ID MED19_HUMAN Reviewed; 244 AA. AC A0JLT2; Q8IV02; Q8IZD1; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 24-JUN-2015, entry version 79. DE RecName: Full=Mediator of RNA polymerase II transcription subunit 19; DE AltName: Full=Lung cancer metastasis-related protein 1; DE AltName: Full=Mediator complex subunit 19; GN Name=MED19; Synonyms=LCMR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-205 (ISOFORM 1). RC TISSUE=Brain, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-244 (ISOFORM 1). RA Chen L.A., Tian Q., Liu Y.N., Fan B.X.; RT "Cloning of a metastasis-related gene cDNA from a human lung cancer RT cell line."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP INTERACTION WITH MED10 AND MED31. RX PubMed=12584197; DOI=10.1074/jbc.C300054200; RA Sato S., Tomomori-Sato C., Banks C.A.S., Sorokina I., Parmely T.J., RA Kong S.E., Jin J., Cai Y., Lane W.S., Brower C.S., Conaway R.C., RA Conaway J.W.; RT "Identification of mammalian Mediator subunits with similarities to RT yeast Mediator subunits Srb5, Srb6, Med11, and Rox3."; RL J. Biol. Chem. 278:15123-15127(2003). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RP MEDIATOR 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., RA Conaway J.W., 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 [6] RP IDENTIFICATION BY 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION RP 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). CC -!- FUNCTION: Component of the Mediator complex, a coactivator CC involved in the regulated transcription of nearly all RNA CC polymerase II-dependent genes. Mediator functions as a bridge to CC convey information from gene-specific regulatory proteins to the CC basal RNA polymerase II transcription machinery. Mediator is CC recruited to promoters by direct interactions with regulatory CC proteins and serves as a scaffold for the assembly of a functional CC preinitiation complex with RNA polymerase II and the general CC transcription factors. CC -!- SUBUNIT: Component of the Mediator complex, which is composed of CC MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, CC MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, CC MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CC CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 CC subunits form a distinct module termed the CDK8 module. Mediator CC containing the CDK8 module is less active than Mediator lacking CC this module in supporting transcriptional activation. Individual CC preparations of the Mediator complex lacking one or more distinct CC subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and CC TRAP. {ECO:0000269|PubMed:15175163}. CC -!- INTERACTION: CC Q9NX70:MED29; NbExp=8; IntAct=EBI-394430, EBI-394656; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=A0JLT2-1; Sequence=Displayed; CC Name=2; CC IsoId=A0JLT2-2; Sequence=VSP_028121, VSP_028122; CC Note=No experimental confirmation available.; CC -!- SIMILARITY: Belongs to the Mediator complex subunit 19 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAN16075.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH471076; EAW73775.1; -; Genomic_DNA. DR EMBL; BC009723; AAH09723.1; -; mRNA. DR EMBL; BC037223; AAH37223.1; -; mRNA. DR EMBL; AY148462; AAN16075.1; ALT_INIT; mRNA. DR CCDS; CCDS7966.1; -. [A0JLT2-2] DR RefSeq; NP_703151.1; NM_153450.1. [A0JLT2-2] DR UniGene; Hs.43619; -. DR ProteinModelPortal; A0JLT2; -. DR BioGrid; 128553; 54. DR DIP; DIP-31467N; -. DR IntAct; A0JLT2; 118. DR MINT; MINT-1370291; -. DR STRING; 9606.ENSP00000337340; -. DR PhosphoSite; A0JLT2; -. DR BioMuta; MED19; -. DR MaxQB; A0JLT2; -. DR PaxDb; A0JLT2; -. DR PRIDE; A0JLT2; -. DR Ensembl; ENST00000337672; ENSP00000337340; ENSG00000156603. [A0JLT2-2] DR GeneID; 219541; -. DR KEGG; hsa:219541; -. DR UCSC; uc001nlb.3; human. [A0JLT2-2] DR CTD; 219541; -. DR GeneCards; GC11M057471; -. DR H-InvDB; HIX0026171; -. DR HGNC; HGNC:29600; MED19. DR HPA; HPA039912; -. DR HPA; HPA040860; -. DR MIM; 612385; gene. DR neXtProt; NX_A0JLT2; -. DR PharmGKB; PA134926032; -. DR eggNOG; NOG264473; -. DR GeneTree; ENSGT00390000001774; -. DR HOGENOM; HOG000047323; -. DR HOVERGEN; HBG055317; -. DR InParanoid; A0JLT2; -. DR KO; K15137; -. DR OrthoDB; EOG7XSTG9; -. DR PhylomeDB; A0JLT2; -. DR TreeFam; TF317417; -. DR Reactome; REACT_116145; PPARA activates gene expression. DR Reactome; REACT_27161; Transcriptional regulation of white adipocyte differentiation. DR GenomeRNAi; 219541; -. DR NextBio; 90685; -. DR PRO; PR:A0JLT2; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; A0JLT2; -. DR CleanEx; HS_MED19; -. DR ExpressionAtlas; A0JLT2; baseline and differential. DR Genevisible; A0JLT2; HS. DR GO; GO:0016592; C:mediator complex; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IEA:InterPro. DR InterPro; IPR019403; Mediator_Med19_met. DR Pfam; PF10278; Med19; 1. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Complete proteome; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 244 Mediator of RNA polymerase II FT transcription subunit 19. FT /FTId=PRO_0000304766. FT COMPBIAS 14 53 Pro-rich. FT COMPBIAS 172 222 Lys-rich. FT MOD_RES 226 226 Phosphoserine. FT {ECO:0000269|PubMed:18669648, FT ECO:0000269|PubMed:20068231}. FT VAR_SEQ 191 194 ETPS -> GKPS (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_028121. FT VAR_SEQ 195 244 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_028122. FT CONFLICT 198 198 H -> P (in Ref. 3; AAN16075). FT {ECO:0000305}. SQ SEQUENCE 244 AA; 26273 MW; 9B85721364F33F02 CRC64; MENFTALFGA QADPPPPPTA LGFGPGKPPP PPPPPAGGGP GTAPPPTAAT APPGADKSGA GCGPFYLMRE LPGSTELTGS TNLITHYNLE QAYNKFCGKK VKEKLSNFLP DLPGMIDLPG SHDNSSLRSL IEKPPILSSS FNPITGTMLA GFRLHTGPLP EQCRLMHIQP PKKKNKHKHK QSRTQDPVPP ETPSDSDHKK KKKKKEEDPD RKRKKKEKKK KKNRHSPDHP GMGSSQASSS SSLR //