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Protein

Mediator of RNA polymerase II transcription subunit 30

Gene

Med30

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

  1. receptor activity Source: MGI
  2. RNA polymerase II transcription cofactor activity Source: MGI
  3. thyroid hormone receptor binding Source: MGI
  4. transcription cofactor activity Source: MGI

GO - Biological processi

  1. androgen receptor signaling pathway Source: MGI
  2. intracellular steroid hormone receptor signaling pathway Source: MGI
  3. positive regulation of transcription, DNA-templated Source: MGI
  4. regulation of transcription from RNA polymerase II promoter Source: MGI
  5. stem cell maintenance Source: MGI
  6. transcription initiation from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_275829. Generic Transcription Pathway.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 30
Alternative name(s):
Mediator complex subunit 30
Thyroid hormone receptor-associated protein 6
Thyroid hormone receptor-associated protein complex 25 kDa component
Short name:
Trap25
Gene namesi
Name:Med30
Synonyms:Thrap6, Trap25
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1917040. Med30.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. mediator complex Source: MGI
  2. nucleoplasm Source: Reactome
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 178177Mediator of RNA polymerase II transcription subunit 30PRO_0000239407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CQI9.
PaxDbiQ9CQI9.
PRIDEiQ9CQI9.

PTM databases

PhosphoSiteiQ9CQI9.

Expressioni

Gene expression databases

BgeeiQ9CQI9.
CleanExiMM_MED30.
GenevestigatoriQ9CQI9.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MED17Q9NVC62EBI-309220,EBI-394562From a different organism.
Med20Q9R0X02EBI-309220,EBI-398698
MED22Q155286EBI-309220,EBI-394687From a different organism.
MED27Q6P2C82EBI-309220,EBI-394603From a different organism.
MED28Q9H2042EBI-309220,EBI-514199From a different organism.
MED29Q9NX702EBI-309220,EBI-394656From a different organism.
Med8Q9D7W52EBI-309220,EBI-7990252

Protein-protein interaction databases

BioGridi213682. 2 interactions.
IntActiQ9CQI9. 14 interactions.
MINTiMINT-217060.
STRINGi10090.ENSMUSP00000042204.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili134 – 17340Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the Mediator complex subunit 30 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG87821.
GeneTreeiENSGT00390000010887.
HOGENOMiHOG000006885.
HOVERGENiHBG107279.
InParanoidiQ9CQI9.
KOiK15143.
OMAiDIVLRTM.
OrthoDBiEOG7C5MB0.
PhylomeDBiQ9CQI9.
TreeFamiTF324588.

Family and domain databases

InterProiIPR021019. Mediator_Med30_met.
[Graphical view]
PfamiPF11315. Med30. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPPLAPTG MASGPFGGPQ AQQAAREVNT ATLCRIGQET VQDIVYRTME
60 70 80 90 100
IFQLLRNMQL PNGVTYHTGT YQDRLTKLQD HLRQLSILFR KLRLVYDKCN
110 120 130 140 150
ENCGGMDPIP VEQLIPYVDE DGSKNDDRAG PPRFASEERR EIVEVNKKLK
160 170
QKNQQLKQIM DQLRNLIWDI NAMLAMRN
Length:178
Mass (Da):20,358
Last modified:May 31, 2001 - v1
Checksum:i8766D3C929C1E98D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007739 mRNA. Translation: BAB25226.1.
AK011104 mRNA. Translation: BAB27401.1.
AK146250 mRNA. Translation: BAE27012.1.
BC020113 mRNA. Translation: AAH20113.1.
CCDSiCCDS27465.1.
RefSeqiNP_081488.1. NM_027212.2.
UniGeneiMm.195562.

Genome annotation databases

EnsembliENSMUST00000037115; ENSMUSP00000042204; ENSMUSG00000038622.
GeneIDi69790.
KEGGimmu:69790.
UCSCiuc007vrg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007739 mRNA. Translation: BAB25226.1.
AK011104 mRNA. Translation: BAB27401.1.
AK146250 mRNA. Translation: BAE27012.1.
BC020113 mRNA. Translation: AAH20113.1.
CCDSiCCDS27465.1.
RefSeqiNP_081488.1. NM_027212.2.
UniGeneiMm.195562.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213682. 2 interactions.
IntActiQ9CQI9. 14 interactions.
MINTiMINT-217060.
STRINGi10090.ENSMUSP00000042204.

PTM databases

PhosphoSiteiQ9CQI9.

Proteomic databases

MaxQBiQ9CQI9.
PaxDbiQ9CQI9.
PRIDEiQ9CQI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037115; ENSMUSP00000042204; ENSMUSG00000038622.
GeneIDi69790.
KEGGimmu:69790.
UCSCiuc007vrg.1. mouse.

Organism-specific databases

CTDi90390.
MGIiMGI:1917040. Med30.

Phylogenomic databases

eggNOGiNOG87821.
GeneTreeiENSGT00390000010887.
HOGENOMiHOG000006885.
HOVERGENiHBG107279.
InParanoidiQ9CQI9.
KOiK15143.
OMAiDIVLRTM.
OrthoDBiEOG7C5MB0.
PhylomeDBiQ9CQI9.
TreeFamiTF324588.

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_275829. Generic Transcription Pathway.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

NextBioi330352.
PROiQ9CQI9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQI9.
CleanExiMM_MED30.
GenevestigatoriQ9CQI9.

Family and domain databases

InterProiIPR021019. Mediator_Med30_met.
[Graphical view]
PfamiPF11315. Med30. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Liver and Pancreas.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiMED30_MOUSE
AccessioniPrimary (citable) accession number: Q9CQI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2006
Last sequence update: May 31, 2001
Last modified: March 31, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.