SPT20_SCHPO
ID SPT20_SCHPO Reviewed; 473 AA.
AC O14174;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=SAGA complex subunit spt20;
GN Name=spt20; ORFNames=SPAC4D7.10c;
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 IDENTIFICATION IN THE SAGA COMPLEX, FUNCTION OF THE SAGA COMPLEX, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19056896; DOI=10.1101/gad.1719908;
RA Helmlinger D., Marguerat S., Villen J., Gygi S.P., Bahler J., Winston F.;
RT "The S. pombe SAGA complex controls the switch from proliferation to sexual
RT differentiation through the opposing roles of its subunits Gcn5 and Spt8.";
RL Genes Dev. 22:3184-3195(2008).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=21642955; DOI=10.1038/emboj.2011.181;
RA Helmlinger D., Marguerat S., Villen J., Swaney D.L., Gygi S.P., Bahler J.,
RA Winston F.;
RT "Tra1 has specific regulatory roles, rather than global functions, within
RT the SAGA co-activator complex.";
RL EMBO J. 30:2843-2852(2011).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complex SAGA. At the promoters, SAGA is
CC required for recruitment of the basal transcription machinery. It
CC influences RNA polymerase II transcriptional activity through different
CC activities such as TBP interaction and promoter selectivity,
CC interaction with transcription activators, and chromatin modification
CC through histone acetylation and deubiquitination. SAGA acetylates
CC nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac
CC and H3K23ac). SAGA interacts with DNA via upstream activating sequences
CC (UASs). {ECO:0000269|PubMed:19056896}.
CC -!- SUBUNIT: Component of the SAGA complex. {ECO:0000269|PubMed:19056896}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased growth at high temperature and
CC sensitivity to several drugs like hydroxyurea, caffeine, canavanine and
CC rapamycin; as well as to raffinose. {ECO:0000269|PubMed:19056896,
CC ECO:0000269|PubMed:21642955}.
CC -!- SIMILARITY: Belongs to the SPT20 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11282.1; -; Genomic_DNA.
DR PIR; T38801; T38801.
DR RefSeq; NP_594963.1; NM_001020394.2.
DR AlphaFoldDB; O14174; -.
DR BioGRID; 280089; 12.
DR IntAct; O14174; 2.
DR MINT; O14174; -.
DR STRING; 4896.SPAC4D7.10c.1; -.
DR MaxQB; O14174; -.
DR PaxDb; O14174; -.
DR PRIDE; O14174; -.
DR EnsemblFungi; SPAC4D7.10c.1; SPAC4D7.10c.1:pep; SPAC4D7.10c.
DR PomBase; SPAC4D7.10c; spt20.
DR VEuPathDB; FungiDB:SPAC4D7.10c; -.
DR eggNOG; ENOG502QS30; Eukaryota.
DR HOGENOM; CLU_577656_0_0_1; -.
DR InParanoid; O14174; -.
DR OMA; RMELIPP; -.
DR PhylomeDB; O14174; -.
DR PRO; PR:O14174; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0036391; C:medial cortex septin ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:PomBase.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR GO; GO:0031106; P:septin ring organization; IMP:PomBase.
DR InterPro; IPR021950; Spt20.
DR Pfam; PF12090; Spt20; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..473
FT /note="SAGA complex subunit spt20"
FT /id="PRO_0000116700"
FT REGION 134..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 54028 MW; C098846120AE3DE5 CRC64;
MERNNGLGDY TYRYHGKELS LDDFQNKQGI ESSDDAFLSK IYENVSNFNV PRKLHDIEHK
FSKEEPSLIL HIHKFHFRFE QQDGAFTYNG PVKSILQYIR MELIPPDCLE VFRNSDVKFY
DGCLTVRIID HRQSPSADQT VQPQPGSTNQ QQQNNTNPIN NQPEDTKPNT NSPPVYHTVL
RPTPETLWQD LCLLSESFAN SLSDEAVLTL ESNILLASEA PLFLTPAKSK AEMIQFMNQL
ADSAPPCTRK KPQGSAQLAD EEAERLEKEN LLLLMDDQRK RDFQPTFQRL QFIENVRRKR
AILQQRQMQM QQQQKAQQQQ SPKAQQPPAH LVQSAPVQRK TTPKIQRLPP SSIQIPPPKP
MQKFPANAAS SESPPNATGN FLPSGPVPAN EPMLKRESVD LIKIRQLAIL FQQRASQLKA
RGATREQITE ILNRQAIAAG TDLATVMTVA RNLHFQQLQM RQQQQQQQMK AER
