MED19_HUMAN
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 03-AUG-2022, entry version 126.
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 A0JLT2; Q9NX70: MED29; NbExp=8; IntAct=EBI-394430, EBI-394656;
CC A0JLT2-2; Q86UW9: DTX2; NbExp=3; IntAct=EBI-13288755, EBI-740376;
CC A0JLT2-2; P62993: GRB2; NbExp=3; IntAct=EBI-13288755, EBI-401755;
CC A0JLT2-2; P50747: HLCS; NbExp=3; IntAct=EBI-13288755, EBI-3915568;
CC A0JLT2-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-13288755, EBI-2556193;
CC A0JLT2-2; Q92993: KAT5; NbExp=3; IntAct=EBI-13288755, EBI-399080;
CC A0JLT2-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-13288755, EBI-11742507;
CC A0JLT2-2; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-13288755, EBI-11746523;
CC A0JLT2-2; P17252: PRKCA; NbExp=3; IntAct=EBI-13288755, EBI-1383528;
CC A0JLT2-2; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-13288755, EBI-10226430;
CC A0JLT2-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-13288755, EBI-9090795;
CC A0JLT2-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-13288755, EBI-372899;
CC A0JLT2-2; P61981: YWHAG; NbExp=3; IntAct=EBI-13288755, EBI-359832;
CC A0JLT2-2; P36508: ZNF76; NbExp=3; IntAct=EBI-13288755, EBI-7254550;
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 PDB; 7EMF; EM; 3.50 A; S=1-244.
DR PDB; 7ENA; EM; 4.07 A; s=1-244.
DR PDB; 7ENC; EM; 4.13 A; s=1-244.
DR PDB; 7ENJ; EM; 4.40 A; S=1-244.
DR PDB; 7LBM; EM; 4.80 A; w=1-244.
DR PDB; 7NVR; EM; 4.50 A; m=1-244.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; A0JLT2; -.
DR SMR; A0JLT2; -.
DR BioGRID; 128553; 88.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; A0JLT2; -.
DR DIP; DIP-31467N; -.
DR IntAct; A0JLT2; 137.
DR MINT; A0JLT2; -.
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 PeptideAtlas; A0JLT2; -.
DR PRIDE; A0JLT2; -.
DR ProteomicsDB; 38; -. [A0JLT2-1]
DR ProteomicsDB; 39; -. [A0JLT2-2]
DR TopDownProteomics; A0JLT2-2; -. [A0JLT2-2]
DR Antibodypedia; 43279; 161 antibodies from 21 providers.
DR DNASU; 219541; -.
DR Ensembl; ENST00000337672.9; ENSP00000337340.4; ENSG00000156603.20. [A0JLT2-2]
DR Ensembl; ENST00000645681.2; ENSP00000493863.2; ENSG00000156603.20. [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; ENSG00000156603; Low tissue specificity.
DR MIM; 612385; gene.
DR neXtProt; NX_A0JLT2; -.
DR OpenTargets; ENSG00000156603; -.
DR PharmGKB; PA134926032; -.
DR VEuPathDB; HostDB:ENSG00000156603; -.
DR eggNOG; KOG4043; Eukaryota.
DR GeneTree; ENSGT00390000001774; -.
DR InParanoid; A0JLT2; -.
DR OrthoDB; 1484317at2759; -.
DR PhylomeDB; A0JLT2; -.
DR TreeFam; TF317417; -.
DR PathwayCommons; A0JLT2; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; A0JLT2; -.
DR SIGNOR; A0JLT2; -.
DR BioGRID-ORCS; 219541; 378 hits in 1110 CRISPR screens.
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 oocyte and 192 other tissues.
DR ExpressionAtlas; A0JLT2; baseline and differential.
DR Genevisible; A0JLT2; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IC:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR InterPro; IPR019403; Mediator_Med19_met.
DR PANTHER; PTHR22536; PTHR22536; 1.
DR Pfam; PF10278; Med19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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 REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..226
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|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"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:7EMF"
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
