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Q80YQ2

- MED23_MOUSE

UniProt

Q80YQ2 - MED23_MOUSE

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Protein
Mediator of RNA polymerase II transcription subunit 23
Gene
Med23, Crsp3, Kiaa1216, Sur2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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 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.4 Publications

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_198602. PPARA activates gene expression.
REACT_206529. Generic Transcription Pathway.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Med23
Synonyms:Crsp3, Kiaa1216, Sur2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1917458. Med23.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. mediator complex Source: MGI
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13671367Mediator of RNA polymerase II transcription subunit 23
PRO_0000305931Add
BLAST

Proteomic databases

MaxQBiQ80YQ2.
PaxDbiQ80YQ2.
PRIDEiQ80YQ2.

PTM databases

PhosphoSiteiQ80YQ2.

Expressioni

Gene expression databases

ArrayExpressiQ80YQ2.
BgeeiQ80YQ2.
CleanExiMM_MED23.
GenevestigatoriQ80YQ2.

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 CEBPB, CTNNB1, and GLI3 By similarity. Interacts with CDK8 and ELK1. Interacts with the adenovirus E1A protein.2 Publications

Protein-protein interaction databases

BioGridi213916. 2 interactions.
DIPiDIP-59234N.
IntActiQ80YQ2. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ80YQ2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG305557.
HOGENOMiHOG000043810.
HOVERGENiHBG051122.
KOiK15166.
PhylomeDBiQ80YQ2.

Family and domain databases

InterProiIPR021629. Mediator_Med23.
[Graphical view]
PfamiPF11573. Med23. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q80YQ2-1) [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

METQLQSIFE EVVKTEIIEE AFPGMFMDTP EDEKTKLISC LAAFRQFWSG     50
LSQESHEQCV QWIVKFIHGQ HSPKRISFLY DCLAMAVETG LLPPRMVCES 100
LINSDSLEWE RTQLWALTFK LVRKIIGGVD YKGVRDLLKA ILEKILTIPN 150
TVSSAVVQQL LAAREVIAYI LERNACLLPA YFAVTEIRKL YPEGKLPHWL 200
LGNLVSDFVD TFRPTARINS ICGRCSLLPV VNNSGAICNS WKLDPATLRF 250
PLKGLLPYDK DLFEPQTALL RYVLEQPYSR DMVCNMLGLN KQHKQRCPVL 300
EDQLVDLVVY AMERSETEEK FDDGGTSQLL WQHLSSQLIF FVLFQFASFP 350
HMVLSLHQKL AGRGLIKGRD HLMWVLLQFI SGSIQKNALA DFLPVMKLFD 400
LLYPEKECIP VPDINKPQST HAFAMTCIWI HLNRKAQNGD STLQIPIPHS 450
LKLHHEFLQQ SLRNKSLQMN DYKIALLCNA YSTNSECFTL PMGALVETIY 500
GNGIMRVPLP GTSCLASASV TPLPMNLLDS LTVHAKMSLI HSIATRVIKL 550
AHTKSSVALA PALVETYSRL LVYMEIESLG IKGFISQLLP TVFKSHAWGI 600
LHTLLEMFSH RMHHIQPHYR VQLLSHLHTL AAVAQTNQNQ LHLCVESTAL 650
RLITALGSSE VQPQFTRFLN DPKTVLSAES EELNRALILT LARATHVTDF 700
FTGSDSIQGT WCKDILQTIM NFTPHNWASH TLSCFPAPLQ AFFKQNNVPQ 750
ESRFNLKKNV EEEYRKWKSM TDENEIITQF SVQGFPPLFL CLLWKMLLET 800
DHISQIGYKV LERIGARALV AHVRTFADFL VYEFSTSAGG QQLNKCIEIL 850
NDMVWKYNIV TLDRLILCLA MRSHEGNEAQ VCYFIIQLLL LKPNDFRNRV 900
SDFVKENSPE HWLQSDWHTK HMSYHKKYPE KLYFEGLAEQ VDPPVPIQSP 950
YLPIYFGNVC LRFLPVFDIV IHRFLELLPV SKSLETLLDH LGGLYKFHDR 1000
PVTYLYNTLH YYEMCLRNRD HLKRKLVHAI IGSLKDNRPQ GWCLSDTYLK 1050
HAMNAREDNP WVPEDSYYCK LIGRLVDTMA GKSPGPFPNC DWRFNEFPNP 1100
AAHALHVTCV ELMALAVPGK DVGNALLNVV LKSQPLVPRE NITAWMNAIG 1150
LIITALPEPY WIVLHDRIVN VISSSSLTSE TEWVGYPFRL FDFTACHQSY 1200
SEMSCSYTLA LAHAVWHHSS IGQLSLIPKF LTEALLPVVK TEFQLLYVYH 1250
LVGPFLQRFQ QERTRCMIEI GVAFYDMLLN VDQCSTHLNY MDPICDFLYH 1300
MKYMFTGDSV KEQVEKIICN LKPALKLRLR FITHISKMEP AVPPQALNSG 1350
SPAPQSNQVP ASLPVTQ 1367
Length:1,367
Mass (Da):156,087
Last modified:October 2, 2007 - v2
Checksum:iFD7764FFB2A52B1A
GO
Isoform 2 (identifier: Q80YQ2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     291-291: K → KQTLNIA

Show »
Length:1,373
Mass (Da):156,728
Checksum:i40B960CADA0749B1
GO
Isoform 3 (identifier: Q80YQ2-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:55
Mass (Da):6,343
Checksum:i54EF12934E0622AA
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei54 – 552ES → IV in isoform 3.
VSP_041583
Alternative sequencei56 – 13671312Missing in isoform 3.
VSP_041584Add
BLAST
Alternative sequencei291 – 2911K → KQTLNIA in isoform 2.
VSP_028382

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771S → F in AAH50916. 1 Publication
Sequence conflicti219 – 2191N → Y in AAM28897. 1 Publication
Sequence conflicti358 – 3581Q → H in AAM28897. 1 Publication
Sequence conflicti364 – 3641G → R in AAM28897. 1 Publication
Sequence conflicti385 – 3851Q → H in AAM28897. 1 Publication
Sequence conflicti809 – 8091K → N in AAM28897. 1 Publication
Sequence conflicti812 – 8132ER → DK in AAM28897. 1 Publication
Sequence conflicti840 – 8401G → S in AAM28897. 1 Publication
Sequence conflicti844 – 8441N → G in AAM28897. 1 Publication
Sequence conflicti1062 – 10654VPED → GSRKN in AAM28897. 1 Publication
Sequence conflicti1091 – 10911D → E in AAM28897. 1 Publication
Sequence conflicti1282 – 12821D → N in AAM28897. 1 Publication
Sequence conflicti1315 – 13151E → K in AAM28897. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_001159888.1. NM_001166416.1.
NP_081623.3. NM_027347.3.
UniGeneiMm.28020.

Genome annotation databases

GeneIDi70208.
KEGGimmu:70208.
UCSCiuc011xbu.1. mouse. [Q80YQ2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_001159888.1. NM_001166416.1.
NP_081623.3. NM_027347.3.
UniGenei Mm.28020.

3D structure databases

ProteinModelPortali Q80YQ2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 213916. 2 interactions.
DIPi DIP-59234N.
IntActi Q80YQ2. 4 interactions.

PTM databases

PhosphoSitei Q80YQ2.

Proteomic databases

MaxQBi Q80YQ2.
PaxDbi Q80YQ2.
PRIDEi Q80YQ2.

Protocols and materials databases

DNASUi 70208.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 70208.
KEGGi mmu:70208.
UCSCi uc011xbu.1. mouse. [Q80YQ2-1 ]

Organism-specific databases

CTDi 9439.
MGIi MGI:1917458. Med23.
Rougei Search...

Phylogenomic databases

eggNOGi NOG305557.
HOGENOMi HOG000043810.
HOVERGENi HBG051122.
KOi K15166.
PhylomeDBi Q80YQ2.

Enzyme and pathway databases

Reactomei REACT_198602. PPARA activates gene expression.
REACT_206529. Generic Transcription Pathway.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

NextBioi 331172.
PROi Q80YQ2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q80YQ2.
Bgeei Q80YQ2.
CleanExi MM_MED23.
Genevestigatori Q80YQ2.

Family and domain databases

InterProi IPR021629. Mediator_Med23.
[Graphical view ]
Pfami PF11573. Med23. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMED23_MOUSE
AccessioniPrimary (citable) accession number: Q80YQ2
Secondary accession number(s): Q6ZPV7
, Q8CEC3, Q8K587, Q9CXY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: September 3, 2014
This is version 70 of the entry and version 2 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

External Data

Dasty 3

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