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Protein

Mediator of RNA polymerase II transcription subunit 4

Gene

MED4

Organism
Homo sapiens (Human)
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.

GO - Molecular functioni

  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • receptor activity Source: UniProtKB
  • RNA polymerase II transcription cofactor activity Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB
  • transcription cofactor activity Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

GO - Biological processi

  • androgen receptor signaling pathway Source: UniProtKB
  • intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription initiation from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-212436. Generic Transcription Pathway.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 4
Alternative name(s):
Activator-recruited cofactor 36 kDa component
Short name:
ARC36
Mediator complex subunit 4
TRAP/SMCC/PC2 subunit p36 subunit
Vitamin D3 receptor-interacting protein complex 36 kDa component
Short name:
DRIP36
Gene namesi
Name:MED4
Synonyms:ARC36, DRIP36, VDRIP
ORF Names:HSPC126
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:17903. MED4.

Subcellular locationi

GO - Cellular componenti

  • core mediator complex Source: GO_Central
  • mediator complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134877001.

Polymorphism and mutation databases

DMDMi29840770.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 270269Mediator of RNA polymerase II transcription subunit 4PRO_0000096383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei32 – 321PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NPJ6.
MaxQBiQ9NPJ6.
PaxDbiQ9NPJ6.
PRIDEiQ9NPJ6.

PTM databases

iPTMnetiQ9NPJ6.
PhosphoSiteiQ9NPJ6.

Expressioni

Gene expression databases

BgeeiQ9NPJ6.
CleanExiHS_MED4.
ExpressionAtlasiQ9NPJ6. baseline and differential.
GenevisibleiQ9NPJ6. HS.

Organism-specific databases

HPAiHPA006232.

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-394607,EBI-717810
AMOTQ4VCS5-23EBI-394607,EBI-3891843
C1orf216Q8TAB53EBI-394607,EBI-747505
CCDC146Q8IYE0-23EBI-394607,EBI-10247802
CCHCR1Q8TD31-33EBI-394607,EBI-10175300
CTNNBL1Q8WYA63EBI-394607,EBI-748128
FAM13CQ8NE313EBI-394607,EBI-751248
FRMD6Q96NE93EBI-394607,EBI-741729
FTCDO959543EBI-394607,EBI-10192648
HAUS1Q96CS23EBI-394607,EBI-2514791
IFT20Q8IY313EBI-394607,EBI-744203
KIFC3Q9BVG83EBI-394607,EBI-2125614
LRRFIP1Q32MZ4-43EBI-394607,EBI-10240044
MAB21L3Q8N8X93EBI-394607,EBI-10268010
MED12Q930746EBI-394607,EBI-394357
MED26O954029EBI-394607,EBI-394392
MED9Q9NWA010EBI-394607,EBI-394653
NDC80O147773EBI-394607,EBI-715849
SDCBPO005603EBI-394607,EBI-727004
SGF29Q96ES73EBI-394607,EBI-743117
SMARCD1Q96GM53EBI-394607,EBI-358489
SMARCE1Q969G33EBI-394607,EBI-455078
SSX3Q999093EBI-394607,EBI-10295431
TNFAIP8O953794EBI-394607,EBI-1049336
TXLNAP402223EBI-394607,EBI-359793
USHBP1Q8N6Y03EBI-394607,EBI-739895

GO - Molecular functioni

  • thyroid hormone receptor binding Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi118849. 358 interactions.
IntActiQ9NPJ6. 77 interactions.
MINTiMINT-1196457.
STRINGi9606.ENSP00000258648.

Structurei

3D structure databases

ProteinModelPortaliQ9NPJ6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili24 – 4825Sequence analysisAdd
BLAST
Coiled coili90 – 13142Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi262 – 2698Poly-Ser

Sequence similaritiesi

Belongs to the Mediator complex subunit 4 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4552. Eukaryota.
ENOG410XQ30. LUCA.
GeneTreeiENSGT00390000012063.
HOGENOMiHOG000043883.
HOVERGENiHBG052450.
InParanoidiQ9NPJ6.
KOiK15146.
OMAiGLEPPGH.
OrthoDBiEOG735405.
PhylomeDBiQ9NPJ6.
TreeFamiTF324421.

Family and domain databases

InterProiIPR019258. Mediator_Med4.
[Graphical view]
PfamiPF10018. Med4. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NPJ6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAASSSGEKE KERLGGGLGV AGGNSTRERL LSALEDLEVL SRELIEMLAI
60 70 80 90 100
SRNQKLLQAG EENQVLELLI HRDGEFQELM KLALNQGKIH HEMQVLEKEV
110 120 130 140 150
EKRDSDIQQL QKQLKEAEQI LATAVYQAKE KLKSIEKARK GAISSEEIIK
160 170 180 190 200
YAHRISASNA VCAPLTWVPG DPRRPYPTDL EMRSGLLGQM NNPSTNGVNG
210 220 230 240 250
HLPGDALAAG RLPDVLAPQY PWQSNDMSMN MLPPNHSSDF LLEPPGHNKE
260 270
NEDDVEIMST DSSSSSSESD
Length:270
Mass (Da):29,745
Last modified:October 1, 2000 - v1
Checksum:i05641357EBFA85F4
GO
Isoform 2 (identifier: Q9NPJ6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Show »
Length:224
Mass (Da):24,947
Checksum:i0598148BFB738B06
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051S → G in AAH05189 (PubMed:15489334).Curated
Sequence conflicti120 – 1201I → T in CAG46629 (Ref. 5) Curated
Sequence conflicti127 – 1271Q → R in BAD96737 (Ref. 6) Curated
Sequence conflicti152 – 1521A → P in CAG33557 (Ref. 5) Curated
Sequence conflicti183 – 1831R → K in AAF37289 (PubMed:10882111).Curated
Sequence conflicti218 – 2181P → S in BAD96433 (Ref. 6) Curated
Sequence conflicti251 – 2511N → D in AAH05189 (PubMed:15489334).Curated
Sequence conflicti265 – 2651S → T in AAF37289 (PubMed:10882111).Curated
Sequence conflicti265 – 2651S → T in CAG46629 (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 2. 1 PublicationVSP_047072Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300618 mRNA. Translation: AAG22542.1.
AF230381 mRNA. Translation: AAF37289.1.
AF161475 mRNA. Translation: AAF29090.1.
AK001934 mRNA. Translation: BAA91987.1.
CR457276 mRNA. Translation: CAG33557.1.
CR541830 mRNA. Translation: CAG46629.1.
AK222713 mRNA. Translation: BAD96433.1.
AK301835 mRNA. Translation: BAG63279.1.
AK223017 mRNA. Translation: BAD96737.1.
AL158196 Genomic DNA. Translation: CAI17018.1.
AL158196 Genomic DNA. Translation: CAI17020.1.
BC005189 mRNA. Translation: AAH05189.1.
CCDSiCCDS59241.1. [Q9NPJ6-2]
CCDS9408.1. [Q9NPJ6-1]
RefSeqiNP_001257558.1. NM_001270629.1. [Q9NPJ6-2]
NP_054885.1. NM_014166.3. [Q9NPJ6-1]
UniGeneiHs.181112.
Hs.741275.

Genome annotation databases

EnsembliENST00000258648; ENSP00000258648; ENSG00000136146. [Q9NPJ6-1]
ENST00000378586; ENSP00000367849; ENSG00000136146. [Q9NPJ6-2]
GeneIDi29079.
KEGGihsa:29079.
UCSCiuc001vby.3. human. [Q9NPJ6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300618 mRNA. Translation: AAG22542.1.
AF230381 mRNA. Translation: AAF37289.1.
AF161475 mRNA. Translation: AAF29090.1.
AK001934 mRNA. Translation: BAA91987.1.
CR457276 mRNA. Translation: CAG33557.1.
CR541830 mRNA. Translation: CAG46629.1.
AK222713 mRNA. Translation: BAD96433.1.
AK301835 mRNA. Translation: BAG63279.1.
AK223017 mRNA. Translation: BAD96737.1.
AL158196 Genomic DNA. Translation: CAI17018.1.
AL158196 Genomic DNA. Translation: CAI17020.1.
BC005189 mRNA. Translation: AAH05189.1.
CCDSiCCDS59241.1. [Q9NPJ6-2]
CCDS9408.1. [Q9NPJ6-1]
RefSeqiNP_001257558.1. NM_001270629.1. [Q9NPJ6-2]
NP_054885.1. NM_014166.3. [Q9NPJ6-1]
UniGeneiHs.181112.
Hs.741275.

3D structure databases

ProteinModelPortaliQ9NPJ6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118849. 358 interactions.
IntActiQ9NPJ6. 77 interactions.
MINTiMINT-1196457.
STRINGi9606.ENSP00000258648.

PTM databases

iPTMnetiQ9NPJ6.
PhosphoSiteiQ9NPJ6.

Polymorphism and mutation databases

DMDMi29840770.

Proteomic databases

EPDiQ9NPJ6.
MaxQBiQ9NPJ6.
PaxDbiQ9NPJ6.
PRIDEiQ9NPJ6.

Protocols and materials databases

DNASUi29079.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258648; ENSP00000258648; ENSG00000136146. [Q9NPJ6-1]
ENST00000378586; ENSP00000367849; ENSG00000136146. [Q9NPJ6-2]
GeneIDi29079.
KEGGihsa:29079.
UCSCiuc001vby.3. human. [Q9NPJ6-1]

Organism-specific databases

CTDi29079.
GeneCardsiMED4.
HGNCiHGNC:17903. MED4.
HPAiHPA006232.
MIMi605718. gene.
neXtProtiNX_Q9NPJ6.
PharmGKBiPA134877001.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4552. Eukaryota.
ENOG410XQ30. LUCA.
GeneTreeiENSGT00390000012063.
HOGENOMiHOG000043883.
HOVERGENiHBG052450.
InParanoidiQ9NPJ6.
KOiK15146.
OMAiGLEPPGH.
OrthoDBiEOG735405.
PhylomeDBiQ9NPJ6.
TreeFamiTF324421.

Enzyme and pathway databases

ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-212436. Generic Transcription Pathway.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

ChiTaRSiMED4. human.
GeneWikiiMED4.
GenomeRNAii29079.
PROiQ9NPJ6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPJ6.
CleanExiHS_MED4.
ExpressionAtlasiQ9NPJ6. baseline and differential.
GenevisibleiQ9NPJ6. HS.

Family and domain databases

InterProiIPR019258. Mediator_Med4.
[Graphical view]
PfamiPF10018. Med4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex."
    Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M., Erdjument-Bromage H., Tempst P., Freedman L.P.
    Nature 398:824-828(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The USA-derived transcriptional coactivator PC2 is a submodule of TRAP/SMCC and acts synergistically with other PCs."
    Malik S., Gu W., Wu W., Qin J., Roeder R.G.
    Mol. Cell 5:753-760(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 14-27 AND 30-42.
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Testis.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Small intestine.
  7. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Brain.
  9. "Composite co-activator ARC mediates chromatin-directed transcriptional activation."
    Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.
    Nature 398:828-832(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN ARC COMPLEX, PROTEIN SEQUENCE OF 81-88; 154-165 AND 173-183.
  10. "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.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMED4_HUMAN
AccessioniPrimary (citable) accession number: Q9NPJ6
Secondary accession number(s): B4DX67
, Q53GB4, Q53H68, Q5T912, Q6FHC4, Q6IA79, Q9BS95, Q9NYR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 140 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 13
    Human chromosome 13: 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

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 one 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.