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MED26_MOUSE
ID   MED26_MOUSE             Reviewed;         588 AA.
AC   Q7TN02; Q8BUP9; Q8R1G7; Q9CS67;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 26;
DE   AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 7;
DE            Short=CRSP complex subunit 7;
DE   AltName: Full=Mediator complex subunit 26;
GN   Name=Med26; Synonyms=Crsp7;
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; TISSUE=Embryo, and Spinal cord;
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 MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, 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   [4]
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). {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). Interacts
CC       with CEBPB (when not methylated)(PubMed:20111005).
CC       {ECO:0000250|UniProtKB:O95402, ECO:0000269|PubMed:20111005}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 26 family.
CC       {ECO:0000305}.
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DR   EMBL; AK017726; BAB30898.1; -; mRNA.
DR   EMBL; AK083035; BAC38738.1; -; mRNA.
DR   EMBL; BC024555; AAH24555.1; -; mRNA.
DR   EMBL; BC054737; AAH54737.1; -; mRNA.
DR   CCDS; CCDS22416.1; -.
DR   RefSeq; NP_081761.2; NM_027485.4.
DR   AlphaFoldDB; Q7TN02; -.
DR   SMR; Q7TN02; -.
DR   BioGRID; 214175; 5.
DR   ComplexPortal; CPX-3264; Core mediator complex.
DR   IntAct; Q7TN02; 6.
DR   MINT; Q7TN02; -.
DR   STRING; 10090.ENSMUSP00000058697; -.
DR   iPTMnet; Q7TN02; -.
DR   PhosphoSitePlus; Q7TN02; -.
DR   EPD; Q7TN02; -.
DR   jPOST; Q7TN02; -.
DR   MaxQB; Q7TN02; -.
DR   PaxDb; Q7TN02; -.
DR   PeptideAtlas; Q7TN02; -.
DR   PRIDE; Q7TN02; -.
DR   ProteomicsDB; 293452; -.
DR   DNASU; 70625; -.
DR   Ensembl; ENSMUST00000058534; ENSMUSP00000058697; ENSMUSG00000045248.
DR   GeneID; 70625; -.
DR   KEGG; mmu:70625; -.
DR   UCSC; uc009mgg.2; mouse.
DR   CTD; 9441; -.
DR   MGI; MGI:1917875; Med26.
DR   VEuPathDB; HostDB:ENSMUSG00000045248; -.
DR   eggNOG; KOG1105; Eukaryota.
DR   GeneTree; ENSGT00390000000259; -.
DR   HOGENOM; CLU_478915_0_0_1; -.
DR   InParanoid; Q7TN02; -.
DR   OMA; NMVVVLE; -.
DR   OrthoDB; 459216at2759; -.
DR   PhylomeDB; Q7TN02; -.
DR   TreeFam; TF328436; -.
DR   Reactome; R-MMU-212436; Generic Transcription Pathway.
DR   BioGRID-ORCS; 70625; 35 hits in 74 CRISPR screens.
DR   ChiTaRS; Med26; mouse.
DR   PRO; PR:Q7TN02; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q7TN02; protein.
DR   Bgee; ENSMUSG00000045248; Expressed in seminiferous tubule of testis and 177 other tissues.
DR   Genevisible; Q7TN02; MM.
DR   GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR   GO; GO:0016592; C:mediator complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR   Gene3D; 1.20.930.10; -; 1.
DR   InterPro; IPR042376; MED26.
DR   InterPro; IPR031416; Med26_C.
DR   InterPro; IPR031417; Med26_Mid.
DR   InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   PANTHER; PTHR15201; PTHR15201; 1.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF15693; Med26_C; 1.
DR   Pfam; PF15694; Med26_M; 1.
DR   SMART; SM00509; TFS2N; 1.
DR   SUPFAM; SSF47676; SSF47676; 1.
DR   PROSITE; PS51319; TFIIS_N; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..588
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   26"
FT                   /id="PRO_0000304959"
FT   DOMAIN          10..87
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT   REGION          112..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..328
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         435
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         458
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95402"
FT   CONFLICT        64
FT                   /note="T -> N (in Ref. 1; BAC38738)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212..214
FT                   /note="SDN -> VII (in Ref. 1; BAB30898)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   588 AA;  64680 MW;  0CAFE5930234B293 CRC64;
     MTAAPASPQQ MRDRLLQAID SQSNIRNMVA VLEVISSLER YPITKEALEE TRLGKLINDV
     RKKTKNEELA KRAKRLLRSW QKLIEPVHQN EVALRALAGA AGSANGGAHN CRPEMGVAGA
     PKSIHDLKNR NDIQRLPGQR LDRLGSRKRR GDQRDLGHPG PPHKVSKGSP DPLVPNASPL
     PTNGISGSPE SLPSPLDGSG HLGPDGSRLE PSDNEKHSTK IPVNAVRPRP SSPGLGKPPV
     PCLQTKAAQL QQLDRADESP GPPYPRGSSR CSFSPRNSRH EGSFSRHRSS YIPKGQVSSP
     SPWPQPPDNT QVPSPLPLAQ PPTPPVRRQE LLPNAESPVH WPEQSEGHPR LTGPACRAGF
     SPDSSKADSD ATSSGGSDSK KKKRYRPRDY TVNLDGQVAE AGVKPVRLKE RKLTFDPMTR
     QIRPLTQKEP VRADSPVPTE QLPRTELEQQ EVKASLQSPF EQTNWKELSR NEIIQSYLSR
     QSSLLSSSGA QTPGAHHFMA EYLKQEESSR QGARQPHVLL PLPTPTDLPG LTREVTQDDL
     DRIQAQQWPG VNGCEDTQGN WYDWTQCISL DPHGDDGRLN ILPYVCLD
 
 
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