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Protein

Mediator of RNA polymerase II transcription subunit 29

Gene

Med29

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 29
Alternative name(s):
Intersex-like protein
Mediator complex subunit 29
Gene namesi
Name:Med29
Synonyms:Ixl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1914474. Med29.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 199198Mediator of RNA polymerase II transcription subunit 29PRO_0000288059Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9DB91.
MaxQBiQ9DB91.
PaxDbiQ9DB91.
PRIDEiQ9DB91.

PTM databases

iPTMnetiQ9DB91.
PhosphoSiteiQ9DB91.

Expressioni

Gene expression databases

BgeeiQ9DB91.
CleanExiMM_MED29.
GenevisibleiQ9DB91. MM.

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. Associates with the MED18/MED20 heteromer (By similarity).By similarity

Protein-protein interaction databases

BioGridi212029. 1 interaction.
DIPiDIP-60702N.
IntActiQ9DB91. 2 interactions.
MINTiMINT-4128141.
STRINGi10090.ENSMUSP00000003536.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi29 – 8355Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the Mediator complex subunit 29 family.Curated

Phylogenomic databases

eggNOGiENOG410IXGN. Eukaryota.
ENOG4111K6Y. LUCA.
GeneTreeiENSGT00390000007540.
HOGENOMiHOG000038041.
HOVERGENiHBG060489.
InParanoidiQ9DB91.
KOiK15142.
OMAiECLSQSI.
OrthoDBiEOG7DVDCQ.
PhylomeDBiQ9DB91.
TreeFamiTF326632.

Family and domain databases

InterProiIPR021018. Mediator_Med29_met.
[Graphical view]
PfamiPF11568. Med29. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DB91-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPQPQAAA VSSASGVSGP GSAGGPGPQQ QPQPTQLVGS AQSGLLQQQQ
60 70 80 90 100
QDFDPVQRYK MLIPQLKESL QTLMKVAAQN LIQNTNIDNG QKSSDAPLQR
110 120 130 140 150
FDKCLEEFYA LCDQLELCLR LAHECLSQSC DSAKHSPTLV PTATKPDAVQ
160 170 180 190
PDSLPYPQYL AVIKAQITCA KDIHTALLDC ANKVTGKTTA PSTGPGGSL
Length:199
Mass (Da):21,011
Last modified:June 1, 2001 - v1
Checksum:i60C50BE919D5A2C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005112 mRNA. Translation: BAB23826.1.
BC023192 mRNA. Translation: AAH23192.1.
BC083314 mRNA. Translation: AAH83314.1.
CCDSiCCDS21042.1.
RefSeqiNP_080318.2. NM_026042.3.
UniGeneiMm.41647.

Genome annotation databases

EnsembliENSMUST00000003536; ENSMUSP00000003536; ENSMUSG00000003444.
GeneIDi67224.
KEGGimmu:67224.
UCSCiuc009fyt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005112 mRNA. Translation: BAB23826.1.
BC023192 mRNA. Translation: AAH23192.1.
BC083314 mRNA. Translation: AAH83314.1.
CCDSiCCDS21042.1.
RefSeqiNP_080318.2. NM_026042.3.
UniGeneiMm.41647.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212029. 1 interaction.
DIPiDIP-60702N.
IntActiQ9DB91. 2 interactions.
MINTiMINT-4128141.
STRINGi10090.ENSMUSP00000003536.

PTM databases

iPTMnetiQ9DB91.
PhosphoSiteiQ9DB91.

Proteomic databases

EPDiQ9DB91.
MaxQBiQ9DB91.
PaxDbiQ9DB91.
PRIDEiQ9DB91.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003536; ENSMUSP00000003536; ENSMUSG00000003444.
GeneIDi67224.
KEGGimmu:67224.
UCSCiuc009fyt.2. mouse.

Organism-specific databases

CTDi55588.
MGIiMGI:1914474. Med29.

Phylogenomic databases

eggNOGiENOG410IXGN. Eukaryota.
ENOG4111K6Y. LUCA.
GeneTreeiENSGT00390000007540.
HOGENOMiHOG000038041.
HOVERGENiHBG060489.
InParanoidiQ9DB91.
KOiK15142.
OMAiECLSQSI.
OrthoDBiEOG7DVDCQ.
PhylomeDBiQ9DB91.
TreeFamiTF326632.

Enzyme and pathway databases

ReactomeiR-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

PROiQ9DB91.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB91.
CleanExiMM_MED29.
GenevisibleiQ9DB91. MM.

Family and domain databases

InterProiIPR021018. Mediator_Med29_met.
[Graphical view]
PfamiPF11568. Med29. 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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary tumor.

Entry informationi

Entry nameiMED29_MOUSE
AccessioniPrimary (citable) accession number: Q9DB91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
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

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.