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Protein

Proteasome subunit beta type-2

Gene

PUP1

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.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei30Nucleophile1 Publication1

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-33674-MONOMER.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-382556. ABC-family proteins mediated transport.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-5668541. TNFR2 non-canonical NF-kB pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-5689880. Ub-specific processing proteases.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SCE-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-2 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PUP1
Multicatalytic endopeptidase complex subunit PUP1
Proteasome component PUP1
Proteinase YSCE subunit PUP1
Gene namesi
Name:PUP1
Ordered Locus Names:YOR157C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR157C.
SGDiS000005683. PUP1.

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)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000266571 – 29Removed in mature formAdd BLAST29
ChainiPRO_000002665830 – 261Proteasome subunit beta type-2Add BLAST232

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiP25043.
PRIDEiP25043.

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
PUP3P254513EBI-14009,EBI-13993

Protein-protein interaction databases

BioGridi34553. 57 interactors.
DIPiDIP-2818N.
IntActiP25043. 9 interactors.
MINTiMINT-498378.

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 25Combined sources3
Beta strandi32 – 37Combined sources6
Beta strandi40 – 45Combined sources6
Beta strandi49 – 51Combined sources3
Beta strandi54 – 59Combined sources6
Beta strandi63 – 67Combined sources5
Beta strandi70 – 76Combined sources7
Helixi78 – 99Combined sources22
Helixi105 – 118Combined sources14
Turni119 – 121Combined sources3
Beta strandi125 – 133Combined sources9
Beta strandi136 – 142Combined sources7
Turni144 – 146Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi152 – 157Combined sources6
Helixi160 – 170Combined sources11
Helixi177 – 194Combined sources18
Beta strandi202 – 208Combined sources7
Beta strandi213 – 220Combined sources8
Beta strandi241 – 246Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20I/W30-261[»]
1G0UX-ray2.40H/V30-251[»]
1G65X-ray2.25H/V30-251[»]
1JD2X-ray3.00H/O30-251[»]
1RYPX-ray1.90I/W30-251[»]
1Z7QX-ray3.22I/W30-251[»]
2F16X-ray2.80H/V30-251[»]
2FAKX-ray2.80H/V30-251[»]
2GPLX-ray2.81H/V30-251[»]
2ZCYX-ray2.90H/V30-261[»]
3BDMX-ray2.70H/V30-261[»]
3D29X-ray2.60H/V30-251[»]
3DY3X-ray2.81H/V30-251[»]
3DY4X-ray2.80H/V30-251[»]
3E47X-ray3.00H/V30-251[»]
3GPJX-ray2.70H/V30-251[»]
3GPTX-ray2.41H/V30-251[»]
3GPWX-ray2.50H/V30-251[»]
3HYEX-ray2.50H/V30-251[»]
3JCOelectron microscopy4.804/i1-261[»]
3JCPelectron microscopy4.604/i1-261[»]
3MG0X-ray2.68H/V30-251[»]
3MG4X-ray3.11H/V30-251[»]
3MG6X-ray2.60H/V30-251[»]
3MG7X-ray2.78H/V30-251[»]
3MG8X-ray2.59H/V30-251[»]
3NZJX-ray2.40H/V1-261[»]
3NZWX-ray2.50H/V1-261[»]
3NZXX-ray2.70H/V1-261[»]
3OEUX-ray2.60H/V30-251[»]
3OEVX-ray2.85H/V30-251[»]
3OKJX-ray2.70H/V30-251[»]
3SDIX-ray2.65H/V30-251[»]
3SDKX-ray2.70H/V30-251[»]
3SHJX-ray2.80H/V30-251[»]
3TDDX-ray2.70H/V30-251[»]
3UN4X-ray3.40H/V30-261[»]
3UN8X-ray2.70H/V30-261[»]
3WXRX-ray3.15I/W1-261[»]
4CR2electron microscopy7.7021-261[»]
4CR3electron microscopy9.3021-261[»]
4CR4electron microscopy8.8021-261[»]
4EU2X-ray2.51I/W30-251[»]
4FZCX-ray2.80H/V30-251[»]
4FZGX-ray3.00H/V30-251[»]
4G4SX-ray2.49I30-261[»]
4GK7X-ray2.80H/V30-251[»]
4HNPX-ray2.80H/V30-251[»]
4HRCX-ray2.80H/V30-251[»]
4HRDX-ray2.80H/V30-251[»]
4INRX-ray2.70H/V30-261[»]
4INTX-ray2.90H/V30-261[»]
4INUX-ray3.10H/V30-261[»]
4J70X-ray2.80H/V30-261[»]
4JSQX-ray2.80H/V30-261[»]
4JSUX-ray2.90H/V30-261[»]
4JT0X-ray3.10H/V30-261[»]
4LQIX-ray2.70H/V30-251[»]
4LTCX-ray2.50H/V30-261[»]
4NNNX-ray2.50H/V30-261[»]
4NNWX-ray2.60H/V30-261[»]
4NO1X-ray2.50H/V30-261[»]
4NO6X-ray3.00H/V30-261[»]
4NO8X-ray2.70H/V30-261[»]
4NO9X-ray2.90H/V30-261[»]
4Q1SX-ray2.60H/V30-261[»]
4QBYX-ray3.00H/V30-261[»]
4QLQX-ray2.40H/V30-261[»]
4QLSX-ray2.80H/V30-261[»]
4QLTX-ray2.80H/V30-261[»]
4QLUX-ray2.80H/V30-261[»]
4QLVX-ray2.90H/V30-261[»]
4QUXX-ray3.00H/V30-261[»]
4QUYX-ray2.80H/V30-261[»]
4QV0X-ray3.10H/V30-261[»]
4QV1X-ray2.50H/V30-261[»]
4QV3X-ray3.00H/V30-261[»]
4QV4X-ray2.70H/V30-261[»]
4QV5X-ray2.70H/V30-261[»]
4QV6X-ray2.80H/V30-261[»]
4QV7X-ray2.60H/V30-261[»]
4QV8X-ray2.90H/V30-261[»]
4QV9X-ray2.60H/V30-261[»]
4QVLX-ray2.80H/V30-261[»]
4QVMX-ray2.80H/V30-261[»]
4QVNX-ray2.90H/V30-261[»]
4QVPX-ray2.30H/V30-261[»]
4QVQX-ray2.60H/V30-261[»]
4QVVX-ray2.80H/V30-261[»]
4QVWX-ray3.00H/V30-261[»]
4QVYX-ray2.51H/V30-261[»]
4QW0X-ray2.90H/V30-261[»]
4QW1X-ray2.90H/V30-261[»]
4QW3X-ray2.90H/V30-261[»]
4QW4X-ray2.80H/V30-261[»]
4QW5X-ray3.00H/V30-261[»]
4QW6X-ray2.90H/V30-261[»]
4QW7X-ray2.70H/V30-261[»]
4QWFX-ray3.00H/V30-261[»]
4QWGX-ray2.60H/V30-261[»]
4QWIX-ray2.60H/V30-261[»]
4QWJX-ray2.90H/V30-261[»]
4QWKX-ray2.80H/V30-261[»]
4QWLX-ray2.60H/V30-261[»]
4QWRX-ray2.90H/V30-261[»]
4QWSX-ray3.00H/V30-261[»]
4QWUX-ray3.00H/V30-261[»]
4QWXX-ray2.90H/V30-261[»]
4QXJX-ray2.80H/V30-261[»]
4QZ0X-ray3.00H/V30-261[»]
4QZ1X-ray3.00H/V30-261[»]
4QZ2X-ray2.70H/V30-261[»]
4QZ3X-ray2.80H/V30-261[»]
4QZ4X-ray3.00H/V30-261[»]
4QZ5X-ray2.80H/V30-261[»]
4QZ6X-ray2.90H/V30-261[»]
4QZ7X-ray2.80H/V30-261[»]
4QZWX-ray3.00H/V30-261[»]
4QZXX-ray2.60H/V30-261[»]
4QZZX-ray2.90H/V30-261[»]
4R00X-ray2.80H/V30-261[»]
4R02X-ray2.50H/V30-261[»]
4R17X-ray2.10H/V30-261[»]
4R18X-ray2.40H/V30-261[»]
4RURX-ray2.50H/V30-261[»]
4V7OX-ray3.00AM/AY/BI/BW30-251[»]
4X6ZX-ray2.70I/W1-261[»]
4Y69X-ray2.90H/V30-261[»]
4Y6AX-ray2.60H/V30-261[»]
4Y6VX-ray2.80H/V30-261[»]
4Y6ZX-ray2.70H/V30-261[»]
4Y70X-ray2.40H/V30-261[»]
4Y74X-ray2.70H/V30-261[»]
4Y75X-ray2.80H/V30-261[»]
4Y77X-ray2.50H/V30-261[»]
4Y78X-ray2.80H/V30-261[»]
4Y7WX-ray2.50H/V30-261[»]
4Y7XX-ray2.60H/V30-261[»]
4Y7YX-ray2.40H/V30-261[»]
4Y80X-ray2.50H/V30-261[»]
4Y81X-ray2.80H/V30-261[»]
4Y82X-ray2.80H/V30-261[»]
4Y84X-ray2.70H/V30-261[»]
4Y8GX-ray2.60H/V30-261[»]
4Y8HX-ray2.50H/V30-261[»]
4Y8IX-ray2.60H/V30-261[»]
4Y8JX-ray2.70H/V30-261[»]
4Y8KX-ray2.60H/V30-261[»]
4Y8LX-ray2.40H/V30-261[»]
4Y8MX-ray2.80H/V30-261[»]
4Y8NX-ray2.60H/V30-261[»]
4Y8OX-ray2.70H/V30-261[»]
4Y8PX-ray2.80H/V30-261[»]
4Y8QX-ray2.60H/V30-261[»]
4Y8RX-ray2.70H/V30-261[»]
4Y8SX-ray2.70H/V30-261[»]
4Y8TX-ray2.70H/V30-261[»]
4Y8UX-ray2.90H/V30-261[»]
4Y9YX-ray2.80H/V30-261[»]
4Y9ZX-ray2.80H/V30-261[»]
4YA0X-ray2.80H/V30-261[»]
4YA1X-ray2.90H/V30-261[»]
4YA2X-ray2.70H/V30-261[»]
4YA3X-ray2.70H/V30-261[»]
4YA4X-ray2.90H/V30-261[»]
4YA5X-ray2.50H/V30-261[»]
4YA7X-ray2.70H/V30-261[»]
4YA9X-ray2.70H/V30-261[»]
4Z1LX-ray3.00H/V30-261[»]
4ZZGX-ray3.00I/W1-261[»]
5A5Belectron microscopy9.5021-261[»]
5AHJX-ray2.80H/V30-261[»]
5BOUX-ray2.60H/V30-261[»]
5BXLX-ray2.80H/V30-261[»]
5BXNX-ray2.80H/V30-261[»]
5CGFX-ray2.80H/V30-261[»]
5CGGX-ray2.90H/V30-261[»]
5CGHX-ray2.50H/V30-261[»]
5CGIX-ray2.80H/V30-261[»]
5CZ4X-ray2.30H/V30-261[»]
5CZ5X-ray2.80H/V30-261[»]
5CZ6X-ray2.70H/V30-261[»]
5CZ7X-ray2.50H/V30-261[»]
5CZ8X-ray2.80H/V30-261[»]
5CZ9X-ray2.90H/V30-261[»]
5CZAX-ray2.50H/V30-261[»]
5D0SX-ray2.50H/V30-261[»]
5D0TX-ray2.60H/V30-261[»]
5D0VX-ray2.90H/V30-261[»]
5D0WX-ray2.80H/V30-261[»]
5D0XX-ray2.60H/V30-261[»]
5D0ZX-ray2.90H/V30-261[»]
5DKIX-ray2.80H/V30-261[»]
5DKJX-ray2.80H/V30-261[»]
5FG7X-ray2.70H/V24-261[»]
5FG9X-ray2.60H/V26-261[»]
5FGAX-ray2.70H/V30-261[»]
5FGDX-ray2.80H/V30-261[»]
5FGEX-ray2.60H/V30-261[»]
5FGFX-ray2.60H/V30-261[»]
5FGGX-ray2.70H/V30-261[»]
5FGHX-ray2.80H/V30-261[»]
5FGIX-ray2.90H/V18-261[»]
5FHSX-ray2.70H/V30-261[»]
5JHRX-ray2.90H/V30-261[»]
5JHSX-ray3.00H/V30-261[»]
ProteinModelPortaliP25043.
SMRiP25043.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25043.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
InParanoidiP25043.
KOiK02739.
OMAiAPQIWCA.
OrthoDBiEOG092C44RU.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. 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.

P25043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLSFDNYQ RNNFLAENSH TQPKATSTGT TIVGVKFNNG VVIAADTRST
60 70 80 90 100
QGPIVADKNC AKLHRISPKI WCAGAGTAAD TEAVTQLIGS NIELHSLYTS
110 120 130 140 150
REPRVVSALQ MLKQHLFKYQ GHIGAYLIVA GVDPTGSHLF SIHAHGSTDV
160 170 180 190 200
GYYLSLGSGS LAAMAVLESH WKQDLTKEEA IKLASDAIQA GIWNDLGSGS
210 220 230 240 250
NVDVCVMEIG KDAEYLRNYL TPNVREEKQK SYKFPRGTTA VLKESIVNIC
260
DIQEEQVDIT A
Length:261
Mass (Da):28,268
Last modified:May 1, 1992 - v1
Checksum:i13A8F2B75584539A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61189 Genomic DNA. Translation: CAA43492.1.
U55020 Genomic DNA. Translation: AAC49643.1.
Z75065 Genomic DNA. Translation: CAA99363.1.
BK006948 Genomic DNA. Translation: DAA10930.1.
PIRiS26996.
RefSeqiNP_014800.3. NM_001183576.3.

Genome annotation databases

EnsemblFungiiYOR157C; YOR157C; YOR157C.
GeneIDi854328.
KEGGisce:YOR157C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61189 Genomic DNA. Translation: CAA43492.1.
U55020 Genomic DNA. Translation: AAC49643.1.
Z75065 Genomic DNA. Translation: CAA99363.1.
BK006948 Genomic DNA. Translation: DAA10930.1.
PIRiS26996.
RefSeqiNP_014800.3. NM_001183576.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20I/W30-261[»]
1G0UX-ray2.40H/V30-251[»]
1G65X-ray2.25H/V30-251[»]
1JD2X-ray3.00H/O30-251[»]
1RYPX-ray1.90I/W30-251[»]
1Z7QX-ray3.22I/W30-251[»]
2F16X-ray2.80H/V30-251[»]
2FAKX-ray2.80H/V30-251[»]
2GPLX-ray2.81H/V30-251[»]
2ZCYX-ray2.90H/V30-261[»]
3BDMX-ray2.70H/V30-261[»]
3D29X-ray2.60H/V30-251[»]
3DY3X-ray2.81H/V30-251[»]
3DY4X-ray2.80H/V30-251[»]
3E47X-ray3.00H/V30-251[»]
3GPJX-ray2.70H/V30-251[»]
3GPTX-ray2.41H/V30-251[»]
3GPWX-ray2.50H/V30-251[»]
3HYEX-ray2.50H/V30-251[»]
3JCOelectron microscopy4.804/i1-261[»]
3JCPelectron microscopy4.604/i1-261[»]
3MG0X-ray2.68H/V30-251[»]
3MG4X-ray3.11H/V30-251[»]
3MG6X-ray2.60H/V30-251[»]
3MG7X-ray2.78H/V30-251[»]
3MG8X-ray2.59H/V30-251[»]
3NZJX-ray2.40H/V1-261[»]
3NZWX-ray2.50H/V1-261[»]
3NZXX-ray2.70H/V1-261[»]
3OEUX-ray2.60H/V30-251[»]
3OEVX-ray2.85H/V30-251[»]
3OKJX-ray2.70H/V30-251[»]
3SDIX-ray2.65H/V30-251[»]
3SDKX-ray2.70H/V30-251[»]
3SHJX-ray2.80H/V30-251[»]
3TDDX-ray2.70H/V30-251[»]
3UN4X-ray3.40H/V30-261[»]
3UN8X-ray2.70H/V30-261[»]
3WXRX-ray3.15I/W1-261[»]
4CR2electron microscopy7.7021-261[»]
4CR3electron microscopy9.3021-261[»]
4CR4electron microscopy8.8021-261[»]
4EU2X-ray2.51I/W30-251[»]
4FZCX-ray2.80H/V30-251[»]
4FZGX-ray3.00H/V30-251[»]
4G4SX-ray2.49I30-261[»]
4GK7X-ray2.80H/V30-251[»]
4HNPX-ray2.80H/V30-251[»]
4HRCX-ray2.80H/V30-251[»]
4HRDX-ray2.80H/V30-251[»]
4INRX-ray2.70H/V30-261[»]
4INTX-ray2.90H/V30-261[»]
4INUX-ray3.10H/V30-261[»]
4J70X-ray2.80H/V30-261[»]
4JSQX-ray2.80H/V30-261[»]
4JSUX-ray2.90H/V30-261[»]
4JT0X-ray3.10H/V30-261[»]
4LQIX-ray2.70H/V30-251[»]
4LTCX-ray2.50H/V30-261[»]
4NNNX-ray2.50H/V30-261[»]
4NNWX-ray2.60H/V30-261[»]
4NO1X-ray2.50H/V30-261[»]
4NO6X-ray3.00H/V30-261[»]
4NO8X-ray2.70H/V30-261[»]
4NO9X-ray2.90H/V30-261[»]
4Q1SX-ray2.60H/V30-261[»]
4QBYX-ray3.00H/V30-261[»]
4QLQX-ray2.40H/V30-261[»]
4QLSX-ray2.80H/V30-261[»]
4QLTX-ray2.80H/V30-261[»]
4QLUX-ray2.80H/V30-261[»]
4QLVX-ray2.90H/V30-261[»]
4QUXX-ray3.00H/V30-261[»]
4QUYX-ray2.80H/V30-261[»]
4QV0X-ray3.10H/V30-261[»]
4QV1X-ray2.50H/V30-261[»]
4QV3X-ray3.00H/V30-261[»]
4QV4X-ray2.70H/V30-261[»]
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4QV6X-ray2.80H/V30-261[»]
4QV7X-ray2.60H/V30-261[»]
4QV8X-ray2.90H/V30-261[»]
4QV9X-ray2.60H/V30-261[»]
4QVLX-ray2.80H/V30-261[»]
4QVMX-ray2.80H/V30-261[»]
4QVNX-ray2.90H/V30-261[»]
4QVPX-ray2.30H/V30-261[»]
4QVQX-ray2.60H/V30-261[»]
4QVVX-ray2.80H/V30-261[»]
4QVWX-ray3.00H/V30-261[»]
4QVYX-ray2.51H/V30-261[»]
4QW0X-ray2.90H/V30-261[»]
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4QW3X-ray2.90H/V30-261[»]
4QW4X-ray2.80H/V30-261[»]
4QW5X-ray3.00H/V30-261[»]
4QW6X-ray2.90H/V30-261[»]
4QW7X-ray2.70H/V30-261[»]
4QWFX-ray3.00H/V30-261[»]
4QWGX-ray2.60H/V30-261[»]
4QWIX-ray2.60H/V30-261[»]
4QWJX-ray2.90H/V30-261[»]
4QWKX-ray2.80H/V30-261[»]
4QWLX-ray2.60H/V30-261[»]
4QWRX-ray2.90H/V30-261[»]
4QWSX-ray3.00H/V30-261[»]
4QWUX-ray3.00H/V30-261[»]
4QWXX-ray2.90H/V30-261[»]
4QXJX-ray2.80H/V30-261[»]
4QZ0X-ray3.00H/V30-261[»]
4QZ1X-ray3.00H/V30-261[»]
4QZ2X-ray2.70H/V30-261[»]
4QZ3X-ray2.80H/V30-261[»]
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4QZ6X-ray2.90H/V30-261[»]
4QZ7X-ray2.80H/V30-261[»]
4QZWX-ray3.00H/V30-261[»]
4QZXX-ray2.60H/V30-261[»]
4QZZX-ray2.90H/V30-261[»]
4R00X-ray2.80H/V30-261[»]
4R02X-ray2.50H/V30-261[»]
4R17X-ray2.10H/V30-261[»]
4R18X-ray2.40H/V30-261[»]
4RURX-ray2.50H/V30-261[»]
4V7OX-ray3.00AM/AY/BI/BW30-251[»]
4X6ZX-ray2.70I/W1-261[»]
4Y69X-ray2.90H/V30-261[»]
4Y6AX-ray2.60H/V30-261[»]
4Y6VX-ray2.80H/V30-261[»]
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4Y70X-ray2.40H/V30-261[»]
4Y74X-ray2.70H/V30-261[»]
4Y75X-ray2.80H/V30-261[»]
4Y77X-ray2.50H/V30-261[»]
4Y78X-ray2.80H/V30-261[»]
4Y7WX-ray2.50H/V30-261[»]
4Y7XX-ray2.60H/V30-261[»]
4Y7YX-ray2.40H/V30-261[»]
4Y80X-ray2.50H/V30-261[»]
4Y81X-ray2.80H/V30-261[»]
4Y82X-ray2.80H/V30-261[»]
4Y84X-ray2.70H/V30-261[»]
4Y8GX-ray2.60H/V30-261[»]
4Y8HX-ray2.50H/V30-261[»]
4Y8IX-ray2.60H/V30-261[»]
4Y8JX-ray2.70H/V30-261[»]
4Y8KX-ray2.60H/V30-261[»]
4Y8LX-ray2.40H/V30-261[»]
4Y8MX-ray2.80H/V30-261[»]
4Y8NX-ray2.60H/V30-261[»]
4Y8OX-ray2.70H/V30-261[»]
4Y8PX-ray2.80H/V30-261[»]
4Y8QX-ray2.60H/V30-261[»]
4Y8RX-ray2.70H/V30-261[»]
4Y8SX-ray2.70H/V30-261[»]
4Y8TX-ray2.70H/V30-261[»]
4Y8UX-ray2.90H/V30-261[»]
4Y9YX-ray2.80H/V30-261[»]
4Y9ZX-ray2.80H/V30-261[»]
4YA0X-ray2.80H/V30-261[»]
4YA1X-ray2.90H/V30-261[»]
4YA2X-ray2.70H/V30-261[»]
4YA3X-ray2.70H/V30-261[»]
4YA4X-ray2.90H/V30-261[»]
4YA5X-ray2.50H/V30-261[»]
4YA7X-ray2.70H/V30-261[»]
4YA9X-ray2.70H/V30-261[»]
4Z1LX-ray3.00H/V30-261[»]
4ZZGX-ray3.00I/W1-261[»]
5A5Belectron microscopy9.5021-261[»]
5AHJX-ray2.80H/V30-261[»]
5BOUX-ray2.60H/V30-261[»]
5BXLX-ray2.80H/V30-261[»]
5BXNX-ray2.80H/V30-261[»]
5CGFX-ray2.80H/V30-261[»]
5CGGX-ray2.90H/V30-261[»]
5CGHX-ray2.50H/V30-261[»]
5CGIX-ray2.80H/V30-261[»]
5CZ4X-ray2.30H/V30-261[»]
5CZ5X-ray2.80H/V30-261[»]
5CZ6X-ray2.70H/V30-261[»]
5CZ7X-ray2.50H/V30-261[»]
5CZ8X-ray2.80H/V30-261[»]
5CZ9X-ray2.90H/V30-261[»]
5CZAX-ray2.50H/V30-261[»]
5D0SX-ray2.50H/V30-261[»]
5D0TX-ray2.60H/V30-261[»]
5D0VX-ray2.90H/V30-261[»]
5D0WX-ray2.80H/V30-261[»]
5D0XX-ray2.60H/V30-261[»]
5D0ZX-ray2.90H/V30-261[»]
5DKIX-ray2.80H/V30-261[»]
5DKJX-ray2.80H/V30-261[»]
5FG7X-ray2.70H/V24-261[»]
5FG9X-ray2.60H/V26-261[»]
5FGAX-ray2.70H/V30-261[»]
5FGDX-ray2.80H/V30-261[»]
5FGEX-ray2.60H/V30-261[»]
5FGFX-ray2.60H/V30-261[»]
5FGGX-ray2.70H/V30-261[»]
5FGHX-ray2.80H/V30-261[»]
5FGIX-ray2.90H/V18-261[»]
5FHSX-ray2.70H/V30-261[»]
5JHRX-ray2.90H/V30-261[»]
5JHSX-ray3.00H/V30-261[»]
ProteinModelPortaliP25043.
SMRiP25043.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34553. 57 interactors.
DIPiDIP-2818N.
IntActiP25043. 9 interactors.
MINTiMINT-498378.

Protein family/group databases

MEROPSiT01.011.

Proteomic databases

MaxQBiP25043.
PRIDEiP25043.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR157C; YOR157C; YOR157C.
GeneIDi854328.
KEGGisce:YOR157C.

Organism-specific databases

EuPathDBiFungiDB:YOR157C.
SGDiS000005683. PUP1.

Phylogenomic databases

GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
InParanoidiP25043.
KOiK02739.
OMAiAPQIWCA.
OrthoDBiEOG092C44RU.

Enzyme and pathway databases

BioCyciYEAST:G3O-33674-MONOMER.
ReactomeiR-SCE-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-SCE-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-382556. ABC-family proteins mediated transport.
R-SCE-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-SCE-5668541. TNFR2 non-canonical NF-kB pathway.
R-SCE-5687128. MAPK6/MAPK4 signaling.
R-SCE-5689880. Ub-specific processing proteases.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-68949. Orc1 removal from chromatin.
R-SCE-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SCE-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SCE-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-SCE-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiP25043.
PROiP25043.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. 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...

Entry informationi

Entry nameiPSB2_YEAST
AccessioniPrimary (citable) accession number: P25043
Secondary accession number(s): D6W2L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 30, 2016
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The side chain of Thr-30 acts as nucleophile, and the N-terminal amino group acts as proton acceptor.
Present with 11400 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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 one 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.