RPN8_YEAST
ID RPN8_YEAST Reviewed; 338 AA.
AC Q08723; D6W2W2; Q6Q5I7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=26S proteasome regulatory subunit RPN8;
GN Name=RPN8; OrderedLocusNames=YOR261C; ORFNames=O5360;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [2]
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 [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 PROTEIN SEQUENCE OF 2-9, AND ACETYLATION AT SER-2.
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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-317; SER-319 AND
RP THR-327, AND 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).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
RX PubMed=22927375; DOI=10.1073/pnas.1213333109;
RA Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E.,
RA Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.;
RT "Near-atomic resolution structural model of the yeast 26S proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012).
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 Q08723; P38348: HSM3; NbExp=4; IntAct=EBI-36176, EBI-21152;
CC Q08723; P43588: RPN11; NbExp=9; IntAct=EBI-36176, EBI-11219;
CC Q08723; P32496: RPN12; NbExp=3; IntAct=EBI-36176, EBI-15953;
CC Q08723; Q12250: RPN5; NbExp=8; IntAct=EBI-36176, EBI-15935;
CC Q08723; Q12377: RPN6; NbExp=3; IntAct=EBI-36176, EBI-308;
CC Q08723; Q04062: RPN9; NbExp=5; IntAct=EBI-36176, EBI-15944;
CC -!- PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
CC -!- MISCELLANEOUS: Present with 19800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR EMBL; Z75169; CAA99483.1; -; Genomic_DNA.
DR EMBL; AY558039; AAS56365.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11028.1; -; Genomic_DNA.
DR PIR; S67158; S67158.
DR RefSeq; NP_014904.3; NM_001183680.3.
DR PDB; 3J47; EM; -; U=188-308.
DR PDB; 3JCK; EM; 3.50 A; E=1-338.
DR PDB; 3JCO; EM; 4.80 A; U=1-338.
DR PDB; 3JCP; EM; 4.60 A; U=1-338.
DR PDB; 4CR2; EM; 7.70 A; U=1-338.
DR PDB; 4CR3; EM; 9.30 A; U=1-338.
DR PDB; 4CR4; EM; 8.80 A; U=1-338.
DR PDB; 4O8X; X-ray; 1.99 A; A=2-178.
DR PDB; 4O8Y; X-ray; 1.95 A; A=2-178.
DR PDB; 4OCL; X-ray; 2.40 A; A/D=1-176.
DR PDB; 4OCM; X-ray; 1.99 A; A/D=1-176.
DR PDB; 4OCN; X-ray; 2.25 A; A/D=1-176.
DR PDB; 4OWP; X-ray; 2.35 A; A=1-186.
DR PDB; 5A5B; EM; 9.50 A; U=1-338.
DR PDB; 5MPB; EM; 7.80 A; U=1-338.
DR PDB; 5MPC; EM; 7.70 A; U=1-338.
DR PDB; 5MPD; EM; 4.10 A; U=1-338.
DR PDB; 5MPE; EM; 4.50 A; U=1-338.
DR PDB; 5U4P; X-ray; 2.50 A; A=1-177.
DR PDB; 5W83; X-ray; 1.55 A; A=1-338.
DR PDB; 5WVI; EM; 6.30 A; U=1-338.
DR PDB; 5WVK; EM; 4.20 A; U=1-338.
DR PDB; 6FVT; EM; 4.10 A; U=1-304.
DR PDB; 6FVU; EM; 4.50 A; U=1-304.
DR PDB; 6FVV; EM; 5.40 A; U=1-304.
DR PDB; 6FVW; EM; 4.50 A; U=1-304.
DR PDB; 6FVX; EM; 4.90 A; U=1-304.
DR PDB; 6FVY; EM; 6.10 A; U=1-304.
DR PDB; 6J2C; EM; 7.00 A; U=1-338.
DR PDB; 6J2N; EM; 7.50 A; U=1-338.
DR PDB; 6J2Q; EM; 3.80 A; U=1-338.
DR PDB; 6J2X; EM; 3.80 A; U=1-338.
DR PDB; 6J30; EM; 4.50 A; U=1-338.
DR PDB; 7QO3; EM; 6.10 A; U=1-338.
DR PDB; 7QO5; EM; 6.00 A; U=1-338.
DR PDB; 7QO6; EM; 6.30 A; U=1-338.
DR PDBsum; 3J47; -.
DR PDBsum; 3JCK; -.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 4O8X; -.
DR PDBsum; 4O8Y; -.
DR PDBsum; 4OCL; -.
DR PDBsum; 4OCM; -.
DR PDBsum; 4OCN; -.
DR PDBsum; 4OWP; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5MPB; -.
DR PDBsum; 5MPC; -.
DR PDBsum; 5MPD; -.
DR PDBsum; 5MPE; -.
DR PDBsum; 5U4P; -.
DR PDBsum; 5W83; -.
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 PDBsum; 7QO6; -.
DR AlphaFoldDB; Q08723; -.
DR SMR; Q08723; -.
DR BioGRID; 34651; 480.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1574N; -.
DR IntAct; Q08723; 38.
DR MINT; Q08723; -.
DR STRING; 4932.YOR261C; -.
DR MEROPS; M67.973; -.
DR iPTMnet; Q08723; -.
DR MaxQB; Q08723; -.
DR PaxDb; Q08723; -.
DR PRIDE; Q08723; -.
DR ABCD; Q08723; 1 sequenced antibody.
DR EnsemblFungi; YOR261C_mRNA; YOR261C; YOR261C.
DR GeneID; 854435; -.
DR KEGG; sce:YOR261C; -.
DR SGD; S000005787; RPN8.
DR VEuPathDB; FungiDB:YOR261C; -.
DR eggNOG; KOG1556; Eukaryota.
DR GeneTree; ENSGT00950000183073; -.
DR HOGENOM; CLU_027018_3_0_1; -.
DR InParanoid; Q08723; -.
DR OMA; HAMSIKT; -.
DR BioCyc; YEAST:G3O-33752-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:Q08723; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08723; protein.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:SGD.
DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:SGD.
DR CDD; cd08062; MPN_RPN7_8; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033858; MPN_RPN7_8.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Phosphoprotein;
KW Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CHAIN 2..338
FT /note="26S proteasome regulatory subunit RPN8"
FT /id="PRO_0000213951"
FT DOMAIN 8..143
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 301..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12504901"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 126
FT /note="K -> E (in Ref. 4; AAS56365)"
FT /evidence="ECO:0000305"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:5W83"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 42..53
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3JCK"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:5W83"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:5W83"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:5W83"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:4OCN"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:5W83"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5W83"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:5W83"
FT HELIX 186..215
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:3JCK"
FT HELIX 261..306
FT /evidence="ECO:0007829|PDB:3JCK"
SQ SEQUENCE 338 AA; 38313 MW; 6EE6009545A3D0EF CRC64;
MSLQHEKVTI APLVLLSALD HYERTQTKEN KRCVGVILGD ANSSTIRVTN SFALPFEEDE
KNSDVWFLDH NYIENMNEMC KKINAKEKLI GWYHSGPKLR ASDLKINELF KKYTQNNPLL
LIVDVKQQGV GLPTDAYVAI EQVKDDGTST EKTFLHLPCT IEAEEAEEIG VEHLLRDVRD
QAAGGLSIRL TNQLKSLKGL QSKLKDVVEY LDKVINKELP INHTILGKLQ DVFNLLPNLG
TPDDDEIDVE NHDRINISNN LQKALTVKTN DELMVIYISN LVRSIIAFDD LIENKIQNKK
IQEQRVKDKQ SKVSDDSESE SGDKEATAPL IQRKNKKN
