RPN4_YEAST
ID RPN4_YEAST Reviewed; 531 AA.
AC Q03465; D6VRX0; E9P944;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protein RPN4;
DE AltName: Full=Nuclear protein SON1;
DE AltName: Full=Ubiquitin fusion degradation protein 5;
GN Name=RPN4; Synonyms=SON1, UFD5; OrderedLocusNames=YDL020C; ORFNames=D2840;
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 [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8514125; DOI=10.1093/genetics/134.1.159;
RA Nelson M.K., Kurihara T., Silver P.A.;
RT "Extragenic suppressors of mutations in the cytoplasmic C-terminus of SEC63
RT define five genes in Saccharomyces cerevisiae.";
RL Genetics 134:159-173(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP CHARACTERIZATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7615550; DOI=10.1074/jbc.270.29.17442;
RA Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.;
RT "A proteolytic pathway that recognizes ubiquitin as a degradation signal.";
RL J. Biol. Chem. 270:17442-17456(1995).
RN [6]
RP PRELIMINARY CHARACTERIZATION.
RX PubMed=9512348; DOI=10.1016/s0014-5793(98)00084-2;
RA Fujimuro M., Tanaka K., Yokosawa H., Toh-e A.;
RT "Son1p is a component of the 26S proteasome of the yeast Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 423:149-154(1998).
RN [7]
RP FUNCTION.
RX PubMed=10350051; DOI=10.1016/s0014-5793(99)00467-6;
RA Mannhaupt G., Schnall R., Karpov V., Vetter I., Feldmann H.;
RT "Rpn4p acts as a transcription factor by binding to PACE, a nonamer box
RT found upstream of 26S proteasomal and other genes in yeast.";
RL FEBS Lett. 450:27-34(1999).
RN [8]
RP FUNCTION.
RX PubMed=11248031; DOI=10.1073/pnas.071022298;
RA Xie Y., Varshavsky A.;
RT "RPN4 is a ligand, substrate, and transcriptional regulator of the 26S
RT proteasome: a negative feedback circuit.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3056-3061(2001).
RN [9]
RP UBIQUITINATION, AND INTERACTION WITH UBR2.
RX PubMed=15504724; DOI=10.1074/jbc.m410085200;
RA Wang L., Mao X., Ju D., Xie Y.;
RT "Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.";
RL J. Biol. Chem. 279:55218-55223(2004).
RN [10]
RP UBIQUITINATION, AND INTERACTION WITH MUB1.
RX PubMed=18070918; DOI=10.1128/mcb.01787-07;
RA Ju D., Wang X., Xu H., Xie Y.;
RT "Genome-wide analysis identifies MYND-domain protein Mub1 as an essential
RT factor for Rpn4 ubiquitylation.";
RL Mol. Cell. Biol. 28:1404-1412(2008).
CC -!- FUNCTION: Acts as a transcriptional activator of a number of genes
CC encoding proteasomal subunits. Binds to a PACE (proteasome-associated
CC control element) DNA sequence 5'-GGTGGCAAA-3'. Its expression is in
CC turn regulated by the 26S proteasome, thereby providing a negative
CC feedback control mechanism. Required for normal growth at low
CC temperatures. {ECO:0000269|PubMed:10350051,
CC ECO:0000269|PubMed:11248031}.
CC -!- SUBUNIT: Probably interacts with SEC63. Interacts with MUB1, UBR2 and
CC RPN2. {ECO:0000269|PubMed:15504724, ECO:0000269|PubMed:18070918}.
CC -!- INTERACTION:
CC Q03465; Q03162: MUB1; NbExp=3; IntAct=EBI-15931, EBI-28207;
CC Q03465; Q07963: UBR2; NbExp=2; IntAct=EBI-15931, EBI-34338;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Ubiquitinated by UBR2 in the presence of UBC2; which leads to
CC proteasomal degradation. {ECO:0000269|PubMed:15504724,
CC ECO:0000269|PubMed:18070918}.
CC -!- DISRUPTION PHENOTYPE: Mutants grow slowly at low temperatures and show
CC partial mislocalization of nuclear antigens.
CC {ECO:0000269|PubMed:8514125}.
CC -!- CAUTION: According to PubMed:9512348, it is a component of the 26S
CC proteasome. {ECO:0000305}.
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DR EMBL; L00928; AAA35067.1; -; Genomic_DNA.
DR EMBL; Z48432; CAA88339.1; -; Genomic_DNA.
DR EMBL; Z74068; CAA98579.1; -; Genomic_DNA.
DR EMBL; AY723763; AAU09680.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11830.1; -; Genomic_DNA.
DR PIR; S41986; S41986.
DR RefSeq; NP_010264.3; NM_001180079.3.
DR AlphaFoldDB; Q03465; -.
DR BioGRID; 32035; 788.
DR DIP; DIP-5779N; -.
DR IntAct; Q03465; 5.
DR MINT; Q03465; -.
DR STRING; 4932.YDL020C; -.
DR iPTMnet; Q03465; -.
DR PaxDb; Q03465; -.
DR PRIDE; Q03465; -.
DR EnsemblFungi; YDL020C_mRNA; YDL020C; YDL020C.
DR GeneID; 851542; -.
DR KEGG; sce:YDL020C; -.
DR SGD; S000002178; RPN4.
DR VEuPathDB; FungiDB:YDL020C; -.
DR eggNOG; ENOG502RBAK; Eukaryota.
DR HOGENOM; CLU_038620_0_0_1; -.
DR InParanoid; Q03465; -.
DR OMA; KYADPSL; -.
DR BioCyc; YEAST:G3O-29449-MON; -.
DR PRO; PR:Q03465; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03465; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; HMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0061395; P:positive regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance; IMP:SGD.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR GO; GO:0006282; P:regulation of DNA repair; IMP:SGD.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..531
FT /note="Protein RPN4"
FT /id="PRO_0000173871"
FT REGION 338..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 382..398
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 338..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 231
FT /note="C -> Y (in Ref. 4; AAU09680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 60153 MW; 4316281AC09FBE7F CRC64;
MASTELSLKR TLTDILEDEL YHTNPGHSQF TSHYQNYHPN ASITPYKLVN KNKENNTFTW
NHSLQHQNES SAASIPPQQT YHFPIFNKYA DPTLTTTTSF TTSEATANDR QINNVHLIPN
EIKGASETPL QKTVNLKNIM KVSDPYVPTR NTFNYDVKIS NDFFDNGDNL YGNDEEVLFY
EDNYNPKMQW SLQDNSAAIN NEDARAIFNN EFDSDDDDIS DDEEDEIEEN CLQQEQHQEE
PLLSLDVTPI SMFGSDQKTG RAKSSSHLFN EYSYVDSNMD SISSVVSEDL LDERGHEKIE
DEDEDNDLDE DDIYDISLLK NRRKQSFVLN KNTIDFERFP SPSTSANVPS TATTGKRKPA
KSSSNRSCVS NSNENGTLER IKKPTSAVVS SNASRRKLIN YTKKHLSSHS STNSNSKPST
ASPSAHTSSS DGNNEIFTCQ IMNLITNEPC GAQFSRSYDL TRHQNTIHAK RKIVFRCSEC
IKILGSEGYQ KTFSRLDALT RHIKSKHEDL SLEQRQEVTK FAKANIGYVM G
