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P32379

- PSA5_YEAST

UniProt

P32379 - PSA5_YEAST

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Protein

Proteasome subunit alpha type-5

Gene

PUP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteasomal ubiquitin-independent protein catabolic process Source: SGD
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciYEAST:G3O-30926-MONOMER.
ReactomeiREACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_83036. Orc1 removal from chromatin.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PUP2
Multicatalytic endopeptidase complex subunit PUP2
Proteasome component PUP2
Proteinase YSCE subunit PUP2
Gene namesi
Name:PUP2
Synonyms:DOA5
Ordered Locus Names:YGR253C
ORF Names:G9155
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR253c.
SGDiS000003485. PUP2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
  3. nucleus Source: SGD
  4. proteasome core complex, alpha-subunit complex Source: SGD
  5. proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491G → D in DOA5-1; slight decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 260260Proteasome subunit alpha type-5PRO_0000124129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551Phosphothreonine1 Publication
Modified residuei56 – 561Phosphoserine1 Publication
Modified residuei251 – 2511Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32379.
PaxDbiP32379.
PeptideAtlasiP32379.
PRIDEiP32379.

Expressioni

Gene expression databases

GenevestigatoriP32379.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.1 Publication

Protein-protein interaction databases

BioGridi33504. 58 interactions.
DIPiDIP-1193N.
IntActiP32379. 9 interactions.
MINTiMINT-386734.
STRINGi4932.YGR253C.

Structurei

Secondary structure

1
260
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104
Beta strandi19 – 213
Helixi22 – 3110
Beta strandi37 – 415
Beta strandi46 – 516
Beta strandi55 – 595
Helixi61 – 633
Beta strandi67 – 715
Beta strandi74 – 818
Helixi82 – 843
Helixi85 – 10319
Helixi109 – 1179
Turni118 – 1214
Beta strandi124 – 1263
Beta strandi128 – 1314
Beta strandi134 – 1363
Beta strandi139 – 14810
Turni149 – 1513
Beta strandi152 – 1587
Turni160 – 1623
Beta strandi164 – 17310
Helixi176 – 18611
Helixi193 – 20715
Beta strandi208 – 2103
Beta strandi216 – 2238
Turni224 – 2263
Beta strandi227 – 2304
Helixi233 – 24715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20E/S1-260[»]
1G0UX-ray2.40D/R1-250[»]
1G65X-ray2.25D/R9-250[»]
1JD2X-ray3.00D/Y9-120[»]
D/Y131-250[»]
1RYPX-ray1.90E/S9-250[»]
1VSYX-ray3.00E/S1-250[»]
1Z7QX-ray3.22E/S1-260[»]
2F16X-ray2.80D/R9-250[»]
2FAKX-ray2.80D/R9-250[»]
2GPLX-ray2.81D/R9-250[»]
2Z5CX-ray2.90C/F1-260[»]
2ZCYX-ray2.90D/R1-260[»]
3BDMX-ray2.70D/R1-260[»]
3D29X-ray2.60D/R9-250[»]
3DY3X-ray2.81D/R9-250[»]
3DY4X-ray2.80D/R9-250[»]
3E47X-ray3.00D/R9-250[»]
3GPJX-ray2.70D/R9-250[»]
3GPTX-ray2.41D/R9-250[»]
3GPWX-ray2.50D/R9-250[»]
3HYEX-ray2.50D/R9-250[»]
3L5QX-ray3.00J/V1-250[»]
3MG0X-ray2.68D/R9-250[»]
3MG4X-ray3.11D/R9-250[»]
3MG6X-ray2.60D/R1-250[»]
3MG7X-ray2.78D/R1-250[»]
3MG8X-ray2.59D/R1-250[»]
3NZJX-ray2.40D/R1-260[»]
3NZWX-ray2.50D/R1-260[»]
3NZXX-ray2.70D/R1-260[»]
3OEUX-ray2.60D/R1-260[»]
3OEVX-ray2.85D/R1-260[»]
3OKJX-ray2.70D/R9-250[»]
3SDIX-ray2.65D/R1-260[»]
3SDKX-ray2.70D/R1-260[»]
3SHJX-ray2.80D/R9-250[»]
3TDDX-ray2.70D/R9-250[»]
3UN4X-ray3.40D/R1-260[»]
3UN8X-ray2.70D/R1-260[»]
4CR2electron microscopy7.70E1-260[»]
4CR3electron microscopy9.30E1-260[»]
4CR4electron microscopy8.80E1-260[»]
4EU2X-ray2.51E/S9-250[»]
4FZCX-ray2.80D/R9-250[»]
4FZGX-ray3.00D/R9-250[»]
4G4SX-ray2.49E1-260[»]
4GK7X-ray2.80D/R9-250[»]
4HNPX-ray2.80D/R9-250[»]
4HRCX-ray2.80D/R9-250[»]
4HRDX-ray2.80D/R9-250[»]
4INRX-ray2.70D/R1-260[»]
4INTX-ray2.90D/R1-260[»]
4INUX-ray3.10D/R1-260[»]
4J70X-ray2.80D/R1-260[»]
4JSQX-ray2.80D/R1-260[»]
4JSUX-ray2.90D/R1-260[»]
4JT0X-ray3.10D/R1-260[»]
4LQIX-ray2.70D/R9-250[»]
4LTCX-ray2.50D/R1-260[»]
4NNNX-ray2.50D/R1-260[»]
4NNWX-ray2.60D/R1-260[»]
4NO1X-ray2.50D/R1-260[»]
4NO6X-ray3.00D/R1-260[»]
4NO8X-ray2.70D/R1-260[»]
4NO9X-ray2.90D/R1-260[»]
4Q1SX-ray2.60D/R1-260[»]
4QBYX-ray3.00D/R1-260[»]
4QLQX-ray2.40D/R1-260[»]
4QLSX-ray2.80D/R1-260[»]
4QLTX-ray2.80D/R1-260[»]
4QLUX-ray2.80D/R1-260[»]
4QLVX-ray2.90D/R1-260[»]
4R02X-ray2.50D/R1-260[»]
ProteinModelPortaliP32379.
SMRiP32379. Positions 9-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32379.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074958.
HOGENOMiHOG000091085.
InParanoidiP32379.
KOiK02729.
OMAiCAMSGLT.
OrthoDBiEOG7SBP0C.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32379-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLTRSEYDR GVSTFSPEGR LFQVEYSLEA IKLGSTAIGI ATKEGVVLGV
60 70 80 90 100
EKRATSPLLE SDSIEKIVEI DRHIGCAMSG LTADARSMIE HARTAAVTHN
110 120 130 140 150
LYYDEDINVE SLTQSVCDLA LRFGEGASGE ERLMSRPFGV ALLIAGHDAD
160 170 180 190 200
DGYQLFHAEP SGTFYRYNAK AIGSGSEGAQ AELLNEWHSS LTLKEAELLV
210 220 230 240 250
LKILKQVMEE KLDENNAQLS CITKQDGFKI YDNEKTAELI KELKEKEAAE
260
SPEEADVEMS
Length:260
Mass (Da):28,617
Last modified:October 1, 1996 - v2
Checksum:iE8EDEB212BF4EC6E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921T → S in CAA46111. (PubMed:1544471)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64918 Genomic DNA. Translation: CAA46111.1.
X99228 Genomic DNA. Translation: CAA67615.1.
Z73038 Genomic DNA. Translation: CAA97282.1.
AY558511 Genomic DNA. Translation: AAS56837.1.
BK006941 Genomic DNA. Translation: DAA08344.1.
PIRiS64585.
RefSeqiNP_011769.1. NM_001181382.1.

Genome annotation databases

EnsemblFungiiYGR253C; YGR253C; YGR253C.
GeneIDi853168.
KEGGisce:YGR253C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64918 Genomic DNA. Translation: CAA46111.1 .
X99228 Genomic DNA. Translation: CAA67615.1 .
Z73038 Genomic DNA. Translation: CAA97282.1 .
AY558511 Genomic DNA. Translation: AAS56837.1 .
BK006941 Genomic DNA. Translation: DAA08344.1 .
PIRi S64585.
RefSeqi NP_011769.1. NM_001181382.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FNT X-ray 3.20 E/S 1-260 [» ]
1G0U X-ray 2.40 D/R 1-250 [» ]
1G65 X-ray 2.25 D/R 9-250 [» ]
1JD2 X-ray 3.00 D/Y 9-120 [» ]
D/Y 131-250 [» ]
1RYP X-ray 1.90 E/S 9-250 [» ]
1VSY X-ray 3.00 E/S 1-250 [» ]
1Z7Q X-ray 3.22 E/S 1-260 [» ]
2F16 X-ray 2.80 D/R 9-250 [» ]
2FAK X-ray 2.80 D/R 9-250 [» ]
2GPL X-ray 2.81 D/R 9-250 [» ]
2Z5C X-ray 2.90 C/F 1-260 [» ]
2ZCY X-ray 2.90 D/R 1-260 [» ]
3BDM X-ray 2.70 D/R 1-260 [» ]
3D29 X-ray 2.60 D/R 9-250 [» ]
3DY3 X-ray 2.81 D/R 9-250 [» ]
3DY4 X-ray 2.80 D/R 9-250 [» ]
3E47 X-ray 3.00 D/R 9-250 [» ]
3GPJ X-ray 2.70 D/R 9-250 [» ]
3GPT X-ray 2.41 D/R 9-250 [» ]
3GPW X-ray 2.50 D/R 9-250 [» ]
3HYE X-ray 2.50 D/R 9-250 [» ]
3L5Q X-ray 3.00 J/V 1-250 [» ]
3MG0 X-ray 2.68 D/R 9-250 [» ]
3MG4 X-ray 3.11 D/R 9-250 [» ]
3MG6 X-ray 2.60 D/R 1-250 [» ]
3MG7 X-ray 2.78 D/R 1-250 [» ]
3MG8 X-ray 2.59 D/R 1-250 [» ]
3NZJ X-ray 2.40 D/R 1-260 [» ]
3NZW X-ray 2.50 D/R 1-260 [» ]
3NZX X-ray 2.70 D/R 1-260 [» ]
3OEU X-ray 2.60 D/R 1-260 [» ]
3OEV X-ray 2.85 D/R 1-260 [» ]
3OKJ X-ray 2.70 D/R 9-250 [» ]
3SDI X-ray 2.65 D/R 1-260 [» ]
3SDK X-ray 2.70 D/R 1-260 [» ]
3SHJ X-ray 2.80 D/R 9-250 [» ]
3TDD X-ray 2.70 D/R 9-250 [» ]
3UN4 X-ray 3.40 D/R 1-260 [» ]
3UN8 X-ray 2.70 D/R 1-260 [» ]
4CR2 electron microscopy 7.70 E 1-260 [» ]
4CR3 electron microscopy 9.30 E 1-260 [» ]
4CR4 electron microscopy 8.80 E 1-260 [» ]
4EU2 X-ray 2.51 E/S 9-250 [» ]
4FZC X-ray 2.80 D/R 9-250 [» ]
4FZG X-ray 3.00 D/R 9-250 [» ]
4G4S X-ray 2.49 E 1-260 [» ]
4GK7 X-ray 2.80 D/R 9-250 [» ]
4HNP X-ray 2.80 D/R 9-250 [» ]
4HRC X-ray 2.80 D/R 9-250 [» ]
4HRD X-ray 2.80 D/R 9-250 [» ]
4INR X-ray 2.70 D/R 1-260 [» ]
4INT X-ray 2.90 D/R 1-260 [» ]
4INU X-ray 3.10 D/R 1-260 [» ]
4J70 X-ray 2.80 D/R 1-260 [» ]
4JSQ X-ray 2.80 D/R 1-260 [» ]
4JSU X-ray 2.90 D/R 1-260 [» ]
4JT0 X-ray 3.10 D/R 1-260 [» ]
4LQI X-ray 2.70 D/R 9-250 [» ]
4LTC X-ray 2.50 D/R 1-260 [» ]
4NNN X-ray 2.50 D/R 1-260 [» ]
4NNW X-ray 2.60 D/R 1-260 [» ]
4NO1 X-ray 2.50 D/R 1-260 [» ]
4NO6 X-ray 3.00 D/R 1-260 [» ]
4NO8 X-ray 2.70 D/R 1-260 [» ]
4NO9 X-ray 2.90 D/R 1-260 [» ]
4Q1S X-ray 2.60 D/R 1-260 [» ]
4QBY X-ray 3.00 D/R 1-260 [» ]
4QLQ X-ray 2.40 D/R 1-260 [» ]
4QLS X-ray 2.80 D/R 1-260 [» ]
4QLT X-ray 2.80 D/R 1-260 [» ]
4QLU X-ray 2.80 D/R 1-260 [» ]
4QLV X-ray 2.90 D/R 1-260 [» ]
4R02 X-ray 2.50 D/R 1-260 [» ]
ProteinModelPortali P32379.
SMRi P32379. Positions 9-250.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33504. 58 interactions.
DIPi DIP-1193N.
IntActi P32379. 9 interactions.
MINTi MINT-386734.
STRINGi 4932.YGR253C.

Proteomic databases

MaxQBi P32379.
PaxDbi P32379.
PeptideAtlasi P32379.
PRIDEi P32379.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR253C ; YGR253C ; YGR253C .
GeneIDi 853168.
KEGGi sce:YGR253C.

Organism-specific databases

CYGDi YGR253c.
SGDi S000003485. PUP2.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074958.
HOGENOMi HOG000091085.
InParanoidi P32379.
KOi K02729.
OMAi CAMSGLT.
OrthoDBi EOG7SBP0C.

Enzyme and pathway databases

BioCyci YEAST:G3O-30926-MONOMER.
Reactomei REACT_100522. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_189025. ER-Phagosome pathway.
REACT_189047. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_189060. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_189250. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_83036. Orc1 removal from chromatin.

Miscellaneous databases

EvolutionaryTracei P32379.
NextBioi 973285.
PROi P32379.

Gene expression databases

Genevestigatori P32379.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of an essential yeast gene encoding a proteasomal subunit."
    Georgatsou E., Georgakopoulos T., Thireos G.
    FEBS Lett. 299:39-43(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Biogenesis, structure and function of the yeast 20S proteasome."
    Chen P., Hochstrasser M.
    EMBO J. 14:2620-2630(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-49.
  3. "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII reveals the presence of three new open reading frames and of a tRNAThr gene."
    Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.
    Yeast 13:369-372(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55; SER-56 AND SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structure of 20S proteasome from yeast at 2.4-A resolution."
    Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R.
    Nature 386:463-471(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
  12. "Structural basis for the activation of 20S proteasomes by 11S regulators."
    Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P.
    Nature 408:115-120(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-250 OF COMPLEX WITH THE 20S PROTEASOME.
  14. "Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor."
    Groll M., Koguchi Y., Huber R., Kohno J.
    J. Mol. Biol. 311:543-548(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
  15. "TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome."
    Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.
    Chem. Biol. 13:607-614(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
  16. "Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding."
    Groll M., Huber R., Potts B.C.M.
    J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
  17. "Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome."
    Groll M., Berkers C.R., Ploegh H.L., Ovaa H.
    Structure 14:451-456(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-250 OF COMPLEX WITH THE 20S PROTEASOME.
  18. "Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
    Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
    Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-250 IN COMPLEX WITH THE PROTEASOME.
  19. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSA5_YEAST
AccessioniPrimary (citable) accession number: P32379
Secondary accession number(s): D6VV33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 17100 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3