RPN10_YEAST
ID RPN10_YEAST Reviewed; 268 AA.
AC P38886; D3DLE9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=26S proteasome regulatory subunit RPN10;
GN Name=RPN10; Synonyms=MCB1 {ECO:0000303|PubMed:8887631}, SUN1;
GN OrderedLocusNames=YHR200W;
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].
RX PubMed=9017604; DOI=10.1091/mbc.8.1.171;
RA Kominami K., Okura N., Kawamura M., Demartino G.N., Slaughter C.A.,
RA Shimbara N., Chung C.H., Fujimuro M., Yokosawa H., Shimizu Y.,
RA Tanahashi N., Tanaka K., Toh-e A.;
RT "Yeast counterparts of subunits S5a and p58 (S3) of the human 26S
RT proteasome are encoded by two multicopy suppressors of nin1-1.";
RL Mol. Biol. Cell 8:171-187(1997).
RN [2]
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 [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 2-8, AND SUBUNIT.
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, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=8887631; DOI=10.1128/mcb.16.11.6020;
RA van Nocker S., Sadis S., Rubin D.M., Glickman M., Fu H., Coux O., Wefes I.,
RA Finley D., Vierstra R.D.;
RT "The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S
RT proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-
RT specific role in protein turnover.";
RL Mol. Cell. Biol. 16:6020-6028(1996).
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 UBIQUITINATION.
RX PubMed=17190603; DOI=10.1016/j.cell.2006.09.051;
RA Crosas B., Hanna J., Kirkpatrick D.S., Zhang D.P., Tone Y., Hathaway N.A.,
RA Buecker C., Leggett D.S., Schmidt M., King R.W., Gygi S.P., Finley D.;
RT "Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin
RT ligase and deubiquitinating activities.";
RL Cell 127:1401-1413(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
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: Multiubiquitin binding protein. {ECO:0000269|PubMed:8887631}.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as
CC the 20S proteasome, capped at one or both ends by the 19S regulatory
CC complex (RC) (PubMed:12504901, PubMed:8887631, PubMed:22927375). The RC
CC is composed of at least 18 different subunits in two subcomplexes, the
CC base and the lid, which form the portions proximal and distal to the
CC 20S proteolytic core, respectively (PubMed:22927375).
CC {ECO:0000269|PubMed:12504901, ECO:0000269|PubMed:22927375,
CC ECO:0000269|PubMed:8887631}.
CC -!- INTERACTION:
CC P38886; P48510: DSK2; NbExp=5; IntAct=EBI-15949, EBI-6174;
CC P38886; P38764: RPN1; NbExp=6; IntAct=EBI-15949, EBI-15913;
CC P38886; P33297: RPT5; NbExp=2; IntAct=EBI-15949, EBI-13920;
CC -!- PTM: Ubiquitinated, leading to its degradation (PubMed:17190603).
CC Ubiquitination is promoted by HUL5 (PubMed:17190603).
CC {ECO:0000269|PubMed:17190603}.
CC -!- DISRUPTION PHENOTYPE: Cells are viable. {ECO:0000269|PubMed:8887631}.
CC -!- MISCELLANEOUS: Present with 17200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5A family.
CC {ECO:0000305}.
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DR EMBL; D78022; BAA11207.1; -; Genomic_DNA.
DR EMBL; U00030; AAB68355.1; -; Genomic_DNA.
DR EMBL; AY558289; AAS56615.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06893.1; -; Genomic_DNA.
DR PIR; S46677; S46677.
DR RefSeq; NP_012070.3; NM_001179331.3.
DR PDB; 3JCO; EM; 4.80 A; W=1-268.
DR PDB; 3JCP; EM; 4.60 A; W=1-268.
DR PDB; 4CR2; EM; 7.70 A; W=1-268.
DR PDB; 4CR3; EM; 9.30 A; W=1-268.
DR PDB; 4CR4; EM; 8.80 A; W=1-268.
DR PDB; 5A5B; EM; 9.50 A; W=1-268.
DR PDB; 5LN1; X-ray; 3.14 A; A=1-191.
DR PDB; 5MPB; EM; 7.80 A; W=1-268.
DR PDB; 5MPC; EM; 7.70 A; W=1-268.
DR PDB; 5MPD; EM; 4.10 A; W=1-268.
DR PDB; 5MPE; EM; 4.50 A; W=1-268.
DR PDB; 5WVI; EM; 6.30 A; W=1-268.
DR PDB; 5WVK; EM; 4.20 A; W=1-268.
DR PDB; 6FVT; EM; 4.10 A; W=1-197.
DR PDB; 6FVU; EM; 4.50 A; W=1-197.
DR PDB; 6FVV; EM; 5.40 A; W=1-197.
DR PDB; 6FVW; EM; 4.50 A; W=1-197.
DR PDB; 6FVX; EM; 4.90 A; W=1-197.
DR PDB; 6FVY; EM; 6.10 A; W=1-197.
DR PDB; 6J2C; EM; 7.00 A; W=1-268.
DR PDB; 6J2N; EM; 7.50 A; W=1-268.
DR PDB; 6J2Q; EM; 3.80 A; W=1-268.
DR PDB; 6J2X; EM; 3.80 A; W=1-268.
DR PDB; 6J30; EM; 4.50 A; W=1-268.
DR PDB; 7QO3; EM; 6.10 A; W=1-268.
DR PDB; 7QO5; EM; 6.00 A; W=1-268.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5LN1; -.
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; P38886; -.
DR BMRB; P38886; -.
DR SMR; P38886; -.
DR BioGRID; 36634; 834.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-2100N; -.
DR IntAct; P38886; 59.
DR MINT; P38886; -.
DR STRING; 4932.YHR200W; -.
DR MEROPS; X13.001; -.
DR iPTMnet; P38886; -.
DR MaxQB; P38886; -.
DR PaxDb; P38886; -.
DR PRIDE; P38886; -.
DR EnsemblFungi; YHR200W_mRNA; YHR200W; YHR200W.
DR GeneID; 856607; -.
DR KEGG; sce:YHR200W; -.
DR SGD; S000001243; RPN10.
DR VEuPathDB; FungiDB:YHR200W; -.
DR eggNOG; KOG2884; Eukaryota.
DR GeneTree; ENSGT00530000064050; -.
DR HOGENOM; CLU_033293_1_0_1; -.
DR InParanoid; P38886; -.
DR OMA; IQGEDGM; -.
DR BioCyc; YEAST:G3O-31228-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-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:P38886; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38886; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IMP:SGD.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:SGD.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:SGD.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0043248; P:proteasome assembly; IGI:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR027040; Proteasome_su_Rpn10.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10223:SF0; PTHR10223:SF0; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Proteasome; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901"
FT CHAIN 2..268
FT /note="26S proteasome regulatory subunit RPN10"
FT /id="PRO_0000173834"
FT DOMAIN 5..190
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 223..242
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 226..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5LN1"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:5LN1"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:5LN1"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:5LN1"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:5LN1"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:5LN1"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5LN1"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:5LN1"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:5LN1"
SQ SEQUENCE 268 AA; 29747 MW; 8A05198B0CD7C0C3 CRC64;
MVLEATVLVI DNSEYSRNGD FPRTRFEAQI DSVEFIFQAK RNSNPENTVG LISGAGANPR
VLSTFTAEFG KILAGLHDTQ IEGKLHMATA LQIAQLTLKH RQNKVQHQRI VAFVCSPISD
SRDELIRLAK TLKKNNVAVD IINFGEIEQN TELLDEFIAA VNNPQEETSH LLTVTPGPRL
LYENIASSPI ILEEGSSGMG AFGGSGGDSD ANGTFMDFGV DPSMDPELAM ALRLSMEEEQ
QRQERLRQQQ QQQDQPEQSE QPEQHQDK
