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UniProtKB - P23639 (PSA2_YEAST)

Protein

Proteasome subunit alpha type-2

Gene

PRE8

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 7060 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
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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-32677-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...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-2 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit Y7
Multicatalytic endopeptidase complex subunit Y7
Proteasome component Y7
Proteinase YSCE subunit 7
<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:PRE8
Synonyms:PRS4
Ordered Locus Names:YML092C
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000004557 PRE8

<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 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_00001240901 – 250Proteasome subunit alpha type-2Add BLAST250

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P23639

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

More...PaxDbi		P23639

PRoteomics IDEntifications database

More...PRIDEi		P23639

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P23639

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		35051, 150 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-2822N

Protein interaction database and analysis system

More...IntActi		P23639, 23 interactors

Molecular INTeraction database

More...MINTi		P23639

STRING: functional protein association networks

More...STRINGi		4932.YML092C

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P23639

<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

1250
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		P23639

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

More...SMRi		P23639

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P23639

<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

More...GeneTreei		ENSGT00550000074870

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000091085

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P23639

KEGG Orthology (KO)

More...KOi		K02726

Identification of Orthologs from Complete Genome Data

More...OMAi		FAWKASA

Database of Orthologous Groups

More...OrthoDBi		EOG092C47D8

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...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
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
IPR034644 Proteasome_subunit_alpha2

The PANTHER Classification System

More...PANTHERi		PTHR11599:SF16 PTHR11599:SF16, 1 hit

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.

P23639-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTDRYSFSLT TFSPSGKLGQ IDYALTAVKQ GVTSLGIKAT NGVVIATEKK 
        60         70         80         90        100
SSSPLAMSET LSKVSLLTPD IGAVYSGMGP DYRVLVDKSR KVAHTSYKRI 
       110        120        130        140        150
YGEYPPTKLL VSEVAKIMQE ATQSGGVRPF GVSLLIAGHD EFNGFSLYQV 
       160        170        180        190        200
DPSGSYFPWK ATAIGKGSVA AKTFLEKRWN DELELEDAIH IALLTLKESV 
       210        220        230        240        250
EGEFNGDTIE LAIIGDENPD LLGYTGIPTD KGPRFRKLTS QEINDRLEAL
Length:250
Mass (Da):27,162
Last modified:November 1, 1991 - v1
<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:i12D7DFB1AA10E9FE
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X56731 Genomic DNA Translation: CAA40055.1
Z46660 Genomic DNA Translation: CAA86646.1
AY557762 Genomic DNA Translation: AAS56088.1
BK006946 Genomic DNA Translation: DAA09807.1

Protein sequence database of the Protein Information Resource

More...PIRi		S12938 SNBYY7

NCBI Reference Sequences

More...RefSeqi		NP_013618.1, NM_001182451.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YML092C_mRNA; YML092C_mRNA; YML092C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854882

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YML092C

<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
X56731 Genomic DNA Translation: CAA40055.1
Z46660 Genomic DNA Translation: CAA86646.1
AY557762 Genomic DNA Translation: AAS56088.1
BK006946 Genomic DNA Translation: DAA09807.1
PIRiS12938 SNBYY7
RefSeqiNP_013618.1, NM_001182451.1

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-ray3.20B/P1-250[»]
1G0UX-ray2.40A/O1-250[»]
1G65X-ray2.25A/O1-250[»]
1JD2X-ray3.00A/V1-250[»]
1RYPX-ray1.90B/P1-250[»]
1Z7QX-ray3.22B/P1-250[»]
2F16X-ray2.80A/O1-250[»]
2FAKX-ray2.80A/O1-250[»]
2GPLX-ray2.81A/O1-250[»]
2ZCYX-ray2.90A/O1-250[»]
3BDMX-ray2.70A/O1-250[»]
3D29X-ray2.60A/O1-250[»]
3DY3X-ray2.81A/O1-250[»]
3DY4X-ray2.80A/O1-250[»]
3E47X-ray3.00A/O1-250[»]
3GPJX-ray2.70A/O1-250[»]
3GPTX-ray2.41A/O1-250[»]
3GPWX-ray2.50A/O1-250[»]
3HYEX-ray2.50A/O1-250[»]
3JCOelectron microscopy4.80B/b1-250[»]
3JCPelectron microscopy4.60B/b1-250[»]
3MG0X-ray2.68A/O1-250[»]
3MG4X-ray3.11A/O1-250[»]
3MG6X-ray2.60A/O1-250[»]
3MG7X-ray2.78A/O1-250[»]
3MG8X-ray2.59A/O1-250[»]
3NZJX-ray2.40A/O1-250[»]
3NZWX-ray2.50A/O1-250[»]
3NZXX-ray2.70A/O1-250[»]
3OEUX-ray2.60A/O1-250[»]
3OEVX-ray2.85A/O1-250[»]
3OKJX-ray2.70A/O1-250[»]
3SDIX-ray2.65A/O1-250[»]
3SDKX-ray2.70A/O1-250[»]
3SHJX-ray2.80A/O1-250[»]
3TDDX-ray2.70A/O1-250[»]
3UN4X-ray3.40A/O1-250[»]
3UN8X-ray2.70A/O1-250[»]
3WXRX-ray3.15B/P1-250[»]
4CR2electron microscopy7.70B1-250[»]
4CR3electron microscopy9.30B1-250[»]
4CR4electron microscopy8.80B1-250[»]
4EU2X-ray2.51B/P1-250[»]
4FZCX-ray2.80A/O1-250[»]
4FZGX-ray3.00A/O1-250[»]
4G4SX-ray2.49B1-250[»]
4GK7X-ray2.80A/O1-250[»]
4HNPX-ray2.80A/O1-250[»]
4HRCX-ray2.80A/O2-250[»]
4HRDX-ray2.80A/O1-250[»]
4INRX-ray2.70A/O1-250[»]
4INTX-ray2.90A/O1-250[»]
4INUX-ray3.10A/O1-250[»]
4J70X-ray2.80A/O1-250[»]
4JSQX-ray2.80A/O1-250[»]
4JSUX-ray2.90A/O1-250[»]
4JT0X-ray3.10A/O1-250[»]
4LQIX-ray2.70A/O1-250[»]
4LTCX-ray2.50A/O1-250[»]
4NNNX-ray2.50A/O1-250[»]
4NNWX-ray2.60A/O1-250[»]
4NO1X-ray2.50A/O1-250[»]
4NO6X-ray3.00A/O1-250[»]
4NO8X-ray2.70A/O1-250[»]
4NO9X-ray2.90A/O1-250[»]
4Q1SX-ray2.60A/O1-250[»]
4QBYX-ray3.00A/O1-250[»]
4QLQX-ray2.40A/O1-250[»]
4QLSX-ray2.80A/O1-250[»]
4QLTX-ray2.80A/O1-250[»]
4QLUX-ray2.80A/O1-250[»]
4QLVX-ray2.90A/O1-250[»]
4QUXX-ray3.00A/O1-250[»]
4QUYX-ray2.80A/O1-250[»]
4QV0X-ray3.10A/O1-250[»]
4QV1X-ray2.50A/O1-250[»]
4QV3X-ray3.00A/O1-250[»]
4QV4X-ray2.70A/O1-250[»]
4QV5X-ray2.70A/O1-250[»]
4QV6X-ray2.80A/O1-250[»]
4QV7X-ray2.60A/O1-250[»]
4QV8X-ray2.90A/O1-250[»]
4QV9X-ray2.60A/O1-250[»]
4QVLX-ray2.80A/O1-250[»]
4QVMX-ray2.80A/O1-250[»]
4QVNX-ray2.90A/O1-250[»]
4QVPX-ray2.30A/O1-250[»]
4QVQX-ray2.60A/O1-250[»]
4QVVX-ray2.80A/O1-250[»]
4QVWX-ray3.00A/O1-250[»]
4QVYX-ray2.51A/O1-250[»]
4QW0X-ray2.90A/O1-250[»]
4QW1X-ray2.90A/O1-250[»]
4QW3X-ray2.90A/O1-250[»]
4QW4X-ray2.80A/O1-250[»]
4QW5X-ray3.00A/O1-250[»]
4QW6X-ray2.90A/O1-250[»]
4QW7X-ray2.70A/O1-250[»]
4QWFX-ray3.00A/O1-250[»]
4QWGX-ray2.60A/O1-250[»]
4QWIX-ray2.60A/O1-250[»]
4QWJX-ray2.90A/O1-250[»]
4QWKX-ray2.80A/O1-250[»]
4QWLX-ray2.60A/O1-250[»]
4QWRX-ray2.90A/O1-250[»]
4QWSX-ray3.00A/O1-250[»]
4QWUX-ray3.00A/O1-250[»]
4QWXX-ray2.90A/O1-250[»]
4QXJX-ray2.80A/O1-250[»]
4QZ0X-ray3.00A/O1-250[»]
4QZ1X-ray3.00A/O1-250[»]
4QZ2X-ray2.70A/O1-250[»]
4QZ3X-ray2.80A/O1-250[»]
4QZ4X-ray3.00A/O1-250[»]
4QZ5X-ray2.80A/O1-250[»]
4QZ6X-ray2.90A/O1-250[»]
4QZ7X-ray2.80A/O1-250[»]
4QZWX-ray3.00A/O1-250[»]
4QZXX-ray2.60A/O1-250[»]
4QZZX-ray2.90A/O1-250[»]
4R00X-ray2.80A/O1-250[»]
4R02X-ray2.50A/O1-250[»]
4R17X-ray2.10A/O1-250[»]
4R18X-ray2.40A/O1-250[»]
4RURX-ray2.50A/O1-250[»]
4V7OX-ray3.00AG/AS/BB/BP20-250[»]
4X6ZX-ray2.70B/P1-250[»]
4Y69X-ray2.90A/O1-250[»]
4Y6AX-ray2.60A/O1-250[»]
4Y6VX-ray2.80A/O1-250[»]
4Y6ZX-ray2.70A/O1-250[»]
4Y70X-ray2.40A/O1-250[»]
4Y74X-ray2.70A/O1-250[»]
4Y75X-ray2.80A/O1-250[»]
4Y77X-ray2.50A/O1-250[»]
4Y78X-ray2.80A/O1-250[»]
4Y7WX-ray2.50A/O1-250[»]
4Y7XX-ray2.60A/O1-250[»]
4Y7YX-ray2.40A/O1-250[»]
4Y80X-ray2.50A/O1-250[»]
4Y81X-ray2.80A/O1-250[»]
4Y82X-ray2.80A/O1-250[»]
4Y84X-ray2.70A/O1-250[»]
4Y8GX-ray2.60A/O1-250[»]
4Y8HX-ray2.50A/O1-250[»]
4Y8IX-ray2.60A/O1-250[»]
4Y8JX-ray2.70A/O1-250[»]
4Y8KX-ray2.60A/O1-250[»]
4Y8LX-ray2.40A/O1-250[»]
4Y8MX-ray2.80A/O1-250[»]
4Y8NX-ray2.60A/O1-250[»]
4Y8OX-ray2.70A/O1-250[»]
4Y8PX-ray2.80A/O1-250[»]
4Y8QX-ray2.60A/O1-250[»]
4Y8RX-ray2.70A/O1-250[»]
4Y8SX-ray2.70A/O1-250[»]
4Y8TX-ray2.70A/O1-250[»]
4Y8UX-ray2.90A/O1-250[»]
4Y9YX-ray2.80A/O1-250[»]
4Y9ZX-ray2.80A/O1-250[»]
4YA0X-ray2.80A/O1-250[»]
4YA1X-ray2.90A/O1-250[»]
4YA2X-ray2.70A/O1-250[»]
4YA3X-ray2.70A/O1-250[»]
4YA4X-ray2.90A/O1-250[»]
4YA5X-ray2.50A/O1-250[»]
4YA7X-ray2.70A/O1-250[»]
4YA9X-ray2.70A/O1-250[»]
4Z1LX-ray3.00A/O1-250[»]
5A5Belectron microscopy9.50B1-250[»]
5AHJX-ray2.80A/O1-250[»]
5BOUX-ray2.60A/O1-250[»]
5BXLX-ray2.80A/O1-250[»]
5BXNX-ray2.80A/O1-250[»]
5CGFX-ray2.80A/O1-250[»]
5CGGX-ray2.90A/O1-250[»]
5CGHX-ray2.50A/O1-250[»]
5CGIX-ray2.80A/O1-250[»]
5CZ4X-ray2.30A/O1-250[»]
5CZ5X-ray2.80A/O1-250[»]
5CZ6X-ray2.70A/O1-250[»]
5CZ7X-ray2.50A/O1-250[»]
5CZ8X-ray2.80A/O1-250[»]
5CZ9X-ray2.90A/O1-250[»]
5CZAX-ray2.50A/O1-250[»]
5D0SX-ray2.50A/O1-250[»]
5D0TX-ray2.60A/O1-250[»]
5D0VX-ray2.90A/O1-250[»]
5D0WX-ray2.80A/O1-250[»]
5D0XX-ray2.60A/O1-250[»]
5D0ZX-ray2.90A/O1-250[»]
5DKIX-ray2.80A/O1-250[»]
5DKJX-ray2.80A/O1-250[»]
5FG7X-ray2.70A/O1-250[»]
5FG9X-ray2.60A/O1-250[»]
5FGAX-ray2.70A/O1-250[»]
5FGDX-ray2.80A/O1-250[»]
5FGEX-ray2.60A/O1-250[»]
5FGFX-ray2.60A/O1-250[»]
5FGGX-ray2.70A/O1-250[»]
5FGHX-ray2.80A/O1-250[»]
5FGIX-ray2.90A/O1-250[»]
5FHSX-ray2.70A/O1-250[»]
5JHRX-ray2.90A/O1-250[»]
5JHSX-ray3.00A/O1-250[»]
5L52X-ray2.70A/O1-250[»]
5L54X-ray2.80A/O1-250[»]
5L55X-ray2.90A/O1-250[»]
5L5AX-ray2.40A/O1-250[»]
5L5BX-ray2.80A/O1-250[»]
5L5DX-ray2.80A/O1-250[»]
5L5EX-ray2.90A/O1-250[»]
5L5FX-ray2.50A/O1-250[»]
5L5HX-ray2.60A/O1-250[»]
5L5IX-ray2.90A/O1-250[»]
5L5JX-ray2.90A/O1-250[»]
5L5OX-ray2.60A/O1-250[»]
5L5PX-ray2.80A/O1-250[»]
5L5QX-ray2.80A/O1-250[»]
5L5RX-ray2.90A/O1-250[»]
5L5SX-ray2.60A/O1-250[»]
5L5TX-ray2.90A/O1-250[»]
5L5UX-ray2.60A/O1-250[»]
5L5VX-ray2.70A/O1-250[»]
5L5WX-ray2.80A/O1-250[»]
5L5XX-ray2.90A/O1-250[»]
5L5YX-ray2.70A/O1-250[»]
5L5ZX-ray2.70A/O1-250[»]
5L60X-ray2.70A/O1-250[»]
5L61X-ray2.80A/O1-250[»]
5L62X-ray2.80A/O1-250[»]
5L63X-ray2.70A/O1-250[»]
5L64X-ray2.70A/O1-250[»]
5L65X-ray2.90A/O1-250[»]
5L66X-ray2.80A/O1-250[»]
5L67X-ray2.60A/O1-250[»]
5L68X-ray2.80A/O1-250[»]
5L69X-ray2.70A/O1-250[»]
5L6AX-ray2.80A/O1-250[»]
5L6BX-ray2.60A/O1-250[»]
5L6CX-ray2.60A/O1-250[»]
5LAIX-ray2.50A/O1-250[»]
5LAJX-ray2.90A/O1-250[»]
5LTTX-ray2.70A/O1-250[»]
5M2BX-ray2.70A/O1-250[»]
5MP9electron microscopy4.10B/b1-250[»]
5MPAelectron microscopy4.50B/b1-250[»]
5MPBelectron microscopy7.80B/b1-250[»]
5MPCelectron microscopy7.70B/b1-250[»]
5NIFX-ray3.00B/P1-250[»]
5WVIelectron microscopy6.30B/j1-250[»]
5WVKelectron microscopy4.20B/j1-250[»]
6EF0electron microscopy4.43B1-250[»]
6EF1electron microscopy4.73B1-250[»]
6EF2electron microscopy4.27B1-249[»]
6EF3electron microscopy4.17B1-250[»]
6FVTelectron microscopy4.10B/b2-250[»]
6FVUelectron microscopy4.50B/b2-250[»]
6FVVelectron microscopy5.40B/b2-250[»]
6FVWelectron microscopy4.50B/b4-250[»]
6FVXelectron microscopy4.90B/b5-250[»]
6FVYelectron microscopy6.10B/b3-250[»]
6G7FX-ray2.70A/O1-250[»]
6G8MX-ray2.70A/O1-250[»]
6G8NX-ray3.00A/O1-250[»]
6GOPX-ray2.90A/O1-250[»]
ProteinModelPortaliP23639
SMRiP23639
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35051, 150 interactors
ComplexPortaliCPX-2262 26S Proteasome complex
DIPiDIP-2822N
IntActiP23639, 23 interactors
MINTiP23639
STRINGi4932.YML092C

Chemistry databases

BindingDBiP23639

PTM databases

iPTMnetiP23639

Proteomic databases

MaxQBiP23639
PaxDbiP23639
PRIDEiP23639

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML092C_mRNA; YML092C_mRNA; YML092C
GeneIDi854882
KEGGisce:YML092C

Organism-specific databases

SGDiS000004557 PRE8

Phylogenomic databases

GeneTreeiENSGT00550000074870
HOGENOMiHOG000091085
InParanoidiP23639
KOiK02726
OMAiFAWKASA
OrthoDBiEOG092C47D8

Enzyme and pathway databases

BioCyciYEAST:G3O-32677-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

EvolutionaryTraceiP23639

Protein Ontology

More...PROi		PR:P23639

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
IPR034644 Proteasome_subunit_alpha2
PANTHERiPTHR11599:SF16 PTHR11599:SF16, 1 hit
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 nameiPSA2_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: P23639
Secondary accession number(s): D6W0J3
<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: November 1, 1991
Last sequence update: November 1, 1991
Last modified: December 5, 2018
This is version 202 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

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