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UniProtKB - P49722 (PSA2_MOUSE)

Entry version 172 (02 Dec 2020)
Sequence version 3 (31 Oct 2012)
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Protein

Proteasome subunit alpha type-2

Gene

Psma2

Organism
Mus musculus (Mouse)
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

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).2 Publications

<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
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1169091, Activation of NF-kappaB in B cells
R-MMU-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1236978, Cross-presentation of soluble exogenous antigens (endosomes)
R-MMU-174084, Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174154, APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-187577, SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253, Degradation of beta-catenin by the destruction complex
R-MMU-202424, Downstream TCR signaling
R-MMU-2467813, Separation of Sister Chromatids
R-MMU-2871837, FCERI mediated NF-kB activation
R-MMU-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-350562, Regulation of ornithine decarboxylase (ODC)
R-MMU-382556, ABC-family proteins mediated transport
R-MMU-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA
R-MMU-4608870, Asymmetric localization of PCP proteins
R-MMU-4641257, Degradation of AXIN
R-MMU-4641258, Degradation of DVL
R-MMU-5358346, Hedgehog ligand biogenesis
R-MMU-5607761, Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764, CLEC7A (Dectin-1) signaling
R-MMU-5610780, Degradation of GLI1 by the proteasome
R-MMU-5610785, GLI3 is processed to GLI3R by the proteasome
R-MMU-5632684, Hedgehog 'on' state
R-MMU-5658442, Regulation of RAS by GAPs
R-MMU-5668541, TNFR2 non-canonical NF-kB pathway
R-MMU-5676590, NIK-->noncanonical NF-kB signaling
R-MMU-5687128, MAPK6/MAPK4 signaling
R-MMU-5689603, UCH proteinases
R-MMU-5689880, Ub-specific processing proteases
R-MMU-6798695, Neutrophil degranulation
R-MMU-68827, CDT1 association with the CDC6:ORC:origin complex
R-MMU-68949, Orc1 removal from chromatin
R-MMU-69017, CDK-mediated phosphorylation and removal of Cdc6
R-MMU-69481, G2/M Checkpoints
R-MMU-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-75815, Ubiquitin-dependent degradation of Cyclin D
R-MMU-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902, Regulation of RUNX2 expression and activity
R-MMU-8941858, Regulation of RUNX3 expression and activity
R-MMU-8948751, Regulation of PTEN stability and activity
R-MMU-8951664, Neddylation
R-MMU-9020702, Interleukin-1 signaling
R-MMU-983168, Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MEROPS protease database

More...MEROPSi		T01.972

<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%5Fand%5Ftaxonomy%5Fsection">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
Alternative name(s):
Macropain subunit C3
Multicatalytic endopeptidase complex subunit C3
Proteasome component C3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Psma2
Synonyms:Lmpc3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 13

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:104885, Psma2

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<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>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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001240782 – 234Proteasome subunit alpha type-2Add BLAST233

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 residuei2N-acetylalanine1 Publication1
Modified residuei6PhosphotyrosineCombined sources1
Modified residuei7PhosphoserineBy similarity1
Modified residuei14PhosphoserineBy similarity1
Modified residuei16PhosphoserineBy similarity1
Modified residuei24PhosphotyrosineBy similarity1
Modified residuei70N6-acetyllysineBy similarity1
Modified residuei76PhosphotyrosineCombined sources1
Modified residuei121PhosphotyrosineBy similarity1
Modified residuei171N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on tyrosine residues; which may be important for nuclear import.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		non-CPTAC-3940

Encyclopedia of Proteome Dynamics

More...EPDi		P49722

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P49722

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

More...PaxDbi		P49722

PeptideAtlas

More...PeptideAtlasi		P49722

PRoteomics IDEntifications database

More...PRIDEi		P49722

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P49722

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...COMPLUYEAST-2DPAGEi		P49722

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		P49722

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P49722

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P49722

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P49722

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P49722

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000015671, Expressed in oocyte and 303 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P49722, MM

<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%5Fsection">'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%5Fsection">'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 a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		202416, 62 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P49722

Protein interaction database and analysis system

More...IntActi		P49722, 9 interactors

Molecular INTeraction database

More...MINTi		P49722

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000129767

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P49722, protein

<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

1234
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P49722

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0181, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074870

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_035750_4_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P49722

Identification of Orthologs from Complete Genome Data

More...OMAi		CVYSGMG

Database of Orthologous Groups

More...OrthoDBi		1222564at2759

TreeFam database of animal gene trees

More...TreeFami		TF106207

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P49722-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK 
        60         70         80         90        100
KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV 
       110        120        130        140        150
YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD 
       160        170        180        190        200
PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE DLELEDAIHT AILTLKESFE 
       210        220        230 
GQMTEDNIEV GICNEAGFRR LTPTEVRDYL AAIA
Length:234
Mass (Da):25,927
Last modified:October 31, 2012 - v3
<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:i4ECB56A233583821
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q8BKE0Q8BKE0_MOUSE
Proteasome subunit alpha type-2
Psma2
183Annotation score:

Annotation score:1 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 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 conflicti3E → K in CAA49782 (PubMed:7697131).Curated1

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
X70303 mRNA Translation: CAA49782.1
AF099733 mRNA Translation: AAD50623.1
AK012119 mRNA Translation: BAB28045.1
AK035578 mRNA Translation: BAC29110.1
AK151883 mRNA Translation: BAE30769.1
AK152862 mRNA Translation: BAE31553.1
AK154011 mRNA Translation: BAE32314.1
AK167752 mRNA Translation: BAE39787.1
AC092710 Genomic DNA No translation available.
CH466561 Genomic DNA Translation: EDL32738.1
BC026768 mRNA Translation: AAH26768.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS36602.1

NCBI Reference Sequences

More...RefSeqi		NP_032970.2, NM_008944.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000170836; ENSMUSP00000129767; ENSMUSG00000015671

Database of genes from NCBI RefSeq genomes

More...GeneIDi		19166

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:19166

UCSC genome browser

More...UCSCi		uc007pnl.1, mouse

<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
X70303 mRNA Translation: CAA49782.1
AF099733 mRNA Translation: AAD50623.1
AK012119 mRNA Translation: BAB28045.1
AK035578 mRNA Translation: BAC29110.1
AK151883 mRNA Translation: BAE30769.1
AK152862 mRNA Translation: BAE31553.1
AK154011 mRNA Translation: BAE32314.1
AK167752 mRNA Translation: BAE39787.1
AC092710 Genomic DNA No translation available.
CH466561 Genomic DNA Translation: EDL32738.1
BC026768 mRNA Translation: AAH26768.1
CCDSiCCDS36602.1
RefSeqiNP_032970.2, NM_008944.2

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
3UNBX-ray2.90A/O/c/q1-234[»]
3UNEX-ray3.20A/O/c/q1-234[»]
3UNFX-ray2.90A/O1-234[»]
3UNHX-ray3.20A/O1-234[»]
SMRiP49722
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi202416, 62 interactors
CORUMiP49722
IntActiP49722, 9 interactors
MINTiP49722
STRINGi10090.ENSMUSP00000129767

Protein family/group databases

MEROPSiT01.972

PTM databases

iPTMnetiP49722
PhosphoSitePlusiP49722
SwissPalmiP49722

2D gel databases

COMPLUYEAST-2DPAGEiP49722
REPRODUCTION-2DPAGEiP49722
SWISS-2DPAGEiP49722

Proteomic databases

CPTACinon-CPTAC-3940
EPDiP49722
jPOSTiP49722
PaxDbiP49722
PeptideAtlasiP49722
PRIDEiP49722
TopDownProteomicsiP49722

Genome annotation databases

EnsembliENSMUST00000170836; ENSMUSP00000129767; ENSMUSG00000015671
GeneIDi19166
KEGGimmu:19166
UCSCiuc007pnl.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5683
MGIiMGI:104885, Psma2

Phylogenomic databases

eggNOGiKOG0181, Eukaryota
GeneTreeiENSGT00550000074870
HOGENOMiCLU_035750_4_1_1
InParanoidiP49722
OMAiCVYSGMG
OrthoDBi1222564at2759
TreeFamiTF106207

Enzyme and pathway databases

ReactomeiR-MMU-1169091, Activation of NF-kappaB in B cells
R-MMU-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1236978, Cross-presentation of soluble exogenous antigens (endosomes)
R-MMU-174084, Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174154, APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-187577, SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253, Degradation of beta-catenin by the destruction complex
R-MMU-202424, Downstream TCR signaling
R-MMU-2467813, Separation of Sister Chromatids
R-MMU-2871837, FCERI mediated NF-kB activation
R-MMU-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-350562, Regulation of ornithine decarboxylase (ODC)
R-MMU-382556, ABC-family proteins mediated transport
R-MMU-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA
R-MMU-4608870, Asymmetric localization of PCP proteins
R-MMU-4641257, Degradation of AXIN
R-MMU-4641258, Degradation of DVL
R-MMU-5358346, Hedgehog ligand biogenesis
R-MMU-5607761, Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764, CLEC7A (Dectin-1) signaling
R-MMU-5610780, Degradation of GLI1 by the proteasome
R-MMU-5610785, GLI3 is processed to GLI3R by the proteasome
R-MMU-5632684, Hedgehog 'on' state
R-MMU-5658442, Regulation of RAS by GAPs
R-MMU-5668541, TNFR2 non-canonical NF-kB pathway
R-MMU-5676590, NIK-->noncanonical NF-kB signaling
R-MMU-5687128, MAPK6/MAPK4 signaling
R-MMU-5689603, UCH proteinases
R-MMU-5689880, Ub-specific processing proteases
R-MMU-6798695, Neutrophil degranulation
R-MMU-68827, CDT1 association with the CDC6:ORC:origin complex
R-MMU-68949, Orc1 removal from chromatin
R-MMU-69017, CDK-mediated phosphorylation and removal of Cdc6
R-MMU-69481, G2/M Checkpoints
R-MMU-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-75815, Ubiquitin-dependent degradation of Cyclin D
R-MMU-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902, Regulation of RUNX2 expression and activity
R-MMU-8941858, Regulation of RUNX3 expression and activity
R-MMU-8948751, Regulation of PTEN stability and activity
R-MMU-8951664, Neddylation
R-MMU-9020702, Interleukin-1 signaling
R-MMU-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		19166, 9 hits in 18 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Psma2, mouse

Protein Ontology

More...PROi		PR:P49722
RNActiP49722, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000015671, Expressed in oocyte and 303 other tissues
GenevisibleiP49722, MM

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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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_MOUSE
<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: P49722
Secondary accession number(s): E9Q3A4, Q6ZWV8
<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%5Fand%5Fisoforms">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, 1996
Last sequence update: October 31, 2012
Last modified: December 2, 2020
This is version 172 of the entry and version 3 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 programChordata 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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