ID RPN12_YEAST Reviewed; 274 AA. AC P32496; D6VTT5; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 198. DE RecName: Full=26S proteasome regulatory subunit RPN12; DE AltName: Full=Nuclear integrity protein 1; GN Name=RPN12; Synonyms=NIN1; OrderedLocusNames=YFR052W; 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=1563492; DOI=10.1016/s0014-4827(05)80070-9; RA Nisogi H., Kominami K., Tanaka K., Toh-e A.; RT "A new essential gene of Saccharomyces cerevisiae, a defect in it may RT result in instability of nucleus."; RL Exp. Cell Res. 200:48-57(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). 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 204511 / S288c / AB972; RX PubMed=8686379; RX DOI=10.1002/(sici)1097-0061(199602)12:2%3c149::aid-yea893%3e3.0.co;2-g; RA Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., RA Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.; RT "Analysis of a 36.2 kb DNA sequence including the right telomere of RT chromosome VI from Saccharomyces cerevisiae."; RL Yeast 12:149-167(1996). RN [5] RP CHARACTERIZATION. RX PubMed=7621825; DOI=10.1002/j.1460-2075.1995.tb07313.x; RA Kominami K., DeMartino G.N., Moomaw C., Slaughter C.A., Shimbara N., RA Fujimuro M., Yokosawa H., Hisamatsu H., Tanahashi N., Shimizu Y., RA Tanaka K., Toh-e A.; RT "Nin1p, a regulatory subunit of the 26S proteasome, is necessary for RT activation of Cdc28p kinase of Saccharomyces cerevisiae."; RL EMBO J. 14:3105-3115(1995). RN [6] 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 [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 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 Necessary for activation of the CDC28 kinase. CC -!- INTERACTION: CC P32496; Q08723: RPN8; NbExp=4; IntAct=EBI-15953, EBI-36176; CC P32496; P33298: RPT3; NbExp=4; IntAct=EBI-15953, EBI-13905; CC -!- MISCELLANEOUS: Present with 9890 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the proteasome subunit S14 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D10515; BAA01390.1; -; Genomic_DNA. DR EMBL; D50617; BAA09291.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12495.1; -; Genomic_DNA. DR PIR; S27434; S27434. DR RefSeq; NP_116710.1; NM_001180017.1. DR PDB; 3J47; EM; -; T=256-272. DR PDB; 3JCK; EM; 3.50 A; H=1-274. DR PDB; 3JCO; EM; 4.80 A; T=1-274. DR PDB; 3JCP; EM; 4.60 A; T=1-274. DR PDB; 4CR2; EM; 7.70 A; T=1-274. DR PDB; 4CR3; EM; 9.30 A; T=1-274. DR PDB; 4CR4; EM; 8.80 A; T=1-274. DR PDB; 5A5B; EM; 9.50 A; T=1-274. DR PDB; 5MPB; EM; 7.80 A; T=1-274. DR PDB; 5MPC; EM; 7.70 A; T=1-274. DR PDB; 5MPD; EM; 4.10 A; T=1-274. DR PDB; 5MPE; EM; 4.50 A; T=1-274. DR PDB; 5WVI; EM; 6.30 A; T=1-274. DR PDB; 5WVK; EM; 4.20 A; T=1-274. DR PDB; 6FVT; EM; 4.10 A; T=7-272. DR PDB; 6FVU; EM; 4.50 A; T=7-272. DR PDB; 6FVV; EM; 5.40 A; T=7-272. DR PDB; 6FVW; EM; 4.50 A; T=7-272. DR PDB; 6FVX; EM; 4.90 A; T=7-272. DR PDB; 6FVY; EM; 6.10 A; T=7-272. DR PDB; 6J2C; EM; 7.00 A; T=1-274. DR PDB; 6J2N; EM; 7.50 A; T=1-274. DR PDB; 6J2Q; EM; 3.80 A; T=1-274. DR PDB; 6J2X; EM; 3.80 A; T=1-274. DR PDB; 6J30; EM; 4.50 A; T=1-274. DR PDB; 7QO3; EM; 6.10 A; T=1-274. DR PDB; 7QO5; EM; 6.00 A; T=1-274. DR PDB; 9CGC; EM; 3.61 A; T=1-274. DR PDB; 9IWR; EM; 9.10 A; T=1-274. DR AlphaFoldDB; P32496; -. DR EMDB; EMD-14082; -. DR EMDB; EMD-14084; -. DR EMDB; EMD-3536; -. DR EMDB; EMD-3537; -. DR EMDB; EMD-4321; -. DR EMDB; EMD-4322; -. DR EMDB; EMD-4323; -. DR EMDB; EMD-4324; -. DR EMDB; EMD-45579; -. DR EMDB; EMD-60960; -. DR EMDB; EMD-6693; -. DR EMDB; EMD-6694; -. DR EMDB; EMD-9769; -. DR EMDB; EMD-9770; -. DR EMDB; EMD-9771; -. DR EMDB; EMD-9772; -. DR EMDB; EMD-9773; -. DR SMR; P32496; -. DR BioGRID; 31210; 503. DR ComplexPortal; CPX-2262; 26S proteasome complex. DR DIP; DIP-1575N; -. DR FunCoup; P32496; 1500. DR IntAct; P32496; 57. DR MINT; P32496; -. DR STRING; 4932.YFR052W; -. DR iPTMnet; P32496; -. DR PaxDb; 4932-YFR052W; -. DR PeptideAtlas; P32496; -. DR EnsemblFungi; YFR052W_mRNA; YFR052W; YFR052W. DR GeneID; 850613; -. DR KEGG; sce:YFR052W; -. DR AGR; SGD:S000001948; -. DR SGD; S000001948; RPN12. DR VEuPathDB; FungiDB:YFR052W; -. DR eggNOG; KOG3151; Eukaryota. DR HOGENOM; CLU_046003_1_0_1; -. DR InParanoid; P32496; -. DR OMA; HKFMGLH; -. DR OrthoDB; 8775810at2759; -. DR BioCyc; YEAST:G3O-30498-MONOMER; -. DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-SCE-5689880; Ub-specific processing proteases. DR Reactome; R-SCE-9907900; Proteasome assembly. DR BioGRID-ORCS; 850613; 1 hit in 10 CRISPR screens. DR EvolutionaryTrace; P32496; -. DR PRO; PR:P32496; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P32496; protein. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD. DR FunFam; 1.25.40.990:FF:000001; 26S proteasome non-ATPase regulatory subunit; 1. DR Gene3D; 1.25.40.990; -; 1. DR InterPro; IPR006746; 26S_Psome_Rpn12. DR InterPro; IPR033464; CSN8_PSD8_EIF3K. DR InterPro; IPR000717; PCI_dom. DR PANTHER; PTHR12387; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 8; 1. DR PANTHER; PTHR12387:SF0; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 8; 1. DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1. DR PROSITE; PS50250; PCI; 1. DR PDBsum; 3J47; -. DR PDBsum; 3JCK; -. 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 PDBsum; 9CGC; -. DR PDBsum; 9IWR; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Proteasome; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12504901" FT CHAIN 2..274 FT /note="26S proteasome regulatory subunit RPN12" FT /id="PRO_0000173851" FT DOMAIN 76..251 FT /note="PCI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185" FT HELIX 8..17 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 20..40 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 52..71 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 75..90 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 101..115 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 119..133 FT /evidence="ECO:0007829|PDB:3JCK" FT TURN 138..142 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 143..154 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 157..166 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 175..196 FT /evidence="ECO:0007829|PDB:3JCK" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 202..209 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 215..223 FT /evidence="ECO:0007829|PDB:3JCK" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:3JCK" FT HELIX 259..271 FT /evidence="ECO:0007829|PDB:3JCK" SQ SEQUENCE 274 AA; 31919 MW; D901AAD4D07ED3D1 CRC64; MPSLAELTKS LSIAFENGDY AACEKLLPPI KIELIKNNLL IPDLSIQNDI YLNDLMITKR ILEVGALASI QTFNFDSFEN YFNQLKPYYF SNNHKLSESD KKSKLISLYL LNLLSQNNTT KFHSELQYLD KHIKNLEDDS LLSYPIKLDR WLMEGSYQKA WDLLQSGSQN ISEFDSFTDI LKSAIRDEIA KNTELSYDFL PLSNIKALLF FNNEKETEKF ALERNWPIVN SKVYFNNQSK EKADYEDEMM HEEDQKTNII EKAMDYAISI ENIV //