RPN1_YEAST
ID RPN1_YEAST Reviewed; 993 AA.
AC P38764; D3DKX4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=26S proteasome regulatory subunit RPN1;
DE AltName: Full=HMG-CoA reductase degradation protein 2;
DE AltName: Full=Proteasome non-ATPase subunit 1;
GN Name=RPN1; Synonyms=HRD2, NAS1, RPD1; OrderedLocusNames=YHR027C;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 PROTEIN SEQUENCE OF 2-8.
RX PubMed=12504901; DOI=10.1016/s0003-9861(02)00639-2;
RA Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.;
RT "N-terminal modifications of the 19S regulatory particle subunits of the
RT yeast proteasome.";
RL Arch. Biochem. Biophys. 409:341-348(2003).
RN [4]
RP FUNCTION.
RX PubMed=9584156; DOI=10.1128/mcb.18.6.3149;
RA Glickman M.H., Rubin D.M., Fried V.A., Finley D.;
RT "The regulatory particle of the Saccharomyces cerevisiae proteasome.";
RL Mol. Cell. Biol. 18:3149-3162(1998).
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 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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-187 AND SER-695, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-19 AND SER-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000269|PubMed:9584156}.
CC -!- INTERACTION:
CC P38764; P32628: RAD23; NbExp=11; IntAct=EBI-15913, EBI-14668;
CC P38764; P38886: RPN10; NbExp=6; IntAct=EBI-15913, EBI-15949;
CC P38764; P32565: RPN2; NbExp=3; IntAct=EBI-15913, EBI-15919;
CC P38764; P33299: RPT1; NbExp=13; IntAct=EBI-15913, EBI-13910;
CC P38764; P40327: RPT2; NbExp=6; IntAct=EBI-15913, EBI-13901;
CC P38764; P33297: RPT5; NbExp=4; IntAct=EBI-15913, EBI-13920;
CC P38764; Q01939: RPT6; NbExp=3; IntAct=EBI-15913, EBI-13914;
CC -!- MISCELLANEOUS: Present with 306000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
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DR EMBL; U10399; AAB68878.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06718.1; -; Genomic_DNA.
DR PIR; S46779; S46779.
DR RefSeq; NP_011892.1; NM_001179157.1.
DR PDB; 2N3T; NMR; -; A=482-612.
DR PDB; 2N3U; NMR; -; A=482-612.
DR PDB; 2N3V; NMR; -; A=482-612.
DR PDB; 2N3W; NMR; -; A=482-612.
DR PDB; 2NBW; NMR; -; A=482-612.
DR PDB; 3JCO; EM; 4.80 A; Z=1-993.
DR PDB; 3JCP; EM; 4.60 A; Z=1-993.
DR PDB; 4CR2; EM; 7.70 A; Z=1-993.
DR PDB; 4CR3; EM; 9.30 A; Z=1-993.
DR PDB; 4CR4; EM; 8.80 A; Z=1-993.
DR PDB; 5A5B; EM; 9.50 A; Z=1-993.
DR PDB; 5MPB; EM; 7.80 A; Z=1-993.
DR PDB; 5MPC; EM; 7.70 A; Z=1-993.
DR PDB; 5MPD; EM; 4.10 A; Z=1-993.
DR PDB; 5MPE; EM; 4.50 A; Z=1-993.
DR PDB; 5WVI; EM; 6.30 A; Z=1-993.
DR PDB; 5WVK; EM; 4.20 A; Z=1-993.
DR PDB; 6FVT; EM; 4.10 A; Z=1-970.
DR PDB; 6FVU; EM; 4.50 A; Z=1-970.
DR PDB; 6FVV; EM; 5.40 A; Z=1-970.
DR PDB; 6FVW; EM; 4.50 A; Z=1-970.
DR PDB; 6FVX; EM; 4.90 A; Z=1-970.
DR PDB; 6FVY; EM; 6.10 A; Z=1-970.
DR PDB; 6J2C; EM; 7.00 A; Z=1-993.
DR PDB; 6J2N; EM; 7.50 A; Z=1-993.
DR PDB; 6J2Q; EM; 3.80 A; Z=1-993.
DR PDB; 6J2X; EM; 3.80 A; Z=1-993.
DR PDB; 6J30; EM; 4.50 A; Z=1-993.
DR PDB; 7QO3; EM; 6.10 A; Z=1-993.
DR PDB; 7QO5; EM; 6.00 A; Z=1-993.
DR PDBsum; 2N3T; -.
DR PDBsum; 2N3U; -.
DR PDBsum; 2N3V; -.
DR PDBsum; 2N3W; -.
DR PDBsum; 2NBW; -.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5MPB; -.
DR PDBsum; 5MPC; -.
DR PDBsum; 5MPD; -.
DR PDBsum; 5MPE; -.
DR PDBsum; 5WVI; -.
DR PDBsum; 5WVK; -.
DR PDBsum; 6FVT; -.
DR PDBsum; 6FVU; -.
DR PDBsum; 6FVV; -.
DR PDBsum; 6FVW; -.
DR PDBsum; 6FVX; -.
DR PDBsum; 6FVY; -.
DR PDBsum; 6J2C; -.
DR PDBsum; 6J2N; -.
DR PDBsum; 6J2Q; -.
DR PDBsum; 6J2X; -.
DR PDBsum; 6J30; -.
DR PDBsum; 7QO3; -.
DR PDBsum; 7QO5; -.
DR AlphaFoldDB; P38764; -.
DR SMR; P38764; -.
DR BioGRID; 36458; 723.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-2876N; -.
DR IntAct; P38764; 129.
DR MINT; P38764; -.
DR STRING; 4932.YHR027C; -.
DR iPTMnet; P38764; -.
DR MaxQB; P38764; -.
DR PaxDb; P38764; -.
DR PRIDE; P38764; -.
DR EnsemblFungi; YHR027C_mRNA; YHR027C; YHR027C.
DR GeneID; 856422; -.
DR KEGG; sce:YHR027C; -.
DR SGD; S000001069; RPN1.
DR VEuPathDB; FungiDB:YHR027C; -.
DR eggNOG; KOG2005; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; P38764; -.
DR OMA; KTVYKHM; -.
DR BioCyc; YEAST:G3O-31087-MON; -.
DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P38764; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38764; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:SGD.
DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR PANTHER; PTHR10943:SF1; PTHR10943:SF1; 1.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CHAIN 2..993
FT /note="26S proteasome regulatory subunit RPN1"
FT /id="PRO_0000173815"
FT REPEAT 417..449
FT /note="PC 1"
FT REPEAT 450..487
FT /note="PC 2"
FT REPEAT 488..522
FT /note="PC 3"
FT REPEAT 523..563
FT /note="PC 4"
FT REPEAT 566..598
FT /note="PC 5"
FT REPEAT 778..809
FT /note="PC 6"
FT REPEAT 810..844
FT /note="PC 7"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..680
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 485..496
FT /evidence="ECO:0007829|PDB:2N3T"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:2N3T"
FT HELIX 503..513
FT /evidence="ECO:0007829|PDB:2N3T"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:2N3T"
FT HELIX 520..534
FT /evidence="ECO:0007829|PDB:2N3T"
FT HELIX 540..552
FT /evidence="ECO:0007829|PDB:2N3T"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:2N3T"
FT HELIX 562..572
FT /evidence="ECO:0007829|PDB:2N3T"
FT TURN 573..576
FT /evidence="ECO:0007829|PDB:2N3T"
FT HELIX 579..590
FT /evidence="ECO:0007829|PDB:2N3T"
FT TURN 594..596
FT /evidence="ECO:0007829|PDB:2N3U"
FT HELIX 597..605
FT /evidence="ECO:0007829|PDB:2N3T"
FT TURN 608..610
FT /evidence="ECO:0007829|PDB:2N3U"
SQ SEQUENCE 993 AA; 109492 MW; B77954F4A998BA7C CRC64;
MVDESDKKQQ TIDEQSQISP EKQTPNKKDK KKEEEEQLSE EDAKLKTDLE LLVERLKEDD
SSLYEASLNA LKESIKNSTS SMTAVPKPLK FLRPTYPDLC SIYDKWTDPN LKSSLADVLS
ILAMTYSENG KHDSLRYRLL SDVSDFEGWG HEYIRHLALE IGEVYNDQVE KDAEDETSSD
GSKSDGSAAT SGFEFSKEDT LRLCLDIVPY FLKHNGEEDA VDLLLEIESI DKLPQFVDEN
TFQRVCQYMV ACVPLLPPPE DVAFLKTAYS IYLSQNELTD AIALAVRLGE EDMIRSVFDA
TSDPVMHKQL AYILAAQKTS FEYEGVQDII GNGKLSEHFL YLAKELNLTG PKVPEDIYKS
HLDNSKSVFS SAGLDSAQQN LASSFVNGFL NLGYCNDKLI VDNDNWVYKT KGDGMTSAVA
SIGSIYQWNL DGLQQLDKYL YVDEPEVKAG ALLGIGISAS GVHDGEVEPA LLLLQDYVTN
PDTKISSAAI LGLGIAFAGS KNDEVLGLLL PIAASTDLPI ETAAMASLAL AHVFVGTCNG
DITTSIMDNF LERTAIELKT DWVRFLALAL GILYMGQGEQ VDDVLETISA IEHPMTSAIE
VLVGSCAYTG TGDVLLIQDL LHRLTPKNVK GEEDADEEET AEGQTNSISD FLGEQVNEPT
KNEEAEIEVD EMEVDAEGEE VEVKAEITEK KNGESLEGEE IKSEEKKGKS SDKDATTDGK
NDDEEEEKEA GIVDELAYAV LGIALIALGE DIGKEMSLRH FGHLMHYGNE HIRRMVPLAM
GIVSVSDPQM KVFDTLTRFS HDADLEVSMN SIFAMGLCGA GTNNARLAQL LRQLASYYSR
EQDALFITRL AQGLLHLGKG TMTMDVFNDA HVLNKVTLAS ILTTAVGLVS PSFMLKHHQL
FYMLNAGIRP KFILALNDEG EPIKVNVRVG QAVETVGQAG RPKKITGWIT QSTPVLLNHG
ERAELETDEY ISYTSHIEGV VILKKNPDYR EEE
