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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

  • 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.
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-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.

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
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001480701 – 205Proteasome subunit beta type-3Add BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31PhosphoserineCombined sources1
Cross-linki70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25451.
PRIDEiP25451.

PTM databases

iPTMnetiP25451.

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. 32 interactors.
DIPiDIP-2039N.
IntActiP25451. 12 interactors.
MINTiMINT-498393.

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi11 – 16Combined sources6
Beta strandi18 – 26Combined sources9
Beta strandi29 – 31Combined sources3
Beta strandi34 – 38Combined sources5
Beta strandi43 – 46Combined sources4
Beta strandi49 – 55Combined sources7
Helixi57 – 78Combined sources22
Helixi84 – 96Combined sources13
Turni97 – 100Combined sources4
Beta strandi105 – 112Combined sources8
Turni114 – 116Combined sources3
Beta strandi119 – 124Combined sources6
Beta strandi130 – 132Combined sources3
Beta strandi134 – 140Combined sources7
Helixi143 – 153Combined sources11
Helixi160 – 175Combined sources16
Beta strandi178 – 181Combined sources4
Beta strandi185 – 193Combined sources9
Beta strandi195 – 200Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3JCOelectron microscopy4.805/j1-205[»]
3JCPelectron microscopy4.605/j1-205[»]
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[»]
4X6ZX-ray2.70J/X1-205[»]
4Y69X-ray2.90I/W1-205[»]
4Y6AX-ray2.60I/W1-205[»]
4Y6VX-ray2.80I/W1-205[»]
4Y6ZX-ray2.70I/W1-205[»]
4Y70X-ray2.40I/W1-205[»]
4Y74X-ray2.70I/W1-205[»]
4Y75X-ray2.80I/W1-205[»]
4Y77X-ray2.50I/W1-205[»]
4Y78X-ray2.80I/W1-205[»]
4Y7WX-ray2.50I/W1-205[»]
4Y7XX-ray2.60I/W1-205[»]
4Y7YX-ray2.40I/W1-205[»]
4Y80X-ray2.50I/W1-205[»]
4Y81X-ray2.80I/W1-205[»]
4Y82X-ray2.80I/W1-205[»]
4Y84X-ray2.70I/W1-205[»]
4Y8GX-ray2.60I/W1-205[»]
4Y8HX-ray2.50I/W1-205[»]
4Y8IX-ray2.60I/W1-205[»]
4Y8JX-ray2.70I/W1-205[»]
4Y8KX-ray2.60I/W1-205[»]
4Y8LX-ray2.40I/W1-205[»]
4Y8MX-ray2.80I/W1-205[»]
4Y8NX-ray2.60I/W1-205[»]
4Y8OX-ray2.70I/W1-205[»]
4Y8PX-ray2.80I/W1-205[»]
4Y8QX-ray2.60I/W1-205[»]
4Y8RX-ray2.70I/W1-205[»]
4Y8SX-ray2.70I/W1-205[»]
4Y8TX-ray2.70I/W1-205[»]
4Y8UX-ray2.90I/W1-205[»]
4Y9YX-ray2.80I/W1-205[»]
4Y9ZX-ray2.80I/W1-205[»]
4YA0X-ray2.80I/W1-205[»]
4YA1X-ray2.90I/W1-205[»]
4YA2X-ray2.70I/W1-205[»]
4YA3X-ray2.70I/W1-205[»]
4YA4X-ray2.90I/W1-205[»]
4YA5X-ray2.50I/W1-205[»]
4YA7X-ray2.70I/W1-205[»]
4YA9X-ray2.70I/W1-205[»]
4Z1LX-ray3.00I/W1-205[»]
4ZZGX-ray3.00J/X1-205[»]
5A5Belectron microscopy9.5031-205[»]
5AHJX-ray2.80I/W1-205[»]
5BOUX-ray2.60I/W1-205[»]
5BXLX-ray2.80I/W1-205[»]
5BXNX-ray2.80I/W1-205[»]
5CGFX-ray2.80I/W1-205[»]
5CGGX-ray2.90I/W1-205[»]
5CGHX-ray2.50I/W1-205[»]
5CGIX-ray2.80I/W1-205[»]
5CZ4X-ray2.30I/W1-205[»]
5CZ5X-ray2.80I/W1-205[»]
5CZ6X-ray2.70I/W1-205[»]
5CZ7X-ray2.50I/W1-205[»]
5CZ8X-ray2.80I/W1-205[»]
5CZ9X-ray2.90I/W1-205[»]
5CZAX-ray2.50I/W1-205[»]
5D0SX-ray2.50I/W1-205[»]
5D0TX-ray2.60I/W1-205[»]
5D0VX-ray2.90I/W1-205[»]
5D0WX-ray2.80I/W1-205[»]
5D0XX-ray2.60I/W1-205[»]
5D0ZX-ray2.90I/W1-205[»]
5DKIX-ray2.80I/W1-205[»]
5DKJX-ray2.80I/W1-205[»]
5FG7X-ray2.70I/W1-205[»]
5FG9X-ray2.60I/W1-205[»]
5FGAX-ray2.70I/W1-205[»]
5FGDX-ray2.80I/W1-205[»]
5FGEX-ray2.60I/W1-205[»]
5FGFX-ray2.60I/W1-205[»]
5FGGX-ray2.70I/W1-205[»]
5FGHX-ray2.80I/W1-205[»]
5FGIX-ray2.90I/W1-205[»]
5FHSX-ray2.70I/W1-205[»]
5JHRX-ray2.90I/W1-205[»]
5JHSX-ray3.00I/W1-205[»]
ProteinModelPortaliP25451.
SMRiP25451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25451.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
InParanoidiP25451.
KOiK02735.
OMAiFNYGPST.
OrthoDBiEOG092C4N9L.

Family and domain databases

CDDicd03759. proteasome_beta_type_3. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033811. Proteasome_beta_3.
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
PDB 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[»]
3JCOelectron microscopy4.805/j1-205[»]
3JCPelectron microscopy4.605/j1-205[»]
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[»]
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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[»]
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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[»]
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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[»]
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4QZ6X-ray2.90I/W1-205[»]
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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[»]
4X6ZX-ray2.70J/X1-205[»]
4Y69X-ray2.90I/W1-205[»]
4Y6AX-ray2.60I/W1-205[»]
4Y6VX-ray2.80I/W1-205[»]
4Y6ZX-ray2.70I/W1-205[»]
4Y70X-ray2.40I/W1-205[»]
4Y74X-ray2.70I/W1-205[»]
4Y75X-ray2.80I/W1-205[»]
4Y77X-ray2.50I/W1-205[»]
4Y78X-ray2.80I/W1-205[»]
4Y7WX-ray2.50I/W1-205[»]
4Y7XX-ray2.60I/W1-205[»]
4Y7YX-ray2.40I/W1-205[»]
4Y80X-ray2.50I/W1-205[»]
4Y81X-ray2.80I/W1-205[»]
4Y82X-ray2.80I/W1-205[»]
4Y84X-ray2.70I/W1-205[»]
4Y8GX-ray2.60I/W1-205[»]
4Y8HX-ray2.50I/W1-205[»]
4Y8IX-ray2.60I/W1-205[»]
4Y8JX-ray2.70I/W1-205[»]
4Y8KX-ray2.60I/W1-205[»]
4Y8LX-ray2.40I/W1-205[»]
4Y8MX-ray2.80I/W1-205[»]
4Y8NX-ray2.60I/W1-205[»]
4Y8OX-ray2.70I/W1-205[»]
4Y8PX-ray2.80I/W1-205[»]
4Y8QX-ray2.60I/W1-205[»]
4Y8RX-ray2.70I/W1-205[»]
4Y8SX-ray2.70I/W1-205[»]
4Y8TX-ray2.70I/W1-205[»]
4Y8UX-ray2.90I/W1-205[»]
4Y9YX-ray2.80I/W1-205[»]
4Y9ZX-ray2.80I/W1-205[»]
4YA0X-ray2.80I/W1-205[»]
4YA1X-ray2.90I/W1-205[»]
4YA2X-ray2.70I/W1-205[»]
4YA3X-ray2.70I/W1-205[»]
4YA4X-ray2.90I/W1-205[»]
4YA5X-ray2.50I/W1-205[»]
4YA7X-ray2.70I/W1-205[»]
4YA9X-ray2.70I/W1-205[»]
4Z1LX-ray3.00I/W1-205[»]
4ZZGX-ray3.00J/X1-205[»]
5A5Belectron microscopy9.5031-205[»]
5AHJX-ray2.80I/W1-205[»]
5BOUX-ray2.60I/W1-205[»]
5BXLX-ray2.80I/W1-205[»]
5BXNX-ray2.80I/W1-205[»]
5CGFX-ray2.80I/W1-205[»]
5CGGX-ray2.90I/W1-205[»]
5CGHX-ray2.50I/W1-205[»]
5CGIX-ray2.80I/W1-205[»]
5CZ4X-ray2.30I/W1-205[»]
5CZ5X-ray2.80I/W1-205[»]
5CZ6X-ray2.70I/W1-205[»]
5CZ7X-ray2.50I/W1-205[»]
5CZ8X-ray2.80I/W1-205[»]
5CZ9X-ray2.90I/W1-205[»]
5CZAX-ray2.50I/W1-205[»]
5D0SX-ray2.50I/W1-205[»]
5D0TX-ray2.60I/W1-205[»]
5D0VX-ray2.90I/W1-205[»]
5D0WX-ray2.80I/W1-205[»]
5D0XX-ray2.60I/W1-205[»]
5D0ZX-ray2.90I/W1-205[»]
5DKIX-ray2.80I/W1-205[»]
5DKJX-ray2.80I/W1-205[»]
5FG7X-ray2.70I/W1-205[»]
5FG9X-ray2.60I/W1-205[»]
5FGAX-ray2.70I/W1-205[»]
5FGDX-ray2.80I/W1-205[»]
5FGEX-ray2.60I/W1-205[»]
5FGFX-ray2.60I/W1-205[»]
5FGGX-ray2.70I/W1-205[»]
5FGHX-ray2.80I/W1-205[»]
5FGIX-ray2.90I/W1-205[»]
5FHSX-ray2.70I/W1-205[»]
5JHRX-ray2.90I/W1-205[»]
5JHSX-ray3.00I/W1-205[»]
ProteinModelPortaliP25451.
SMRiP25451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36840. 32 interactors.
DIPiDIP-2039N.
IntActiP25451. 12 interactors.
MINTiMINT-498393.

PTM databases

iPTMnetiP25451.

Proteomic databases

MaxQBiP25451.
PRIDEiP25451.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YER094C.
SGDiS000000896. PUP3.

Phylogenomic databases

GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
InParanoidiP25451.
KOiK02735.
OMAiFNYGPST.
OrthoDBiEOG092C4N9L.

Enzyme and pathway databases

BioCyciYEAST:G3O-30261-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-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

EvolutionaryTraceiP25451.
PROiP25451.

Family and domain databases

CDDicd03759. proteasome_beta_type_3. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033811. Proteasome_beta_3.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 172 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

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.