MED30_HUMAN
ID MED30_HUMAN Reviewed; 178 AA.
AC Q96HR3; C6GKU9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 30;
DE AltName: Full=Mediator complex subunit 30;
DE AltName: Full=TRAP/Mediator complex component TRAP25;
DE AltName: Full=Thyroid hormone receptor-associated protein 6;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 25 kDa component;
DE Short=Trap25;
GN Name=MED30; Synonyms=THRAP6, TRAP25;
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 [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11909976; DOI=10.1128/mcb.22.8.2842-2852.2002;
RA Baek H.J., Malik S., Qin J., Roeder R.G.;
RT "Requirement of TRAP/mediator for both activator-independent and activator-
RT dependent transcription in conjunction with TFIID-associated TAF(II)s.";
RL Mol. Cell. Biol. 22:2842-2852(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Bone marrow, and Peripheral blood;
RA Rienzo M., Casamassimi A., Giovane A., Napoli C.;
RT "Identification of MED30 alternative mRNA in human progenitor cells.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [5]
RP INTERACTION WITH MED22.
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 [6]
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 [7]
RP INTERACTION WITH MED1; MED6; MED12; MED13; MED16; MED17; MED20; MED21 AND
RP MED24, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND ASSOCIATION OF THE MEDIATOR 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 [8]
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 [9]
RP IDENTIFICATION BY 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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. {ECO:0000269|PubMed:11909976,
CC ECO:0000269|PubMed:16595664}.
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:11909976, ECO:0000269|PubMed:15175163,
CC ECO:0000269|PubMed:15989967}.
CC -!- INTERACTION:
CC Q96HR3; Q8NF50-2: DOCK8; NbExp=3; IntAct=EBI-394659, EBI-10174653;
CC Q96HR3; O14964: HGS; NbExp=5; IntAct=EBI-394659, EBI-740220;
CC Q96HR3; P42858: HTT; NbExp=3; IntAct=EBI-394659, EBI-466029;
CC Q96HR3; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-394659, EBI-9091197;
CC Q96HR3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-394659, EBI-10172052;
CC Q96HR3; Q9H204: MED28; NbExp=6; IntAct=EBI-394659, EBI-514199;
CC Q96HR3; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-394659, EBI-3911716;
CC Q96HR3; Q9Y5B8: NME7; NbExp=5; IntAct=EBI-394659, EBI-744782;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96HR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HR3-2; Sequence=VSP_053904;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:11909976}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 30 family.
CC {ECO:0000305}.
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DR EMBL; AY083305; AAL89787.1; -; mRNA.
DR EMBL; FM179284; CAQ76893.1; -; mRNA.
DR EMBL; AC024329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008226; AAH08226.1; -; mRNA.
DR CCDS; CCDS6323.1; -. [Q96HR3-1]
DR CCDS; CCDS64959.1; -. [Q96HR3-2]
DR RefSeq; NP_001269915.1; NM_001282986.1. [Q96HR3-2]
DR RefSeq; NP_542382.1; NM_080651.3. [Q96HR3-1]
DR PDB; 7EMF; EM; 3.50 A; 3=1-178.
DR PDB; 7ENA; EM; 4.07 A; l=1-178.
DR PDB; 7ENC; EM; 4.13 A; l=1-178.
DR PDB; 7ENJ; EM; 4.40 A; 3=1-178.
DR PDB; 7LBM; EM; 4.80 A; q=1-178.
DR PDB; 7NVR; EM; 4.50 A; s=1-178.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q96HR3; -.
DR SMR; Q96HR3; -.
DR BioGRID; 124707; 79.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q96HR3; -.
DR IntAct; Q96HR3; 58.
DR MINT; Q96HR3; -.
DR STRING; 9606.ENSP00000297347; -.
DR GlyGen; Q96HR3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96HR3; -.
DR PhosphoSitePlus; Q96HR3; -.
DR BioMuta; MED30; -.
DR DMDM; 74731968; -.
DR EPD; Q96HR3; -.
DR jPOST; Q96HR3; -.
DR MassIVE; Q96HR3; -.
DR MaxQB; Q96HR3; -.
DR PaxDb; Q96HR3; -.
DR PeptideAtlas; Q96HR3; -.
DR PRIDE; Q96HR3; -.
DR ProteomicsDB; 7605; -.
DR ProteomicsDB; 76778; -. [Q96HR3-1]
DR Antibodypedia; 26728; 202 antibodies from 25 providers.
DR DNASU; 90390; -.
DR Ensembl; ENST00000297347.7; ENSP00000297347.3; ENSG00000164758.7. [Q96HR3-1]
DR Ensembl; ENST00000522839.1; ENSP00000431051.1; ENSG00000164758.7. [Q96HR3-2]
DR GeneID; 90390; -.
DR KEGG; hsa:90390; -.
DR MANE-Select; ENST00000297347.7; ENSP00000297347.3; NM_080651.4; NP_542382.1.
DR UCSC; uc003yoj.4; human. [Q96HR3-1]
DR CTD; 90390; -.
DR DisGeNET; 90390; -.
DR GeneCards; MED30; -.
DR HGNC; HGNC:23032; MED30.
DR HPA; ENSG00000164758; Low tissue specificity.
DR MIM; 610237; gene.
DR neXtProt; NX_Q96HR3; -.
DR OpenTargets; ENSG00000164758; -.
DR PharmGKB; PA162395656; -.
DR VEuPathDB; HostDB:ENSG00000164758; -.
DR eggNOG; ENOG502QV3C; Eukaryota.
DR GeneTree; ENSGT00390000010887; -.
DR HOGENOM; CLU_074190_1_1_1; -.
DR InParanoid; Q96HR3; -.
DR OMA; KHDDRGV; -.
DR OrthoDB; 1549016at2759; -.
DR PhylomeDB; Q96HR3; -.
DR TreeFam; TF324588; -.
DR PathwayCommons; Q96HR3; -.
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; Q96HR3; -.
DR SIGNOR; Q96HR3; -.
DR BioGRID-ORCS; 90390; 777 hits in 1091 CRISPR screens.
DR ChiTaRS; MED30; human.
DR GeneWiki; MED30; -.
DR GenomeRNAi; 90390; -.
DR Pharos; Q96HR3; Tbio.
DR PRO; PR:Q96HR3; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96HR3; protein.
DR Bgee; ENSG00000164758; Expressed in oocyte and 188 other tissues.
DR Genevisible; Q96HR3; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; NAS:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA: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:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
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:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR InterPro; IPR021019; Mediator_Med30_met.
DR PANTHER; PTHR31705; PTHR31705; 1.
DR Pfam; PF11315; Med30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Coiled coil;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..178
FT /note="Mediator of RNA polymerase II transcription subunit
FT 30"
FT /id="PRO_0000239406"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..94
FT /evidence="ECO:0000255"
FT COILED 133..173
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 113..147
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053904"
FT HELIX 30..57
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 70..101
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 137..175
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 178 AA; 20277 MW; 1FD31212EDDF6238 CRC64;
MSTPPLAASG MAPGPFAGPQ AQQAAREVNT ASLCRIGQET VQDIVYRTME IFQLLRNMQL
PNGVTYHTGT YQDRLTKLQD NLRQLSVLFR KLRLVYDKCN ENCGGMDPIP VEQLIPYVEE
DGSKNDDRAG PPRFASEERR EIAEVNKKLK QKNQQLKQIM DQLRNLIWDI NAMLAMRN
