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Protein

Proteasome subunit alpha type-5

Gene

PUP2

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.

Miscellaneous

Present with 17100 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

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-30926-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

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit PUP2
Multicatalytic endopeptidase complex subunit PUP2
Proteasome component PUP2
Proteinase YSCE subunit PUP2
Gene namesi
Name:PUP2
Synonyms:DOA5
Ordered Locus Names:YGR253C
ORF Names:G9155
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR253C
SGDiS000003485 PUP2

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49G → D in DOA5-1; slight decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241291 – 260Proteasome subunit alpha type-5Add BLAST260

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei55PhosphothreonineCombined sources1
Modified residuei56PhosphoserineCombined sources1
Modified residuei251PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32379
PaxDbiP32379
PRIDEiP32379

PTM databases

iPTMnetiP32379

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

BioGridi33504, 169 interactors
DIPiDIP-1193N
IntActiP32379, 28 interactors
MINTiP32379
STRINGi4932.YGR253C

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 21Combined sources3
Helixi22 – 31Combined sources10
Beta strandi37 – 41Combined sources5
Beta strandi46 – 51Combined sources6
Beta strandi55 – 59Combined sources5
Helixi61 – 63Combined sources3
Beta strandi67 – 71Combined sources5
Beta strandi74 – 81Combined sources8
Helixi82 – 84Combined sources3
Helixi85 – 103Combined sources19
Helixi109 – 117Combined sources9
Turni118 – 121Combined sources4
Beta strandi124 – 126Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi139 – 148Combined sources10
Turni149 – 151Combined sources3
Beta strandi152 – 158Combined sources7
Turni160 – 162Combined sources3
Beta strandi164 – 173Combined sources10
Helixi176 – 186Combined sources11
Helixi193 – 207Combined sources15
Beta strandi208 – 210Combined sources3
Beta strandi216 – 223Combined sources8
Turni224 – 226Combined sources3
Beta strandi227 – 230Combined sources4
Helixi233 – 247Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20E/S1-260[»]
1G0UX-ray2.40D/R1-250[»]
1G65X-ray2.25D/R9-250[»]
1JD2X-ray3.00D/Y9-120[»]
D/Y131-250[»]
1RYPX-ray1.90E/S9-250[»]
1Z7QX-ray3.22E/S1-260[»]
2F16X-ray2.80D/R9-250[»]
2FAKX-ray2.80D/R9-250[»]
2GPLX-ray2.81D/R9-250[»]
2Z5CX-ray2.90C/F1-260[»]
2ZCYX-ray2.90D/R1-260[»]
3BDMX-ray2.70D/R1-260[»]
3D29X-ray2.60D/R9-250[»]
3DY3X-ray2.81D/R9-250[»]
3DY4X-ray2.80D/R9-250[»]
3E47X-ray3.00D/R9-250[»]
3GPJX-ray2.70D/R9-250[»]
3GPTX-ray2.41D/R9-250[»]
3GPWX-ray2.50D/R9-250[»]
3HYEX-ray2.50D/R9-250[»]
3JCOelectron microscopy4.80E/e1-260[»]
3JCPelectron microscopy4.60E/e1-260[»]
3MG0X-ray2.68D/R9-250[»]
3MG4X-ray3.11D/R9-250[»]
3MG6X-ray2.60D/R1-250[»]
3MG7X-ray2.78D/R1-250[»]
3MG8X-ray2.59D/R1-250[»]
3NZJX-ray2.40D/R1-260[»]
3NZWX-ray2.50D/R1-260[»]
3NZXX-ray2.70D/R1-260[»]
3OEUX-ray2.60D/R1-260[»]
3OEVX-ray2.85D/R1-260[»]
3OKJX-ray2.70D/R9-250[»]
3SDIX-ray2.65D/R1-260[»]
3SDKX-ray2.70D/R1-260[»]
3SHJX-ray2.80D/R9-250[»]
3TDDX-ray2.70D/R9-250[»]
3UN4X-ray3.40D/R1-260[»]
3UN8X-ray2.70D/R1-260[»]
3WXRX-ray3.15E/S1-260[»]
4CR2electron microscopy7.70E1-260[»]
4CR3electron microscopy9.30E1-260[»]
4CR4electron microscopy8.80E1-260[»]
4EU2X-ray2.51E/S9-250[»]
4FZCX-ray2.80D/R9-250[»]
4FZGX-ray3.00D/R9-250[»]
4G4SX-ray2.49E1-260[»]
4GK7X-ray2.80D/R9-250[»]
4HNPX-ray2.80D/R9-250[»]
4HRCX-ray2.80D/R9-250[»]
4HRDX-ray2.80D/R9-250[»]
4INRX-ray2.70D/R1-260[»]
4INTX-ray2.90D/R1-260[»]
4INUX-ray3.10D/R1-260[»]
4J70X-ray2.80D/R1-260[»]
4JSQX-ray2.80D/R1-260[»]
4JSUX-ray2.90D/R1-260[»]
4JT0X-ray3.10D/R1-260[»]
4LQIX-ray2.70D/R9-250[»]
4LTCX-ray2.50D/R1-260[»]
4NNNX-ray2.50D/R1-260[»]
4NNWX-ray2.60D/R1-260[»]
4NO1X-ray2.50D/R1-260[»]
4NO6X-ray3.00D/R1-260[»]
4NO8X-ray2.70D/R1-260[»]
4NO9X-ray2.90D/R1-260[»]
4Q1SX-ray2.60D/R1-260[»]
4QBYX-ray3.00D/R1-260[»]
4QLQX-ray2.40D/R1-260[»]
4QLSX-ray2.80D/R1-260[»]
4QLTX-ray2.80D/R1-260[»]
4QLUX-ray2.80D/R1-260[»]
4QLVX-ray2.90D/R1-260[»]
4QUXX-ray3.00D/R1-260[»]
4QUYX-ray2.80D/R1-260[»]
4QV0X-ray3.10D/R1-260[»]
4QV1X-ray2.50D/R1-260[»]
4QV3X-ray3.00D/R1-260[»]
4QV4X-ray2.70D/R1-260[»]
4QV5X-ray2.70D/R1-260[»]
4QV6X-ray2.80D/R1-260[»]
4QV7X-ray2.60D/R1-260[»]
4QV8X-ray2.90D/R1-260[»]
4QV9X-ray2.60D/R1-260[»]
4QVLX-ray2.80D/R1-260[»]
4QVMX-ray2.80D/R1-260[»]
4QVNX-ray2.90D/R1-260[»]
4QVPX-ray2.30D/R1-260[»]
4QVQX-ray2.60D/R1-260[»]
4QVVX-ray2.80D/R1-260[»]
4QVWX-ray3.00D/R1-260[»]
4QVYX-ray2.51D/R1-260[»]
4QW0X-ray2.90D/R1-260[»]
4QW1X-ray2.90D/R1-260[»]
4QW3X-ray2.90D/R1-260[»]
4QW4X-ray2.80D/R1-260[»]
4QW5X-ray3.00D/R1-260[»]
4QW6X-ray2.90D/R1-260[»]
4QW7X-ray2.70D/R1-260[»]
4QWFX-ray3.00D/R1-260[»]
4QWGX-ray2.60D/R1-260[»]
4QWIX-ray2.60D/R1-260[»]
4QWJX-ray2.90D/R1-260[»]
4QWKX-ray2.80D/R1-260[»]
4QWLX-ray2.60D/R1-260[»]
4QWRX-ray2.90D/R1-260[»]
4QWSX-ray3.00D/R1-260[»]
4QWUX-ray3.00D/R1-260[»]
4QWXX-ray2.90D/R1-260[»]
4QXJX-ray2.80D/R1-260[»]
4QZ0X-ray3.00D/R1-260[»]
4QZ1X-ray3.00D/R1-260[»]
4QZ2X-ray2.70D/R1-260[»]
4QZ3X-ray2.80D/R1-260[»]
4QZ4X-ray3.00D/R1-260[»]
4QZ5X-ray2.80D/R1-260[»]
4QZ6X-ray2.90D/R1-260[»]
4QZ7X-ray2.80D/R1-260[»]
4QZWX-ray3.00D/R1-260[»]
4QZXX-ray2.60D/R1-260[»]
4QZZX-ray2.90D/R1-260[»]
4R00X-ray2.80D/R1-260[»]
4R02X-ray2.50D/R1-260[»]
4R17X-ray2.10D/R1-260[»]
4R18X-ray2.40D/R1-260[»]
4RURX-ray2.50D/R1-260[»]
4V7OX-ray3.00AJ/AV/BE/BS1-250[»]
4X6ZX-ray2.70E/S1-260[»]
4Y69X-ray2.90D/R1-260[»]
4Y6AX-ray2.60D/R1-260[»]
4Y6VX-ray2.80D/R1-260[»]
4Y6ZX-ray2.70D/R1-260[»]
4Y70X-ray2.40D/R1-260[»]
4Y74X-ray2.70D/R1-260[»]
4Y75X-ray2.80D/R1-260[»]
4Y77X-ray2.50D/R1-260[»]
4Y78X-ray2.80D/R1-260[»]
4Y7WX-ray2.50D/R1-260[»]
4Y7XX-ray2.60D/R1-260[»]
4Y7YX-ray2.40D/R1-260[»]
4Y80X-ray2.50D/R1-260[»]
4Y81X-ray2.80D/R1-260[»]
4Y82X-ray2.80D/R1-260[»]
4Y84X-ray2.70D/R1-260[»]
4Y8GX-ray2.60D/R1-260[»]
4Y8HX-ray2.50D/R1-260[»]
4Y8IX-ray2.60D/R1-260[»]
4Y8JX-ray2.70D/R1-260[»]
4Y8KX-ray2.60D/R1-260[»]
4Y8LX-ray2.40D/R1-260[»]
4Y8MX-ray2.80D/R1-260[»]
4Y8NX-ray2.60D/R1-260[»]
4Y8OX-ray2.70D/R1-260[»]
4Y8PX-ray2.80D/R1-260[»]
4Y8QX-ray2.60D/R1-260[»]
4Y8RX-ray2.70D/R1-260[»]
4Y8SX-ray2.70D/R1-260[»]
4Y8TX-ray2.70D/R1-260[»]
4Y8UX-ray2.90D/R1-260[»]
4Y9YX-ray2.80D/R1-260[»]
4Y9ZX-ray2.80D/R1-260[»]
4YA0X-ray2.80D/R1-260[»]
4YA1X-ray2.90D/R1-260[»]
4YA2X-ray2.70D/R1-260[»]
4YA3X-ray2.70D/R1-260[»]
4YA4X-ray2.90D/R1-260[»]
4YA5X-ray2.50D/R1-260[»]
4YA7X-ray2.70D/R1-260[»]
4YA9X-ray2.70D/R1-260[»]
4Z1LX-ray3.00D/R1-260[»]
5A5Belectron microscopy9.50E1-260[»]
5AHJX-ray2.80D/R1-260[»]
5BOUX-ray2.60D/R1-260[»]
5BXLX-ray2.80D/R1-260[»]
5BXNX-ray2.80D/R1-260[»]
5CGFX-ray2.80D/R1-260[»]
5CGGX-ray2.90D/R1-260[»]
5CGHX-ray2.50D/R1-260[»]
5CGIX-ray2.80D/R1-260[»]
5CZ4X-ray2.30D/R1-260[»]
5CZ5X-ray2.80D/R1-260[»]
5CZ6X-ray2.70D/R1-260[»]
5CZ7X-ray2.50D/R1-260[»]
5CZ8X-ray2.80D/R1-260[»]
5CZ9X-ray2.90D/R1-260[»]
5CZAX-ray2.50D/R1-260[»]
5D0SX-ray2.50D/R1-260[»]
5D0TX-ray2.60D/R1-260[»]
5D0VX-ray2.90D/R1-260[»]
5D0WX-ray2.80D/R1-260[»]
5D0XX-ray2.60D/R1-260[»]
5D0ZX-ray2.90D/R1-260[»]
5DKIX-ray2.80D/R1-260[»]
5DKJX-ray2.80D/R1-260[»]
5FG7X-ray2.70D/R1-260[»]
5FG9X-ray2.60D/R1-260[»]
5FGAX-ray2.70D/R1-260[»]
5FGDX-ray2.80D/R1-260[»]
5FGEX-ray2.60D/R1-260[»]
5FGFX-ray2.60D/R1-260[»]
5FGGX-ray2.70D/R1-260[»]
5FGHX-ray2.80D/R1-260[»]
5FGIX-ray2.90D/R1-260[»]
5FHSX-ray2.70D/R1-260[»]
5JHRX-ray2.90D/R1-260[»]
5JHSX-ray3.00D/R1-260[»]
5L52X-ray2.70D/R1-260[»]
5L54X-ray2.80D/R1-260[»]
5L55X-ray2.90D/R1-260[»]
5L5AX-ray2.40D/R1-260[»]
5L5BX-ray2.80D/R1-260[»]
5L5DX-ray2.80D/R1-260[»]
5L5EX-ray2.90D/R1-260[»]
5L5FX-ray2.50D/R1-260[»]
5L5HX-ray2.60D/R1-260[»]
5L5IX-ray2.90D/R1-260[»]
5L5JX-ray2.90D/R1-260[»]
5L5OX-ray2.60D/R1-260[»]
5L5PX-ray2.80D/R1-260[»]
5L5QX-ray2.80D/R1-260[»]
5L5RX-ray2.90D/R1-260[»]
5L5SX-ray2.60D/R1-260[»]
5L5TX-ray2.90D/R1-260[»]
5L5UX-ray2.60D/R1-260[»]
5L5VX-ray2.70D/R1-260[»]
5L5WX-ray2.80D/R1-260[»]
5L5XX-ray2.90D/R1-260[»]
5L5YX-ray2.70D/R1-260[»]
5L5ZX-ray2.70D/R1-260[»]
5L60X-ray2.70D/R1-260[»]
5L61X-ray2.80D/R1-260[»]
5L62X-ray2.80D/R1-260[»]
5L63X-ray2.70D/R1-260[»]
5L64X-ray2.70D/R1-260[»]
5L65X-ray2.90D/R1-260[»]
5L66X-ray2.80D/R1-260[»]
5L67X-ray2.60D/R1-260[»]
5L68X-ray2.80D/R1-260[»]
5L69X-ray2.70D/R1-260[»]
5L6AX-ray2.80D/R1-260[»]
5L6BX-ray2.60D/R1-260[»]
5L6CX-ray2.60D/R1-260[»]
5LAIX-ray2.50D/R1-260[»]
5LAJX-ray2.90D/R1-260[»]
5LTTX-ray2.70D/R1-260[»]
5M2BX-ray2.70D/R1-260[»]
5MP9electron microscopy4.10E/e1-260[»]
5MPAelectron microscopy4.50E/e1-260[»]
5MPBelectron microscopy7.80E/e1-260[»]
5MPCelectron microscopy7.70E/e1-260[»]
5NIFX-ray3.00E/S1-260[»]
5WVIelectron microscopy6.30E/m1-260[»]
5WVKelectron microscopy4.20E/m1-260[»]
ProteinModelPortaliP32379
SMRiP32379
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32379

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074958
HOGENOMiHOG000091085
InParanoidiP32379
KOiK02729
OMAiFQVEYAR
OrthoDBiEOG092C47D8

Family and domain databases

CDDicd03753 proteasome_alpha_type_5, 1 hit
Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR033812 Proteasome_alpha_type_5
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PF10584 Proteasome_A_N, 1 hit
SMARTiView protein in SMART
SM00948 Proteasome_A_N, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00388 PROTEASOME_ALPHA_1, 1 hit
PS51475 PROTEASOME_ALPHA_2, 1 hit

Sequencei

Sequence statusi: Complete.

P32379-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLTRSEYDR GVSTFSPEGR LFQVEYSLEA IKLGSTAIGI ATKEGVVLGV
60 70 80 90 100
EKRATSPLLE SDSIEKIVEI DRHIGCAMSG LTADARSMIE HARTAAVTHN
110 120 130 140 150
LYYDEDINVE SLTQSVCDLA LRFGEGASGE ERLMSRPFGV ALLIAGHDAD
160 170 180 190 200
DGYQLFHAEP SGTFYRYNAK AIGSGSEGAQ AELLNEWHSS LTLKEAELLV
210 220 230 240 250
LKILKQVMEE KLDENNAQLS CITKQDGFKI YDNEKTAELI KELKEKEAAE
260
SPEEADVEMS
Length:260
Mass (Da):28,617
Last modified:October 1, 1996 - v2
Checksum:iE8EDEB212BF4EC6E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti192T → S in CAA46111 (PubMed:1544471).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64918 Genomic DNA Translation: CAA46111.1
X99228 Genomic DNA Translation: CAA67615.1
Z73038 Genomic DNA Translation: CAA97282.1
AY558511 Genomic DNA Translation: AAS56837.1
BK006941 Genomic DNA Translation: DAA08344.1
PIRiS64585
RefSeqiNP_011769.1, NM_001181382.1

Genome annotation databases

EnsemblFungiiYGR253C; YGR253C; YGR253C
GeneIDi853168
KEGGisce:YGR253C

Similar proteinsi

Entry informationi

Entry nameiPSA5_YEAST
AccessioniPrimary (citable) accession number: P32379
Secondary accession number(s): D6VV33
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 195 of the entry and version 2 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
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Main funding by: National Institutes of Health