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Protein

Proteasome subunit beta type-3

Gene

PUP3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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. This subunit may participate in the trypsin-like activity of the enzyme complex.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  • endopeptidase activator activity Source: SGD
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  • positive regulation of endopeptidase activity Source: GOC
  • proteasomal ubiquitin-independent protein catabolic process Source: SGD
  • 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-30261-MONOMER.
ReactomeiREACT_291351. Orc1 removal from chromatin.
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_343770. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_344477. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_346191. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_347103. ER-Phagosome pathway.
REACT_354180. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-3 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PUP3
Multicatalytic endopeptidase complex subunit PUP3
Proteasome component PUP3
Gene namesi
Name:PUP3
Ordered Locus Names:YER094C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

CYGDiYER094c.
EuPathDBiFungiDB:YER094C.
SGDiS000000896. PUP3.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: SGD
  • nucleus Source: SGD
  • proteasome core complex, beta-subunit complex Source: SGD
  • proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205Proteasome subunit beta type-3PRO_0000148070Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25451.
PaxDbiP25451.
PeptideAtlasiP25451.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
PUP1P250433EBI-13993,EBI-14009

Protein-protein interaction databases

BioGridi36840. 36 interactions.
DIPiDIP-2039N.
IntActiP25451. 12 interactions.
MINTiMINT-498393.
STRINGi4932.YER094C.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi11 – 166Combined sources
Beta strandi18 – 269Combined sources
Beta strandi29 – 313Combined sources
Beta strandi34 – 385Combined sources
Beta strandi43 – 464Combined sources
Beta strandi49 – 557Combined sources
Helixi57 – 7822Combined sources
Helixi84 – 9613Combined sources
Turni97 – 1004Combined sources
Beta strandi105 – 1128Combined sources
Turni114 – 1163Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi134 – 1407Combined sources
Helixi143 – 15311Combined sources
Helixi160 – 17516Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi185 – 1939Combined sources
Beta strandi195 – 2006Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20J/X1-205[»]
1G0UX-ray2.40I/W1-205[»]
1G65X-ray2.25I/W2-205[»]
1JD2X-ray3.00I/P2-205[»]
1RYPX-ray1.90J/X2-205[»]
1Z7QX-ray3.22J/X1-205[»]
2F16X-ray2.80I/W2-205[»]
2FAKX-ray2.80I/W2-205[»]
2GPLX-ray2.81I/W2-205[»]
2ZCYX-ray2.90I/W1-205[»]
3BDMX-ray2.70I/W1-205[»]
3D29X-ray2.60I/W2-205[»]
3DY3X-ray2.81I/W2-205[»]
3DY4X-ray2.80I/W2-205[»]
3E47X-ray3.00I/W2-205[»]
3GPJX-ray2.70I/W2-205[»]
3GPTX-ray2.41I/W2-205[»]
3GPWX-ray2.50I/W2-205[»]
3HYEX-ray2.50I/W2-205[»]
3MG0X-ray2.68I/W2-205[»]
3MG4X-ray3.11I/W2-205[»]
3MG6X-ray2.60I/W1-205[»]
3MG7X-ray2.78I/W1-205[»]
3MG8X-ray2.59I/W1-205[»]
3NZJX-ray2.40I/W1-205[»]
3NZWX-ray2.50I/W1-205[»]
3NZXX-ray2.70I/W1-205[»]
3OEUX-ray2.60I/W2-205[»]
3OEVX-ray2.85I/W2-205[»]
3OKJX-ray2.70I/W2-205[»]
3SDIX-ray2.65I/W2-205[»]
3SDKX-ray2.70I/W2-205[»]
3SHJX-ray2.80I/W2-205[»]
3TDDX-ray2.70I/W2-205[»]
3UN4X-ray3.40I/W1-205[»]
3UN8X-ray2.70I/W1-205[»]
3WXRX-ray3.15J/X1-205[»]
4CR2electron microscopy7.7031-205[»]
4CR3electron microscopy9.3031-205[»]
4CR4electron microscopy8.8031-205[»]
4EU2X-ray2.51J/X2-205[»]
4FZCX-ray2.80I/W2-205[»]
4FZGX-ray3.00I/W2-205[»]
4G4SX-ray2.49J1-205[»]
4GK7X-ray2.80I/W2-205[»]
4HNPX-ray2.80I/W2-205[»]
4HRCX-ray2.80I/W2-205[»]
4HRDX-ray2.80I/W2-205[»]
4INRX-ray2.70I/W1-205[»]
4INTX-ray2.90I/W1-205[»]
4INUX-ray3.10I/W1-205[»]
4J70X-ray2.80I/W1-205[»]
4JSQX-ray2.80I/W1-205[»]
4JSUX-ray2.90I/W1-205[»]
4JT0X-ray3.10I/W1-205[»]
4LQIX-ray2.70I/W2-205[»]
4LTCX-ray2.50I/W1-205[»]
4NNNX-ray2.50I/W1-205[»]
4NNWX-ray2.60I/W1-205[»]
4NO1X-ray2.50I/W1-205[»]
4NO6X-ray3.00I/W1-205[»]
4NO8X-ray2.70I/W1-205[»]
4NO9X-ray2.90I/W1-205[»]
4Q1SX-ray2.60I/W1-205[»]
4QBYX-ray3.00I/W1-205[»]
4QLQX-ray2.40I/W1-205[»]
4QLSX-ray2.80I/W1-205[»]
4QLTX-ray2.80I/W1-205[»]
4QLUX-ray2.80I/W1-205[»]
4QLVX-ray2.90I/W1-205[»]
4QUXX-ray3.00I/W1-205[»]
4QUYX-ray2.80I/W1-205[»]
4QV0X-ray3.10I/W1-205[»]
4QV1X-ray2.50I/W1-205[»]
4QV3X-ray3.00I/W1-205[»]
4QV4X-ray2.70I/W1-205[»]
4QV5X-ray2.70I/W1-205[»]
4QV6X-ray2.80I/W1-205[»]
4QV7X-ray2.60I/W1-205[»]
4QV8X-ray2.90I/W1-205[»]
4QV9X-ray2.60I/W1-205[»]
4QVLX-ray2.80I/W1-205[»]
4QVMX-ray2.80I/W1-205[»]
4QVNX-ray2.90I/W1-205[»]
4QVPX-ray2.30I/W1-205[»]
4QVQX-ray2.60I/W1-205[»]
4QVVX-ray2.80I/W1-205[»]
4QVWX-ray3.00I/W1-205[»]
4QVYX-ray2.51I/W1-205[»]
4QW0X-ray2.90I/W1-205[»]
4QW1X-ray2.90I/W1-205[»]
4QW3X-ray2.90I/W1-205[»]
4QW4X-ray2.80I/W1-205[»]
4QW5X-ray3.00I/W1-205[»]
4QW6X-ray2.90I/W1-205[»]
4QW7X-ray2.70I/W1-205[»]
4QWFX-ray3.00I/W1-205[»]
4QWGX-ray2.60I/W1-205[»]
4QWIX-ray2.60I/W1-205[»]
4QWJX-ray2.90I/W1-205[»]
4QWKX-ray2.80I/W1-205[»]
4QWLX-ray2.60I/W1-205[»]
4QWRX-ray2.90I/W1-205[»]
4QWSX-ray3.00I/W1-205[»]
4QWUX-ray3.00I/W1-205[»]
4QWXX-ray2.90I/W1-205[»]
4QXJX-ray2.80I/W1-205[»]
4QZ0X-ray3.00I/W1-205[»]
4QZ1X-ray3.00I/W1-205[»]
4QZ2X-ray2.70I/W1-205[»]
4QZ3X-ray2.80I/W1-205[»]
4QZ4X-ray3.00I/W1-205[»]
4QZ5X-ray2.80I/W1-205[»]
4QZ6X-ray2.90I/W1-205[»]
4QZ7X-ray2.80I/W1-205[»]
4QZWX-ray3.00I/W1-205[»]
4QZXX-ray2.60I/W1-205[»]
4QZZX-ray2.90I/W1-205[»]
4R00X-ray2.80I/W1-205[»]
4R02X-ray2.50I/W1-205[»]
4R17X-ray2.10I/W1-205[»]
4R18X-ray2.40I/W1-205[»]
4RURX-ray2.50I/W1-205[»]
4V7OX-ray3.00AN/AZ/BJ/BX2-205[»]
5AHJX-ray2.80I/W1-205[»]
ProteinModelPortaliP25451.
SMRiP25451. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25451.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
InParanoidiP25451.
KOiK02735.
OMAiGCLNFAK.
OrthoDBiEOG7SJDGM.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25451-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDPSSINGG IVVAMTGKDC VAIACDLRLG SQSLGVSNKF EKIFHYGHVF
60 70 80 90 100
LGITGLATDV TTLNEMFRYK TNLYKLKEER AIEPETFTQL VSSSLYERRF
110 120 130 140 150
GPYFVGPVVA GINSKSGKPF IAGFDLIGCI DEAKDFIVSG TASDQLFGMC
160 170 180 190 200
ESLYEPNLEP EDLFETISQA LLNAADRDAL SGWGAVVYII KKDEVVKRYL

KMRQD
Length:205
Mass (Da):22,605
Last modified:May 1, 1992 - v1
Checksum:i5AA92D746454BCB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88470 Genomic DNA. Translation: AAA34946.1.
U18839 Genomic DNA. Translation: AAB64649.1.
BK006939 Genomic DNA. Translation: DAA07756.1.
PIRiS29251.
RefSeqiNP_011020.3. NM_001178985.3.

Genome annotation databases

EnsemblFungiiYER094C; YER094C; YER094C.
GeneIDi856830.
KEGGisce:YER094C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88470 Genomic DNA. Translation: AAA34946.1.
U18839 Genomic DNA. Translation: AAB64649.1.
BK006939 Genomic DNA. Translation: DAA07756.1.
PIRiS29251.
RefSeqiNP_011020.3. NM_001178985.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20J/X1-205[»]
1G0UX-ray2.40I/W1-205[»]
1G65X-ray2.25I/W2-205[»]
1JD2X-ray3.00I/P2-205[»]
1RYPX-ray1.90J/X2-205[»]
1Z7QX-ray3.22J/X1-205[»]
2F16X-ray2.80I/W2-205[»]
2FAKX-ray2.80I/W2-205[»]
2GPLX-ray2.81I/W2-205[»]
2ZCYX-ray2.90I/W1-205[»]
3BDMX-ray2.70I/W1-205[»]
3D29X-ray2.60I/W2-205[»]
3DY3X-ray2.81I/W2-205[»]
3DY4X-ray2.80I/W2-205[»]
3E47X-ray3.00I/W2-205[»]
3GPJX-ray2.70I/W2-205[»]
3GPTX-ray2.41I/W2-205[»]
3GPWX-ray2.50I/W2-205[»]
3HYEX-ray2.50I/W2-205[»]
3MG0X-ray2.68I/W2-205[»]
3MG4X-ray3.11I/W2-205[»]
3MG6X-ray2.60I/W1-205[»]
3MG7X-ray2.78I/W1-205[»]
3MG8X-ray2.59I/W1-205[»]
3NZJX-ray2.40I/W1-205[»]
3NZWX-ray2.50I/W1-205[»]
3NZXX-ray2.70I/W1-205[»]
3OEUX-ray2.60I/W2-205[»]
3OEVX-ray2.85I/W2-205[»]
3OKJX-ray2.70I/W2-205[»]
3SDIX-ray2.65I/W2-205[»]
3SDKX-ray2.70I/W2-205[»]
3SHJX-ray2.80I/W2-205[»]
3TDDX-ray2.70I/W2-205[»]
3UN4X-ray3.40I/W1-205[»]
3UN8X-ray2.70I/W1-205[»]
3WXRX-ray3.15J/X1-205[»]
4CR2electron microscopy7.7031-205[»]
4CR3electron microscopy9.3031-205[»]
4CR4electron microscopy8.8031-205[»]
4EU2X-ray2.51J/X2-205[»]
4FZCX-ray2.80I/W2-205[»]
4FZGX-ray3.00I/W2-205[»]
4G4SX-ray2.49J1-205[»]
4GK7X-ray2.80I/W2-205[»]
4HNPX-ray2.80I/W2-205[»]
4HRCX-ray2.80I/W2-205[»]
4HRDX-ray2.80I/W2-205[»]
4INRX-ray2.70I/W1-205[»]
4INTX-ray2.90I/W1-205[»]
4INUX-ray3.10I/W1-205[»]
4J70X-ray2.80I/W1-205[»]
4JSQX-ray2.80I/W1-205[»]
4JSUX-ray2.90I/W1-205[»]
4JT0X-ray3.10I/W1-205[»]
4LQIX-ray2.70I/W2-205[»]
4LTCX-ray2.50I/W1-205[»]
4NNNX-ray2.50I/W1-205[»]
4NNWX-ray2.60I/W1-205[»]
4NO1X-ray2.50I/W1-205[»]
4NO6X-ray3.00I/W1-205[»]
4NO8X-ray2.70I/W1-205[»]
4NO9X-ray2.90I/W1-205[»]
4Q1SX-ray2.60I/W1-205[»]
4QBYX-ray3.00I/W1-205[»]
4QLQX-ray2.40I/W1-205[»]
4QLSX-ray2.80I/W1-205[»]
4QLTX-ray2.80I/W1-205[»]
4QLUX-ray2.80I/W1-205[»]
4QLVX-ray2.90I/W1-205[»]
4QUXX-ray3.00I/W1-205[»]
4QUYX-ray2.80I/W1-205[»]
4QV0X-ray3.10I/W1-205[»]
4QV1X-ray2.50I/W1-205[»]
4QV3X-ray3.00I/W1-205[»]
4QV4X-ray2.70I/W1-205[»]
4QV5X-ray2.70I/W1-205[»]
4QV6X-ray2.80I/W1-205[»]
4QV7X-ray2.60I/W1-205[»]
4QV8X-ray2.90I/W1-205[»]
4QV9X-ray2.60I/W1-205[»]
4QVLX-ray2.80I/W1-205[»]
4QVMX-ray2.80I/W1-205[»]
4QVNX-ray2.90I/W1-205[»]
4QVPX-ray2.30I/W1-205[»]
4QVQX-ray2.60I/W1-205[»]
4QVVX-ray2.80I/W1-205[»]
4QVWX-ray3.00I/W1-205[»]
4QVYX-ray2.51I/W1-205[»]
4QW0X-ray2.90I/W1-205[»]
4QW1X-ray2.90I/W1-205[»]
4QW3X-ray2.90I/W1-205[»]
4QW4X-ray2.80I/W1-205[»]
4QW5X-ray3.00I/W1-205[»]
4QW6X-ray2.90I/W1-205[»]
4QW7X-ray2.70I/W1-205[»]
4QWFX-ray3.00I/W1-205[»]
4QWGX-ray2.60I/W1-205[»]
4QWIX-ray2.60I/W1-205[»]
4QWJX-ray2.90I/W1-205[»]
4QWKX-ray2.80I/W1-205[»]
4QWLX-ray2.60I/W1-205[»]
4QWRX-ray2.90I/W1-205[»]
4QWSX-ray3.00I/W1-205[»]
4QWUX-ray3.00I/W1-205[»]
4QWXX-ray2.90I/W1-205[»]
4QXJX-ray2.80I/W1-205[»]
4QZ0X-ray3.00I/W1-205[»]
4QZ1X-ray3.00I/W1-205[»]
4QZ2X-ray2.70I/W1-205[»]
4QZ3X-ray2.80I/W1-205[»]
4QZ4X-ray3.00I/W1-205[»]
4QZ5X-ray2.80I/W1-205[»]
4QZ6X-ray2.90I/W1-205[»]
4QZ7X-ray2.80I/W1-205[»]
4QZWX-ray3.00I/W1-205[»]
4QZXX-ray2.60I/W1-205[»]
4QZZX-ray2.90I/W1-205[»]
4R00X-ray2.80I/W1-205[»]
4R02X-ray2.50I/W1-205[»]
4R17X-ray2.10I/W1-205[»]
4R18X-ray2.40I/W1-205[»]
4RURX-ray2.50I/W1-205[»]
4V7OX-ray3.00AN/AZ/BJ/BX2-205[»]
5AHJX-ray2.80I/W1-205[»]
ProteinModelPortaliP25451.
SMRiP25451. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36840. 36 interactions.
DIPiDIP-2039N.
IntActiP25451. 12 interactions.
MINTiMINT-498393.
STRINGi4932.YER094C.

Proteomic databases

MaxQBiP25451.
PaxDbiP25451.
PeptideAtlasiP25451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER094C; YER094C; YER094C.
GeneIDi856830.
KEGGisce:YER094C.

Organism-specific databases

CYGDiYER094c.
EuPathDBiFungiDB:YER094C.
SGDiS000000896. PUP3.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
InParanoidiP25451.
KOiK02735.
OMAiGCLNFAK.
OrthoDBiEOG7SJDGM.

Enzyme and pathway databases

BioCyciYEAST:G3O-30261-MONOMER.
ReactomeiREACT_291351. Orc1 removal from chromatin.
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_343770. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_344477. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_346191. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_347103. ER-Phagosome pathway.
REACT_354180. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Miscellaneous databases

EvolutionaryTraceiP25451.
NextBioi983127.
PROiP25451.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
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Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and transcriptional regulation of the yeast recombinational repair gene RAD51."
    Basile G.M., Aker M., Mortimer R.K.
    Mol. Cell. Biol. 12:3235-3246(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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 COMPLEX WITH THE 20S PROTEASOME.
  7. "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) OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
  9. "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 COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
  10. "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 COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
  11. "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 COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
  12. "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 2-205 IN COMPLEX WITH THE PROTEASOME.
  13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSB3_YEAST
AccessioniPrimary (citable) accession number: P25451
Secondary accession number(s): D3DM02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.