MED20_SCHPO
ID MED20_SCHPO Reviewed; 193 AA.
AC Q10317;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 20;
DE AltName: Full=Mediator complex subunit 20;
GN Name=med20; ORFNames=SPAC17G8.05;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
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 [4]
RP FUNCTION, AND IDENTIFICATION IN THE MEDIATOR COMPLEX.
RX PubMed=18310102; DOI=10.1093/nar/gkn070;
RA Linder T., Rasmussen N.N., Samuelsen C.O., Chatzidaki E., Baraznenok V.,
RA Beve J., Henriksen P., Gustafsson C.M., Holmberg S.;
RT "Two conserved modules of Schizosaccharomyces pombe Mediator regulate
RT distinct cellular pathways.";
RL Nucleic Acids Res. 36:2489-2504(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. The Mediator complex, having a compact
CC conformation in its free form, is recruited to promoters by direct
CC interactions with regulatory proteins and serves for the assembly of a
CC functional preinitiation complex with RNA polymerase II and the general
CC transcription factors. {ECO:0000269|PubMed:18310102}.
CC -!- SUBUNIT: Component of the Mediator complex.
CC {ECO:0000269|PubMed:18310102}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 20 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA93688.2; -; Genomic_DNA.
DR PIR; T37857; T37857.
DR RefSeq; NP_593728.2; NM_001019159.2.
DR PDB; 5N9J; X-ray; 3.40 A; Y=1-193.
DR PDB; 5U0P; EM; 4.40 A; T=1-193.
DR PDB; 5U0S; EM; 7.80 A; T=1-193.
DR PDBsum; 5N9J; -.
DR PDBsum; 5U0P; -.
DR PDBsum; 5U0S; -.
DR AlphaFoldDB; Q10317; -.
DR SMR; Q10317; -.
DR BioGRID; 278884; 101.
DR DIP; DIP-60135N; -.
DR IntAct; Q10317; 3.
DR STRING; 4896.SPAC17G8.05.1; -.
DR iPTMnet; Q10317; -.
DR PaxDb; Q10317; -.
DR EnsemblFungi; SPAC17G8.05.1; SPAC17G8.05.1:pep; SPAC17G8.05.
DR GeneID; 2542421; -.
DR KEGG; spo:SPAC17G8.05; -.
DR PomBase; SPAC17G8.05; med20.
DR VEuPathDB; FungiDB:SPAC17G8.05; -.
DR eggNOG; ENOG502SBIU; Eukaryota.
DR HOGENOM; CLU_089405_0_0_1; -.
DR InParanoid; Q10317; -.
DR OMA; IVRTKLW; -.
DR PRO; PR:Q10317; -.
DR Proteomes; UP000002485; Chromosome I.
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; 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; IBA:GO_Central.
DR InterPro; IPR013921; Mediator_Med20.
DR PANTHER; PTHR12465; PTHR12465; 1.
DR Pfam; PF08612; Med20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome.
FT CHAIN 1..193
FT /note="Mediator of RNA polymerase II transcription subunit
FT 20"
FT /id="PRO_0000116590"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 32..45
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:5N9J"
FT TURN 153..157
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:5N9J"
SQ SEQUENCE 193 AA; 22350 MW; 05AD4D96C2452EA0 CRC64;
MPVHGVIYYS SPSMATFLSP AQDNLVRTYF AQHLKKWVVQ YKLYRNAVTP KTLEFLKQNI
NPSMLACVDE ATMIDAEPEL EDIIVRTKLW NFRQSFTIEG SIYEVGSFKV AIANVLQKSV
WKGILFHVTY DGTESVDLAR PIIQEFFLKC FLQNNKSVTP VYESFFNQPR HSLDSKLLLQ
LFKQRIDTVS QRT
