UAF30_SCHPO
ID UAF30_SCHPO Reviewed; 233 AA.
AC O74503;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Upstream activation factor subunit spp27;
DE AltName: Full=Upstream activation factor 27 KDa subunit;
DE Short=p27;
DE AltName: Full=Upstream activation factor 30 KDa subunit;
DE Short=p30;
DE AltName: Full=Upstream activation factor subunit uaf30;
GN Name=spp27; Synonyms=uaf30; ORFNames=SPCC285.17;
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 FUNCTION, IDENTIFICATION IN THE UAF COMPLEX, AND INTERACTION WITH RRN10.
RX PubMed=12490702; DOI=10.1093/nar/gkf683;
RA Liu M., Guo A., Boukhgalter B., Van Den Heuvel K., Tripp M., Pape L.;
RT "Characterization of the fission yeast ribosomal DNA binding factor:
RT components share homology with upstream activating factor and with SWI/SNF
RT subunits.";
RL Nucleic Acids Res. 30:5347-5359(2002).
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).
CC -!- FUNCTION: Component of the UAF (upstream activation factor) complex
CC which interacts with the upstream element of the RNA polymerase I
CC promoter and forms a stable preinitiation complex. UAF seems to
CC stimulate basal transcription to a fully activated level.
CC {ECO:0000269|PubMed:12490702}.
CC -!- SUBUNIT: Component of the UAF (upstream activation factor) complex
CC which consists of spp27/uaf30, rrn5, rrn10, and histones H3 and H4.
CC Interacts with rrn10. {ECO:0000269|PubMed:12490702}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAA20856.1; -; Genomic_DNA.
DR PIR; T41263; T41263.
DR RefSeq; NP_588345.1; NM_001023336.2.
DR AlphaFoldDB; O74503; -.
DR SMR; O74503; -.
DR BioGRID; 275877; 69.
DR STRING; 4896.SPCC285.17.1; -.
DR iPTMnet; O74503; -.
DR MaxQB; O74503; -.
DR PaxDb; O74503; -.
DR PRIDE; O74503; -.
DR EnsemblFungi; SPCC285.17.1; SPCC285.17.1:pep; SPCC285.17.
DR GeneID; 2539310; -.
DR KEGG; spo:SPCC285.17; -.
DR PomBase; SPCC285.17; spp27.
DR VEuPathDB; FungiDB:SPCC285.17; -.
DR eggNOG; KOG1946; Eukaryota.
DR HOGENOM; CLU_046065_1_1_1; -.
DR InParanoid; O74503; -.
DR OMA; DKRTILC; -.
DR PhylomeDB; O74503; -.
DR Reactome; R-SPO-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-69541; Stabilization of p53.
DR PRO; PR:O74503; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000500; C:RNA polymerase I upstream activating factor complex; EXP:PomBase.
DR GO; GO:0001165; F:RNA polymerase I cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IC:PomBase.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; EXP:PomBase.
DR Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..233
FT /note="Upstream activation factor subunit spp27"
FT /id="PRO_0000290654"
FT DOMAIN 1..53
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DOMAIN 116..193
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 55..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 233 AA; 26651 MW; C452BE747CA765F2 CRC64;
MEEYETDIKQ ILGTVDRQTV SAKQVRQLLE ERRKVDLSAH KKDLNALILK CFDETAAPSE
KESLEKQAPA RKTKGKRATE NGTEEGKKPA KRTRKRKEDG EEGGKRKRNQ DPANNPLNKP
MKLSPKLAEF LGLEQLSRPQ TVKKLWEYIK AHDLQDPNDK RTILCDDKLK SVFEVDTLHM
FTMNKYLTNL MTKIPDDQLP KPQPKNEEPA APNDLPKQEE KELVEPPTAE STA
