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Q9Z2U0

- PSA7_MOUSE

UniProt

Q9Z2U0 - PSA7_MOUSE

Protein

Proteasome subunit alpha type-7

Gene

Psma7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (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. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions By similarity. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions By similarity. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response By similarity.By similarity

    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

    MEROPSiT01.979.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-7 (EC:3.4.25.1)
    Alternative name(s):
    Proteasome subunit RC6-1
    Gene namesi
    Name:Psma7
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1347070. Psma7.

    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 – 248248Proteasome subunit alpha type-7PRO_0000124143Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi130 – 1301O-linked (GlcNAc)1 Publication
    Modified residuei153 – 1531Phosphotyrosine; by ABL1 and ABL2By similarity
    Modified residuei227 – 2271N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks.

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z2U0.
    PaxDbiQ9Z2U0.
    PRIDEiQ9Z2U0.

    2D gel databases

    REPRODUCTION-2DPAGEQ9Z2U0.

    PTM databases

    PhosphoSiteiQ9Z2U0.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Inductioni

    Up-regulated in liver tumor tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9Z2U0.
    BgeeiQ9Z2U0.
    GenevestigatoriQ9Z2U0.

    Interactioni

    Subunit structurei

    PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly. Interacts with HIF1A By similarity. Interacts with RAB7A By similarity. Interacts with PARK2 By similarity. Interacts with EMAP2 By similarity. Interacts with MAVS By similarity. 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.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi204995. 3 interactions.
    IntActiQ9Z2U0. 5 interactions.
    MINTiMINT-1856843.

    Structurei

    Secondary structure

    1
    248
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 2711
    Beta strandi32 – 365
    Beta strandi38 – 458
    Beta strandi52 – 543
    Turni56 – 594
    Beta strandi62 – 643
    Beta strandi66 – 7510
    Helixi77 – 9721
    Beta strandi98 – 1003
    Helixi104 – 11714
    Beta strandi120 – 1223
    Beta strandi129 – 1368
    Beta strandi142 – 1476
    Beta strandi153 – 16210
    Helixi165 – 17511
    Turni178 – 1814
    Helixi184 – 19512
    Turni196 – 1983
    Beta strandi199 – 2013
    Beta strandi203 – 2053
    Beta strandi207 – 2159
    Beta strandi217 – 2193
    Helixi222 – 23615

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.90C/Q/e/s1-248[»]
    3UNEX-ray3.20C/Q/e/s1-248[»]
    3UNFX-ray2.90C/Q1-248[»]
    3UNHX-ray3.20C/Q1-248[»]
    ProteinModelPortaliQ9Z2U0.
    SMRiQ9Z2U0. Positions 2-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074753.
    HOGENOMiHOG000091085.
    HOVERGENiHBG003005.
    InParanoidiQ9Z2U0.
    KOiK02731.
    OMAiITRHIAG.
    OrthoDBiEOG71VSTG.
    PhylomeDBiQ9Z2U0.
    TreeFamiTF106212.

    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.

    Q9Z2U0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGKDI VVLGVEKKSV    50
    AKLQDERTVR KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED 100
    PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS 150
    GTYHAWKANA IGRGAKSVRE FLEKNYTDDA IETDDLTIKL VIKALLEVVQ 200
    SGGKNIELAV MRRDQPLKIL NPEEIEKYVA EIEKEKEENE KKKQKKAS 248
    Length:248
    Mass (Da):27,855
    Last modified:May 1, 1999 - v1
    Checksum:iE2C8D607D8E2BC9C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019662 mRNA. Translation: AAC69150.1.
    BC008222 mRNA. Translation: AAH08222.1.
    CCDSiCCDS17166.1.
    RefSeqiNP_036099.1. NM_011969.2.
    UniGeneiMm.21728.

    Genome annotation databases

    EnsembliENSMUST00000029082; ENSMUSP00000029082; ENSMUSG00000027566.
    GeneIDi26444.
    KEGGimmu:26444.
    UCSCiuc008oib.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019662 mRNA. Translation: AAC69150.1 .
    BC008222 mRNA. Translation: AAH08222.1 .
    CCDSi CCDS17166.1.
    RefSeqi NP_036099.1. NM_011969.2.
    UniGenei Mm.21728.

    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 C/Q/e/s 1-248 [» ]
    3UNE X-ray 3.20 C/Q/e/s 1-248 [» ]
    3UNF X-ray 2.90 C/Q 1-248 [» ]
    3UNH X-ray 3.20 C/Q 1-248 [» ]
    ProteinModelPortali Q9Z2U0.
    SMRi Q9Z2U0. Positions 2-239.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204995. 3 interactions.
    IntActi Q9Z2U0. 5 interactions.
    MINTi MINT-1856843.

    Protein family/group databases

    MEROPSi T01.979.

    PTM databases

    PhosphoSitei Q9Z2U0.

    2D gel databases

    REPRODUCTION-2DPAGE Q9Z2U0.

    Proteomic databases

    MaxQBi Q9Z2U0.
    PaxDbi Q9Z2U0.
    PRIDEi Q9Z2U0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029082 ; ENSMUSP00000029082 ; ENSMUSG00000027566 .
    GeneIDi 26444.
    KEGGi mmu:26444.
    UCSCi uc008oib.1. mouse.

    Organism-specific databases

    CTDi 5688.
    MGIi MGI:1347070. Psma7.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074753.
    HOGENOMi HOG000091085.
    HOVERGENi HBG003005.
    InParanoidi Q9Z2U0.
    KOi K02731.
    OMAi ITRHIAG.
    OrthoDBi EOG71VSTG.
    PhylomeDBi Q9Z2U0.
    TreeFami TF106212.

    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 304533.
    PROi Q9Z2U0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2U0.
    Bgeei Q9Z2U0.
    Genevestigatori Q9Z2U0.

    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.BR.
    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: FVB/N.
      Tissue: Mammary tumor.
    3. Lubec G., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 96-109.
      Tissue: Brain.
    4. "The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice."
      Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X.
      Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    5. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
    6. "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-130.
      Tissue: Brain and Spleen.
    7. "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 nameiPSA7_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 119 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