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Q96HR3 (MED30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of RNA polymerase II transcription subunit 30
Alternative name(s):
Mediator complex subunit 30
TRAP/Mediator complex component TRAP25
Thyroid hormone receptor-associated protein 6
Thyroid hormone receptor-associated protein complex 25 kDa component
Short name=Trap25
Gene names
Name:MED30
Synonyms:THRAP6, TRAP25
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.8

Subunit structure

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. Ref.1 Ref.6 Ref.7

Subcellular location

Nucleus Probable.

Tissue specificity

Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. Ref.1

Sequence similarities

Belongs to the Mediator complex subunit 30 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionActivator
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Inferred from direct assay PubMed 12218053. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

intracellular steroid hormone receptor signaling pathway

Inferred from direct assay PubMed 11867769. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10198638. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10198638. Source: GOC

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 12218053. Source: UniProtKB

   Cellular_componentmediator complex

Inferred from direct assay PubMed 10198638. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10235267. Source: UniProtKB

   Molecular_functionRNA polymerase II transcription cofactor activity

Inferred from direct assay PubMed 10198638. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Non-traceable author statement PubMed 10235266. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21784977. Source: UniProtKB

receptor activity

Inferred from direct assay PubMed 12218053. Source: UniProtKB

thyroid hormone receptor binding

Inferred from direct assay PubMed 10198638. Source: UniProtKB

transcription cofactor activity

Inferred from direct assay PubMed 12218053. Source: UniProtKB

vitamin D receptor binding

Non-traceable author statement PubMed 10235266. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96HR3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96HR3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     113-147: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 178177Mediator of RNA polymerase II transcription subunit 30
PRO_0000239406

Regions

Coiled coil70 – 9425 Potential
Coiled coil133 – 17341 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.10 Ref.11 Ref.12 Ref.13

Natural variations

Alternative sequence113 – 14735Missing in isoform 2.
VSP_053904

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1FD31212EDDF6238

FASTA17820,277
        10         20         30         40         50         60 
MSTPPLAASG MAPGPFAGPQ AQQAAREVNT ASLCRIGQET VQDIVYRTME IFQLLRNMQL 

        70         80         90        100        110        120 
PNGVTYHTGT YQDRLTKLQD NLRQLSVLFR KLRLVYDKCN ENCGGMDPIP VEQLIPYVEE 

       130        140        150        160        170 
DGSKNDDRAG PPRFASEERR EIAEVNKKLK QKNQQLKQIM DQLRNLIWDI NAMLAMRN 

« Hide

Isoform 2 [UniParc].

Checksum: EF5F536FFCDAC22F
Show »

FASTA14316,279

References

« Hide 'large scale' references
[1]"Requirement of TRAP/mediator for both activator-independent and activator-dependent transcription in conjunction with TFIID-associated TAF(II)s."
Baek H.J., Malik S., Qin J., Roeder R.G.
Mol. Cell. Biol. 22:2842-2852(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, FUNCTION, TISSUE SPECIFICITY.
[2]"Identification of MED30 alternative mRNA in human progenitor cells."
Rienzo M., Casamassimi A., Giovane A., Napoli C.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
Tissue: Bone marrow and Peripheral blood.
[3]"DNA sequence and analysis of human chromosome 8."
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. expand/collapse author list , 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.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye.
[5]"Identification of mammalian Mediator subunits with similarities to yeast Mediator subunits Srb5, Srb6, Med11, and Rox3."
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.
J. Biol. Chem. 278:15123-15127(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MED22.
[6]"A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology."
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.
Mol. Cell 14:685-691(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX.
[7]"MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription."
Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T., Roeder R.G.
Mol. Cell 19:89-100(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MED1; MED6; MED12; MED13; MED16; MED17; MED20; MED21 AND MED24, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[8]"Human Mediator enhances basal transcription by facilitating recruitment of transcription factor IIB during preinitiation complex assembly."
Baek H.J., Kang Y.K., Roeder R.G.
J. Biol. Chem. 281:15172-15181(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MED1 AND MED10.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY083305 mRNA. Translation: AAL89787.1.
FM179284 mRNA. Translation: CAQ76893.1.
AC024329 Genomic DNA. No translation available.
AC087361 Genomic DNA. No translation available.
BC008226 mRNA. Translation: AAH08226.1.
CCDSCCDS6323.1.
RefSeqNP_001269915.1. NM_001282986.1. [Q96HR3-2]
NP_542382.1. NM_080651.3. [Q96HR3-1]
UniGeneHs.492612.

3D structure databases

ProteinModelPortalQ96HR3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124707. 36 interactions.
IntActQ96HR3. 10 interactions.
MINTMINT-3053560.
STRING9606.ENSP00000297347.

PTM databases

PhosphoSiteQ96HR3.

Polymorphism databases

DMDM74731968.

Proteomic databases

MaxQBQ96HR3.
PaxDbQ96HR3.
PRIDEQ96HR3.

Protocols and materials databases

DNASU90390.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297347; ENSP00000297347; ENSG00000164758.
ENST00000522839; ENSP00000431051; ENSG00000164758.
GeneID90390.
KEGGhsa:90390.
UCSCuc003yoj.3. human. [Q96HR3-1]

Organism-specific databases

CTD90390.
GeneCardsGC08P118603.
HGNCHGNC:23032. MED30.
MIM610237. gene.
neXtProtNX_Q96HR3.
PharmGKBPA162395656.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87821.
HOGENOMHOG000006885.
HOVERGENHBG107279.
InParanoidQ96HR3.
KOK15143.
OMAGSKHDDR.
OrthoDBEOG7C5MB0.
PhylomeDBQ96HR3.
TreeFamTF324588.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ96HR3.
BgeeQ96HR3.
CleanExHS_MED30.
GenevestigatorQ96HR3.

Family and domain databases

InterProIPR021019. Mediator_Med30_met.
[Graphical view]
PfamPF11315. Med30. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMED30.
GenomeRNAi90390.
NextBio35483018.
PROQ96HR3.
SOURCESearch...

Entry information

Entry nameMED30_HUMAN
AccessionPrimary (citable) accession number: Q96HR3
Secondary accession number(s): C6GKU9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM