORCS; 9282; 408 hits in 806 CRISPR screens. DR ChiTaRS; MED14; human. DR GeneWiki; MED14; -. DR GenomeRNAi; 9282; -. DR Pharos; O60244; Tbio. DR PRO; PR:O60244; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; O60244; Protein. DR Bgee; ENSG00000180182; Expressed in secondary oocyte and 203 other cell types or tissues. DR ExpressionAtlas; O60244; baseline and differential. DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal. DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0030374; F:nuclear receptor coactivator activity; NAS:UniProtKB. DR GO; GO:0042809; F:nuclear vitamin D receptor binding; NAS:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; NAS:ComplexPortal. DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl. DR InterPro; IPR013947; Mediator_Med14. DR PANTHER; PTHR12809; MEDIATOR COMPLEX SUBUNIT; 1. DR PANTHER; PTHR12809:SF2; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 14; 1. DR Pfam; PF08638; Med14; 1. DR Genevisible; O60244; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Direct protein sequencing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation. FT CHAIN 1..1454 FT /note="Mediator of RNA polymerase II transcription subunit FT 14" FT /id="PRO_0000079357" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 188..566 FT /note="Interaction with STAT2" FT /evidence="ECO:0000269|PubMed:12509459" FT REGION 500..824 FT /note="Interaction with SREBF1" FT /evidence="ECO:0000269|PubMed:15340088" FT REGION 973..1167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 69..73 FT /note="LXXLL motif 1" FT MOTIF 1182..1186 FT /note="LXXLL motif 2" FT COMPBIAS 1011..1050 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1088..1115 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1135..1157 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 617 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163" FT MOD_RES 986 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 1112 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1119 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1128 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1136 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1144 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VARIANT 1325 FT /note="F -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036608" FT CONFLICT 309..310 FT /note="HS -> LT (in Ref. 4; AAD24360)" FT /evidence="ECO:0000305" FT CONFLICT 1265 FT /note="V -> L (in Ref. 1; BAA28626, 2; AAD12725 and 3; FT AAG22547)" FT /evidence="ECO:0000305" FT CONFLICT 1451 FT /note="G -> V (in Ref. 1; BAA28626, 2; AAD12725 and 3; FT AAG22547)" FT /evidence="ECO:0000305" FT HELIX 51..72 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 78..105 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 109..141 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 142..147 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 154..161 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 172..177 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 187..203 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 230..236 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 245..252 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 268..283 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 288..317 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 321..330 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 334..340 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 355..360 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 375..377 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 383..388 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 397..423 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 430..432 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 433..436 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 437..445 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 448..456 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 463..466 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 472..484 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 486..488 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 489..506 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 507..509 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 510..518 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 526..528 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 529..532 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 537..545 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 547..556 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 564..573 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 584..587 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 639..651 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 653..663 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 675..678 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 681..685 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 695..701 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 702..704 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 705..714 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 715..717 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 719..728 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 734..736 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 739..749 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 753..755 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 760..786 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 787..789 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 794..797 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 798..803 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 808..812 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 813..816 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 818..825 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 826..829 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 830..837 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 839..842 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 852..861 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 865..882 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 904..908 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 913..918 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 919..921 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 922..929 FT /evidence="ECO:0007829|PDB:7EMF" FT TURN 930..932 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 933..936 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 939..941 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 959..966 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 1180..1186 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 1206..1225 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 1240..1242 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 1245..1247 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 1249..1253 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 1255..1259 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 1261..1264 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 1277..1288 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 1296..1305 FT /evidence="ECO:0007829|PDB:7EMF" FT HELIX 1312..1324 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 1342..1344 FT /evidence="ECO:0007829|PDB:7EMF" FT STRAND 1358..1360 FT /evidence="ECO:0007829|PDB:7EMF" SQ SEQUENCE 1454 AA; 160607 MW; 144308E3F08D3D9B CRC64; MAPVQLENHQ LVPPGGGGGG SGGPPSAPAP PPPGAAVAAA AAAAASPGYR LSTLIEFLLH RAYSELMVLT DLLPRKSDVE RKIEIVQFAS RTRQLFVRLL ALVKWANNAG KVEKCAMISS FLDQQAILFV DTADRLASLA RDALVHARLP SFAIPYAIDV LTTGSYPRLP TCIRDKIIPP DPITKIEKQA TLHQLNQILR HRLVTTDLPP QLANLTVANG RVKFRVEGEF EATLTVMGDD PDVPWRLLKL EILVEDKETG DGRALVHSMQ ISFIHQLVQS RLFADEKPLQ DMYNCLHSFC LSLQLEVLHS QTLMLIRERW GDLVQVERYH AGKCLSLSVW NQQVLGRKTG TASVHKVTIK IDENDVSKPL QIFHDPPLPA SDSKLVERAM KIDHLSIEKL LIDSVHARAH QKLQELKAIL RGFNANENSS IETALPALVV PILEPCGNSE CLHIFVDLHS GMFQLMLYGL DQATLDDMEK SVNDDMKRII PWIQQLKFWL GQQRCKQSIK HLPTISSETL QLSNYSTHPI GNLSKNKLFI KLTRLPQYYI VVEMLEVPNK PTQLSYKYYF MSVNAADRED SPAMALLLQQ FKENIQDLVF RTKTGKQTRT NAKRKLSDDP CPVESKKTKR AGEMCAFNKV LAHFVAMCDT NMPFVGLRLE LSNLEIPHQG VQVEGDGFSH AIRLLKIPPC KGITEETQKA LDRSLLDCTF RLQGRNNRTW VAELVFANCP LNGTSTREQG PSRHVYLTYE NLLSEPVGGR KVVEMFLNDW NSIARLYECV LEFARSLPDI PAHLNIFSEV RVYNYRKLIL CYGTTKGSSI SIQWNSIHQK FHISLGTVGP NSGCSNCHNT ILHQLQEMFN KTPNVVQLLQ VLFDTQAPLN AINKLPTVPM LGLTQRTNTA YQCFSILPQS STHIRLAFRN MYCIDIYCRS RGVVAIRDGA YSLFDNSKLV EGFYPAPGLK TFLNMFVDSN QDARRRSVNE DDNPPSPIGG DMMDSLISQL QPPPQQQPFP KQPGTSGAYP LTSPPTSYHS TVNQSPSMMH TQSPGNLHAA SSPSGALRAP SPASFVPTPP PSSHGISIGP GASFASPHGT LDPSSPYTMV SPSGRAGNWP GSPQVSGPSP AARMPGMSPA NPSLHSPVPD ASHSPRAGTS SQTMPTNMPP PRKLPQRSWA ASIPTILTHS ALNILLLPSP TPGLVPGLAG SYLCSPLERF LGSVIMRRHL QRIIQQETLQ LINSNEPGVI MFKTDALKCR VALSPKTNQT LQLKVTPENA GQWKPDELQV LEKFFETRVA GPPFKANTLI AFTKLLGAPT HILRDCVHIM KLELFPDQAT QLKWNVQFCL TIPPSAPPIA PPGTPAVVLK SKMLFFLQLT QKTSVPPQEP VSIIVPIIYD MASGTTQQAD IPRQQNSSVA APMMVSNILK RFAEMNPPRQ GECTIFAAVR DLMANLTLPP GGRP //