PSMD9_YEAST
ID PSMD9_YEAST Reviewed; 220 AA.
AC P40555; D6VVS3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Probable 26S proteasome regulatory subunit p27;
DE AltName: Full=Proteasome non-ATPase subunit 2;
GN Name=NAS2; OrderedLocusNames=YIL007C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 CHARACTERIZATION.
RX PubMed=9653651; DOI=10.1006/geno.1998.5301;
RA Watanabe T.K., Saito A., Suzuki M., Fujiwara T., Takahashi E.,
RA Slaughter C.A., DeMartino G.N., Hendil K.B., Chung C.H., Tanahashi N.,
RA Tanaka K.;
RT "cDNA cloning and characterization of a human proteasomal modulator
RT subunit, p27 (PSMD9).";
RL Genomics 50:241-250(1998).
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 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 [7]
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).
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the base subcomplex of the 19S regulatory
CC complex (RC). During the base subcomplex assembly is part of a
CC NAS2:RPT4:RPT5 module; NAS2 is released during the further base
CC assembly process. {ECO:0000269|PubMed:19446322}.
CC -!- SUBUNIT: Part of a transient complex containing NAS2, RPT4 and RPT5
CC formed during the assembly of the 26S proteasome.
CC -!- INTERACTION:
CC P40555; P38872: PFS1; NbExp=3; IntAct=EBI-14024, EBI-24859;
CC P40555; P33297: RPT5; NbExp=8; IntAct=EBI-14024, EBI-13920;
CC -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome subunit p27 family.
CC {ECO:0000305}.
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DR EMBL; Z38113; CAA86244.1; -; Genomic_DNA.
DR EMBL; AY558294; AAS56620.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08539.1; -; Genomic_DNA.
DR PIR; S48450; S48450.
DR RefSeq; NP_012259.3; NM_001179357.3.
DR PDB; 3WHJ; X-ray; 1.65 A; A=1-120.
DR PDB; 3WHL; X-ray; 4.00 A; B/D/F/H=1-120.
DR PDB; 4O06; X-ray; 1.15 A; A=126-220.
DR PDBsum; 3WHJ; -.
DR PDBsum; 3WHL; -.
DR PDBsum; 4O06; -.
DR AlphaFoldDB; P40555; -.
DR SMR; P40555; -.
DR BioGRID; 34985; 131.
DR DIP; DIP-1893N; -.
DR IntAct; P40555; 19.
DR MINT; P40555; -.
DR STRING; 4932.YIL007C; -.
DR MaxQB; P40555; -.
DR PaxDb; P40555; -.
DR PRIDE; P40555; -.
DR EnsemblFungi; YIL007C_mRNA; YIL007C; YIL007C.
DR GeneID; 854810; -.
DR KEGG; sce:YIL007C; -.
DR SGD; S000001269; NAS2.
DR VEuPathDB; FungiDB:YIL007C; -.
DR eggNOG; KOG3129; Eukaryota.
DR GeneTree; ENSGT00390000004147; -.
DR HOGENOM; CLU_073146_0_0_1; -.
DR InParanoid; P40555; -.
DR OMA; GCNIVPL; -.
DR BioCyc; YEAST:G3O-31286-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:P40555; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40555; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IDA:SGD.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR040815; Nas2_N.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR035269; PSMD9.
DR PANTHER; PTHR12651; PTHR12651; 1.
DR Pfam; PF18265; Nas2_N; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Reference proteome.
FT CHAIN 1..220
FT /note="Probable 26S proteasome regulatory subunit p27"
FT /id="PRO_0000173856"
FT DOMAIN 119..196
FT /note="PDZ"
FT HELIX 2..11
FT /evidence="ECO:0007829|PDB:3WHJ"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:3WHJ"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:3WHJ"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:3WHJ"
FT HELIX 73..110
FT /evidence="ECO:0007829|PDB:3WHJ"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:4O06"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:4O06"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4O06"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4O06"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:4O06"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:4O06"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4O06"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:4O06"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:4O06"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:4O06"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4O06"
SQ SEQUENCE 220 AA; 24846 MW; 1BA966C5B7B2D02B CRC64;
MEEEELSKLL ANVKIDPSLT SRISQIDSFK LSELMVLKTD IETQLEAYFS VLEQQGIGMD
SALVTPDGYP RSDVDVLQVT MIRKNVNMLK NDLNHLLQRS HVLLNQHFDN MNVKSNQDAR
RNNDDQAIQY TIPFAFISEV VPGSPSDKAD IKVDDKLISI GNVHAANHSK LQNIQMVVMK
NEDRPLPVLL LREGQILKTS LTPSRNWNGR GLLGCRIQEL
