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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

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

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, 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-446652. Interleukin-1 family signaling.
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-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs.
R-MMU-8941858. Regulation of RUNX3 expression and activity.
R-MMU-8948751. Regulation of PTEN stability and activity.
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:3.4.25.1By similarity)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:104885. Psma2.

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; Source: COMPARTMENTS

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-2DPAGEiP49722.
REPRODUCTION-2DPAGEiP49722.
SWISS-2DPAGEiP49722.

PTM databases

iPTMnetiP49722.
PhosphoSitePlusiP49722.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000015671.
ExpressionAtlasiP49722. baseline and differential.
GenevisibleiP49722. MM.

Interactioni

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

BioGridi202416. 8 interactors.
CORUMiP49722.
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.
OMAiSGAYFGW.
OrthoDBiEOG091G0GX6.
TreeFamiTF106207.

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.

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.

Similar proteinsi

Entry informationi

Entry nameiPSA2_MOUSE
AccessioniPrimary (citable) accession number: P49722
Secondary accession number(s): E9Q3A4, Q6ZWV8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 31, 2012
Last modified: October 25, 2017
This is version 151 of the entry and version 3 of the sequence. See 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