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Q9H944

- MED20_HUMAN

UniProt

Q9H944 - MED20_HUMAN

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Protein

Mediator of RNA polymerase II transcription subunit 20

Gene
MED20, TRFP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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.

GO - Molecular functioni

  1. DNA-directed RNA polymerase activity Source: UniProtKB
  2. protein binding Source: IntAct
  3. RNA polymerase II transcription cofactor activity Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  3. transcription, DNA-templated Source: UniProtKB
  4. transcription from RNA polymerase II promoter Source: ProtInc
  5. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_12627. Generic Transcription Pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 20
Alternative name(s):
Mediator complex subunit 20
TRF-proximal protein homolog
Short name:
hTRFP
Gene namesi
Name:MED20
Synonyms:TRFP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:16840. MED20.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. mediator complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162395472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Mediator of RNA polymerase II transcription subunit 20PRO_0000065731Add
BLAST

Proteomic databases

MaxQBiQ9H944.
PaxDbiQ9H944.
PeptideAtlasiQ9H944.
PRIDEiQ9H944.

PTM databases

PhosphoSiteiQ9H944.

Expressioni

Gene expression databases

ArrayExpressiQ9H944.
BgeeiQ9H944.
CleanExiHS_MED20.
GenevestigatoriQ9H944.

Organism-specific databases

HPAiHPA040717.

Interactioni

Subunit structurei

Interacts with PPARG By similarity. 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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED29Q9NX705EBI-394644,EBI-394656

Protein-protein interaction databases

BioGridi114862. 24 interactions.
IntActiQ9H944. 11 interactions.
MINTiMINT-275845.
STRINGi9606.ENSP00000265350.

Structurei

3D structure databases

ProteinModelPortaliQ9H944.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG268717.
HOGENOMiHOG000290707.
HOVERGENiHBG106543.
InParanoidiQ9H944.
KOiK13528.
OMAiKSHFQNA.
OrthoDBiEOG7XSTFN.
PhylomeDBiQ9H944.
TreeFamiTF315156.

Family and domain databases

InterProiIPR013921. Mediator_Med20.
[Graphical view]
PfamiPF08612. Med20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H944-1 [UniParc]FASTAAdd to Basket

« Hide

MGVTCVSQMP VAEGKSVQQT VELLTRKLEM LGAEKQGTFC VDCETYHTAA    50
STLGSQGQTG KLMYVMHNSE YPLSCFALFE NGPCLIADTN FDVLMVKLKG 100
FFQSAKASKI ETRGTRYQYC DFLVKVGTVT MGPSARGISV EVEYGPCVVA 150
SDCWSLLLEF LQSFLGSHTP GAPAVFGNRH DAVYGPADTM VQYMELFNKI 200
RKQQQVPVAG IR 212
Length:212
Mass (Da):23,222
Last modified:March 1, 2001 - v1
Checksum:i5AA7A39981EB1498
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1363SAR → VP in AAD16169. 1 Publication
Sequence conflicti206 – 2072Missing in AAD16169. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF097725 mRNA. Translation: AAD16169.1.
AK023092 mRNA. Translation: BAB14399.1.
AL160163 Genomic DNA. Translation: CAI23487.1.
BC012618 mRNA. Translation: AAH12618.1.
BC019866 mRNA. Translation: AAH19866.1.
BC032552 mRNA. Translation: AAH32552.1.
BC040950 mRNA. Translation: AAH40950.1.
AL050196 mRNA. Translation: CAB43314.1.
CCDSiCCDS4862.1.
PIRiT08801.
RefSeqiNP_004266.2. NM_004275.3.
UniGeneiHs.278434.

Genome annotation databases

EnsembliENST00000265350; ENSP00000265350; ENSG00000124641.
GeneIDi9477.
KEGGihsa:9477.
UCSCiuc003orj.3. human.

Polymorphism databases

DMDMi29428258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF097725 mRNA. Translation: AAD16169.1 .
AK023092 mRNA. Translation: BAB14399.1 .
AL160163 Genomic DNA. Translation: CAI23487.1 .
BC012618 mRNA. Translation: AAH12618.1 .
BC019866 mRNA. Translation: AAH19866.1 .
BC032552 mRNA. Translation: AAH32552.1 .
BC040950 mRNA. Translation: AAH40950.1 .
AL050196 mRNA. Translation: CAB43314.1 .
CCDSi CCDS4862.1.
PIRi T08801.
RefSeqi NP_004266.2. NM_004275.3.
UniGenei Hs.278434.

3D structure databases

ProteinModelPortali Q9H944.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114862. 24 interactions.
IntActi Q9H944. 11 interactions.
MINTi MINT-275845.
STRINGi 9606.ENSP00000265350.

PTM databases

PhosphoSitei Q9H944.

Polymorphism databases

DMDMi 29428258.

Proteomic databases

MaxQBi Q9H944.
PaxDbi Q9H944.
PeptideAtlasi Q9H944.
PRIDEi Q9H944.

Protocols and materials databases

DNASUi 9477.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265350 ; ENSP00000265350 ; ENSG00000124641 .
GeneIDi 9477.
KEGGi hsa:9477.
UCSCi uc003orj.3. human.

Organism-specific databases

CTDi 9477.
GeneCardsi GC06M041877.
HGNCi HGNC:16840. MED20.
HPAi HPA040717.
MIMi 612915. gene.
neXtProti NX_Q9H944.
PharmGKBi PA162395472.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG268717.
HOGENOMi HOG000290707.
HOVERGENi HBG106543.
InParanoidi Q9H944.
KOi K13528.
OMAi KSHFQNA.
OrthoDBi EOG7XSTFN.
PhylomeDBi Q9H944.
TreeFami TF315156.

Enzyme and pathway databases

Reactomei REACT_116145. PPARA activates gene expression.
REACT_12627. Generic Transcription Pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSi MED20. human.
GenomeRNAii 9477.
NextBioi 35516.
PROi Q9H944.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H944.
Bgeei Q9H944.
CleanExi HS_MED20.
Genevestigatori Q9H944.

Family and domain databases

InterProi IPR013921. Mediator_Med20.
[Graphical view ]
Pfami PF08612. Med20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human homologue of Drosophila TRF-proximal protein is associated with an RNA polymerase II-SRB complex."
    Xiao H., Tao Y., Roeder R.G.
    J. Biol. Chem. 274:3937-3940(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-26; 36-51 AND 205-212, INTERACTION WITH RNA POLYMERASE II AND MED21.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [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].
    Tissue: Liver, Prostate, Testis and Uterus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-212.
    Tissue: Uterus.
  6. "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 MED18.
  7. "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.
  8. "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; MED18; MED21; MED28; MED29 AND MED31, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMED20_HUMAN
AccessioniPrimary (citable) accession number: Q9H944
Secondary accession number(s): O95821, Q5T8J4, Q9Y429
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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