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Mediator of RNA polymerase II transcription subunit 30 (Mediator complex subunit 30) (TRAP/Mediator complex component TRAP25) (Thyroid hormone receptor-associated protein 6) (Thyroid hormone receptor-associated protein complex 25 kDa component) (Trap25)

 MED30_HUMAN             Reviewed;         178 AA.
Q96HR3; C6GKU9;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 133.
RecName: Full=Mediator of RNA polymerase II transcription subunit 30;
AltName: Full=Mediator complex subunit 30;
AltName: Full=TRAP/Mediator complex component TRAP25;
AltName: Full=Thyroid hormone receptor-associated protein 6;
AltName: Full=Thyroid hormone receptor-associated protein complex 25 kDa component;
Short=Trap25;
Name=MED30; Synonyms=THRAP6, TRAP25;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, FUNCTION, AND
TISSUE SPECIFICITY.
PubMed=11909976; DOI=10.1128/MCB.22.8.2842-2852.2002;
Baek H.J., Malik S., Qin J., Roeder R.G.;
"Requirement of TRAP/mediator for both activator-independent and
activator-dependent transcription in conjunction with TFIID-associated
TAF(II)s.";
Mol. Cell. Biol. 22:2842-2852(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
TISSUE=Bone marrow, and Peripheral blood;
Rienzo M., Casamassimi A., Giovane A., Napoli C.;
"Identification of MED30 alternative mRNA in human progenitor cells.";
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH MED22.
PubMed=12584197; DOI=10.1074/jbc.C300054200;
Sato S., Tomomori-Sato C., Banks C.A.S., Sorokina I., Parmely T.J.,
Kong S.E., Jin J., Cai Y., Lane W.S., Brower C.S., Conaway R.C.,
Conaway J.W.;
"Identification of mammalian Mediator subunits with similarities to
yeast Mediator subunits Srb5, Srb6, Med11, and Rox3.";
J. Biol. Chem. 278:15123-15127(2003).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
MEDIATOR COMPLEX.
PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P.,
Conaway J.W., Conaway R.C.;
"A set of consensus mammalian mediator subunits identified by
multidimensional protein identification technology.";
Mol. Cell 14:685-691(2004).
[7]
INTERACTION WITH MED1; MED6; MED12; MED13; MED16; MED17; MED20; MED21
AND MED24, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
MEDIATOR COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA
POLYMERASE II.
PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
Roeder R.G.;
"MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
enriched in RNA polymerase II and is required for ER-mediated
transcription.";
Mol. Cell 19:89-100(2005).
[8]
FUNCTION, AND INTERACTION WITH MED1 AND MED10.
PubMed=16595664; DOI=10.1074/jbc.M601983200;
Baek H.J., Kang Y.K., Roeder R.G.;
"Human Mediator enhances basal transcription by facilitating
recruitment of transcription factor IIB during preinitiation complex
assembly.";
J. Biol. Chem. 281:15172-15181(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Component of the Mediator complex, a coactivator
involved in the regulated transcription of nearly all RNA
polymerase II-dependent genes. Mediator functions as a bridge to
convey information from gene-specific regulatory proteins to the
basal RNA polymerase II transcription machinery. Mediator is
recruited to promoters by direct interactions with regulatory
proteins and serves as a scaffold for the assembly of a functional
preinitiation complex with RNA polymerase II and the general
transcription factors. {ECO:0000269|PubMed:11909976,
ECO:0000269|PubMed:16595664}.
-!- SUBUNIT: Component of the Mediator complex, which is composed of
MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
subunits form a distinct module termed the CDK8 module. Mediator
containing the CDK8 module is less active than Mediator lacking
this module in supporting transcriptional activation. Individual
preparations of the Mediator complex lacking one or more distinct
subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
TRAP. {ECO:0000269|PubMed:11909976, ECO:0000269|PubMed:15175163,
ECO:0000269|PubMed:15989967}.
-!- INTERACTION:
Q8NF50-2:DOCK8; NbExp=3; IntAct=EBI-394659, EBI-10174653;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-394659, EBI-10172052;
Q9H204:MED28; NbExp=6; IntAct=EBI-394659, EBI-514199;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96HR3-1; Sequence=Displayed;
Name=2;
IsoId=Q96HR3-2; Sequence=VSP_053904;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
lung, pancreas, placenta and skeletal muscle.
{ECO:0000269|PubMed:11909976}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 30 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY083305; AAL89787.1; -; mRNA.
EMBL; FM179284; CAQ76893.1; -; mRNA.
EMBL; AC024329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008226; AAH08226.1; -; mRNA.
CCDS; CCDS6323.1; -. [Q96HR3-1]
CCDS; CCDS64959.1; -. [Q96HR3-2]
RefSeq; NP_001269915.1; NM_001282986.1. [Q96HR3-2]
RefSeq; NP_542382.1; NM_080651.3. [Q96HR3-1]
UniGene; Hs.492612; -.
ProteinModelPortal; Q96HR3; -.
BioGrid; 124707; 48.
CORUM; Q96HR3; -.
IntAct; Q96HR3; 18.
MINT; MINT-3053560; -.
STRING; 9606.ENSP00000297347; -.
iPTMnet; Q96HR3; -.
PhosphoSitePlus; Q96HR3; -.
DMDM; 74731968; -.
EPD; Q96HR3; -.
MaxQB; Q96HR3; -.
PaxDb; Q96HR3; -.
PeptideAtlas; Q96HR3; -.
PRIDE; Q96HR3; -.
DNASU; 90390; -.
Ensembl; ENST00000297347; ENSP00000297347; ENSG00000164758. [Q96HR3-1]
Ensembl; ENST00000522839; ENSP00000431051; ENSG00000164758. [Q96HR3-2]
GeneID; 90390; -.
KEGG; hsa:90390; -.
UCSC; uc003yoj.4; human. [Q96HR3-1]
CTD; 90390; -.
DisGeNET; 90390; -.
EuPathDB; HostDB:ENSG00000164758.7; -.
GeneCards; MED30; -.
HGNC; HGNC:23032; MED30.
HPA; HPA045767; -.
MIM; 610237; gene.
neXtProt; NX_Q96HR3; -.
OpenTargets; ENSG00000164758; -.
PharmGKB; PA162395656; -.
eggNOG; ENOG410IITZ; Eukaryota.
eggNOG; ENOG4110Q3G; LUCA.
GeneTree; ENSGT00390000010887; -.
HOGENOM; HOG000006885; -.
HOVERGEN; HBG107279; -.
InParanoid; Q96HR3; -.
KO; K15143; -.
OMA; CNENCAG; -.
OrthoDB; EOG091G0NPP; -.
PhylomeDB; Q96HR3; -.
TreeFam; TF324588; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-212436; Generic Transcription Pathway.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
ChiTaRS; MED30; human.
GeneWiki; MED30; -.
GenomeRNAi; 90390; -.
PRO; PR:Q96HR3; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164758; -.
CleanEx; HS_MED30; -.
Genevisible; Q96HR3; HS.
GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; NAS:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
GO; GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
InterPro; IPR021019; Mediator_Med30_met.
Pfam; PF11315; Med30; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Coiled coil;
Complete proteome; Nucleus; Reference proteome; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378}.
CHAIN 2 178 Mediator of RNA polymerase II
transcription subunit 30.
/FTId=PRO_0000239406.
COILED 70 94 {ECO:0000255}.
COILED 133 173 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378}.
VAR_SEQ 113 147 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_053904.
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


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