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O70435

- PSA3_MOUSE

UniProt

O70435 - PSA3_MOUSE

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Protein

Proteasome subunit alpha type-3

Gene
Psma3
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. protein binding Source: MGI
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Protein family/group databases

MEROPSiT01.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8
Proteasome subunit K
Gene namesi
Name:Psma3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:104883. Psma3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: UniProtKB
  4. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed Inferred
Chaini2 – 255254Proteasome subunit alpha type-3PRO_0000124092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei57 – 571N6-acetyllysine1 Publication
Modified residuei206 – 2061N6-acetyllysine By similarity
Modified residuei230 – 2301N6-acetyllysine By similarity
Modified residuei243 – 2431Phosphoserine By similarity
Modified residuei250 – 2501Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO70435.
PaxDbiO70435.
PRIDEiO70435.

PTM databases

PhosphoSiteiO70435.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiO70435.
GenevestigatoriO70435.

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. Interacts with AURKB.2 Publications

Protein-protein interaction databases

BioGridi202417. 1 interaction.
IntActiO70435. 9 interactions.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106
Helixi22 – 3211
Beta strandi37 – 426
Beta strandi45 – 539
Beta strandi67 – 715
Beta strandi74 – 807
Helixi82 – 10322
Helixi109 – 12214
Beta strandi125 – 1295
Beta strandi134 – 1407
Turni143 – 1453
Beta strandi148 – 1525
Beta strandi158 – 16710
Helixi170 – 1778
Turni182 – 1843
Helixi187 – 20115
Turni204 – 2063
Beta strandi210 – 2189
Turni219 – 2235
Helixi230 – 24213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90F/T/h/v1-255[»]
3UNEX-ray3.20F/T/h/v1-255[»]
3UNFX-ray2.90F/T1-255[»]
3UNHX-ray3.20F/T1-255[»]
ProteinModelPortaliO70435.
SMRiO70435. Positions 2-245.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.

Phylogenomic databases

eggNOGiCOG0638.
HOVERGENiHBG105566.
InParanoidiO70435.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG73JKW6.
PhylomeDBiO70435.
TreeFamiTF106208.

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.

O70435-1 [UniParc]FASTAAdd to Basket

« Hide

MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV    50
EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR 100
SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSANDGAQLY 150
MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL QMKEMTCRDV VKEVAKIIYI 200
VHDEVKDKAF ELELSWVGEL TKGRHEIVPK DIREEAEKYA KESLKEEDES 250
DDDNM 255
Length:255
Mass (Da):28,405
Last modified:January 23, 2007 - v3
Checksum:iCFB4405E143CEB23
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF055983 mRNA. Translation: AAC12943.1.
AF060089 mRNA. Translation: AAD50534.1.
CCDSiCCDS25961.1.
RefSeqiNP_035314.3. NM_011184.4.
UniGeneiMm.296338.

Genome annotation databases

EnsembliENSMUST00000160027; ENSMUSP00000125548; ENSMUSG00000060073.
GeneIDi19167.
KEGGimmu:19167.
UCSCiuc007ntz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF055983 mRNA. Translation: AAC12943.1 .
AF060089 mRNA. Translation: AAD50534.1 .
CCDSi CCDS25961.1.
RefSeqi NP_035314.3. NM_011184.4.
UniGenei Mm.296338.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNB X-ray 2.90 F/T/h/v 1-255 [» ]
3UNE X-ray 3.20 F/T/h/v 1-255 [» ]
3UNF X-ray 2.90 F/T 1-255 [» ]
3UNH X-ray 3.20 F/T 1-255 [» ]
ProteinModelPortali O70435.
SMRi O70435. Positions 2-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202417. 1 interaction.
IntActi O70435. 9 interactions.

Protein family/group databases

MEROPSi T01.977.

PTM databases

PhosphoSitei O70435.

Proteomic databases

MaxQBi O70435.
PaxDbi O70435.
PRIDEi O70435.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000160027 ; ENSMUSP00000125548 ; ENSMUSG00000060073 .
GeneIDi 19167.
KEGGi mmu:19167.
UCSCi uc007ntz.2. mouse.

Organism-specific databases

CTDi 5684.
MGIi MGI:104883. Psma3.

Phylogenomic databases

eggNOGi COG0638.
HOVERGENi HBG105566.
InParanoidi O70435.
KOi K02727.
OMAi VPDGRHF.
OrthoDBi EOG73JKW6.
PhylomeDBi O70435.
TreeFami TF106208.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Miscellaneous databases

NextBioi 295834.
PROi O70435.
SOURCEi Search...

Gene expression databases

Bgeei O70435.
Genevestigatori O70435.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Gao Y., Simons M.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  3. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 73-86.
    Tissue: Brain.
  4. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX, ACETYLATION AT SER-2.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity."
    Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M.
    Cell 148:727-738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPSA3_MOUSE
AccessioniPrimary (citable) accession number: O70435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 122 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

External Data

Dasty 3

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