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Protein

Proteasome subunit alpha type-5

Gene

Psma5

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.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. 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_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_275732. degradation of AXIN.
REACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_289441. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_294625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_297888. degradation of DVL.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_301078. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_308964. ER-Phagosome pathway.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_315933. Orc1 removal from chromatin.
REACT_321346. Separation of Sister Chromatids.
REACT_324511. Degradation of GLI1 by the proteasome.
REACT_326233. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329431. APC/C:Cdc20 mediated degradation of Securin.
REACT_331452. Hh ligand biogenesis disease.
REACT_334737. Regulation of ornithine decarboxylase (ODC).
REACT_336463. CDK-mediated phosphorylation and removal of Cdc6.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_337766. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_341075. ER-Phagosome pathway.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_343561. CDT1 association with the CDC6:ORC:origin complex.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345193. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_347264. Hedgehog ligand biogenesis.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.

Protein family/group databases

MEROPSiT01.975.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain zeta chain
Multicatalytic endopeptidase complex zeta chain
Proteasome zeta chain
Gene namesi
Name:Psma5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1347009. Psma5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: MGI
  4. nucleoplasm Source: MGI
  5. nucleus Source: MGI
  6. proteasome complex Source: MGI
  7. proteasome core complex Source: UniProtKB
  8. 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
Chaini1 – 241241Proteasome subunit alpha type-5PRO_0000124118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei16 – 161PhosphoserineBy similarity
Modified residuei55 – 551PhosphothreonineBy similarity
Modified residuei56 – 561PhosphoserineBy similarity
Glycosylationi198 – 1981O-linked (GlcNAc)1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9Z2U1.
PaxDbiQ9Z2U1.
PRIDEiQ9Z2U1.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2U1.

PTM databases

PhosphoSiteiQ9Z2U1.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiQ9Z2U1.
ExpressionAtlasiQ9Z2U1. baseline and differential.
GenevestigatoriQ9Z2U1.

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. PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.2 Publications

Protein-protein interaction databases

BioGridi204993. 3 interactions.
IntActiQ9Z2U1. 6 interactions.
MINTiMINT-1856766.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 213Combined sources
Helixi22 – 3110Combined sources
Beta strandi37 – 426Combined sources
Beta strandi45 – 517Combined sources
Helixi61 – 633Combined sources
Beta strandi67 – 715Combined sources
Beta strandi74 – 807Combined sources
Helixi82 – 10322Combined sources
Helixi109 – 1179Combined sources
Turni118 – 1214Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi162 – 17110Combined sources
Helixi174 – 18411Combined sources
Helixi191 – 20515Combined sources
Turni212 – 2143Combined sources
Beta strandi215 – 2206Combined sources
Beta strandi222 – 2243Combined sources
Helixi231 – 2388Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90D/R/f/t1-241[»]
3UNEX-ray3.20D/R/f/t1-241[»]
3UNFX-ray2.90D/R1-241[»]
3UNHX-ray3.20D/R1-241[»]
ProteinModelPortaliQ9Z2U1.
SMRiQ9Z2U1. Positions 9-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074958.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9Z2U1.
KOiK02729.
OMAiKLDQHNV.
OrthoDBiEOG769ZKB.
PhylomeDBiQ9Z2U1.
TreeFamiTF106211.

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.

Q9Z2U1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV
60 70 80 90 100
EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW
110 120 130 140 150
FTYNETMTVE SVTQAVSNLA LQFGEEDADP GAMSRPFGVA LLFGGVDEKG
160 170 180 190 200
PQLFHMDPSG TFVQCDARAI GSASEGAQSS LQEVYHKSMT LKEAIKSSLI
210 220 230 240
ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD I
Length:241
Mass (Da):26,411
Last modified:May 1, 1999 - v1
Checksum:i5610CDA00469120A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019661 mRNA. Translation: AAC69149.1.
BC010709 mRNA. Translation: AAH10709.1.
BC083342 mRNA. Translation: AAH83342.1.
CCDSiCCDS17755.1.
RefSeqiNP_036097.1. NM_011967.3.
UniGeneiMm.208883.

Genome annotation databases

EnsembliENSMUST00000090569; ENSMUSP00000088057; ENSMUSG00000068749.
GeneIDi26442.
KEGGimmu:26442.
UCSCiuc008qyq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019661 mRNA. Translation: AAC69149.1.
BC010709 mRNA. Translation: AAH10709.1.
BC083342 mRNA. Translation: AAH83342.1.
CCDSiCCDS17755.1.
RefSeqiNP_036097.1. NM_011967.3.
UniGeneiMm.208883.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90D/R/f/t1-241[»]
3UNEX-ray3.20D/R/f/t1-241[»]
3UNFX-ray2.90D/R1-241[»]
3UNHX-ray3.20D/R1-241[»]
ProteinModelPortaliQ9Z2U1.
SMRiQ9Z2U1. Positions 9-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204993. 3 interactions.
IntActiQ9Z2U1. 6 interactions.
MINTiMINT-1856766.

Protein family/group databases

MEROPSiT01.975.

PTM databases

PhosphoSiteiQ9Z2U1.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2U1.

Proteomic databases

MaxQBiQ9Z2U1.
PaxDbiQ9Z2U1.
PRIDEiQ9Z2U1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090569; ENSMUSP00000088057; ENSMUSG00000068749.
GeneIDi26442.
KEGGimmu:26442.
UCSCiuc008qyq.1. mouse.

Organism-specific databases

CTDi5686.
MGIiMGI:1347009. Psma5.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074958.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9Z2U1.
KOiK02729.
OMAiKLDQHNV.
OrthoDBiEOG769ZKB.
PhylomeDBiQ9Z2U1.
TreeFamiTF106211.

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_275732. degradation of AXIN.
REACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_289441. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_294625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_297888. degradation of DVL.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_301078. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_308964. ER-Phagosome pathway.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_315933. Orc1 removal from chromatin.
REACT_321346. Separation of Sister Chromatids.
REACT_324511. Degradation of GLI1 by the proteasome.
REACT_326233. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329431. APC/C:Cdc20 mediated degradation of Securin.
REACT_331452. Hh ligand biogenesis disease.
REACT_334737. Regulation of ornithine decarboxylase (ODC).
REACT_336463. CDK-mediated phosphorylation and removal of Cdc6.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_337766. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_341075. ER-Phagosome pathway.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_343561. CDT1 association with the CDC6:ORC:origin complex.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345193. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_347264. Hedgehog ligand biogenesis.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.

Miscellaneous databases

NextBioi304525.
PROiQ9Z2U1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2U1.
ExpressionAtlasiQ9Z2U1. baseline and differential.
GenevestigatoriQ9Z2U1.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: B10.A.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Mammary tumor.
  3. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUN-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 21-32.
    Tissue: Brain.
  4. "Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag."
    Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A., Siele D., Kloetzel P.M., Janek K.
    Mol. Cell. Proteomics 11:467-477(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-198.
    Tissue: Brain and Spleen.
  5. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX, ACETYLATION AT MET-1.
  6. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPSA5_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 1999
Last modified: April 1, 2015
This is version 138 of the entry and version 1 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

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 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.