MED15_MOUSE
ID MED15_MOUSE Reviewed; 789 AA.
AC Q924H2; G3X8S4;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 15;
DE AltName: Full=Mediator complex subunit 15;
DE AltName: Full=Positive cofactor 2 glutamine/Q-rich-associated protein;
DE Short=PC2 glutamine/Q-rich-associated protein;
DE Short=mPcqap;
GN Name=Med15; Synonyms=Pcqap;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11414760; DOI=10.1006/geno.2001.6566;
RA Berti L., Mittler G., Przemeck G.K.H., Stelzer G., Guenzler B., Amati F.,
RA Conti E., Dallapiccola B., Hrabe' de Angelis M., Novelli G.,
RA Meisterernst M.;
RT "Isolation and characterization of a novel gene from the DiGeorge
RT chromosomal region that encodes for a mediator subunit.";
RL Genomics 74:320-332(2001).
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, 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).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-347, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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. Required for cholesterol-
CC dependent gene regulation. Positively regulates the Nodal signaling
CC pathway (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 SMAD2,
CC SMAD3, SREBF1 and SREBF2. Interacts with WWTR1 (By similarity).
CC Interacts with TRIM11 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc ubiquitously expressed at low levels
CC with slightly elevated levels in the pharyngeal arches and in the
CC forelimb buds. At 10.5 dpc expression was more pronounced in the first
CC and second pharyngeal arches, the nasal processes and the limb buds. At
CC 11.5 dpc expression is high in frontonasal region, maxillary and
CC mandibular processes of the first and second pharyngeal arch and
CC developing fore and hindlimbs. From 11.5 dpc-12.5 dpc expression is
CC seen in the distal parts of the developing limbs and in the facial
CC region. At 12.5 dpc transcripts were found in the developing hair
CC follicles of the vibrissae.
CC -!- PTM: Ubiquitinated by TRIM11, leading to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 15 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK58424.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF328770; AAK58424.1; ALT_FRAME; mRNA.
DR EMBL; AC087802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97476.1; -; Genomic_DNA.
DR CCDS; CCDS37274.1; -.
DR RefSeq; NP_291087.2; NM_033609.3.
DR PDB; 6W1S; EM; 4.02 A; J=620-786.
DR PDBsum; 6W1S; -.
DR AlphaFoldDB; Q924H2; -.
DR BMRB; Q924H2; -.
DR SMR; Q924H2; -.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR DIP; DIP-59237N; -.
DR IntAct; Q924H2; 5.
DR MINT; Q924H2; -.
DR STRING; 10090.ENSMUSP00000012259; -.
DR iPTMnet; Q924H2; -.
DR PhosphoSitePlus; Q924H2; -.
DR EPD; Q924H2; -.
DR jPOST; Q924H2; -.
DR MaxQB; Q924H2; -.
DR PaxDb; Q924H2; -.
DR PRIDE; Q924H2; -.
DR ProteomicsDB; 293451; -.
DR Antibodypedia; 282; 305 antibodies from 32 providers.
DR DNASU; 94112; -.
DR Ensembl; ENSMUST00000012259; ENSMUSP00000012259; ENSMUSG00000012114.
DR GeneID; 94112; -.
DR KEGG; mmu:94112; -.
DR UCSC; uc007yls.2; mouse.
DR CTD; 51586; -.
DR MGI; MGI:2137379; Med15.
DR VEuPathDB; HostDB:ENSMUSG00000012114; -.
DR eggNOG; KOG4274; Eukaryota.
DR GeneTree; ENSGT00730000111140; -.
DR InParanoid; Q924H2; -.
DR OMA; CCLDDKR; -.
DR OrthoDB; 1424577at2759; -.
DR PhylomeDB; Q924H2; -.
DR TreeFam; TF324988; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 94112; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Med15; mouse.
DR PRO; PR:Q924H2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q924H2; protein.
DR Bgee; ENSMUSG00000012114; Expressed in animal zygote and 249 other tissues.
DR ExpressionAtlas; Q924H2; baseline and differential.
DR GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
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:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR Gene3D; 1.10.246.20; -; 1.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR019087; Med15.
DR Pfam; PF09606; Med15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..789
FT /note="Mediator of RNA polymerase II transcription subunit
FT 15"
FT /id="PRO_0000058265"
FT REGION 9..73
FT /note="Interaction with SREBF1"
FT /evidence="ECO:0000250"
FT REGION 88..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 548..565
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 283..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 347
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 4
FT /note="S -> W (in Ref. 1; AAK58424)"
FT CONFLICT 17
FT /note="Q -> L (in Ref. 1; AAK58424)"
FT CONFLICT 147
FT /note="A -> T (in Ref. 1; AAK58424)"
FT CONFLICT 166
FT /note="Q -> R (in Ref. 1; AAK58424)"
FT CONFLICT 327
FT /note="Q -> R (in Ref. 1; AAK58424)"
SQ SEQUENCE 789 AA; 86607 MW; A536FF2A75AE0771 CRC64;
MDVSGQETDW RSAAFRQKLV SQIEDAMRKA GVAHSKSSKD MESHVFLKAK TRDEYLSLVA
RLIIHFRDIH NKKSQASVSD PMNALQSLTG GPTPGAAGIG MPPRGPGQSL GGMGGLGAMG
QPLPLSGQPP PGTSGMAPHG MAVVSTATPQ TQLQLQQVAL QQQQQQQQQQ QFQQQQAALQ
QQQQQQQQQQ QQQQFQAQQN AMQQQFQAVV QQQQLQQQQQ QQHLIKLHHQ SQQQQIQQQQ
LQRMAQLQLQ QQQQQQQQQA LQAQPPMQQP SMQQPQPPPS QALPQQLSQL HHPQHHQPPP
QAQQSPIAQN QPPQIPPQSQ SQPLVSQAQA LPGPMLYAAQ QQLKFVRAPM VVQQPQVQPQ
VQQVQPQVQP QAAVQAAQSA QMVAPGVQMI AEALAQGGMH VRARFPPTST MSAGPSSSIS
LGGQPTTQVS QSSLTMLSSP SPGQQVQTPQ SMPPPPQPSP QPGSQPNSNV SSGPAPSPSS
FLPSPSPQPS QSPVTARTPQ NFSVPSPGPL NTPVNPSSVM SPAGSSQAEE QQYLDKLKQL
SKYIEPLRRM INKIDKNEDR KKDLSKMKSL LDILTDPSKR CPLKTLQKCE IALEKLKNDM
AVPTPPPPPV LPTKQQDLCQ PLLDAVLANI RSPVFNHSLY RTFVPAMMAI HGPPIVSPVV
CSRKRRFEED ERQSIPNVLQ GEVARLDPKF LVNLDPSHCS NNGTVHLICK LDDKDLPSVP
PLELSVPADY PAQSPMWIDR QWQYDANPFL QSVHRCMTSR LLQLPDKHSV TALLNTWAQS
IHQACLSAA
