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Protein

Proteasome subunit beta type-1

Gene

PRE3

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. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.
This subunit is necessary for the peptidylglutamyl-peptide hydrolyzing activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei20 – 201Nucleophile1 Publication

GO - Molecular functioni

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

GO - Biological processi

  • 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-31481-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.

Protein family/group databases

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PRE3
Multicatalytic endopeptidase complex subunit PRE3
Proteasome component PRE3
Proteinase YSCE subunit PRE3
Gene namesi
Name:PRE3
Ordered Locus Names:YJL001W
ORF Names:J1407
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome X

Organism-specific databases

CYGDiYJL001w.
EuPathDBiFungiDB:YJL001W.
SGDiS000003538. PRE3.

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
Propeptidei1 – 1919Removed in mature formPRO_0000026643Add
BLAST
Chaini20 – 215196Proteasome subunit beta type-1PRO_0000026644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

MaxQBiP38624.
PaxDbiP38624.
PeptideAtlasiP38624.

2D gel databases

UCD-2DPAGEP38624.

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

BioGridi33756. 77 interactions.
DIPiDIP-1527N.
IntActiP38624. 21 interactions.
MINTiMINT-401012.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 276Combined sources
Beta strandi30 – 356Combined sources
Beta strandi39 – 413Combined sources
Beta strandi44 – 496Combined sources
Beta strandi53 – 575Combined sources
Beta strandi60 – 678Combined sources
Helixi68 – 8922Combined sources
Helixi94 – 10714Combined sources
Turni108 – 1114Combined sources
Beta strandi114 – 1229Combined sources
Turni123 – 1253Combined sources
Beta strandi126 – 1327Combined sources
Turni134 – 1363Combined sources
Beta strandi139 – 1479Combined sources
Helixi148 – 1536Combined sources
Helixi154 – 1607Combined sources
Helixi167 – 18418Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi192 – 1987Combined sources
Beta strandi201 – 2077Combined sources
Helixi209 – 2124Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20H/V20-215[»]
1G0UX-ray2.402/N20-215[»]
1G65X-ray2.252/N20-215[»]
1JD2X-ray3.00N/U20-215[»]
1RYPX-ray1.90H/V11-215[»]
1Z7QX-ray3.22H/V20-215[»]
2F16X-ray2.802/N20-215[»]
2FAKX-ray2.802/N20-205[»]
2GPLX-ray2.812/N20-215[»]
2ZCYX-ray2.901/N20-215[»]
3BDMX-ray2.701/N20-215[»]
3D29X-ray2.602/N20-215[»]
3DY3X-ray2.812/N20-215[»]
3DY4X-ray2.802/N20-215[»]
3E47X-ray3.002/N20-215[»]
3GPJX-ray2.702/N20-215[»]
3GPTX-ray2.412/N20-215[»]
3GPWX-ray2.502/N20-215[»]
3HYEX-ray2.502/N20-215[»]
3MG0X-ray2.682/N20-215[»]
3MG4X-ray3.112/N20-215[»]
3MG6X-ray2.602/N20-215[»]
3MG7X-ray2.782/N20-215[»]
3MG8X-ray2.592/N20-215[»]
3NZJX-ray2.402/N1-215[»]
3NZWX-ray2.502/N1-215[»]
3NZXX-ray2.702/N1-215[»]
3OEUX-ray2.602/N20-215[»]
3OEVX-ray2.852/N20-215[»]
3OKJX-ray2.702/N20-215[»]
3SDIX-ray2.652/N20-215[»]
3SDKX-ray2.702/N20-215[»]
3SHJX-ray2.802/N20-215[»]
3TDDX-ray2.702/N20-215[»]
3UN4X-ray3.40N/b20-215[»]
3UN8X-ray2.70N/b20-215[»]
3WXRX-ray3.15H/V1-215[»]
4CR2electron microscopy7.7011-215[»]
4CR3electron microscopy9.3011-215[»]
4CR4electron microscopy8.8011-215[»]
4EU2X-ray2.51H/V20-215[»]
4FZCX-ray2.80N/b20-215[»]
4FZGX-ray3.00N/b20-215[»]
4G4SX-ray2.49H20-215[»]
4GK7X-ray2.80N/b20-215[»]
4HNPX-ray2.80N/b20-215[»]
4HRCX-ray2.80N/b20-215[»]
4HRDX-ray2.80N/b20-215[»]
4INRX-ray2.70N/b20-215[»]
4INTX-ray2.90N/b20-215[»]
4INUX-ray3.10N/b20-215[»]
4J70X-ray2.80N/b20-215[»]
4JSQX-ray2.80N/b20-215[»]
4JSUX-ray2.90N/b20-215[»]
4JT0X-ray3.10N/b20-215[»]
4LQIX-ray2.70N/b20-215[»]
4LTCX-ray2.50N/b20-215[»]
4NNNX-ray2.50N/b20-215[»]
4NNWX-ray2.60N/b20-215[»]
4NO1X-ray2.50N/b20-215[»]
4NO6X-ray3.00N/b20-215[»]
4NO8X-ray2.70N/b20-215[»]
4NO9X-ray2.90N/b20-215[»]
4Q1SX-ray2.60N/b20-215[»]
4QBYX-ray3.00N/b20-215[»]
4QLQX-ray2.40N/b20-215[»]
4QLSX-ray2.80N/b20-215[»]
4QLTX-ray2.80N/b20-215[»]
4QLUX-ray2.80N/b20-215[»]
4QLVX-ray2.90N/b20-215[»]
4QUXX-ray3.00N/b20-215[»]
4QUYX-ray2.80N/b20-215[»]
4QV0X-ray3.10N/b20-215[»]
4QV1X-ray2.50N/b20-215[»]
4QV3X-ray3.00N/b20-215[»]
4QV4X-ray2.70N/b20-215[»]
4QV5X-ray2.70N/b20-215[»]
4QV6X-ray2.80N/b20-215[»]
4QV7X-ray2.60N/b20-215[»]
4QV8X-ray2.90N/b20-215[»]
4QV9X-ray2.60N/b20-215[»]
4QVLX-ray2.80N/b20-215[»]
4QVMX-ray2.80N/b20-215[»]
4QVNX-ray2.90N/b20-215[»]
4QVPX-ray2.30N/b20-215[»]
4QVQX-ray2.60N/b20-215[»]
4QVVX-ray2.80N/b20-215[»]
4QVWX-ray3.00N/b20-215[»]
4QVYX-ray2.51N/b20-215[»]
4QW0X-ray2.90N/b20-215[»]
4QW1X-ray2.90N/b20-215[»]
4QW3X-ray2.90N/b20-215[»]
4QW4X-ray2.80N/b20-215[»]
4QW5X-ray3.00N/b20-215[»]
4QW6X-ray2.90N/b20-215[»]
4QW7X-ray2.70N/b20-215[»]
4QWFX-ray3.00N/b20-215[»]
4QWGX-ray2.60N/b20-215[»]
4QWIX-ray2.60N/b20-215[»]
4QWJX-ray2.90N/b20-215[»]
4QWKX-ray2.80N/b20-215[»]
4QWLX-ray2.60N/b20-215[»]
4QWRX-ray2.90N/b20-215[»]
4QWSX-ray3.00N/b20-215[»]
4QWUX-ray3.00N/b20-215[»]
4QWXX-ray2.90N/b20-215[»]
4QXJX-ray2.80N/b20-215[»]
4QZ0X-ray3.00N/b20-215[»]
4QZ1X-ray3.00N/b20-215[»]
4QZ2X-ray2.70N/b20-215[»]
4QZ3X-ray2.80N/b20-215[»]
4QZ4X-ray3.00N/b20-215[»]
4QZ5X-ray2.80N/b20-215[»]
4QZ6X-ray2.90N/b20-215[»]
4QZ7X-ray2.80N/b20-215[»]
4QZWX-ray3.00N/b20-215[»]
4QZXX-ray2.60N/b20-215[»]
4QZZX-ray2.90N/b20-215[»]
4R00X-ray2.80N/b20-215[»]
4R02X-ray2.50N/b20-215[»]
4R17X-ray2.10N/b20-215[»]
4R18X-ray2.40N/b20-215[»]
4RURX-ray2.50N/b20-215[»]
4V7OX-ray3.00AB/AD/BH/BV21-215[»]
4Z1LX-ray3.00N/b20-215[»]
5AHJX-ray2.80N/b20-215[»]
ProteinModelPortaliP38624.
SMRiP38624. Positions 20-215.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38624.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
InParanoidiP38624.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG7XDBSV.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38624-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGIQVDINR LKKGEVSLGT SIMAVTFKDG VILGADSRTT TGAYIANRVT
60 70 80 90 100
DKLTRVHDKI WCCRSGSAAD TQAIADIVQY HLELYTSQYG TPSTETAASV
110 120 130 140 150
FKELCYENKD NLTAGIIVAG YDDKNKGEVY TIPLGGSVHK LPYAIAGSGS
160 170 180 190 200
TFIYGYCDKN FRENMSKEET VDFIKHSLSQ AIKWDGSSGG VIRMVVLTAA
210
GVERLIFYPD EYEQL
Length:215
Mass (Da):23,548
Last modified:November 1, 1995 - v2
Checksum:iBD1FCE649678D86B
GO

Sequence cautioni

The sequence CAA55591.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA60921.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78991 Genomic DNA. Translation: CAA55591.1. Different initiation.
Z49276 Genomic DNA. Translation: CAA89290.1.
Z49277 Genomic DNA. Translation: CAA89292.1.
X87611 Genomic DNA. Translation: CAA60921.1. Different initiation.
X86020 mRNA. Translation: CAA60015.1.
S78566 mRNA. Translation: AAB34629.1.
BK006943 Genomic DNA. Translation: DAA08790.1.
PIRiS61337.
RefSeqiNP_012533.1. NM_001181435.1.

Genome annotation databases

EnsemblFungiiYJL001W; YJL001W; YJL001W.
GeneIDi853456.
KEGGisce:YJL001W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78991 Genomic DNA. Translation: CAA55591.1. Different initiation.
Z49276 Genomic DNA. Translation: CAA89290.1.
Z49277 Genomic DNA. Translation: CAA89292.1.
X87611 Genomic DNA. Translation: CAA60921.1. Different initiation.
X86020 mRNA. Translation: CAA60015.1.
S78566 mRNA. Translation: AAB34629.1.
BK006943 Genomic DNA. Translation: DAA08790.1.
PIRiS61337.
RefSeqiNP_012533.1. NM_001181435.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20H/V20-215[»]
1G0UX-ray2.402/N20-215[»]
1G65X-ray2.252/N20-215[»]
1JD2X-ray3.00N/U20-215[»]
1RYPX-ray1.90H/V11-215[»]
1Z7QX-ray3.22H/V20-215[»]
2F16X-ray2.802/N20-215[»]
2FAKX-ray2.802/N20-205[»]
2GPLX-ray2.812/N20-215[»]
2ZCYX-ray2.901/N20-215[»]
3BDMX-ray2.701/N20-215[»]
3D29X-ray2.602/N20-215[»]
3DY3X-ray2.812/N20-215[»]
3DY4X-ray2.802/N20-215[»]
3E47X-ray3.002/N20-215[»]
3GPJX-ray2.702/N20-215[»]
3GPTX-ray2.412/N20-215[»]
3GPWX-ray2.502/N20-215[»]
3HYEX-ray2.502/N20-215[»]
3MG0X-ray2.682/N20-215[»]
3MG4X-ray3.112/N20-215[»]
3MG6X-ray2.602/N20-215[»]
3MG7X-ray2.782/N20-215[»]
3MG8X-ray2.592/N20-215[»]
3NZJX-ray2.402/N1-215[»]
3NZWX-ray2.502/N1-215[»]
3NZXX-ray2.702/N1-215[»]
3OEUX-ray2.602/N20-215[»]
3OEVX-ray2.852/N20-215[»]
3OKJX-ray2.702/N20-215[»]
3SDIX-ray2.652/N20-215[»]
3SDKX-ray2.702/N20-215[»]
3SHJX-ray2.802/N20-215[»]
3TDDX-ray2.702/N20-215[»]
3UN4X-ray3.40N/b20-215[»]
3UN8X-ray2.70N/b20-215[»]
3WXRX-ray3.15H/V1-215[»]
4CR2electron microscopy7.7011-215[»]
4CR3electron microscopy9.3011-215[»]
4CR4electron microscopy8.8011-215[»]
4EU2X-ray2.51H/V20-215[»]
4FZCX-ray2.80N/b20-215[»]
4FZGX-ray3.00N/b20-215[»]
4G4SX-ray2.49H20-215[»]
4GK7X-ray2.80N/b20-215[»]
4HNPX-ray2.80N/b20-215[»]
4HRCX-ray2.80N/b20-215[»]
4HRDX-ray2.80N/b20-215[»]
4INRX-ray2.70N/b20-215[»]
4INTX-ray2.90N/b20-215[»]
4INUX-ray3.10N/b20-215[»]
4J70X-ray2.80N/b20-215[»]
4JSQX-ray2.80N/b20-215[»]
4JSUX-ray2.90N/b20-215[»]
4JT0X-ray3.10N/b20-215[»]
4LQIX-ray2.70N/b20-215[»]
4LTCX-ray2.50N/b20-215[»]
4NNNX-ray2.50N/b20-215[»]
4NNWX-ray2.60N/b20-215[»]
4NO1X-ray2.50N/b20-215[»]
4NO6X-ray3.00N/b20-215[»]
4NO8X-ray2.70N/b20-215[»]
4NO9X-ray2.90N/b20-215[»]
4Q1SX-ray2.60N/b20-215[»]
4QBYX-ray3.00N/b20-215[»]
4QLQX-ray2.40N/b20-215[»]
4QLSX-ray2.80N/b20-215[»]
4QLTX-ray2.80N/b20-215[»]
4QLUX-ray2.80N/b20-215[»]
4QLVX-ray2.90N/b20-215[»]
4QUXX-ray3.00N/b20-215[»]
4QUYX-ray2.80N/b20-215[»]
4QV0X-ray3.10N/b20-215[»]
4QV1X-ray2.50N/b20-215[»]
4QV3X-ray3.00N/b20-215[»]
4QV4X-ray2.70N/b20-215[»]
4QV5X-ray2.70N/b20-215[»]
4QV6X-ray2.80N/b20-215[»]
4QV7X-ray2.60N/b20-215[»]
4QV8X-ray2.90N/b20-215[»]
4QV9X-ray2.60N/b20-215[»]
4QVLX-ray2.80N/b20-215[»]
4QVMX-ray2.80N/b20-215[»]
4QVNX-ray2.90N/b20-215[»]
4QVPX-ray2.30N/b20-215[»]
4QVQX-ray2.60N/b20-215[»]
4QVVX-ray2.80N/b20-215[»]
4QVWX-ray3.00N/b20-215[»]
4QVYX-ray2.51N/b20-215[»]
4QW0X-ray2.90N/b20-215[»]
4QW1X-ray2.90N/b20-215[»]
4QW3X-ray2.90N/b20-215[»]
4QW4X-ray2.80N/b20-215[»]
4QW5X-ray3.00N/b20-215[»]
4QW6X-ray2.90N/b20-215[»]
4QW7X-ray2.70N/b20-215[»]
4QWFX-ray3.00N/b20-215[»]
4QWGX-ray2.60N/b20-215[»]
4QWIX-ray2.60N/b20-215[»]
4QWJX-ray2.90N/b20-215[»]
4QWKX-ray2.80N/b20-215[»]
4QWLX-ray2.60N/b20-215[»]
4QWRX-ray2.90N/b20-215[»]
4QWSX-ray3.00N/b20-215[»]
4QWUX-ray3.00N/b20-215[»]
4QWXX-ray2.90N/b20-215[»]
4QXJX-ray2.80N/b20-215[»]
4QZ0X-ray3.00N/b20-215[»]
4QZ1X-ray3.00N/b20-215[»]
4QZ2X-ray2.70N/b20-215[»]
4QZ3X-ray2.80N/b20-215[»]
4QZ4X-ray3.00N/b20-215[»]
4QZ5X-ray2.80N/b20-215[»]
4QZ6X-ray2.90N/b20-215[»]
4QZ7X-ray2.80N/b20-215[»]
4QZWX-ray3.00N/b20-215[»]
4QZXX-ray2.60N/b20-215[»]
4QZZX-ray2.90N/b20-215[»]
4R00X-ray2.80N/b20-215[»]
4R02X-ray2.50N/b20-215[»]
4R17X-ray2.10N/b20-215[»]
4R18X-ray2.40N/b20-215[»]
4RURX-ray2.50N/b20-215[»]
4V7OX-ray3.00AB/AD/BH/BV21-215[»]
4Z1LX-ray3.00N/b20-215[»]
5AHJX-ray2.80N/b20-215[»]
ProteinModelPortaliP38624.
SMRiP38624. Positions 20-215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33756. 77 interactions.
DIPiDIP-1527N.
IntActiP38624. 21 interactions.
MINTiMINT-401012.

Protein family/group databases

MEROPSiT01.010.

2D gel databases

UCD-2DPAGEP38624.

Proteomic databases

MaxQBiP38624.
PaxDbiP38624.
PeptideAtlasiP38624.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL001W; YJL001W; YJL001W.
GeneIDi853456.
KEGGisce:YJL001W.

Organism-specific databases

CYGDiYJL001w.
EuPathDBiFungiDB:YJL001W.
SGDiS000003538. PRE3.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
InParanoidiP38624.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG7XDBSV.

Enzyme and pathway databases

BioCyciYEAST:G3O-31481-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

EvolutionaryTraceiP38624.
NextBioi974026.
PROiP38624.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PRE3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity."
    Enenkel C., Lehmann H., Kipper J., Gueckel R., Hilt W., Wolf D.H.
    FEBS Lett. 341:193-196(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  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: SEQUENCE REVISION TO N-TERMINUS.
  3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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 11-215 OF COMPLEX WITH THE 20S PROTEASOME, PROTEOLYTIC PROCESSING, ACTIVE SITE.
  9. "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 20-215 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-215 OF COMPLEX WITH THE 20S PROTEASOME.
  11. "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 20-215 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
  12. "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 20-215 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
  13. "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 20-215 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
  14. "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 21-215 IN COMPLEX WITH THE PROTEASOME.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSB1_YEAST
AccessioniPrimary (citable) accession number: P38624
Secondary accession number(s): D6VWH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The side chain of Thr-20 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
Present with 7250 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.