MED15_SCHPO
ID MED15_SCHPO Reviewed; 1063 AA.
AC Q9Y808; Q9P788;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 15;
GN Name=med15;
GN ORFNames=SPBC146.01 {ECO:0000312|PomBase:SPBC146.01}, SPBP35G2.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH HRP1.
RX PubMed=20622008; DOI=10.1074/jbc.m110.153858;
RA Khorosjutina O., Wanrooij P.H., Walfridsson J., Szilagyi Z., Zhu X.,
RA Baraznenok V., Ekwall K., Gustafsson C.M.;
RT "A chromatin-remodeling protein is a component of fission yeast mediator.";
RL J. Biol. Chem. 285:29729-29737(2010).
RN [5]
RP GENE MODEL REVISION.
RX PubMed=24929437; DOI=10.1038/nsmb.2843;
RA Duncan C.D., Mata J.;
RT "The translational landscape of fission-yeast meiosis and sporulation.";
RL Nat. Struct. Mol. Biol. 21:641-647(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. Component of a med15-hrp1
CC subcomplex, linking the Mediator complex to the chromatin-remodeling
CC activity of hrp1 at a distinct subset of hrp1-bound gene promoters.
CC {ECO:0000269|PubMed:20622008}.
CC -!- SUBUNIT: Component of the Mediator complex. Component of a med15-hrp1
CC subcomplex, which flexibly associates with the other Mediator
CC components. {ECO:0000269|PubMed:20622008}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 15 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87377.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU329671; CAB87377.1; ALT_SEQ; Genomic_DNA.
DR PIR; T39415; T39415.
DR RefSeq; NP_595390.2; NM_001021297.2.
DR AlphaFoldDB; Q9Y808; -.
DR SMR; Q9Y808; -.
DR BioGRID; 276265; 5.
DR STRING; 4896.SPBC146.01.1; -.
DR iPTMnet; Q9Y808; -.
DR PaxDb; Q9Y808; -.
DR PRIDE; Q9Y808; -.
DR EnsemblFungi; SPBC146.01.1; SPBC146.01.1:pep; SPBC146.01.
DR GeneID; 2539712; -.
DR KEGG; spo:SPBC146.01; -.
DR PomBase; SPBC146.01; med15.
DR VEuPathDB; FungiDB:SPBC146.01; -.
DR eggNOG; ENOG502QVXD; Eukaryota.
DR HOGENOM; CLU_297391_0_0_1; -.
DR InParanoid; Q9Y808; -.
DR PRO; PR:Q9Y808; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0016592; C:mediator complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0036033; F:mediator complex binding; IPI:PomBase.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:PomBase.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR CDD; cd12191; gal11_coact; 1.
DR Gene3D; 1.10.246.20; -; 1.
DR InterPro; IPR033789; Gal11_coact.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR036546; MED15_KIX.
DR InterPro; IPR008626; Mediator_Med15_fun.
DR Pfam; PF16987; KIX_2; 1.
DR Pfam; PF05397; Med15_fungi; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1063
FT /note="Mediator of RNA polymerase II transcription subunit
FT 15"
FT /id="PRO_0000116849"
FT REGION 149..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1063 AA; 118453 MW; 9C8C105AA82CF71C CRC64;
MNRNVDKGWQ AQIRPNERQS IALQIAQTLR IISPSISEVQ LMNMALSFER QAFDGASSKN
EYLTTCGKKT AQLRDQIRDT LQATQMKQMP SVYNNAGNVG ALPTAGPNRL ANNPRVMPRL
QNQNVPMQAG MQQFARNMKL TPQQRQFLLQ QSQIQQQRQQ QQQQSQQPQQ TQQPQASSPT
APNTEANQQR SGSVPGRIVP ALTQQQLNNL CNQITALLAR NGNPPIPMQK LQSMPPARLI
SIYQNQIQKF RSLQHMQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQK QAPQNAFFPN
PQGNVGAQSL QSMSPQDQPS TQQQQPQRTA APPNNPNVNA TNNNRINIEM LNIPVPKQLF
DQIPNLPPNV KIWRDVLELG QSQRLPPEQL KLIGMLYRKH LQIILQHRQQ QLNKIQNARM
NSQNAPNTNK LGNPQPDNTG NPQAFSQQAF AQQQQQQQQQ LHRTSNPTSA SVTSQNGQQP
INTKLSANAA KTNYQSYLTN KARNATQPTQ PPVSQVDYSN NLPPNLDTSS TFRSSASPPS
AFTKAGNEAL SVPLSGARNT AASRPTNLAA GNSSASIVQQ LLECGGTMGQ QKMTSRIREL
TERVMHSLMR PVPLDLPHDQ KVMIASLIKS AYPMFSRTNQ LICLFYCLTG NEEATIQLIQ
MRHIFKLQLE GLQQGVFTCA PQTLAKIKEK TSRYFAFVKA QLLRLHHEVN NNNMSIQNAL
AHISSLRTAS INQQQQPQPQ SQQQQQASQF PQAPSVSSNV RPINGSIPNA QPSVPGQAQP
AAKANSVGNT SFPVDSKLAF QSLDVSQPDL QAKQKIASQV MKHGLKPEDL KLPPSKKKKI
ENLSTVQKPK DSVVNTPDVI MSSVDEIPSS VSPGTIAKEE GMAKAREEAI ANPLKYAIDA
FVAVDHEEEV SAIKSSQTPS SILKTPQSFF IPPSTPDLSF TDNKNSLSPS NILSLDGKFS
FNDDSELWAD LGNEINSEIG FLKEPDTMNL ALDADKDKTK MQNKLTQINF DESCFLDPAI
DDKDPWNEML HEKKVLLKQL QVGNEDEDNI AFPTSTNIWQ VVI
