Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proteasome subunit alpha type-5

Gene

PUP2

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.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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, 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

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
  • nucleus Source: SGD
  • proteasome core complex, alpha-subunit complex Source: SGD
  • proteasome storage granule Source: SGD
Complete GO annotation...

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.
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

Protein-protein interaction databases

BioGridi33504. 62 interactors.
DIPiDIP-1193N.
IntActiP32379. 9 interactors.
MINTiMINT-386734.

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[»]
4ZZGX-ray3.00E/S1-260[»]
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[»]
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.
OMAiELQNEFH.
OrthoDBiEOG092C47D8.

Family and domain databases

CDDicd03753. proteasome_alpha_type_5. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033812. Proteasome_alpha_type_5.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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[»]
4ZZGX-ray3.00E/S1-260[»]
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[»]
ProteinModelPortaliP32379.
SMRiP32379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33504. 62 interactors.
DIPiDIP-1193N.
IntActiP32379. 9 interactors.
MINTiMINT-386734.

PTM databases

iPTMnetiP32379.

Proteomic databases

MaxQBiP32379.
PRIDEiP32379.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR253C; YGR253C; YGR253C.
GeneIDi853168.
KEGGisce:YGR253C.

Organism-specific databases

EuPathDBiFungiDB:YGR253C.
SGDiS000003485. PUP2.

Phylogenomic databases

GeneTreeiENSGT00550000074958.
HOGENOMiHOG000091085.
InParanoidiP32379.
KOiK02729.
OMAiELQNEFH.
OrthoDBiEOG092C47D8.

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.

Miscellaneous databases

EvolutionaryTraceiP32379.
PROiP32379.

Family and domain databases

CDDicd03753. proteasome_alpha_type_5. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033812. Proteasome_alpha_type_5.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSA5_YEAST
AccessioniPrimary (citable) accession number: P32379
Secondary accession number(s): D6VV33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 17100 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.