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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: -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

Keywordsi

Molecular functionHydrolase, 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP25451
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

Show more details

Protein-protein interaction databases

BioGridi36840422 interactors.
DIPiDIP-2039N
IntActiP25451 17 interactors.
MINTiP25451
STRINGi4932.YER094C

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[»]
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[»]
5L52X-ray2.70I/W1-205[»]
5L54X-ray2.80I/W1-205[»]
5L55X-ray2.90I/W1-205[»]
5L5AX-ray2.40I/W1-205[»]
5L5BX-ray2.80I/W1-205[»]
5L5DX-ray2.80I/W1-205[»]
5L5EX-ray2.90I/W1-205[»]
5L5FX-ray2.50I/W1-205[»]
5L5HX-ray2.60I/W1-205[»]
5L5IX-ray2.90I/W1-205[»]
5L5JX-ray2.90I/W1-205[»]
5L5OX-ray2.60I/W1-205[»]
5L5PX-ray2.80I/W1-205[»]
5L5QX-ray2.80I/W1-205[»]
5L5RX-ray2.90I/W1-205[»]
5L5SX-ray2.60I/W1-205[»]
5L5TX-ray2.90I/W1-205[»]
5L5UX-ray2.60I/W1-205[»]
5L5VX-ray2.70I/W1-205[»]
5L5WX-ray2.80I/W1-205[»]
5L5XX-ray2.90I/W1-205[»]
5L5YX-ray2.70I/W1-205[»]
5L5ZX-ray2.70I/W1-205[»]
5L60X-ray2.70I/W1-205[»]
5L61X-ray2.80I/W1-205[»]
5L62X-ray2.80I/W1-205[»]
5L63X-ray2.70I/W1-205[»]
5L64X-ray2.70I/W1-205[»]
5L65X-ray2.90I/W1-205[»]
5L66X-ray2.80I/W1-205[»]
5L67X-ray2.60I/W1-205[»]
5L68X-ray2.80I/W1-205[»]
5L69X-ray2.70I/W1-205[»]
5L6AX-ray2.80I/W1-205[»]
5L6BX-ray2.60I/W1-205[»]
5L6CX-ray2.60I/W1-205[»]
5LAIX-ray2.50I/W1-205[»]
5LAJX-ray2.90I/W1-205[»]
5LTTX-ray2.70I/W1-205[»]
5M2BX-ray2.70I/W1-205[»]
5MP9electron microscopy4.103/j1-205[»]
5MPAelectron microscopy4.503/j1-205[»]
5MPBelectron microscopy7.803/j1-205[»]
5MPCelectron microscopy7.703/j1-205[»]
5NIFX-ray3.00J/X1-205[»]
5WVIelectron microscopy6.303/h1-205[»]
5WVKelectron microscopy4.203/h1-205[»]
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
OMAiEQLFGMC
OrthoDBiEOG092C4N9L

Family and domain databases

CDDicd03759 proteasome_beta_type_3, 1 hit
Gene3Di3.60.20.101 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR033811 Proteasome_beta_3
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF62 PTHR11599:SF62, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPSB3_YEAST
AccessioniPrimary (citable) accession number: P25451
Secondary accession number(s): D3DM02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: March 28, 2018
This is version 185 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome