PSD10_YEAST
ID PSD10_YEAST Reviewed; 228 AA.
AC P50086; D6VV12;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Probable 26S proteasome regulatory subunit p28;
DE AltName: Full=Proteasome non-ATPase subunit 6;
GN Name=NAS6; OrderedLocusNames=YGR232W; ORFNames=G8564;
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 204508 / S288c;
RX PubMed=8701610;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 12:385-390(1996).
RN [2]
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 [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 FUNCTION.
RX PubMed=9714768; DOI=10.1016/s0378-1119(98)00309-6;
RA Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A., Takeuchi J.,
RA Toh-e A., Tanaka K.;
RT "cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two
RT novel regulatory subunits of the 26S proteasome.";
RL Gene 216:113-122(1998).
RN [6]
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 [7]
RP FUNCTION AS PROTEASOME CHAPERONE.
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 [8]
RP FUNCTION AS PROTEASOME CHAPERONE, AND INTERACTION WITH RPT3.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=14583612; DOI=10.1074/jbc.m310266200;
RA Padmanabhan B., Adachi N., Kataoka K., Horikoshi M.;
RT "Crystal structure of the homolog of the oncoprotein gankyrin, an
RT interactor of Rb and CDK4/6.";
RL J. Biol. Chem. 279:1546-1552(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Structural comparison of NAS6p protein structures in two different crystal
RT forms.";
RL Submitted (JUN-2005) to the PDB data bank.
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the 19S regulatory complex (RC) and appears
CC to have an overlapping role with RPN14. {ECO:0000269|PubMed:19412159,
CC ECO:0000269|PubMed:19446322, ECO:0000269|PubMed:9714768}.
CC -!- SUBUNIT: Interacts with RPT3. {ECO:0000269|PubMed:19412159}.
CC -!- INTERACTION:
CC P50086; P38348: HSM3; NbExp=7; IntAct=EBI-14028, EBI-21152;
CC P50086; P53196: RPN14; NbExp=5; IntAct=EBI-14028, EBI-23691;
CC P50086; P33298: RPT3; NbExp=10; IntAct=EBI-14028, EBI-13905;
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X87941; CAA61182.1; -; Genomic_DNA.
DR EMBL; Z73017; CAA97260.1; -; Genomic_DNA.
DR EMBL; AY558275; AAS56601.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08323.1; -; Genomic_DNA.
DR PIR; S57697; S57697.
DR RefSeq; NP_011748.3; NM_001181361.3.
DR PDB; 1IXV; X-ray; 2.30 A; A=1-228.
DR PDB; 1WG0; X-ray; 2.53 A; A=1-228.
DR PDB; 2DZN; X-ray; 2.20 A; A/C/E=1-228.
DR PDB; 2DZO; X-ray; 3.00 A; A/C=1-228.
DR PDBsum; 1IXV; -.
DR PDBsum; 1WG0; -.
DR PDBsum; 2DZN; -.
DR PDBsum; 2DZO; -.
DR AlphaFoldDB; P50086; -.
DR SMR; P50086; -.
DR BioGRID; 33484; 75.
DR DIP; DIP-1591N; -.
DR IntAct; P50086; 29.
DR MINT; P50086; -.
DR STRING; 4932.YGR232W; -.
DR CarbonylDB; P50086; -.
DR iPTMnet; P50086; -.
DR MaxQB; P50086; -.
DR PaxDb; P50086; -.
DR PRIDE; P50086; -.
DR EnsemblFungi; YGR232W_mRNA; YGR232W; YGR232W.
DR GeneID; 853147; -.
DR KEGG; sce:YGR232W; -.
DR SGD; S000003464; NAS6.
DR VEuPathDB; FungiDB:YGR232W; -.
DR eggNOG; KOG4412; Eukaryota.
DR GeneTree; ENSGT00940000153404; -.
DR HOGENOM; CLU_000134_18_2_1; -.
DR InParanoid; P50086; -.
DR OMA; WAVAYNR; -.
DR BioCyc; YEAST:G3O-30910-MON; -.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR EvolutionaryTrace; P50086; -.
DR PRO; PR:P50086; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P50086; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1904855; F:proteasome regulatory particle binding; IDA:SGD.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IMP:SGD.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13606; Ank_3; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Chaperone; Reference proteome; Repeat.
FT CHAIN 1..228
FT /note="Probable 26S proteasome regulatory subunit p28"
FT /id="PRO_0000067048"
FT REPEAT 1..30
FT /note="ANK 1"
FT REPEAT 35..64
FT /note="ANK 2"
FT REPEAT 71..100
FT /note="ANK 3"
FT REPEAT 106..135
FT /note="ANK 4"
FT REPEAT 139..168
FT /note="ANK 5"
FT REPEAT 173..203
FT /note="ANK 6"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:2DZN"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:2DZN"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:2DZN"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:2DZN"
SQ SEQUENCE 228 AA; 25616 MW; 6B30C0DD034A6289 CRC64;
MSNYPLHQAC MENEFFKVQE LLHSKPSLLL QKDQDGRIPL HWSVSFQAHE ITSFLLSKME
NVNLDDYPDD SGWTPFHIAC SVGNLEVVKS LYDRPLKPDL NKITNQGVTC LHLAVGKKWF
EVSQFLIENG ASVRIKDKFN QIPLHRAASV GSLKLIELLC GLGKSAVNWQ DKQGWTPLFH
ALAEGHGDAA VLLVEKYGAE YDLVDNKGAK AEDVALNEQV KKFFLNNV
