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Q9CXU1 (MED31_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Mediator of RNA polymerase II transcription subunit 31
Alternative name(s):
Mediator complex subunit 31
Mediator complex subunit SOH1
Gene names
Name:Med31
Synonyms:Soh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Nucleus Probable.

Sequence similarities

Belongs to the Mediator complex subunit 31 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionActivator
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein complex assembly

Inferred from electronic annotation. Source: Compara

   Cellular_componentmediator complex

Inferred from direct assay PubMed 20508642. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA polymerase II transcription cofactor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Med19Q8C1S02EBI-309355,EBI-398761

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 131131Mediator of RNA polymerase II transcription subunit 31
PRO_0000212528

Regions

Compositional bias122 – 1254Poly-Gln

Experimental info

Sequence conflict861K → E in BAB29102. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CXU1 [UniParc].

Last modified October 31, 2003. Version 2.
Checksum: A9837A88EC94D014

FASTA13115,771
        10         20         30         40         50         60 
MAAAVAMETD DAGNRLRFQL ELEFVQCLAN PNYLNFLAQR GYFKDKAFVN YLKYLLYWKE 

        70         80         90        100        110        120 
PEYAKYLKYP QCLHMLELLQ YEHFRKELVN AQCAKFIDEQ QILHWQHYSR KRVRLQQALA 

       130 
EQQQQNNTAG K

« Hide

References

[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. expand/collapse author list , 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: Embryo and Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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/6.
Tissue: Brain and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK005655 mRNA. Translation: BAB24169.1.
AK013990 mRNA. Translation: BAB29102.1.
BX119911 Genomic DNA. Translation: CAI24479.1.
BC019685 mRNA. Translation: AAH19685.1.
BC051929 mRNA. Translation: AAH51929.1.
IPIIPI00321251.
RefSeqNP_080344.2. NM_026068.2.
UniGeneMm.159496.

3D structure databases

ProteinModelPortalQ9CXU1.
SMRQ9CXU1. Positions 17-79.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9CXU1. 4 interactions.
MINTMINT-219187.
STRING10090.ENSMUSP00000021157.

PTM databases

PhosphoSiteQ9CXU1.

Proteomic databases

PaxDbQ9CXU1.
PRIDEQ9CXU1.

Protocols and materials databases

DNASU67279.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021157; ENSMUSP00000021157; ENSMUSG00000020801.
GeneID67279.
KEGGmmu:67279.
UCSCuc007jyk.1. mouse.

Organism-specific databases

CTD51003.
MGIMGI:1914529. Med31.

Phylogenomic databases

eggNOGCOG5088.
GeneTreeENSGT00390000015531.
HOGENOMHOG000242147.
HOVERGENHBG052449.
InParanoidQ9CXU1.
KOK15153.
OMAHCLHMLE.
OrthoDBEOG4GF3GK.

Enzyme and pathway databases

ReactomeREACT_127416. Developmental Biology.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Gene expression databases

BgeeQ9CXU1.
GenevestigatorQ9CXU1.
GermOnlineENSMUSG00000020801. Mus musculus.

Family and domain databases

InterProIPR008831. Mediator_Med31.
[Graphical view]
PANTHERPTHR13186. PTHR13186. 1 hit.
PfamPF05669. Med31. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio324090.
SOURCESearch...

Entry information

Entry nameMED31_MOUSE
AccessionPrimary (citable) accession number: Q9CXU1
Secondary accession number(s): Q9DAP5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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