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Protein

Mediator of RNA polymerase II transcription subunit 6

Gene

MED6

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.1 Publication

GO - Molecular functioni

GO - Biological processi

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 6
Alternative name(s):
Activator-recruited cofactor 33 kDa component
Short name:
ARC33
Mediator complex subunit 6
Short name:
hMed6
Renal carcinoma antigen NY-REN-28
Gene namesi
Name:MED6
Synonyms:ARC33
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:19970. MED6.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134868263.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Mediator of RNA polymerase II transcription subunit 6PRO_0000096388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei236 – 2361N6-acetyllysineCombined sources
Modified residuei241 – 2411N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO75586.
MaxQBiO75586.
PaxDbiO75586.
PeptideAtlasiO75586.
PRIDEiO75586.

PTM databases

iPTMnetiO75586.
PhosphoSiteiO75586.

Expressioni

Gene expression databases

BgeeiO75586.
CleanExiHS_MED6.
ExpressionAtlasiO75586. baseline and differential.
GenevisibleiO75586. HS.

Organism-specific databases

HPAiHPA030764.
HPA069039.

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. Interacts with CTNNB1 and GLI3.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED17Q9NVC62EBI-394624,EBI-394562
Med20Q9R0X02EBI-394624,EBI-398698From a different organism.
MED27Q6P2C82EBI-394624,EBI-394603
MED29Q9NX703EBI-394624,EBI-394656
Med8Q9D7W52EBI-394624,EBI-7990252From a different organism.

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115319. 57 interactions.
DIPiDIP-31456N.
IntActiO75586. 26 interactions.
MINTiMINT-244143.
STRINGi9606.ENSP00000256379.

Structurei

3D structure databases

ProteinModelPortaliO75586.
SMRiO75586. Positions 13-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Mediator complex subunit 6 family.Curated

Phylogenomic databases

eggNOGiKOG3169. Eukaryota.
COG5097. LUCA.
GeneTreeiENSGT00390000017666.
HOGENOMiHOG000035127.
HOVERGENiHBG006825.
InParanoidiO75586.
KOiK15128.
PhylomeDBiO75586.
TreeFamiTF313577.

Family and domain databases

InterProiIPR007018. Mediator_Med6.
IPR016820. Mediator_Med6_met/pln.
[Graphical view]
PANTHERiPTHR13104. PTHR13104. 1 hit.
PfamiPF04934. Med6. 1 hit.
[Graphical view]
PIRSFiPIRSF023869. Mediator_MED6_meta/pln. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75586-1) [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
MAAVDIRDNL LGISWVDSSW IPILNSGSVL DYFSERSNPF YDRTCNNEVV
60 70 80 90 100
KMQRLTLEHL NQMVGIEYIL LHAQEPILFI IRKQQRQSPA QVIPLADYYI
110 120 130 140 150
IAGVIYQAPD LGSVINSRVL TAVHGIQSAF DEAMSYCRYH PSKGYWWHFK
160 170 180 190 200
DHEEQDKVRP KAKRKEEPSS IFQRQRVDAL LLDLRQKFPP KFVQLKPGEK
210 220 230 240
PVPVDQTKKE AEPIPETVKP EEKETTKNVQ QTVSAKGPPE KRMRLQ
Length:246
Mass (Da):28,425
Last modified:February 28, 2003 - v2
Checksum:i9B173626F583B48B
GO
Isoform 2 (identifier: O75586-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     119-119: V → VSLFSFYK

Note: No experimental confirmation available.
Show »
Length:253
Mass (Da):29,298
Checksum:i3D89AD48C96C3CD7
GO
Isoform 3 (identifier: O75586-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     156-246: DKVRPKAKRK...GPPEKRMRLQ → AKAWRKACSSGSNKERGRTYTRNCKT

Note: No experimental confirmation available.
Show »
Length:181
Mass (Da):20,859
Checksum:i672B435005F9E984
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511D → V in AAC26869 (PubMed:9734358).Curated
Sequence conflicti156 – 1561D → G in AAB84363 (PubMed:10508479).Curated
Sequence conflicti203 – 2031P → S in BAD97066 (Ref. 5) Curated
Sequence conflicti224 – 2241E → G in BAD96307 (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei119 – 1191V → VSLFSFYK in isoform 2. 1 PublicationVSP_054589
Alternative sequencei156 – 24691DKVRP…RMRLQ → AKAWRKACSSGSNKERGRTY TRNCKT in isoform 3. 1 PublicationVSP_054590Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074723 mRNA. Translation: AAC26869.1.
BT006831 mRNA. Translation: AAP35477.1.
CR541697 mRNA. Translation: CAG46498.1.
AK300460 mRNA. Translation: BAG62179.1.
AK304361 mRNA. Translation: BAG65202.1.
AK222587 mRNA. Translation: BAD96307.1.
AK223346 mRNA. Translation: BAD97066.1.
AL357153 Genomic DNA. No translation available.
BC004106 mRNA. Translation: AAH04106.1.
U78082 mRNA. Translation: AAB84363.1.
AF155104 mRNA. Translation: AAD42870.1.
CCDSiCCDS61483.1. [O75586-3]
CCDS61484.1. [O75586-2]
CCDS9805.1. [O75586-1]
RefSeqiNP_001271138.1. NM_001284209.1. [O75586-2]
NP_001271139.1. NM_001284210.1. [O75586-3]
NP_001271140.1. NM_001284211.1.
NP_005457.2. NM_005466.3. [O75586-1]
UniGeneiHs.497353.

Genome annotation databases

EnsembliENST00000256379; ENSP00000256379; ENSG00000133997. [O75586-1]
ENST00000430055; ENSP00000413343; ENSG00000133997. [O75586-2]
ENST00000440435; ENSP00000394502; ENSG00000133997. [O75586-3]
GeneIDi10001.
KEGGihsa:10001.
UCSCiuc001xmf.5. human. [O75586-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074723 mRNA. Translation: AAC26869.1.
BT006831 mRNA. Translation: AAP35477.1.
CR541697 mRNA. Translation: CAG46498.1.
AK300460 mRNA. Translation: BAG62179.1.
AK304361 mRNA. Translation: BAG65202.1.
AK222587 mRNA. Translation: BAD96307.1.
AK223346 mRNA. Translation: BAD97066.1.
AL357153 Genomic DNA. No translation available.
BC004106 mRNA. Translation: AAH04106.1.
U78082 mRNA. Translation: AAB84363.1.
AF155104 mRNA. Translation: AAD42870.1.
CCDSiCCDS61483.1. [O75586-3]
CCDS61484.1. [O75586-2]
CCDS9805.1. [O75586-1]
RefSeqiNP_001271138.1. NM_001284209.1. [O75586-2]
NP_001271139.1. NM_001284210.1. [O75586-3]
NP_001271140.1. NM_001284211.1.
NP_005457.2. NM_005466.3. [O75586-1]
UniGeneiHs.497353.

3D structure databases

ProteinModelPortaliO75586.
SMRiO75586. Positions 13-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115319. 57 interactions.
DIPiDIP-31456N.
IntActiO75586. 26 interactions.
MINTiMINT-244143.
STRINGi9606.ENSP00000256379.

PTM databases

iPTMnetiO75586.
PhosphoSiteiO75586.

Proteomic databases

EPDiO75586.
MaxQBiO75586.
PaxDbiO75586.
PeptideAtlasiO75586.
PRIDEiO75586.

Protocols and materials databases

DNASUi10001.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256379; ENSP00000256379; ENSG00000133997. [O75586-1]
ENST00000430055; ENSP00000413343; ENSG00000133997. [O75586-2]
ENST00000440435; ENSP00000394502; ENSG00000133997. [O75586-3]
GeneIDi10001.
KEGGihsa:10001.
UCSCiuc001xmf.5. human. [O75586-1]

Organism-specific databases

CTDi10001.
GeneCardsiMED6.
HGNCiHGNC:19970. MED6.
HPAiHPA030764.
HPA069039.
MIMi602984. gene.
neXtProtiNX_O75586.
PharmGKBiPA134868263.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3169. Eukaryota.
COG5097. LUCA.
GeneTreeiENSGT00390000017666.
HOGENOMiHOG000035127.
HOVERGENiHBG006825.
InParanoidiO75586.
KOiK15128.
PhylomeDBiO75586.
TreeFamiTF313577.

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

GeneWikiiMED6.
GenomeRNAii10001.
PROiO75586.
SOURCEiSearch...

Gene expression databases

BgeeiO75586.
CleanExiHS_MED6.
ExpressionAtlasiO75586. baseline and differential.
GenevisibleiO75586. HS.

Family and domain databases

InterProiIPR007018. Mediator_Med6.
IPR016820. Mediator_Med6_met/pln.
[Graphical view]
PANTHERiPTHR13104. PTHR13104. 1 hit.
PfamiPF04934. Med6. 1 hit.
[Graphical view]
PIRSFiPIRSF023869. Mediator_MED6_meta/pln. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NAT, a human complex containing Srb polypeptides that functions as a negative regulator of activated transcription."
    Sun X., Zhang Y., Cho H., Rickert P., Lees E., Lane W.S., Reinberg D.
    Mol. Cell 2:213-222(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A FORM OF THE MEDIATOR COMPLEX.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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).
  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 2 AND 3).
    Tissue: Placenta and Trachea.
  5. 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: Coronary arterial endothelium and Testis.
  6. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Lung.
  8. Kim Y.-J.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-157 (ISOFORM 1).
  9. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-246 (ISOFORM 1), IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  10. "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: PROTEIN SEQUENCE OF 200-208 AND 227-236, IDENTIFICATION IN THE ARC COMPLEX.
  11. "A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation."
    Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G.
    Mol. Cell 3:97-108(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SMCC COMPLEX.
  12. "TFIIH is negatively regulated by cdk8-containing mediator complexes."
    Akoulitchev S., Chuikov S., Reinberg D.
    Nature 407:102-106(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCNC; MED10 AND MED23.
  13. "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro."
    Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.
    Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
  14. "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.
  15. "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; MED21 AND MED30, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  16. "Regulation of Aurora-A kinase gene expression via GABP recruitment of TRAP220/MED1."
    Udayakumar T.S., Belakavadi M., Choi K.-H., Pandey P.K., Fondell J.D.
    J. Biol. Chem. 281:14691-14699(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH PROMOTER REGIONS.
  17. "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 MED 1 AND MED10.
  18. "Mediator modulates Gli3-dependent Sonic hedgehog signaling."
    Zhou H., Kim S., Ishii S., Boyer T.G.
    Mol. Cell. Biol. 26:8667-8682(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK8; CTNNB1 AND GLI3.
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-236 AND LYS-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMED6_HUMAN
AccessioniPrimary (citable) accession number: O75586
Secondary accession number(s): B4DU17
, B4E2P0, O15401, Q53FE3, Q53HJ3, Q6FHQ4, Q9BTH1, Q9UHL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: February 28, 2003
Last modified: June 8, 2016
This is version 144 of the entry and version 2 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 14
    Human chromosome 14: 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.