MED4_SCHPO
ID MED4_SCHPO Reviewed; 239 AA.
AC Q9Y821;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 4;
DE AltName: Full=Mediator complex subunit 4;
DE AltName: Full=RNA polymerase II mediator complex protein pmc4;
GN Name=med4; Synonyms=pmc4; ORFNames=SPBC1105.06;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10625684; DOI=10.1074/jbc.275.2.1351;
RA Spaehr H., Beve J., Larsson T., Bergstroem J., Karlsson K.-A.,
RA Gustafsson C.M.;
RT "Purification and characterization of RNA polymerase II holoenzyme from
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 275:1351-1356(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=11572939; DOI=10.1073/pnas.211253898;
RA Spaehr H., Samuelsen C.O., Baraznenok V., Ernest I., Huylebroeck D.,
RA Remacle J.E., Samuelsson T., Kieselbach T., Holmberg S., Gustafsson C.M.;
RT "Analysis of Schizosaccharomyces pombe mediator reveals a set of essential
RT subunits conserved between yeast and metazoan cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11985-11990(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND SER-218, AND
RP IDENTIFICATION BY 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).
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.
CC -!- SUBUNIT: Component of the Mediator complex.
CC {ECO:0000269|PubMed:10625684, ECO:0000269|PubMed:11572939}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 4 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB50969.1; -; Genomic_DNA.
DR PIR; T39283; T39283.
DR RefSeq; NP_596462.1; NM_001022381.2.
DR PDB; 5N9J; X-ray; 3.40 A; G=1-239.
DR PDBsum; 5N9J; -.
DR AlphaFoldDB; Q9Y821; -.
DR SMR; Q9Y821; -.
DR BioGRID; 276538; 10.
DR IntAct; Q9Y821; 1.
DR STRING; 4896.SPBC1105.06.1; -.
DR iPTMnet; Q9Y821; -.
DR MaxQB; Q9Y821; -.
DR PaxDb; Q9Y821; -.
DR PRIDE; Q9Y821; -.
DR EnsemblFungi; SPBC1105.06.1; SPBC1105.06.1:pep; SPBC1105.06.
DR GeneID; 2539994; -.
DR KEGG; spo:SPBC1105.06; -.
DR PomBase; SPBC1105.06; -.
DR VEuPathDB; FungiDB:SPBC1105.06; -.
DR eggNOG; ENOG502REXJ; Eukaryota.
DR HOGENOM; CLU_1125090_0_0_1; -.
DR InParanoid; Q9Y821; -.
DR OMA; YPWPSED; -.
DR PhylomeDB; Q9Y821; -.
DR PRO; PR:Q9Y821; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0070847; C:core mediator complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016592; C:mediator complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003713; F:transcription coactivator activity; IC:PomBase.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
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; IBA:GO_Central.
DR InterPro; IPR019258; Mediator_Med4.
DR PANTHER; PTHR13208; PTHR13208; 1.
DR Pfam; PF10018; Med4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..239
FT /note="Mediator of RNA polymerase II transcription subunit
FT 4"
FT /id="PRO_0000096385"
FT REGION 168..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 3..23
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 27..85
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:5N9J"
SQ SEQUENCE 239 AA; 27340 MW; AE026602067F0DB3 CRC64;
MEYQRAIDSI EECLNKQLRL SSEKVDQYVL IENWTSLVGH LKTLHSLISN YTNGRELQNE
ISSLLKQDKE LDLQIQDCMR EMTSIYDTHL PKTVSGRKRQ KVNAETLLDY GRKLSKFSSA
PPGYNPETGQ DAKAPVHYPW PSEDQMRKTL LFQFSTSMVP NLSATASQLF SEQPPKTNEP
TETETEIDAN KAVEEKTKMN YPASPTFTTQ EENKEVESPA NKDVFAGFDL FDPEMEEDF
