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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:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation EC:3.4.25.1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • endopeptidase activity Source: GO_Central
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30926-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-SCE-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-SCE-174113 SCF-beta-TrCP mediated degradation of Emi1
R-SCE-187577 SCF(Skp2)-mediated degradation of p27/p21
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-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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PUP2
Synonyms:DOA5
Ordered Locus Names:YGR253C
ORF Names:G9155
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003485 PUP2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi49G → D in DOA5-1; slight decrease in activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001241291 – 260Proteasome subunit alpha type-5Add BLAST260

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei55PhosphothreonineCombined sources1
Modified residuei56PhosphoserineCombined sources1
Modified residuei251PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32379

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P32379

PRoteomics IDEntifications database

More...
PRIDEi
P32379

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32379

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
POC4Q122452EBI-13971,EBI-2343020

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33504, 171 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2262 26S Proteasome complex

Database of interacting proteins

More...
DIPi
DIP-1193N

Protein interaction database and analysis system

More...
IntActi
P32379, 13 interactors

Molecular INTeraction database

More...
MINTi
P32379

STRING: functional protein association networks

More...
STRINGi
4932.YGR253C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P32379

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P32379

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P32379

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00550000074958

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000091085

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P32379

KEGG Orthology (KO)

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KOi
K02729

Identification of Orthologs from Complete Genome Data

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OMAi
FQVEYAR

Database of Orthologous Groups

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OrthoDBi
EOG092C47D8

Family and domain databases

Conserved Domains Database

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CDDi
cd03753 proteasome_alpha_type_5, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.60.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR033812 Proteasome_alpha_type_5
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00227 Proteasome, 1 hit
PF10584 Proteasome_A_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00948 Proteasome_A_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56235 SSF56235, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00388 PROTEASOME_ALPHA_1, 1 hit
PS51475 PROTEASOME_ALPHA_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE8EDEB212BF4EC6E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti192T → S in CAA46111 (PubMed:1544471).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S64585

NCBI Reference Sequences

More...
RefSeqi
NP_011769.1, NM_001181382.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGR253C_mRNA; YGR253C_mRNA; YGR253C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853168

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGR253C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
6EF0electron microscopy4.43E1-249[»]
6EF1electron microscopy4.73E9-250[»]
6EF2electron microscopy4.27E2-248[»]
6EF3electron microscopy4.17E1-260[»]
6FVTelectron microscopy4.10E/e7-250[»]
6FVUelectron microscopy4.50E/e2-250[»]
6FVVelectron microscopy5.40E/e7-250[»]
6FVWelectron microscopy4.50E/e6-250[»]
6FVXelectron microscopy4.90E/e7-250[»]
6FVYelectron microscopy6.10E/e6-250[»]
6G7FX-ray2.70D/R1-260[»]
6G8MX-ray2.70D/R1-260[»]
6G8NX-ray3.00D/R1-260[»]
6GOPX-ray2.90D/R1-260[»]
ProteinModelPortaliP32379
SMRiP32379
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33504, 171 interactors
ComplexPortaliCPX-2262 26S Proteasome complex
DIPiDIP-1193N
IntActiP32379, 13 interactors
MINTiP32379
STRINGi4932.YGR253C

PTM databases

iPTMnetiP32379

Proteomic databases

MaxQBiP32379
PaxDbiP32379
PRIDEiP32379

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR253C_mRNA; YGR253C_mRNA; YGR253C
GeneIDi853168
KEGGisce:YGR253C

Organism-specific databases

SGDiS000003485 PUP2

Phylogenomic databases

GeneTreeiENSGT00550000074958
HOGENOMiHOG000091085
InParanoidiP32379
KOiK02729
OMAiFQVEYAR
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-187577 SCF(Skp2)-mediated degradation of p27/p21
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-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

Protein Ontology

More...
PROi
PR:P32379

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPSA5_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P32379
Secondary accession number(s): D6VV33
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 202 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Peptidase families
    Classification of peptidase families and list of entries
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