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-JAN-2024, entry version 134. 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}; 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; CCDS7966.3; -. [A0JLT2-2] DR CCDS; CCDS86203.2; -. [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 PDB; 8GXQ; EM; 5.04 A; s=1-244. DR PDB; 8GXS; EM; 4.16 A; s=1-244. 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; A0JLT2; -. 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; A0JLT2; -. DR BioGRID; 128553; 101. DR ComplexPortal; CPX-3227; Core mediator complex. DR CORUM; A0JLT2; -. DR DIP; DIP-31467N; -. DR IntAct; A0JLT2; 139. DR MINT; A0JLT2; -. DR STRING; 9606.ENSP00000498791; -. DR GlyGen; A0JLT2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; A0JLT2; -. DR PhosphoSitePlus; A0JLT2; -. DR BioMuta; MED19; -. DR EPD; A0JLT2; -. DR jPOST; A0JLT2; -. DR MassIVE; A0JLT2; -. DR MaxQB; A0JLT2; -. DR PaxDb; 9606-ENSP00000337340; -. DR PeptideAtlas; A0JLT2; -. DR ProteomicsDB; 38; -. [A0JLT2-1] DR ProteomicsDB; 39; -. [A0JLT2-2] DR Pumba; A0JLT2; -. DR TopDownProteomics; A0JLT2-2; -. [A0JLT2-2] DR Antibodypedia; 43279; 201 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 AGR; HGNC:29600; -. 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; 3560223at2759; -. 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; 390 hits in 1182 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 194 other cell types or tissues. DR ExpressionAtlas; A0JLT2; baseline and differential. 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 by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; NAS:ComplexPortal. DR InterPro; IPR019403; Mediator_Med19_met. DR PANTHER; PTHR22536; LUNG CANCER METASTASIS-RELATED LCMR1 PROTEIN; 1. DR PANTHER; PTHR22536:SF1; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 19; 1. DR Pfam; PF10278; Med19; 1. DR Genevisible; A0JLT2; HS. 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 //