RPN14_YEAST
ID RPN14_YEAST Reviewed; 417 AA.
AC P53196; D6VUD4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=26S proteasome regulatory subunit RPN14;
DE AltName: Full=Proteasome non-ATPase subunit 14;
GN Name=RPN14; OrderedLocusNames=YGL004C;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 FUNCTION, AND INTERACTION WITH RPT5.
RX PubMed=17499717; DOI=10.1016/j.febslet.2007.04.064;
RA Seong K.M., Baek J.H., Yu M.H., Kim J.;
RT "Rpn13p and Rpn14p are involved in the recognition of ubiquitinated Gcn4p
RT by the 26S proteasome.";
RL FEBS Lett. 581:2567-2573(2007).
RN [7]
RP FUNCTION, AND ASSOCIATION WITH THE PROTEASOME REGULATORY PARTICLE.
RX PubMed=19412159; DOI=10.1038/nature08063;
RA Roelofs J., Park S., Haas W., Tian G., McAllister F.E., Huo Y., Lee B.H.,
RA Zhang F., Shi Y., Gygi S.P., Finley D.;
RT "Chaperone-mediated pathway of proteasome regulatory particle assembly.";
RL Nature 459:861-865(2009).
RN [8]
RP FUNCTION, ASSOCIATION WITH THE 19S REGULATORY PARTICLE OF THE PROTEASOME,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19446322; DOI=10.1016/j.cell.2009.04.061;
RA Funakoshi M., Tomko R.J. Jr., Kobayashi H., Hochstrasser M.;
RT "Multiple assembly chaperones govern biogenesis of the proteasome
RT regulatory particle base.";
RL Cell 137:887-899(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE 19S REGULATORY
RP PARTICLE OF THE PROTEASOME, AND INTERACTION WITH RPT6.
RX PubMed=19446323; DOI=10.1016/j.cell.2009.05.005;
RA Saeki Y., Toh-E A., Kudo T., Kawamura H., Tanaka K.;
RT "Multiple proteasome-interacting proteins assist the assembly of the yeast
RT 19S regulatory particle.";
RL Cell 137:900-913(2009).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins. Is
CC not a genuine component of the 26S proteasome, but an auxiliary factor
CC that interacts with the proteasomal ATPase of 19S regulatory particle
CC (RP). Acts as a chaperone which regulates the highly structured
CC assembly of the 19S regulatory particle. Involved in the substrate
CC specificity of the 26S proteasome and is especially involved in the
CC degradation of ubiquitinated GCN4. May contribute to the stability of
CC the 26S proteasome in some stress conditions.
CC {ECO:0000269|PubMed:17499717, ECO:0000269|PubMed:19412159,
CC ECO:0000269|PubMed:19446322, ECO:0000269|PubMed:19446323}.
CC -!- SUBUNIT: Associates with the 19S proteasome regulatory particle (RP).
CC Interacts directly with RPT5 and RPT6. {ECO:0000269|PubMed:17499717,
CC ECO:0000269|PubMed:19446323}.
CC -!- INTERACTION:
CC P53196; P38348: HSM3; NbExp=8; IntAct=EBI-23691, EBI-21152;
CC P53196; P50086: NAS6; NbExp=5; IntAct=EBI-23691, EBI-14028;
CC P53196; P33299: RPT1; NbExp=7; IntAct=EBI-23691, EBI-13910;
CC P53196; P33297: RPT5; NbExp=5; IntAct=EBI-23691, EBI-13920;
CC P53196; Q01939: RPT6; NbExp=9; IntAct=EBI-23691, EBI-13914;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 2210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat PAAF1/RPN14 family. {ECO:0000305}.
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DR EMBL; Z72526; CAA96704.1; -; Genomic_DNA.
DR EMBL; AY692599; AAT92618.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08095.1; -; Genomic_DNA.
DR PIR; S64006; S64006.
DR RefSeq; NP_011511.3; NM_001180869.3.
DR PDB; 3ACP; X-ray; 2.00 A; A=1-417.
DR PDB; 3VL1; X-ray; 1.60 A; A/B=1-417.
DR PDBsum; 3ACP; -.
DR PDBsum; 3VL1; -.
DR AlphaFoldDB; P53196; -.
DR SMR; P53196; -.
DR BioGRID; 33241; 50.
DR DIP; DIP-6617N; -.
DR IntAct; P53196; 44.
DR MINT; P53196; -.
DR STRING; 4932.YGL004C; -.
DR MaxQB; P53196; -.
DR PaxDb; P53196; -.
DR PRIDE; P53196; -.
DR EnsemblFungi; YGL004C_mRNA; YGL004C; YGL004C.
DR GeneID; 852880; -.
DR KEGG; sce:YGL004C; -.
DR SGD; S000002972; RPN14.
DR VEuPathDB; FungiDB:YGL004C; -.
DR eggNOG; KOG0266; Eukaryota.
DR HOGENOM; CLU_037051_3_1_1; -.
DR InParanoid; P53196; -.
DR OMA; ITVAHIQ; -.
DR BioCyc; YEAST:G3O-30528-MON; -.
DR EvolutionaryTrace; P53196; -.
DR PRO; PR:P53196; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53196; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Nucleus; Proteasome;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..417
FT /note="26S proteasome regulatory subunit RPN14"
FT /id="PRO_0000051475"
FT REPEAT 134..173
FT /note="WD 1"
FT REPEAT 176..215
FT /note="WD 2"
FT REPEAT 242..281
FT /note="WD 3"
FT REPEAT 285..325
FT /note="WD 4"
FT REPEAT 330..371
FT /note="WD 5"
FT REPEAT 380..416
FT /note="WD 6"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3VL1"
FT HELIX 14..19
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:3VL1"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3VL1"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:3VL1"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:3VL1"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3VL1"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:3VL1"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:3VL1"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:3VL1"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3ACP"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:3VL1"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:3VL1"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:3VL1"
SQ SEQUENCE 417 AA; 46383 MW; 025CAB9A872E1AB8 CRC64;
MTKTITVAHI QYDFKAVLEE NDENDDEFYI NVDKNLNEIK EHKIVVLGNS RGVDAGKGNT
FEKVGSHLYK ARLDGHDFLF NTIIRDGSKM LKRADYTAVD TAKLQMRRFI LGTTEGDIKV
LDSNFNLQRE IDQAHVSEIT KLKFFPSGEA LISSSQDMQL KIWSVKDGSN PRTLIGHRAT
VTDIAIIDRG RNVLSASLDG TIRLWECGTG TTIHTFNRKE NPHDGVNSIA LFVGTDRQLH
EISTSKKNNL EFGTYGKYVI AGHVSGVITV HNVFSKEQTI QLPSKFTCSC NSLTVDGNNA
NYIYAGYENG MLAQWDLRSP ECPVGEFLIN EGTPINNVYF AAGALFVSSG FDTSIKLDII
SDPESERPAI EFETPTFLVS NDDEVSQFCY VSDDESNGEV LEVGKNNFCA LYNLSNP
