MED14_HUMAN
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 03-AUG-2022, entry version 183.
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; 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}.
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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 PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; O60244; -.
DR SMR; O60244; -.
DR BioGRID; 114699; 159.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; O60244; -.
DR DIP; DIP-31460N; -.
DR IntAct; O60244; 64.
DR MINT; O60244; -.
DR STRING; 9606.ENSP00000323720; -.
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; O60244; -.
DR PeptideAtlas; O60244; -.
DR PRIDE; O60244; -.
DR ProteomicsDB; 49278; -.
DR Antibodypedia; 10773; 165 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 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; SPAGSFM; -.
DR OrthoDB; 1215335at2759; -.
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; 372 hits in 727 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 201 other tissues.
DR ExpressionAtlas; O60244; baseline and differential.
DR Genevisible; O60244; HS.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR InterPro; IPR013947; Mediator_Med14.
DR PANTHER; PTHR12809; PTHR12809; 1.
DR Pfam; PF08638; Med14; 1.
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
