RPN12_YEAST
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 03-AUG-2022, entry version 181.
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<149::aid-yea893>3.0.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=3; IntAct=EBI-15953, EBI-36176;
CC P32496; P33298: RPT3; NbExp=3; 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}.
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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 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 AlphaFoldDB; P32496; -.
DR SMR; P32496; -.
DR BioGRID; 31210; 490.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-1575N; -.
DR IntAct; P32496; 38.
DR MINT; P32496; -.
DR STRING; 4932.YFR052W; -.
DR iPTMnet; P32496; -.
DR MaxQB; P32496; -.
DR PaxDb; P32496; -.
DR PRIDE; P32496; -.
DR EnsemblFungi; YFR052W_mRNA; YFR052W; YFR052W.
DR GeneID; 850613; -.
DR KEGG; sce:YFR052W; -.
DR SGD; S000001948; RPN12.
DR VEuPathDB; FungiDB:YFR052W; -.
DR eggNOG; KOG3151; Eukaryota.
DR GeneTree; ENSGT00390000014682; -.
DR HOGENOM; CLU_046003_1_0_1; -.
DR InParanoid; P32496; -.
DR OMA; HKFMGLH; -.
DR BioCyc; YEAST:G3O-30498-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 ChiTaRS; RPN12; yeast.
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:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR InterPro; IPR006746; 26S_Psome_Rpn12.
DR InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR12387; PTHR12387; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR PROSITE; PS50250; PCI; 1.
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 174..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
