MED14_MOUSE
ID MED14_MOUSE Reviewed; 1459 AA.
AC A2ABV5; Q3TQU3; Q6P1H5; Q9R0T1; Q9WTN9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 14;
DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 2;
DE Short=CRSP complex subunit 2;
DE AltName: Full=Mediator complex subunit 14;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 170 kDa component;
DE Short=Trap170;
GN Name=Med14; Synonyms=Crsp2, Gm641, Trap170;
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 [GENOMIC DNA / MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=10512684; DOI=10.1006/geno.1999.5944;
RA Takada S., Kamiya M., Arima T., Kagebayashi H., Shibata H., Muramatsu M.,
RA Chapman V.M., Wake N., Hayashizaki Y., Takagi N.;
RT "Detection and cloning of an X-linked locus associated with a NotI site
RT that is not methylated on mouse inactivated X chromosome by the RLGS-M
RT method.";
RL Genomics 61:92-100(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 INTERACTION WITH GATA1.
RX PubMed=17132730; DOI=10.1073/pnas.0604494103;
RA Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P., Zhang X.,
RA Guyot B., Roeder R.G., Borggrefe T.;
RT "The mediator complex functions as a coactivator for GATA-1 in
RT erythropoiesis via subunit Med1/TRAP220.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18504-18509(2006).
RN [6]
RP ERRATUM OF PUBMED:17132730.
RA Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P., Zhang X.,
RA Guyot B., Roeder R.G., Borggrefe T.;
RL Proc. Natl. Acad. Sci. U.S.A. 104:1442-1442(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117; SER-1124; SER-1133;
RP SER-1141 AND SER-1149, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
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. Interacts with AR, ESR1,
CC SREBF1 and STAT2 (By similarity). Interacts with GATA1. {ECO:0000250,
CC ECO:0000269|PubMed:17132730}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2ABV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2ABV5-2; Sequence=VSP_028037, VSP_028038;
CC Name=3;
CC IsoId=A2ABV5-3; Sequence=VSP_028035, VSP_028036;
CC Name=4;
CC IsoId=A2ABV5-4; Sequence=VSP_028033, VSP_028034;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 14 family.
CC {ECO:0000305}.
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DR EMBL; AB019028; BAA76610.1; -; mRNA.
DR EMBL; AB019029; BAA76611.1; -; Genomic_DNA.
DR EMBL; AK163306; BAE37289.1; -; mRNA.
DR EMBL; AL662925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX000537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065072; AAH65072.1; -; mRNA.
DR CCDS; CCDS40874.1; -. [A2ABV5-1]
DR RefSeq; NP_001041673.1; NM_001048208.1. [A2ABV5-1]
DR RefSeq; NP_036135.3; NM_012005.3.
DR PDB; 6W1S; EM; 4.02 A; I=1-1459.
DR PDBsum; 6W1S; -.
DR AlphaFoldDB; A2ABV5; -.
DR SMR; A2ABV5; -.
DR BioGRID; 205047; 6.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR CORUM; A2ABV5; -.
DR IntAct; A2ABV5; 4.
DR MINT; A2ABV5; -.
DR STRING; 10090.ENSMUSP00000094239; -.
DR iPTMnet; A2ABV5; -.
DR PhosphoSitePlus; A2ABV5; -.
DR EPD; A2ABV5; -.
DR MaxQB; A2ABV5; -.
DR PaxDb; A2ABV5; -.
DR PeptideAtlas; A2ABV5; -.
DR PRIDE; A2ABV5; -.
DR ProteomicsDB; 292179; -. [A2ABV5-1]
DR ProteomicsDB; 292180; -. [A2ABV5-2]
DR ProteomicsDB; 292181; -. [A2ABV5-3]
DR ProteomicsDB; 292182; -. [A2ABV5-4]
DR Antibodypedia; 10773; 165 antibodies from 30 providers.
DR DNASU; 26896; -.
DR Ensembl; ENSMUST00000096495; ENSMUSP00000094239; ENSMUSG00000064127. [A2ABV5-1]
DR GeneID; 26896; -.
DR KEGG; mmu:26896; -.
DR UCSC; uc009sqz.1; mouse. [A2ABV5-1]
DR UCSC; uc009srd.1; mouse. [A2ABV5-3]
DR CTD; 9282; -.
DR MGI; MGI:1349442; Med14.
DR VEuPathDB; HostDB:ENSMUSG00000064127; -.
DR eggNOG; KOG1875; Eukaryota.
DR GeneTree; ENSGT00390000001021; -.
DR HOGENOM; CLU_001928_0_0_1; -.
DR InParanoid; A2ABV5; -.
DR OMA; SPAGSFM; -.
DR OrthoDB; 1215335at2759; -.
DR PhylomeDB; A2ABV5; -.
DR TreeFam; TF314388; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 26896; 31 hits in 72 CRISPR screens.
DR ChiTaRS; Med14; mouse.
DR PRO; PR:A2ABV5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2ABV5; protein.
DR Bgee; ENSMUSG00000064127; Expressed in metanephric cortical collecting duct and 242 other tissues.
DR ExpressionAtlas; A2ABV5; baseline and differential.
DR Genevisible; A2ABV5; MM.
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:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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; 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:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR InterPro; IPR013947; Mediator_Med14.
DR PANTHER; PTHR12809; PTHR12809; 1.
DR Pfam; PF08638; Med14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1459
FT /note="Mediator of RNA polymerase II transcription subunit
FT 14"
FT /id="PRO_0000304585"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..572
FT /note="Interaction with STAT2"
FT /evidence="ECO:0000250"
FT REGION 506..830
FT /note="Interaction with SREBF1"
FT /evidence="ECO:0000250"
FT REGION 979..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 75..79
FT /note="LXXLL motif 1"
FT MOTIF 1187..1191
FT /note="LXXLL motif 2"
FT COMPBIAS 1003..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60244"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60244"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028033"
FT VAR_SEQ 435..1459
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028034"
FT VAR_SEQ 436..471
FT /note="SIETALPALIVPILEPCGNSECLHIFVDLHSGMFQL -> KHSRAGEMAQQL
FT RVPTALPKVLSSNPINHMVAHNHL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10512684"
FT /id="VSP_028035"
FT VAR_SEQ 472..1459
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10512684"
FT /id="VSP_028036"
FT VAR_SEQ 747..770
FT /note="PSRHVYLTYENLLSEPVGGRKVVE -> KIFHTVFLLMSIFLKVLVTISFFL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028037"
FT VAR_SEQ 771..1459
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028038"
FT CONFLICT 158
FT /note="F -> C (in Ref. 2; BAE37289)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..347
FT /note="WN -> C (in Ref. 1; BAA76611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1459 AA; 160966 MW; FE61E45E8E99E4E9 CRC64;
MAPVQLDNHQ LIPPGGGGGS SGGGGSSSGS ASAPAPPPPA AAVAAAAAAA ASPGYRLSTL
IEFLLHRAYS ELMVLTDLLP RKSDVERKIE IVQFASRTRQ LFVRLLALVK WANDAGKVEK
CAMISSFLDQ QAILFVDTAD RLASLARDAL VHARLPSFAI PYAIDVLTTG SYPRLPTCIR
DKIIPPDPIT KIEKQATLHQ LNQILRHRLV TTDLPPQLAN LTVANGRVKF RVEGEFEATL
TVMGDDPEVP WRLLKLEILV EDKETGDGRA LVHSMQIDFI HQLVQSRLFA DEKPLQDMYN
CLHCFCLSLQ LEVLHSQTLM LIRERWGDLV QVERYHAGKS LSLSVWNQQV LGRKTGTASV
HKVTIKIDEN DVSKPLQIFH DPPLPASDSK LVERAMKIDH LSIEKLLIDS VHARAHQRLQ
ELKAILRSFN ANESSSIETA LPALIVPILE PCGNSECLHI FVDLHSGMFQ LMLYGLDPAT
LEDMEKSLND DMKRIIPWIQ QLKFWLGQQR CKQSIKHLPT ITTETLQLAN YSTHPIGSLS
KNKLFIKLTR LPQYYIVVEM LEVPNKPTQL SYNYYFMSVS TADREDSPVM ALLLQQFKDN
IQDLMSYTKT GKQTRTGTKH KLSDDPCPID SKKAKRSGEM CAFNKVLAHF VAMCDTNMPF
VGLRLELSNL EIPHQGVQVE GDGFNHAIRL LKIPPCKGIS EETQKALDRS LLDCTFRLQG
RNNRTWVAEL VFANCPLNGT STREQGPSRH VYLTYENLLS EPVGGRKVVE MFLNDWSSIA
RLYECVLEFA RSLPEIPAHL NIFSEVRVYN YRKLILCYGT TKGSSISIQW NSIHQKFHIA
LGTVGPNSGC SNCHNTILHQ LQEMFNKTPN VVQLLQVLFD TQAPLNAINK LPTVPMLGLT
QRTNTAYQCF SILPQSSTHI RLAFRNMYCI DIYCRSRGVV AIRDGAYSLF DNSKLVEGFY
PAPGLKTFLN MFVDSNQDAR RRSVNEDDNP PSPIGGDMMD SLISQLQPPQ QQPFPKQPGT
SGAYPLTSPP TSYHSTVNQS PSMMHTQSPG NLHAASSPSG ALRAPSPASF VPTPPPSSHG
ISIGPGASFA SPHGTLDPSS PYTMVSPSGR AGNWPGSPQV SGPSPATRLP GMSPANPSLH
SPVPDVSHSP RAGTSSQTMP TNMPPPRKLP QRSWAASIPT ILTHSALNIL LLPSPTPGLV
PGLAGSYLCS PLERFLGSVI MRRHLQRIIQ QETLQLINSN EPGVIMFKTD ALKCRVALSP
KTNQTLQLKV TPENAGQWKP DELQVLEKFF ETRVAGPPFK ANTLIAFTKL LGAPTHILRD
CVHIMKLELF PDQATQLKWN VQFCLTIPPS APPIAPPGTP AVVLKSKMLF FLQLTQKTSV
PPQEPVSIIV PIIYDMASGT TQQADIPRQQ NSSVAAPMMV SNILKRFAEM NPPRQGECTI
FAAVRDLMAN LTLPPGGRP
