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Q9Z2U1

- PSA5_MOUSE

UniProt

Q9Z2U1 - PSA5_MOUSE

Protein

Proteasome subunit alpha type-5

Gene

Psma5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    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

    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

    MEROPSiT01.975.

    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: Chromosome 3

    Organism-specific databases

    MGIiMGI:1347009. Psma5.

    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

    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

    ArrayExpressiQ9Z2U1.
    BgeeiQ9Z2U1.
    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 – 213
    Helixi22 – 3110
    Beta strandi37 – 426
    Beta strandi45 – 517
    Helixi61 – 633
    Beta strandi67 – 715
    Beta strandi74 – 807
    Helixi82 – 10322
    Helixi109 – 1179
    Turni118 – 1214
    Beta strandi125 – 1273
    Beta strandi133 – 1353
    Beta strandi139 – 1468
    Beta strandi151 – 1566
    Beta strandi162 – 17110
    Helixi174 – 18411
    Helixi191 – 20515
    Turni212 – 2143
    Beta strandi215 – 2206
    Beta strandi222 – 2243
    Helixi231 – 2388

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiCAMSGLT.
    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

    MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV    50
    EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW 100
    FTYNETMTVE SVTQAVSNLA LQFGEEDADP GAMSRPFGVA LLFGGVDEKG 150
    PQLFHMDPSG TFVQCDARAI GSASEGAQSS LQEVYHKSMT LKEAIKSSLI 200
    ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD I 241
    Length:241
    Mass (Da):26,411
    Last modified:May 1, 1999 - v1
    Checksum:i5610CDA00469120A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019661 mRNA. Translation: AAC69149.1 .
    BC010709 mRNA. Translation: AAH10709.1 .
    BC083342 mRNA. Translation: AAH83342.1 .
    CCDSi CCDS17755.1.
    RefSeqi NP_036097.1. NM_011967.3.
    UniGenei Mm.208883.

    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 D/R/f/t 1-241 [» ]
    3UNE X-ray 3.20 D/R/f/t 1-241 [» ]
    3UNF X-ray 2.90 D/R 1-241 [» ]
    3UNH X-ray 3.20 D/R 1-241 [» ]
    ProteinModelPortali Q9Z2U1.
    SMRi Q9Z2U1. Positions 9-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204993. 3 interactions.
    IntActi Q9Z2U1. 6 interactions.
    MINTi MINT-1856766.

    Protein family/group databases

    MEROPSi T01.975.

    PTM databases

    PhosphoSitei Q9Z2U1.

    2D gel databases

    REPRODUCTION-2DPAGE Q9Z2U1.

    Proteomic databases

    MaxQBi Q9Z2U1.
    PaxDbi Q9Z2U1.
    PRIDEi Q9Z2U1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090569 ; ENSMUSP00000088057 ; ENSMUSG00000068749 .
    GeneIDi 26442.
    KEGGi mmu:26442.
    UCSCi uc008qyq.1. mouse.

    Organism-specific databases

    CTDi 5686.
    MGIi MGI:1347009. Psma5.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074958.
    HOGENOMi HOG000091085.
    HOVERGENi HBG003005.
    InParanoidi Q9Z2U1.
    KOi K02729.
    OMAi CAMSGLT.
    OrthoDBi EOG769ZKB.
    PhylomeDBi Q9Z2U1.
    TreeFami TF106211.

    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 304525.
    PROi Q9Z2U1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2U1.
    Bgeei Q9Z2U1.
    Genevestigatori Q9Z2U1.

    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

    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(2004) [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 (JUL-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(2012) [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(2012) [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: October 1, 2014
    This is version 132 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