MED23_MOUSE
ID MED23_MOUSE Reviewed; 1367 AA.
AC Q80YQ2; Q6ZPV7; Q8CEC3; Q8K587; Q9CXY8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 23;
DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 3;
DE Short=CRSP complex subunit 3;
DE AltName: Full=Mediator complex subunit 23;
DE AltName: Full=Protein sur-2 homolog;
DE Short=mSur-2;
GN Name=Med23; Synonyms=Crsp3, Kiaa1216, Sur2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, AND INTERACTION WITH CDK8; E1A AND ELK1.
RC STRAIN=C3H/HeJ;
RX PubMed=11934987; DOI=10.1126/science.1068943;
RA Stevens J.L., Cantin G.T., Wang G., Shevchenko A., Shevchenko A.,
RA Berk A.J.;
RT "Transcription control by E1A and MAP kinase pathway via Sur2 mediator
RT subunit.";
RL Science 296:755-758(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1114-1367 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 673-1367 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH E1A.
RX PubMed=15542641; DOI=10.1128/jvi.78.23.12888-12900.2004;
RA Fang L., Stevens J.L., Berk A.J., Spindler K.R.;
RT "Requirement of Sur2 for efficient replication of mouse adenovirus type
RT 1.";
RL J. Virol. 78:12888-12900(2004).
RN [6]
RP FUNCTION.
RX PubMed=14759369; DOI=10.1016/s1097-2765(03)00521-5;
RA Mo X., Kowenz-Leutz E., Xu H., Leutz A.;
RT "Ras induces mediator complex exchange on C/EBP beta.";
RL Mol. Cell 13:241-250(2004).
RN [7]
RP ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=16137621; DOI=10.1016/j.molcel.2005.08.008;
RA Park S.W., Li G., Lin Y.-P., Barrero M.J., Ge K., Roeder R.G., Wei L.-N.;
RT "Thyroid hormone-induced juxtaposition of regulatory elements/factors and
RT chromatin remodeling of Crabp1 dependent on MED1/TRAP220.";
RL Mol. Cell 19:643-653(2005).
RN [8]
RP FUNCTION.
RX PubMed=15749018; DOI=10.1016/j.molcel.2005.02.010;
RA Wang G., Balamotis M.A., Stevens J.L., Yamaguchi Y., Handa H., Berk A.J.;
RT "Mediator requirement for both recruitment and postrecruitment steps in
RT transcription initiation.";
RL Mol. Cell 17:683-694(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH CEBPB.
RX PubMed=20111005; DOI=10.1038/emboj.2010.3;
RA Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
RT "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and
RT SWI/SNF/Mediator implies an indexing transcription factor code.";
RL EMBO J. 29:1105-1115(2010).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional pre-initiation complex with RNA polymerase II
CC and the general transcription factors (By similarity). Also required
CC for transcriptional activation subsequent to the assembly of the pre-
CC initiation complex. Required for transcriptional activation by
CC adenovirus E1A protein. Required for ELK1-dependent transcriptional
CC activation in response to activated Ras signaling. {ECO:0000250,
CC ECO:0000269|PubMed:11934987, ECO:0000269|PubMed:14759369,
CC ECO:0000269|PubMed:15542641, ECO:0000269|PubMed:15749018}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Interacts with CEBPB (when
CC not methylated), CTNNB1, and GLI3. Interacts with CDK8 and ELK1.
CC {ECO:0000250|UniProtKB:Q9ULK4, ECO:0000269|PubMed:11934987,
CC ECO:0000269|PubMed:15542641, ECO:0000269|PubMed:20111005}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80YQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YQ2-2; Sequence=VSP_028382;
CC Name=3;
CC IsoId=Q80YQ2-3; Sequence=VSP_041583, VSP_041584;
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 23 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM28897.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB29019.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC26001.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAC98122.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF507918; AAM28897.1; ALT_INIT; mRNA.
DR EMBL; AK129312; BAC98122.1; ALT_INIT; mRNA.
DR EMBL; AK013854; BAB29019.1; ALT_INIT; mRNA.
DR EMBL; AK028545; BAC26001.1; ALT_SEQ; mRNA.
DR EMBL; BC005508; AAH05508.2; -; mRNA.
DR EMBL; BC050916; AAH50916.1; -; mRNA.
DR RefSeq; NP_001159888.1; NM_001166416.1.
DR RefSeq; NP_081623.3; NM_027347.3.
DR PDB; 6W1S; EM; 4.02 A; R=1-1367.
DR PDBsum; 6W1S; -.
DR AlphaFoldDB; Q80YQ2; -.
DR SMR; Q80YQ2; -.
DR BioGRID; 213916; 12.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR CORUM; Q80YQ2; -.
DR DIP; DIP-59234N; -.
DR IntAct; Q80YQ2; 10.
DR MINT; Q80YQ2; -.
DR STRING; 10090.ENSMUSP00000090316; -.
DR iPTMnet; Q80YQ2; -.
DR PhosphoSitePlus; Q80YQ2; -.
DR EPD; Q80YQ2; -.
DR MaxQB; Q80YQ2; -.
DR PaxDb; Q80YQ2; -.
DR PeptideAtlas; Q80YQ2; -.
DR PRIDE; Q80YQ2; -.
DR ProteomicsDB; 295864; -. [Q80YQ2-1]
DR ProteomicsDB; 295865; -. [Q80YQ2-2]
DR ProteomicsDB; 295866; -. [Q80YQ2-3]
DR DNASU; 70208; -.
DR GeneID; 70208; -.
DR KEGG; mmu:70208; -.
DR UCSC; uc011xbu.2; mouse. [Q80YQ2-1]
DR CTD; 9439; -.
DR MGI; MGI:1917458; Med23.
DR eggNOG; KOG1883; Eukaryota.
DR InParanoid; Q80YQ2; -.
DR OrthoDB; 94121at2759; -.
DR PhylomeDB; Q80YQ2; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 70208; 19 hits in 77 CRISPR screens.
DR ChiTaRS; Med23; mouse.
DR PRO; PR:Q80YQ2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80YQ2; protein.
DR GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:2000409; P:positive regulation of T cell extravasation; IMP:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR InterPro; IPR021629; Mediator_Med23.
DR PANTHER; PTHR12691; PTHR12691; 1.
DR Pfam; PF11573; Med23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1367
FT /note="Mediator of RNA polymerase II transcription subunit
FT 23"
FT /id="PRO_0000305931"
FT REGION 1343..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 54..55
FT /note="ES -> IV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041583"
FT VAR_SEQ 56..1367
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041584"
FT VAR_SEQ 291
FT /note="K -> KQTLNIA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11934987"
FT /id="VSP_028382"
FT CONFLICT 77
FT /note="S -> F (in Ref. 4; AAH50916)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="N -> Y (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="Q -> H (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="G -> R (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="Q -> H (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="K -> N (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 812..813
FT /note="ER -> DK (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="G -> S (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="N -> G (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062..1065
FT /note="VPED -> GSRKN (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1091
FT /note="D -> E (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1282
FT /note="D -> N (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1315
FT /note="E -> K (in Ref. 1; AAM28897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1367 AA; 156087 MW; FD7764FFB2A52B1A CRC64;
METQLQSIFE EVVKTEIIEE AFPGMFMDTP EDEKTKLISC LAAFRQFWSG LSQESHEQCV
QWIVKFIHGQ HSPKRISFLY DCLAMAVETG LLPPRMVCES LINSDSLEWE RTQLWALTFK
LVRKIIGGVD YKGVRDLLKA ILEKILTIPN TVSSAVVQQL LAAREVIAYI LERNACLLPA
YFAVTEIRKL YPEGKLPHWL LGNLVSDFVD TFRPTARINS ICGRCSLLPV VNNSGAICNS
WKLDPATLRF PLKGLLPYDK DLFEPQTALL RYVLEQPYSR DMVCNMLGLN KQHKQRCPVL
EDQLVDLVVY AMERSETEEK FDDGGTSQLL WQHLSSQLIF FVLFQFASFP HMVLSLHQKL
AGRGLIKGRD HLMWVLLQFI SGSIQKNALA DFLPVMKLFD LLYPEKECIP VPDINKPQST
HAFAMTCIWI HLNRKAQNGD STLQIPIPHS LKLHHEFLQQ SLRNKSLQMN DYKIALLCNA
YSTNSECFTL PMGALVETIY GNGIMRVPLP GTSCLASASV TPLPMNLLDS LTVHAKMSLI
HSIATRVIKL AHTKSSVALA PALVETYSRL LVYMEIESLG IKGFISQLLP TVFKSHAWGI
LHTLLEMFSH RMHHIQPHYR VQLLSHLHTL AAVAQTNQNQ LHLCVESTAL RLITALGSSE
VQPQFTRFLN DPKTVLSAES EELNRALILT LARATHVTDF FTGSDSIQGT WCKDILQTIM
NFTPHNWASH TLSCFPAPLQ AFFKQNNVPQ ESRFNLKKNV EEEYRKWKSM TDENEIITQF
SVQGFPPLFL CLLWKMLLET DHISQIGYKV LERIGARALV AHVRTFADFL VYEFSTSAGG
QQLNKCIEIL NDMVWKYNIV TLDRLILCLA MRSHEGNEAQ VCYFIIQLLL LKPNDFRNRV
SDFVKENSPE HWLQSDWHTK HMSYHKKYPE KLYFEGLAEQ VDPPVPIQSP YLPIYFGNVC
LRFLPVFDIV IHRFLELLPV SKSLETLLDH LGGLYKFHDR PVTYLYNTLH YYEMCLRNRD
HLKRKLVHAI IGSLKDNRPQ GWCLSDTYLK HAMNAREDNP WVPEDSYYCK LIGRLVDTMA
GKSPGPFPNC DWRFNEFPNP AAHALHVTCV ELMALAVPGK DVGNALLNVV LKSQPLVPRE
NITAWMNAIG LIITALPEPY WIVLHDRIVN VISSSSLTSE TEWVGYPFRL FDFTACHQSY
SEMSCSYTLA LAHAVWHHSS IGQLSLIPKF LTEALLPVVK TEFQLLYVYH LVGPFLQRFQ
QERTRCMIEI GVAFYDMLLN VDQCSTHLNY MDPICDFLYH MKYMFTGDSV KEQVEKIICN
LKPALKLRLR FITHISKMEP AVPPQALNSG SPAPQSNQVP ASLPVTQ
