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Q80YQ2 (MED23_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of RNA polymerase II transcription subunit 23
Alternative name(s):
Cofactor required for Sp1 transcriptional activation subunit 3
Short name=CRSP complex subunit 3
Mediator complex subunit 23
Protein sur-2 homolog
Short name=mSur-2
Gene names
Name:Med23
Synonyms:Crsp3, Kiaa1216, Sur2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1367 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. Also required for transcriptional activation subsequent to the assembly of the preinitiation complex. Required for transcriptional activation by adenovirus E1A protein. Required for ELK1-dependent transcriptional activation in response to activated Ras signaling. Ref.1 Ref.5 Ref.6 Ref.8

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. Interacts with CEBPB, CTNNB1, and GLI3 By similarity. Interacts with CDK8 and ELK1. Interacts with the adenovirus E1A protein. Ref.1 Ref.5

Subcellular location

Nucleus Probable.

Sequence similarities

Belongs to the Mediator complex subunit 23 family.

Sequence caution

The sequence AAM28897.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB29019.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC26001.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence BAC98122.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionActivator
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmediator complex

Inferred from direct assay PubMed 15340084PubMed 20508642. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80YQ2-1)

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.
Isoform 2 (identifier: Q80YQ2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     291-291: K → KQTLNIA
Isoform 3 (identifier: Q80YQ2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     54-55: ES → IV
     56-1367: Missing.
Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13671367Mediator of RNA polymerase II transcription subunit 23
PRO_0000305931

Natural variations

Alternative sequence54 – 552ES → IV in isoform 3.
VSP_041583
Alternative sequence56 – 13671312Missing in isoform 3.
VSP_041584
Alternative sequence2911K → KQTLNIA in isoform 2.
VSP_028382

Experimental info

Sequence conflict771S → F in AAH50916. Ref.4
Sequence conflict2191N → Y in AAM28897. Ref.1
Sequence conflict3581Q → H in AAM28897. Ref.1
Sequence conflict3641G → R in AAM28897. Ref.1
Sequence conflict3851Q → H in AAM28897. Ref.1
Sequence conflict8091K → N in AAM28897. Ref.1
Sequence conflict812 – 8132ER → DK in AAM28897. Ref.1
Sequence conflict8401G → S in AAM28897. Ref.1
Sequence conflict8441N → G in AAM28897. Ref.1
Sequence conflict1062 – 10654VPED → GSRKN in AAM28897. Ref.1
Sequence conflict10911D → E in AAM28897. Ref.1
Sequence conflict12821D → N in AAM28897. Ref.1
Sequence conflict13151E → K in AAM28897. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: FD7764FFB2A52B1A

FASTA1,367156,087
        10         20         30         40         50         60 
METQLQSIFE EVVKTEIIEE AFPGMFMDTP EDEKTKLISC LAAFRQFWSG LSQESHEQCV 

        70         80         90        100        110        120 
QWIVKFIHGQ HSPKRISFLY DCLAMAVETG LLPPRMVCES LINSDSLEWE RTQLWALTFK 

       130        140        150        160        170        180 
LVRKIIGGVD YKGVRDLLKA ILEKILTIPN TVSSAVVQQL LAAREVIAYI LERNACLLPA 

       190        200        210        220        230        240 
YFAVTEIRKL YPEGKLPHWL LGNLVSDFVD TFRPTARINS ICGRCSLLPV VNNSGAICNS 

       250        260        270        280        290        300 
WKLDPATLRF PLKGLLPYDK DLFEPQTALL RYVLEQPYSR DMVCNMLGLN KQHKQRCPVL 

       310        320        330        340        350        360 
EDQLVDLVVY AMERSETEEK FDDGGTSQLL WQHLSSQLIF FVLFQFASFP HMVLSLHQKL 

       370        380        390        400        410        420 
AGRGLIKGRD HLMWVLLQFI SGSIQKNALA DFLPVMKLFD LLYPEKECIP VPDINKPQST 

       430        440        450        460        470        480 
HAFAMTCIWI HLNRKAQNGD STLQIPIPHS LKLHHEFLQQ SLRNKSLQMN DYKIALLCNA 

       490        500        510        520        530        540 
YSTNSECFTL PMGALVETIY GNGIMRVPLP GTSCLASASV TPLPMNLLDS LTVHAKMSLI 

       550        560        570        580        590        600 
HSIATRVIKL AHTKSSVALA PALVETYSRL LVYMEIESLG IKGFISQLLP TVFKSHAWGI 

       610        620        630        640        650        660 
LHTLLEMFSH RMHHIQPHYR VQLLSHLHTL AAVAQTNQNQ LHLCVESTAL RLITALGSSE 

       670        680        690        700        710        720 
VQPQFTRFLN DPKTVLSAES EELNRALILT LARATHVTDF FTGSDSIQGT WCKDILQTIM 

       730        740        750        760        770        780 
NFTPHNWASH TLSCFPAPLQ AFFKQNNVPQ ESRFNLKKNV EEEYRKWKSM TDENEIITQF 

       790        800        810        820        830        840 
SVQGFPPLFL CLLWKMLLET DHISQIGYKV LERIGARALV AHVRTFADFL VYEFSTSAGG 

       850        860        870        880        890        900 
QQLNKCIEIL NDMVWKYNIV TLDRLILCLA MRSHEGNEAQ VCYFIIQLLL LKPNDFRNRV 

       910        920        930        940        950        960 
SDFVKENSPE HWLQSDWHTK HMSYHKKYPE KLYFEGLAEQ VDPPVPIQSP YLPIYFGNVC 

       970        980        990       1000       1010       1020 
LRFLPVFDIV IHRFLELLPV SKSLETLLDH LGGLYKFHDR PVTYLYNTLH YYEMCLRNRD 

      1030       1040       1050       1060       1070       1080 
HLKRKLVHAI IGSLKDNRPQ GWCLSDTYLK HAMNAREDNP WVPEDSYYCK LIGRLVDTMA 

      1090       1100       1110       1120       1130       1140 
GKSPGPFPNC DWRFNEFPNP AAHALHVTCV ELMALAVPGK DVGNALLNVV LKSQPLVPRE 

      1150       1160       1170       1180       1190       1200 
NITAWMNAIG LIITALPEPY WIVLHDRIVN VISSSSLTSE TEWVGYPFRL FDFTACHQSY 

      1210       1220       1230       1240       1250       1260 
SEMSCSYTLA LAHAVWHHSS IGQLSLIPKF LTEALLPVVK TEFQLLYVYH LVGPFLQRFQ 

      1270       1280       1290       1300       1310       1320 
QERTRCMIEI GVAFYDMLLN VDQCSTHLNY MDPICDFLYH MKYMFTGDSV KEQVEKIICN 

      1330       1340       1350       1360 
LKPALKLRLR FITHISKMEP AVPPQALNSG SPAPQSNQVP ASLPVTQ 

« Hide

Isoform 2 [UniParc].

Checksum: 40B960CADA0749B1
Show »

FASTA1,373156,728
Isoform 3 [UniParc].

Checksum: 54EF12934E0622AA
Show »

FASTA556,343

References

« Hide 'large scale' references
[1]"Transcription control by E1A and MAP kinase pathway via Sur2 mediator subunit."
Stevens J.L., Cantin G.T., Wang G., Shevchenko A., Shevchenko A., Berk A.J.
Science 296:755-758(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH CDK8; E1A AND ELK1.
Strain: C3H.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Embryonic tail.
[3]"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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1114-1367 (ISOFORMS 1/2).
Strain: C57BL/6J.
Tissue: Embryonic head and Skin.
[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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 673-1367 (ISOFORMS 1/2).
Strain: C57BL/6.
Tissue: Brain and Mammary tumor.
[5]"Requirement of Sur2 for efficient replication of mouse adenovirus type 1."
Fang L., Stevens J.L., Berk A.J., Spindler K.R.
J. Virol. 78:12888-12900(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH E1A.
[6]"Ras induces mediator complex exchange on C/EBP beta."
Mo X., Kowenz-Leutz E., Xu H., Leutz A.
Mol. Cell 13:241-250(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Thyroid hormone-induced juxtaposition of regulatory elements/factors and chromatin remodeling of Crabp1 dependent on MED1/TRAP220."
Park S.W., Li G., Lin Y.-P., Barrero M.J., Ge K., Roeder R.G., Wei L.-N.
Mol. Cell 19:643-653(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH PROMOTER REGIONS.
[8]"Mediator requirement for both recruitment and postrecruitment steps in transcription initiation."
Wang G., Balamotis M.A., Stevens J.L., Yamaguchi Y., Handa H., Berk A.J.
Mol. Cell 17:683-694(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF507918 mRNA. Translation: AAM28897.1. Different initiation.
AK129312 mRNA. Translation: BAC98122.1. Different initiation.
AK013854 mRNA. Translation: BAB29019.1. Different initiation.
AK028545 mRNA. Translation: BAC26001.1. Sequence problems.
BC005508 mRNA. Translation: AAH05508.2.
BC050916 mRNA. Translation: AAH50916.1.
RefSeqNP_001159888.1. NM_001166416.1.
NP_081623.3. NM_027347.3.
UniGeneMm.28020.

3D structure databases

ProteinModelPortalQ80YQ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid213916. 2 interactions.
DIPDIP-59234N.
IntActQ80YQ2. 4 interactions.

PTM databases

PhosphoSiteQ80YQ2.

Proteomic databases

MaxQBQ80YQ2.
PaxDbQ80YQ2.
PRIDEQ80YQ2.

Protocols and materials databases

DNASU70208.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID70208.
KEGGmmu:70208.
UCSCuc011xbu.1. mouse. [Q80YQ2-1]

Organism-specific databases

CTD9439.
MGIMGI:1917458. Med23.
RougeSearch...

Phylogenomic databases

eggNOGNOG305557.
HOGENOMHOG000043810.
HOVERGENHBG051122.
KOK15166.
PhylomeDBQ80YQ2.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressQ80YQ2.
BgeeQ80YQ2.
CleanExMM_MED23.
GenevestigatorQ80YQ2.

Family and domain databases

InterProIPR021629. Mediator_Med23.
[Graphical view]
PfamPF11573. Med23. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio331172.
PROQ80YQ2.
SOURCESearch...

Entry information

Entry nameMED23_MOUSE
AccessionPrimary (citable) accession number: Q80YQ2
Secondary accession number(s): Q6ZPV7 expand/collapse secondary AC list , Q8CEC3, Q8K587, Q9CXY8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: May 14, 2014
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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