MED14_SCHPO
ID MED14_SCHPO Reviewed; 879 AA.
AC Q9P7Y4; O74344;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 14;
DE AltName: Full=Mediator complex subunit 14;
DE AltName: Full=Mediator of RNA polymerase II complex subunit pmc1;
GN Name=med14; Synonyms=pmc1; ORFNames=SPBC1A4.10c, SPBP23A10.01c;
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).
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}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 14 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA20115.1; -; Genomic_DNA.
DR PIR; T39859; T50388.
DR RefSeq; NP_595813.2; NM_001021716.3.
DR PDB; 5N9J; X-ray; 3.40 A; A=2-580.
DR PDB; 5U0P; EM; 4.40 A; N=1-879.
DR PDB; 5U0S; EM; 7.80 A; N=1-879.
DR PDBsum; 5N9J; -.
DR PDBsum; 5U0P; -.
DR PDBsum; 5U0S; -.
DR AlphaFoldDB; Q9P7Y4; -.
DR SMR; Q9P7Y4; -.
DR BioGRID; 277203; 71.
DR IntAct; Q9P7Y4; 1.
DR STRING; 4896.SPBC1A4.10c.1; -.
DR MaxQB; Q9P7Y4; -.
DR PaxDb; Q9P7Y4; -.
DR PRIDE; Q9P7Y4; -.
DR EnsemblFungi; SPBC1A4.10c.1; SPBC1A4.10c.1:pep; SPBC1A4.10c.
DR GeneID; 2540678; -.
DR KEGG; spo:SPBC1A4.10c; -.
DR PomBase; SPBC1A4.10c; med14.
DR VEuPathDB; FungiDB:SPBC1A4.10c; -.
DR eggNOG; KOG1875; Eukaryota.
DR HOGENOM; CLU_327363_0_0_1; -.
DR InParanoid; Q9P7Y4; -.
DR OMA; LQGQKFC; -.
DR PRO; PR:Q9P7Y4; -.
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; IPR013947; Mediator_Med14.
DR PANTHER; PTHR12809; PTHR12809; 1.
DR Pfam; PF08638; Med14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..879
FT /note="Mediator of RNA polymerase II transcription subunit
FT 14"
FT /id="PRO_0000096361"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 16..37
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 43..70
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 74..111
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 151..171
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 235..254
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 258..287
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 356..364
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 379..401
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 435..445
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 448..458
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 464..485
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 553..575
FT /evidence="ECO:0007829|PDB:5N9J"
SQ SEQUENCE 879 AA; 100834 MW; C6449D586FB613E8 CRC64;
MEPPAIPHIT EGFYPLPEIV ETFSHHVLQE LVSLAEVLPS MSNVEKKKKI LDWLLRSRAF
TMRLLVLARW VHLSPSVHRC IDVVAFLQGQ KFCFQNLVHV LQDIRYQLSF ARLRNSDLVT
ALDILSTGTS LRLANAPTSK LYMLSESPLS TKQILQTLHA LNMLIRIRLS LYEIIPTPFQ
HFTIANGRCT FTVPNEFSVS LTTNSQDPKS TGISFQWIVV DFQFHLPDFS STPAKYRVFI
ELHLNEEIAA AFVLQKPILP LIYNILHKFC LYQRLNLLSQ QTFQLSRESW LGHLRGVYDE
KPPRLRLYYW PQLNVKKEGK PGKIGHYIHI FVNTQPISAF ERTLSSKRSS CEYDHFLLLV
EWHHDGIVEH VPLDDHMDAQ HLLLLITQKH AQLILEQIRK ELHPNIFSEH VGGGLKIHVF
DNEIIVKVNS VTGRLVLSSS ASPLSPPRHL RAAEKNIALN TQPPAQILNR LYFFCIQTQL
LEVAQCAELH AVQGYYSFPY LTFSKGKWRK DGDSLWVLAY NVESNSWSVR LLNAAGQTLY
TQDVHTTKGT LSIESFSRLS YLLEVQILLF NVQTACQARG MPFEYLPIPP KALIEDDFTT
YVQTGCLCIM MPSSNEDMLP VVFVRAHDGQ LIFDSRIKGK LPYQSETETE KNCYIDWRTG
RITIRVQNFS SFEKTWIGLL KLVALSKTSA FNVDCITLKH VDFTYLDDEK FRATIHDDNT
FTLHFFNRHS PFHLISQFLQ DTFSDGPSAI QPLRVIMDRT RGVLVAQELG YVVLARSLRQ
YRIILSKNHG IQVLLNRHGC ILQDLSYLSA DSRYLEGTQT LTSQWEPCSW LNTVWEGDLG
DDELNGQIEA APEMHLIKMN KTADLTAILK RILAISRKK
