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