UAF30_YEAST
ID UAF30_YEAST Reviewed; 228 AA.
AC Q08747; D6W2Z4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Upstream activation factor subunit UAF30;
DE AltName: Full=Upstream activation factor 30 KDa subunit;
DE Short=p30;
GN Name=UAF30; OrderedLocusNames=YOR295W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION IN THE UAF COMPLEX.
RX PubMed=11500378; DOI=10.1093/emboj/20.16.4512;
RA Siddiqi I.N., Dodd J.A., Vu L., Eliason K., Oakes M.L., Keener J.,
RA Moore R., Young M.K., Nomura M.;
RT "Transcription of chromosomal rRNA genes by both RNA polymerase I and II in
RT yeast uaf30 mutants lacking the 30 kDa subunit of transcription factor
RT UAF.";
RL EMBO J. 20:4512-4521(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-220 AND SER-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
CC -!- FUNCTION: Nonessential component of the UAF (upstream activation
CC factor) complex which interacts with the upstream element of the RNA
CC polymerase I promoter and forms a stable preinitiation complex.
CC Together with SPT15/TBP UAF seems to stimulate basal transcription to a
CC fully activated level. UAF30 seems to play a role in silencing
CC transcription by RNA polymerase II.
CC -!- SUBUNIT: Component of the UAF (upstream activation factor) complex
CC which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4.
CC {ECO:0000269|PubMed:11500378}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z75203; CAA99523.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11060.1; -; Genomic_DNA.
DR PIR; S67199; S67199.
DR RefSeq; NP_014938.3; NM_001183714.3.
DR AlphaFoldDB; Q08747; -.
DR SMR; Q08747; -.
DR BioGRID; 34683; 168.
DR ComplexPortal; CPX-1101; RNA polymerase I upstream activating factor complex.
DR IntAct; Q08747; 5.
DR MINT; Q08747; -.
DR STRING; 4932.YOR295W; -.
DR iPTMnet; Q08747; -.
DR MaxQB; Q08747; -.
DR PaxDb; Q08747; -.
DR PRIDE; Q08747; -.
DR EnsemblFungi; YOR295W_mRNA; YOR295W; YOR295W.
DR GeneID; 854470; -.
DR KEGG; sce:YOR295W; -.
DR SGD; S000005821; UAF30.
DR VEuPathDB; FungiDB:YOR295W; -.
DR eggNOG; KOG1946; Eukaryota.
DR GeneTree; ENSGT00940000176588; -.
DR HOGENOM; CLU_046065_1_0_1; -.
DR InParanoid; Q08747; -.
DR OMA; DKRTILC; -.
DR BioCyc; YEAST:G3O-33780-MON; -.
DR Reactome; R-SCE-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SCE-69541; Stabilization of p53.
DR PRO; PR:Q08747; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08747; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000500; C:RNA polymerase I upstream activating factor complex; IDA:SGD.
DR GO; GO:0001165; F:RNA polymerase I cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IMP:SGD.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IBA:GO_Central.
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 Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..228
FT /note="Upstream activation factor subunit UAF30"
FT /id="PRO_0000245507"
FT DOMAIN 1..56
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DOMAIN 119..195
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 89..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 228 AA; 25967 MW; C480D943D728021A CRC64;
MAELNDYSTM IDILLSDMDL ETVTTKKVRM ALKEVYAIDV ESQGKAINKL IRKHLDLVKE
RPRFERSLED LLKENATLAI ELTKEITVSK RSSGEEKNDS ETKGTHVEKK KGTVSKSPIS
TRKVTLSKSL ASLLGEHELT RTEVVRRLWA YIKAHNLQNP NNKKEILCDE KLELILGKST
NMFEMHKILA SHMTEPKKIS DCPPLIQEVR RKEKPIVSDS EQSDTKGI
