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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-Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which 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. The proteasome has an ATP-dependent proteolytic activity. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.1 Publication

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

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-174113. SCF-beta-TrCP mediated degradation of Emi1.
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-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-2 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C3
Multicatalytic endopeptidase complex subunit C3
Proteasome component C3
Gene namesi
Name:Psma2
Synonyms:Lmpc3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:104885. Psma2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
  • proteasome complex Source: MGI
  • proteasome core complex Source: UniProtKB
  • proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001240782 – 234Proteasome subunit alpha type-2Add BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 residuei171N6-acetyllysineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP49722.
PaxDbiP49722.
PeptideAtlasiP49722.
PRIDEiP49722.
TopDownProteomicsiP49722.

2D gel databases

COMPLUYEAST-2DPAGEP49722.
REPRODUCTION-2DPAGEP49722.
SWISS-2DPAGEP49722.

PTM databases

iPTMnetiP49722.
PhosphoSitePlusiP49722.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000015671.
GenevisibleiP49722. MM.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.2 Publications

Protein-protein interaction databases

BioGridi202416. 8 interactors.
IntActiP49722. 7 interactors.
MINTiMINT-4262697.
STRINGi10090.ENSMUSP00000129767.

Structurei

Secondary structure

1234
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Beta strandi15 – 17Combined sources3
Helixi20 – 30Combined sources11
Beta strandi35 – 39Combined sources5
Beta strandi44 – 49Combined sources6
Beta strandi53 – 55Combined sources3
Helixi59 – 61Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi72 – 78Combined sources7
Helixi80 – 101Combined sources22
Helixi107 – 120Combined sources14
Turni121 – 123Combined sources3
Beta strandi131 – 140Combined sources10
Beta strandi143 – 149Combined sources7
Beta strandi155 – 164Combined sources10
Helixi167 – 177Combined sources11
Helixi184 – 196Combined sources13
Turni205 – 207Combined sources3
Beta strandi208 – 214Combined sources7
Beta strandi217 – 220Combined sources4
Helixi223 – 229Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP49722.
SMRiP49722.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0181. Eukaryota.
ENOG410XPQ8. LUCA.
GeneTreeiENSGT00550000074870.
HOVERGENiHBG003005.
InParanoidiP49722.
KOiK02726.
OMAiWKATALG.
OrthoDBiEOG091G0GX6.
TreeFamiTF106207.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i4ECB56A233583821
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3E → K in CAA49782 (PubMed:7697131).Curated1

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.
UniGeneiMm.252255.

Genome annotation databases

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

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.
UniGeneiMm.252255.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP49722.
SMRiP49722.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202416. 8 interactors.
IntActiP49722. 7 interactors.
MINTiMINT-4262697.
STRINGi10090.ENSMUSP00000129767.

Protein family/group databases

MEROPSiT01.972.

PTM databases

iPTMnetiP49722.
PhosphoSitePlusiP49722.

2D gel databases

COMPLUYEAST-2DPAGEP49722.
REPRODUCTION-2DPAGEP49722.
SWISS-2DPAGEP49722.

Proteomic databases

EPDiP49722.
PaxDbiP49722.
PeptideAtlasiP49722.
PRIDEiP49722.
TopDownProteomicsiP49722.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5683.
MGIiMGI:104885. Psma2.

Phylogenomic databases

eggNOGiKOG0181. Eukaryota.
ENOG410XPQ8. LUCA.
GeneTreeiENSGT00550000074870.
HOVERGENiHBG003005.
InParanoidiP49722.
KOiK02726.
OMAiWKATALG.
OrthoDBiEOG091G0GX6.
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-174113. SCF-beta-TrCP mediated degradation of Emi1.
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-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
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-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiP49722.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000015671.
GenevisibleiP49722. MM.

Family and domain databases

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

Entry informationi

Entry nameiPSA2_MOUSE
AccessioniPrimary (citable) accession number: P49722
Secondary accession number(s): E9Q3A4, Q6ZWV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 31, 2012
Last modified: November 30, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.