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   26-FEB-2020, entry version 114.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., 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 (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [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 project:
RT   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 cell
RT   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 yeast
RT   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 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   [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., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, 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   [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., 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   [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 BY
RP   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-226, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [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).
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.
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC       MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC       MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC       MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC       CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC       module termed the CDK8 module. Mediator containing the CDK8 module is
CC       less active than Mediator lacking this module in supporting
CC       transcriptional activation. Individual preparations of the Mediator
CC       complex lacking one or more distinct subunits have been variously
CC       termed ARC, CRSP, DRIP, PC2, SMCC and TRAP.
CC       {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   -!- 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};
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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; CCDS7966.2; -. [A0JLT2-2]
DR   CCDS; CCDS86203.1; -. [A0JLT2-1]
DR   RefSeq; NP_001304007.1; NM_001317078.1.
DR   RefSeq; NP_703151.2; NM_153450.2. [A0JLT2-2]
DR   BioGrid; 128553; 58.
DR   ComplexPortal; CPX-3227; Core mediator complex.
DR   CORUM; A0JLT2; -.
DR   DIP; DIP-31467N; -.
DR   IntAct; A0JLT2; 128.
DR   STRING; 9606.ENSP00000337340; -.
DR   iPTMnet; A0JLT2; -.
DR   PhosphoSitePlus; A0JLT2; -.
DR   BioMuta; MED19; -.
DR   EPD; A0JLT2; -.
DR   jPOST; A0JLT2; -.
DR   MassIVE; A0JLT2; -.
DR   MaxQB; A0JLT2; -.
DR   PaxDb; A0JLT2; -.
DR   PRIDE; A0JLT2; -.
DR   ProteomicsDB; 38; -. [A0JLT2-1]
DR   ProteomicsDB; 39; -. [A0JLT2-2]
DR   TopDownProteomics; A0JLT2-2; -. [A0JLT2-2]
DR   Ensembl; ENST00000337672; ENSP00000337340; ENSG00000156603. [A0JLT2-2]
DR   Ensembl; ENST00000645681; ENSP00000493863; ENSG00000156603. [A0JLT2-2]
DR   GeneID; 219541; -.
DR   KEGG; hsa:219541; -.
DR   UCSC; uc001nlb.4; human. [A0JLT2-1]
DR   CTD; 219541; -.
DR   DisGeNET; 219541; -.
DR   GeneCards; MED19; -.
DR   HGNC; HGNC:29600; MED19.
DR   HPA; HPA039912; -.
DR   HPA; HPA040860; -.
DR   MIM; 612385; gene.
DR   neXtProt; NX_A0JLT2; -.
DR   OpenTargets; ENSG00000156603; -.
DR   PharmGKB; PA134926032; -.
DR   eggNOG; KOG4043; Eukaryota.
DR   eggNOG; ENOG4111KKA; LUCA.
DR   GeneTree; ENSGT00390000001774; -.
DR   InParanoid; A0JLT2; -.
DR   KO; K15137; -.
DR   OrthoDB; 106971at2759; -.
DR   PhylomeDB; A0JLT2; -.
DR   TreeFam; TF317417; -.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR   ChiTaRS; MED19; human.
DR   GenomeRNAi; 219541; -.
DR   Pharos; A0JLT2; Tbio.
DR   PRO; PR:A0JLT2; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; A0JLT2; protein.
DR   Bgee; ENSG00000156603; Expressed in epithelium of mammary gland and 207 other tissues.
DR   ExpressionAtlas; A0JLT2; baseline and differential.
DR   Genevisible; A0JLT2; HS.
DR   GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR019403; Mediator_Med19_met.
DR   PANTHER; PTHR22536; PTHR22536; 1.
DR   Pfam; PF10278; Med19; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..244
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   19"
FT                   /id="PRO_0000304766"
FT   COMPBIAS        14..53
FT                   /note="Pro-rich"
FT   COMPBIAS        172..222
FT                   /note="Lys-rich"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
FT   VAR_SEQ         191..194
FT                   /note="ETPS -> GKPS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028121"
FT   VAR_SEQ         195..244
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028122"
FT   CONFLICT        198
FT                   /note="H -> P (in Ref. 3; AAN16075)"
FT                   /evidence="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
//