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MED13_MOUSE
ID   MED13_MOUSE             Reviewed;        2171 AA.
AC   Q5SWW4; Q3V3P6; Q6ZQ90;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
DE   AltName: Full=Thyroid hormone receptor-associated protein 1;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 240 kDa component;
DE            Short=Trap240;
GN   Name=Med13; Synonyms=Kiaa0593, Thrap1, Trap240;
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 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 931-2171.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 803-2029.
RC   TISSUE=Brain;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND SER-537, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, 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 13 family.
CC       {ECO:0000305}.
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DR   EMBL; AL592065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL596256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK037303; BAE20510.1; -; mRNA.
DR   EMBL; AK129168; BAC97978.1; -; mRNA.
DR   CCDS; CCDS36267.1; -.
DR   RefSeq; NP_001074400.1; NM_001080931.1.
DR   AlphaFoldDB; Q5SWW4; -.
DR   BioGRID; 236522; 6.
DR   ComplexPortal; CPX-3266; CKM complex variant 1.
DR   ComplexPortal; CPX-3267; CKM complex variant 2.
DR   DIP; DIP-61082N; -.
DR   IntAct; Q5SWW4; 4.
DR   MINT; Q5SWW4; -.
DR   STRING; 10090.ENSMUSP00000044268; -.
DR   iPTMnet; Q5SWW4; -.
DR   PhosphoSitePlus; Q5SWW4; -.
DR   EPD; Q5SWW4; -.
DR   jPOST; Q5SWW4; -.
DR   MaxQB; Q5SWW4; -.
DR   PaxDb; Q5SWW4; -.
DR   PeptideAtlas; Q5SWW4; -.
DR   PRIDE; Q5SWW4; -.
DR   ProteomicsDB; 292287; -.
DR   Antibodypedia; 31215; 82 antibodies from 23 providers.
DR   DNASU; 327987; -.
DR   Ensembl; ENSMUST00000043624; ENSMUSP00000044268; ENSMUSG00000034297.
DR   GeneID; 327987; -.
DR   KEGG; mmu:327987; -.
DR   UCSC; uc007ksk.1; mouse.
DR   CTD; 9969; -.
DR   MGI; MGI:3029632; Med13.
DR   VEuPathDB; HostDB:ENSMUSG00000034297; -.
DR   eggNOG; KOG3600; Eukaryota.
DR   GeneTree; ENSGT00390000013680; -.
DR   HOGENOM; CLU_000508_0_0_1; -.
DR   InParanoid; Q5SWW4; -.
DR   OMA; WWGEDPS; -.
DR   OrthoDB; 177884at2759; -.
DR   PhylomeDB; Q5SWW4; -.
DR   TreeFam; TF316867; -.
DR   Reactome; R-MMU-212436; Generic Transcription Pathway.
DR   BioGRID-ORCS; 327987; 20 hits in 76 CRISPR screens.
DR   ChiTaRS; Med13; mouse.
DR   PRO; PR:Q5SWW4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SWW4; protein.
DR   Bgee; ENSMUSG00000034297; Expressed in manus and 212 other tissues.
DR   Genevisible; Q5SWW4; MM.
DR   GO; GO:0016592; C:mediator complex; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR   GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0070328; P:triglyceride homeostasis; IDA:BHF-UCL.
DR   InterPro; IPR009401; Med13_C.
DR   InterPro; IPR041285; MID_MedPIWI.
DR   Pfam; PF06333; Med13_C; 1.
DR   Pfam; PF18296; MID_MedPIWI; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..2171
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   13"
FT                   /id="PRO_0000314240"
FT   REGION          318..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1483..1503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1532..1626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2012..2042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1187..1191
FT                   /note="LXXLL motif 1"
FT   MOTIF           1278..1282
FT                   /note="LXXLL motif 2"
FT   COMPBIAS        434..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        971..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1053
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1532..1609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHV7"
FT   MOD_RES         500
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHV7"
FT   MOD_RES         504
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHV7"
FT   MOD_RES         530
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         825
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHV7"
FT   MOD_RES         889
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHV7"
FT   MOD_RES         1028
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHV7"
FT   CONFLICT        1299..1322
FT                   /note="RPWGVQGPLTWQQFHKMAGRGSYG -> GTDESAVVPEIHQFHKSLGQPFYE
FT                   (in Ref. 3; BAC97978)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2171 AA;  238591 MW;  FD54462F5DC387B9 CRC64;
     MSSSFVSNGA SLEDCHCNLF CLADLTGIKW KRYVWQGPTS APILFPVTEE DPILSSFSRC
     LKADVLGVWR RDQRPGRREL WIFWWGKDPN FADLIHHDLS EEEDGVWENG LSYECRTLLF
     KAVHNLLERC LMNRNFVRIG KWFVKPYEKD EKPINKSEHL SCSFTFFLHG DSNVCTSVEI
     NQHQPVYLLS EEHVTLAQQS NSPFQVILSP FGLNGTLTGQ AFKMSDSATK KLIGEWKQFY
     PISCGLKEMS EEKQDDMDWE DDSLAAVEVL VAGVRMIYPA CFVLVPQSDI PAPSSVGASH
     CSASCLGIHQ VPASTRDPAM SSVTLTPPTS PEEVQTVDPQ SAQKWVKFSS VSDGFSTDST
     SHHGGKIPRK LANHVVDRVW QECNMNRLQN KRKYSATSSG LCEEETADKI GCWDFVEATQ
     RTSCSCLRHK SLKTRNTGQQ GQAPSLGQQQ QVLPKHKTNE KQDKSEKPQK RPLTPFHHRV
     SVSDEIGMDT DSASQRLVIS AADSQVRFSN IRTNDVAKTP QMHGTELANS PQPPPLSPHP
     CDVVDEGVTK TPSTPQSQHF YQMPTPDPLV PTKPMEDRID SLSQSFPPPF QEAVEPTVYV
     GTAVSLEEDE ANVAWKYYKV PKKKDVEFLP PQLPNDKFKD DPVGPFGQES VTSVTELMVQ
     CKKPLKVSDE IVQQYQIKNQ YLSAIASDTE QEPKIDPYAF VEGDEEFIFT DKKDRQNSER
     EAGKKHKVED GTSAVTVLSH EEDAMSLFSP SKQDAPRPTN HARPPSTSLI YDSDLAVSYT
     DLDNLFNSDE DELTPGSKKS ASGSDDKASS KESKTGNLDP LSCISTADLH KMYPTPPSLE
     QHIMGFSPMN MNNKEYGSVD TAPGGTVLEG NSSSVGTQFR IEVEEGFCSP KPSEIKDFSY
     VYKPENCQVL VGCSMFAPLK TLPSHCLPPI KLPEECVYRQ SWTVGKLDLL PSGPSMPFIK
     EGDGSNLDQD YGPAYTPQTH ASFGMPPSSA PPSNGGAGIL PSPSTPRFPT PRTPRTPRTP
     RGAGGPASAQ GSVKYENSDL YSPASTPSTC RPLNSVEPAT VPSIPEAHSL YVNLILSESV
     MNLFKDCNFD SCCICVCNMN IKGADVGVYI PDPTQEAQYR CTCGFSAVMN RKFGNNSGLF
     LEDELDIIGR NTDCGKEAEK RFEALRASSV ENVNGGLKES EKVPDELILL LQDQCTNLFS
     PFGAADQDPF PKVGISSNWV RVEERDCCSD CCLALEHGRQ FMDNMSGGKV DEALVRSSCL
     HPWAKQNDAS VQCSQDILRM LLSLQPVLQD AIQKKRTVRP WGVQGPLTWQ QFHKMAGRGS
     YGTDESPEPL PIPTFLLGYD YDFLVLSPFA LPYWEKLMLE PYGSQRDIAY VVLCPENEAL
     LNGARSFFRD LTAIYESCRL GQHRPISRLL TDGIMKVGAT ASKKLSEKFV TEWFSQAADG
     NNEAFSKLKL YAQVCRYDLG PYLASQPLDS SLLSQPNLVA PPNQSLVTAP QMTNTGNANA
     PSATLASAAS STMTMTSGVP ISTSVATANS TLTTTSSSSS SSLSSGVSSN KLPSFPPFGS
     MNTSGTGSMS AQASTVQSGQ LGGQQSSSLQ AAGISGESAS LPTQPHPDVS ESTMDRDKVG
     IPTDGDSHAI TYPPAIVVYI IDPFTYENKD ESTNSSNVWT LGLLRCFLEM VQTLPPHIKS
     TVSVQIVPCQ YLLQPVKHDD RQIYSQHLKS LAFSVFTQCR RPLPTSTNVK TLTGFGPGLA
     METALKSPDR PECIRLYTPP FILAPVKDKQ TELGETFGEA GQKYNVLFVG YCLSHDQRWI
     LASCTDLYGE LLETCIINID VPNRARRKKG SARRFGLQKL WEWCLGLVQM SSLPWRVVIG
     RLGRIGHGEL KDWSCLLSRR NLQSLSKRLK DMCRMCGISA ADSPSILSAC LVAMEPQGSF
     VIMPDSVSTG SVFGRSTTLN MQTPQLNTPQ DTSCTHILVF PTSASVQVAS ATYTTENLDL
     AFNPNNDGAD GMGIFDLLDT GDDLDPDIIN ILPASPTASP VHSPGSHYPH GGDAGKGQGT
     DRLLSTESHD EVTNILQQPL ALGYFVSTAK AGPLPDWFWS ACPQAQYQCP LFLKASLHLH
     VPSVQSDELL HSKHSHPLDS NQTSDVLRFV LEQYNALSWL TCDPAVQDRR SCLPVHFVVL
     NQLYNFIMNM L
 
 
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