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Protein

Proteasome subunit beta type-5

Gene

PRE2

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 unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib.
This subunit is necessary for chymotryptic activity and degradation of ubiquitinated proteins.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei76 – 761Nucleophile1 Publication
Binding sitei124 – 1241Bortezomib; via amide nitrogen

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 core complex assembly 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-34243-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

MEROPSiT01.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PRE2
Multicatalytic endopeptidase complex subunit PRE2
Proteasome component PRE2
Proteinase YSCE subunit PRE2
Gene namesi
Name:PRE2
Synonyms:DOA3, PRG1
Ordered Locus Names:YPR103W
ORF Names:P8283.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XVI

Organism-specific databases

CYGDiYPR103w.
EuPathDBiFungiDB:YPR103W.
SGDiS000006307. PRE2.

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi126 – 1261D → N in DOA3-1; decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 7575Removed in mature form1 PublicationPRO_0000026611Add
BLAST
Chaini76 – 287212Proteasome subunit beta type-5PRO_0000026612Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiP30656.
PaxDbiP30656.
PeptideAtlasiP30656.

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
BLM10P435833EBI-14001,EBI-22761

Protein-protein interaction databases

BioGridi36269. 122 interactions.
DIPiDIP-2806N.
IntActiP30656. 20 interactions.
MINTiMINT-489734.

Structurei

Secondary structure

1
287
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi78 – 836Combined sources
Beta strandi86 – 916Combined sources
Beta strandi95 – 973Combined sources
Beta strandi100 – 1045Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi121 – 1233Combined sources
Helixi124 – 14522Combined sources
Helixi151 – 16414Combined sources
Turni165 – 1673Combined sources
Beta strandi172 – 1809Combined sources
Turni181 – 1833Combined sources
Beta strandi184 – 1918Combined sources
Turni192 – 1943Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi200 – 2056Combined sources
Helixi208 – 21811Combined sources
Helixi225 – 24218Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi248 – 2569Combined sources
Beta strandi259 – 2679Combined sources
Helixi268 – 27912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20L/Z76-287[»]
1G0UX-ray2.40K/Y76-287[»]
1G65X-ray2.25K/Y76-287[»]
1JD2X-ray3.00K/R76-287[»]
1RYPX-ray1.90L/Z76-287[»]
1Z7QX-ray3.22L/Z76-287[»]
2F16X-ray2.80K/Y76-287[»]
2FAKX-ray2.80K/Y76-287[»]
2GPLX-ray2.81K/Y76-287[»]
2ZCYX-ray2.90K/Y76-287[»]
3BDMX-ray2.70K/Y76-287[»]
3D29X-ray2.60K/Y76-287[»]
3DY3X-ray2.81K/Y76-287[»]
3DY4X-ray2.80K/Y76-287[»]
3E47X-ray3.00K/Y76-287[»]
3GPJX-ray2.70K/Y76-287[»]
3GPTX-ray2.41K/Y76-287[»]
3GPWX-ray2.50K/Y76-287[»]
3HYEX-ray2.50K/Y76-287[»]
3MG0X-ray2.68K/Y76-287[»]
3MG4X-ray3.11K/Y76-287[»]
3MG6X-ray2.60K/Y76-287[»]
3MG7X-ray2.78K/Y76-287[»]
3MG8X-ray2.59K/Y76-287[»]
3NZJX-ray2.40K/Y1-287[»]
3NZWX-ray2.50K/Y1-287[»]
3NZXX-ray2.70K/Y1-287[»]
3OEUX-ray2.60K/Y76-287[»]
3OEVX-ray2.85K/Y76-287[»]
3OKJX-ray2.70K/Y76-287[»]
3SDIX-ray2.65K/Y76-287[»]
3SDKX-ray2.70K/Y76-287[»]
3SHJX-ray2.80K/Y76-287[»]
3TDDX-ray2.70K/Y76-287[»]
3UN4X-ray3.40K/Y76-287[»]
3UN8X-ray2.70K/Y76-287[»]
3WXRX-ray3.15L/Z1-287[»]
4CR2electron microscopy7.7051-287[»]
4CR3electron microscopy9.3051-287[»]
4CR4electron microscopy8.8051-287[»]
4EU2X-ray2.51L/Z76-287[»]
4FZCX-ray2.80K/Y76-287[»]
4FZGX-ray3.00K/Y76-287[»]
4G4SX-ray2.49L76-287[»]
4GK7X-ray2.80K/Y76-287[»]
4HNPX-ray2.80K/Y76-287[»]
4HRCX-ray2.80K/Y76-287[»]
4HRDX-ray2.80K/Y76-287[»]
4INRX-ray2.70K/Y76-287[»]
4INTX-ray2.90K/Y76-287[»]
4INUX-ray3.10K/Y76-287[»]
4J70X-ray2.80K/Y76-287[»]
4JSQX-ray2.80K/Y76-287[»]
4JSUX-ray2.90K/Y76-287[»]
4JT0X-ray3.10K/Y76-287[»]
4LQIX-ray2.70K/Y76-287[»]
4LTCX-ray2.50K/Y76-287[»]
4NNNX-ray2.50K/Y76-287[»]
4NNWX-ray2.60K/Y76-287[»]
4NO1X-ray2.50K/Y76-287[»]
4NO6X-ray3.00K/Y76-287[»]
4NO8X-ray2.70K/Y76-287[»]
4NO9X-ray2.90K/Y76-287[»]
4Q1SX-ray2.60K/Y76-287[»]
4QBYX-ray3.00K/Y76-287[»]
4QLQX-ray2.40K/Y76-287[»]
4QLSX-ray2.80K/Y76-287[»]
4QLTX-ray2.80K/Y76-287[»]
4QLUX-ray2.80K/Y76-287[»]
4QLVX-ray2.90K/Y76-287[»]
4QUXX-ray3.00K/Y76-287[»]
4QUYX-ray2.80K/Y76-287[»]
4QV0X-ray3.10K/Y76-287[»]
4QV1X-ray2.50K/Y76-287[»]
4QV3X-ray3.00K/Y76-287[»]
4QV4X-ray2.70K/Y76-287[»]
4QV5X-ray2.70K/Y76-287[»]
4QV6X-ray2.80K/Y76-287[»]
4QV7X-ray2.60K/Y76-287[»]
4QV8X-ray2.90K/Y76-287[»]
4QV9X-ray2.60K/Y76-287[»]
4QVLX-ray2.80K/Y76-287[»]
4QVMX-ray2.80K/Y76-287[»]
4QVNX-ray2.90K/Y76-287[»]
4QVPX-ray2.30K/Y76-287[»]
4QVQX-ray2.60K/Y76-287[»]
4QVVX-ray2.80K/Y76-287[»]
4QVWX-ray3.00K/Y76-287[»]
4QVYX-ray2.51K/Y76-287[»]
4QW0X-ray2.90K/Y76-287[»]
4QW1X-ray2.90K/Y76-287[»]
4QW3X-ray2.90K/Y76-287[»]
4QW4X-ray2.80K/Y76-287[»]
4QW5X-ray3.00K/Y76-287[»]
4QW6X-ray2.90K/Y76-287[»]
4QW7X-ray2.70K/Y76-287[»]
4QWFX-ray3.00K/Y76-287[»]
4QWGX-ray2.60K/Y76-287[»]
4QWIX-ray2.60K/Y76-287[»]
4QWJX-ray2.90K/Y76-287[»]
4QWKX-ray2.80K/Y76-287[»]
4QWLX-ray2.60K/Y76-287[»]
4QWRX-ray2.90K/Y76-287[»]
4QWSX-ray3.00K/Y76-287[»]
4QWUX-ray3.00K/Y76-287[»]
4QWXX-ray2.90K/Y76-287[»]
4QXJX-ray2.80K/Y76-287[»]
4QZ0X-ray3.00K/Y76-287[»]
4QZ1X-ray3.00K/Y76-287[»]
4QZ2X-ray2.70K/Y76-287[»]
4QZ3X-ray2.80K/Y76-287[»]
4QZ4X-ray3.00K/Y76-287[»]
4QZ5X-ray2.80K/Y76-287[»]
4QZ6X-ray2.90K/Y76-287[»]
4QZ7X-ray2.80K/Y76-287[»]
4QZWX-ray3.00K/Y76-287[»]
4QZXX-ray2.60K/Y76-287[»]
4QZZX-ray2.90K/Y76-287[»]
4R00X-ray2.80K/Y76-287[»]
4R02X-ray2.50K/Y76-287[»]
4R17X-ray2.10K/Y76-287[»]
4R18X-ray2.40K/Y76-287[»]
4RURX-ray2.50K/Y76-287[»]
4V7OX-ray3.00A2/AP/BL/BZ76-287[»]
4Z1LX-ray3.00K/Y76-287[»]
5AHJX-ray2.80K/Y76-287[»]
ProteinModelPortaliP30656.
SMRiP30656. Positions 49-287.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30656.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
InParanoidiP30656.
KOiK02737.
OMAiTMCAGVT.
OrthoDBiEOG70W3R5.

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.

P30656-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAIADSFSV PNRLVKELQY DNEQNLESDF VTGASQFQRL APSLTVPPIA
60 70 80 90 100
SPQQFLRAHT DDSRNPDCKI KIAHGTTTLA FRFQGGIIVA VDSRATAGNW
110 120 130 140 150
VASQTVKKVI EINPFLLGTM AGGAADCQFW ETWLGSQCRL HELREKERIS
160 170 180 190 200
VAAASKILSN LVYQYKGAGL SMGTMICGYT RKEGPTIYYV DSDGTRLKGD
210 220 230 240 250
IFCVGSGQTF AYGVLDSNYK WDLSVEDALY LGKRSILAAA HRDAYSGGSV
260 270 280
NLYHVTEDGW IYHGNHDVGE LFWKVKEEEG SFNNVIG
Length:287
Mass (Da):31,637
Last modified:February 1, 1995 - v3
Checksum:iD0EBAC611F7A4F37
GO

Sequence cautioni

The sequence CAA82203.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2876FNNVIG → STTLLAK in AAA34906 (PubMed:1452031).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96667 Genomic DNA. Translation: AAA34906.1.
X68662 Genomic DNA. Translation: CAA48628.1.
U32445 Genomic DNA. Translation: AAB68073.1.
Z28348 Genomic DNA. Translation: CAA82203.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11517.1.
PIRiA45411.
RefSeqiNP_015428.1. NM_001184200.1.

Genome annotation databases

EnsemblFungiiYPR103W; YPR103W; YPR103W.
GeneIDi856218.
KEGGisce:YPR103W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96667 Genomic DNA. Translation: AAA34906.1.
X68662 Genomic DNA. Translation: CAA48628.1.
U32445 Genomic DNA. Translation: AAB68073.1.
Z28348 Genomic DNA. Translation: CAA82203.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11517.1.
PIRiA45411.
RefSeqiNP_015428.1. NM_001184200.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20L/Z76-287[»]
1G0UX-ray2.40K/Y76-287[»]
1G65X-ray2.25K/Y76-287[»]
1JD2X-ray3.00K/R76-287[»]
1RYPX-ray1.90L/Z76-287[»]
1Z7QX-ray3.22L/Z76-287[»]
2F16X-ray2.80K/Y76-287[»]
2FAKX-ray2.80K/Y76-287[»]
2GPLX-ray2.81K/Y76-287[»]
2ZCYX-ray2.90K/Y76-287[»]
3BDMX-ray2.70K/Y76-287[»]
3D29X-ray2.60K/Y76-287[»]
3DY3X-ray2.81K/Y76-287[»]
3DY4X-ray2.80K/Y76-287[»]
3E47X-ray3.00K/Y76-287[»]
3GPJX-ray2.70K/Y76-287[»]
3GPTX-ray2.41K/Y76-287[»]
3GPWX-ray2.50K/Y76-287[»]
3HYEX-ray2.50K/Y76-287[»]
3MG0X-ray2.68K/Y76-287[»]
3MG4X-ray3.11K/Y76-287[»]
3MG6X-ray2.60K/Y76-287[»]
3MG7X-ray2.78K/Y76-287[»]
3MG8X-ray2.59K/Y76-287[»]
3NZJX-ray2.40K/Y1-287[»]
3NZWX-ray2.50K/Y1-287[»]
3NZXX-ray2.70K/Y1-287[»]
3OEUX-ray2.60K/Y76-287[»]
3OEVX-ray2.85K/Y76-287[»]
3OKJX-ray2.70K/Y76-287[»]
3SDIX-ray2.65K/Y76-287[»]
3SDKX-ray2.70K/Y76-287[»]
3SHJX-ray2.80K/Y76-287[»]
3TDDX-ray2.70K/Y76-287[»]
3UN4X-ray3.40K/Y76-287[»]
3UN8X-ray2.70K/Y76-287[»]
3WXRX-ray3.15L/Z1-287[»]
4CR2electron microscopy7.7051-287[»]
4CR3electron microscopy9.3051-287[»]
4CR4electron microscopy8.8051-287[»]
4EU2X-ray2.51L/Z76-287[»]
4FZCX-ray2.80K/Y76-287[»]
4FZGX-ray3.00K/Y76-287[»]
4G4SX-ray2.49L76-287[»]
4GK7X-ray2.80K/Y76-287[»]
4HNPX-ray2.80K/Y76-287[»]
4HRCX-ray2.80K/Y76-287[»]
4HRDX-ray2.80K/Y76-287[»]
4INRX-ray2.70K/Y76-287[»]
4INTX-ray2.90K/Y76-287[»]
4INUX-ray3.10K/Y76-287[»]
4J70X-ray2.80K/Y76-287[»]
4JSQX-ray2.80K/Y76-287[»]
4JSUX-ray2.90K/Y76-287[»]
4JT0X-ray3.10K/Y76-287[»]
4LQIX-ray2.70K/Y76-287[»]
4LTCX-ray2.50K/Y76-287[»]
4NNNX-ray2.50K/Y76-287[»]
4NNWX-ray2.60K/Y76-287[»]
4NO1X-ray2.50K/Y76-287[»]
4NO6X-ray3.00K/Y76-287[»]
4NO8X-ray2.70K/Y76-287[»]
4NO9X-ray2.90K/Y76-287[»]
4Q1SX-ray2.60K/Y76-287[»]
4QBYX-ray3.00K/Y76-287[»]
4QLQX-ray2.40K/Y76-287[»]
4QLSX-ray2.80K/Y76-287[»]
4QLTX-ray2.80K/Y76-287[»]
4QLUX-ray2.80K/Y76-287[»]
4QLVX-ray2.90K/Y76-287[»]
4QUXX-ray3.00K/Y76-287[»]
4QUYX-ray2.80K/Y76-287[»]
4QV0X-ray3.10K/Y76-287[»]
4QV1X-ray2.50K/Y76-287[»]
4QV3X-ray3.00K/Y76-287[»]
4QV4X-ray2.70K/Y76-287[»]
4QV5X-ray2.70K/Y76-287[»]
4QV6X-ray2.80K/Y76-287[»]
4QV7X-ray2.60K/Y76-287[»]
4QV8X-ray2.90K/Y76-287[»]
4QV9X-ray2.60K/Y76-287[»]
4QVLX-ray2.80K/Y76-287[»]
4QVMX-ray2.80K/Y76-287[»]
4QVNX-ray2.90K/Y76-287[»]
4QVPX-ray2.30K/Y76-287[»]
4QVQX-ray2.60K/Y76-287[»]
4QVVX-ray2.80K/Y76-287[»]
4QVWX-ray3.00K/Y76-287[»]
4QVYX-ray2.51K/Y76-287[»]
4QW0X-ray2.90K/Y76-287[»]
4QW1X-ray2.90K/Y76-287[»]
4QW3X-ray2.90K/Y76-287[»]
4QW4X-ray2.80K/Y76-287[»]
4QW5X-ray3.00K/Y76-287[»]
4QW6X-ray2.90K/Y76-287[»]
4QW7X-ray2.70K/Y76-287[»]
4QWFX-ray3.00K/Y76-287[»]
4QWGX-ray2.60K/Y76-287[»]
4QWIX-ray2.60K/Y76-287[»]
4QWJX-ray2.90K/Y76-287[»]
4QWKX-ray2.80K/Y76-287[»]
4QWLX-ray2.60K/Y76-287[»]
4QWRX-ray2.90K/Y76-287[»]
4QWSX-ray3.00K/Y76-287[»]
4QWUX-ray3.00K/Y76-287[»]
4QWXX-ray2.90K/Y76-287[»]
4QXJX-ray2.80K/Y76-287[»]
4QZ0X-ray3.00K/Y76-287[»]
4QZ1X-ray3.00K/Y76-287[»]
4QZ2X-ray2.70K/Y76-287[»]
4QZ3X-ray2.80K/Y76-287[»]
4QZ4X-ray3.00K/Y76-287[»]
4QZ5X-ray2.80K/Y76-287[»]
4QZ6X-ray2.90K/Y76-287[»]
4QZ7X-ray2.80K/Y76-287[»]
4QZWX-ray3.00K/Y76-287[»]
4QZXX-ray2.60K/Y76-287[»]
4QZZX-ray2.90K/Y76-287[»]
4R00X-ray2.80K/Y76-287[»]
4R02X-ray2.50K/Y76-287[»]
4R17X-ray2.10K/Y76-287[»]
4R18X-ray2.40K/Y76-287[»]
4RURX-ray2.50K/Y76-287[»]
4V7OX-ray3.00A2/AP/BL/BZ76-287[»]
4Z1LX-ray3.00K/Y76-287[»]
5AHJX-ray2.80K/Y76-287[»]
ProteinModelPortaliP30656.
SMRiP30656. Positions 49-287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36269. 122 interactions.
DIPiDIP-2806N.
IntActiP30656. 20 interactions.
MINTiMINT-489734.

Chemistry

BindingDBiP30656.
ChEMBLiCHEMBL4659.

Protein family/group databases

MEROPSiT01.012.

Proteomic databases

MaxQBiP30656.
PaxDbiP30656.
PeptideAtlasiP30656.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR103W; YPR103W; YPR103W.
GeneIDi856218.
KEGGisce:YPR103W.

Organism-specific databases

CYGDiYPR103w.
EuPathDBiFungiDB:YPR103W.
SGDiS000006307. PRE2.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
InParanoidiP30656.
KOiK02737.
OMAiTMCAGVT.
OrthoDBiEOG70W3R5.

Enzyme and pathway databases

BioCyciYEAST:G3O-34243-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

EvolutionaryTraceiP30656.
NextBioi981441.
PROiP30656.

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. "A homolog of the proteasome-related RING10 gene is essential for yeast cell growth."
    Friedman H., Goebel M., Snyder M.
    Gene 122:203-206(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins."
    Heinemeyer W., Gruhler A., Moehrle V., Mahe Y., Wolf D.H.
    J. Biol. Chem. 268:5115-5120(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 5288C.
  3. "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], PROTEIN SEQUENCE OF 76-90, MUTAGENESIS OF ASP-126.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(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. "Suppression of yeast RNA polymerase III mutations by FHL1, a gene coding for a fork head protein involved in rRNA processing."
    Hermann-Ledenmat S., Werner M., Sentenac A., Thuriaux P.
    Mol. Cell. Biol. 14:2905-2913(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 176-287.
    Strain: ATCC 28383 / FL100 / VTT C-80102.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [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 76-287 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 76-287 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 76-287 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 76-287 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 76-287 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 76-287 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 76-287 IN COMPLEX WITH THE PROTEASOME.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSB5_YEAST
AccessioniPrimary (citable) accession number: P30656
Secondary accession number(s): D6W4A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The side chain of Thr-76 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
Present with 8530 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.