MED7_MOUSE
ID MED7_MOUSE Reviewed; 233 AA.
AC Q9CZB6; Q3UGV1; Q91VN3; Q9CWV8; Q9D0V9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 7;
DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 9;
DE Short=CRSP complex subunit 9;
DE AltName: Full=Mediator complex subunit 7;
GN Name=Med7; Synonyms=Crsp9;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Embryonic stem cell, Mammary gland, Melanocyte, and
RC Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
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 preinitiation complex with RNA polymerase II
CC and the general transcription factors (By similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 7 family.
CC {ECO:0000305}.
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DR EMBL; AK004354; BAB23272.1; -; mRNA.
DR EMBL; AK010357; BAB26877.1; -; mRNA.
DR EMBL; AK012799; BAB28478.1; -; mRNA.
DR EMBL; AK144918; BAE26135.1; -; mRNA.
DR EMBL; AK147739; BAE28106.1; -; mRNA.
DR EMBL; AK167407; BAE39496.1; -; mRNA.
DR EMBL; AL669948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011333; AAH11333.1; -; mRNA.
DR CCDS; CCDS36134.1; -.
DR RefSeq; NP_001098000.1; NM_001104530.1.
DR RefSeq; NP_001098026.1; NM_001104556.1.
DR RefSeq; NP_001098027.1; NM_001104557.1.
DR RefSeq; NP_079702.3; NM_025426.3.
DR RefSeq; XP_006533994.1; XM_006533931.3.
DR RefSeq; XP_006533995.1; XM_006533932.3.
DR RefSeq; XP_006533996.1; XM_006533933.3.
DR RefSeq; XP_006533997.1; XM_006533934.3.
DR PDB; 6W1S; EM; 4.02 A; D=11-167.
DR PDBsum; 6W1S; -.
DR AlphaFoldDB; Q9CZB6; -.
DR SMR; Q9CZB6; -.
DR BioGRID; 211303; 3.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR CORUM; Q9CZB6; -.
DR IntAct; Q9CZB6; 2.
DR STRING; 10090.ENSMUSP00000104855; -.
DR iPTMnet; Q9CZB6; -.
DR PhosphoSitePlus; Q9CZB6; -.
DR SwissPalm; Q9CZB6; -.
DR EPD; Q9CZB6; -.
DR MaxQB; Q9CZB6; -.
DR PaxDb; Q9CZB6; -.
DR PeptideAtlas; Q9CZB6; -.
DR PRIDE; Q9CZB6; -.
DR ProteomicsDB; 293454; -.
DR Antibodypedia; 16528; 248 antibodies from 25 providers.
DR DNASU; 66213; -.
DR Ensembl; ENSMUST00000020665; ENSMUSP00000020665; ENSMUSG00000020397.
DR Ensembl; ENSMUST00000109232; ENSMUSP00000104855; ENSMUSG00000020397.
DR Ensembl; ENSMUST00000170928; ENSMUSP00000131852; ENSMUSG00000020397.
DR GeneID; 66213; -.
DR KEGG; mmu:66213; -.
DR UCSC; uc007iok.2; mouse.
DR CTD; 9443; -.
DR MGI; MGI:1913463; Med7.
DR VEuPathDB; HostDB:ENSMUSG00000020397; -.
DR eggNOG; KOG0570; Eukaryota.
DR GeneTree; ENSGT00940000154444; -.
DR InParanoid; Q9CZB6; -.
DR OMA; PQHFDRR; -.
DR OrthoDB; 1356482at2759; -.
DR PhylomeDB; Q9CZB6; -.
DR TreeFam; TF314411; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 66213; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Med7; mouse.
DR PRO; PR:Q9CZB6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CZB6; protein.
DR Bgee; ENSMUSG00000020397; Expressed in metanephric loop of Henle and 249 other tissues.
DR ExpressionAtlas; Q9CZB6; baseline and differential.
DR Genevisible; Q9CZB6; MM.
DR GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO: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:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO: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; ISO:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR Gene3D; 6.10.140.200; -; 1.
DR InterPro; IPR037212; Med7/Med21-like.
DR InterPro; IPR009244; Mediatior_Med7.
DR InterPro; IPR044888; Mediatior_Med7_sf.
DR Pfam; PF05983; Med7; 1.
DR SUPFAM; SSF140718; SSF140718; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..233
FT /note="Mediator of RNA polymerase II transcription subunit
FT 7"
FT /id="PRO_0000079409"
FT REGION 187..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43513"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43513"
FT CONFLICT 26
FT /note="I -> S (in Ref. 3; AAH11333)"
FT /evidence="ECO:0000305"
FT CONFLICT 33..34
FT /note="KP -> GR (in Ref. 3; AAH11333)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..50
FT /note="FQ -> KR (in Ref. 3; AAH11333)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="D -> Y (in Ref. 1; BAB23272)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="N -> T (in Ref. 1; BAB23272)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="D -> N (in Ref. 1; BAB28478)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="K -> N (in Ref. 1; BAB28478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 27205 MW; CB340CCF5770541C CRC64;
MGEPQQVSAL PPPPMQYIKE YTDENIQEGL APKPPPPIKD SYMMFGNQFQ CDDLIIRPLE
SQGIERLHPM QFDHKKELRK LNMSILINFL DLLDILIRSP GSIKREEKLE DLKLLFVHVH
HLINEYRPHQ ARETLRVMME VQKRQRLETA ERFQKHLERV IEMIQNCLAS LPDDLPHSEA
GMRVKAEPMD TDDNSNCPGQ NEQQRESSGH RRDQIIEKDA ALCVLIDEMN ERP