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Q9R1P4

- PSA1_MOUSE

UniProt

Q9R1P4 - PSA1_MOUSE

Protein

Proteasome subunit alpha type-1

Gene

Psma1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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. Mediates the lipopolysaccharide-induced signal macrophage proteasome. Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells.3 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. lipopolysaccharide binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. immune system process Source: UniProtKB-KW
    2. negative regulation of inflammatory response to antigenic stimulus Source: UniProtKB
    3. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Immunity

    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

    MEROPSiT01.976.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-1 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C2
    Multicatalytic endopeptidase complex subunit C2
    Proteasome component C2
    Proteasome nu chain
    Gene namesi
    Name:Psma1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1347005. Psma1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome complex Source: MGI
    4. proteasome core complex Source: UniProtKB
    5. 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 – 263263Proteasome subunit alpha type-1PRO_0000124062Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei14 – 141PhosphoserineBy similarity
    Glycosylationi110 – 1101O-linked (GlcNAc)1 Publication
    Cross-linki115 – 115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki208 – 208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    C-terminal extension is partially cleaved off by limited proteolysis leading to a conversion of the proteasome from its latent into its active form.

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9R1P4.
    PaxDbiQ9R1P4.
    PRIDEiQ9R1P4.

    2D gel databases

    COMPLUYEAST-2DPAGEQ9R1P4.
    REPRODUCTION-2DPAGEIPI00283862.
    Q9R1P4.

    PTM databases

    PhosphoSiteiQ9R1P4.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Inductioni

    Up-regulated in liver tumor tissues. Up-regulated by the antioxidant dithiolethione (D3T) in liver, lung and colon (at the protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ9R1P4.
    BgeeiQ9R1P4.
    GenevestigatoriQ9R1P4.

    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 bacterial lipopolysaccharide (LPS). Interacts with NOTCH3.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NOTCH3Q9UM472EBI-991653,EBI-1236377From a different organism.

    Protein-protein interaction databases

    BioGridi204991. 5 interactions.
    DIPiDIP-35147N.
    IntActiQ9R1P4. 20 interactions.
    MINTiMINT-1856889.

    Structurei

    Secondary structure

    1
    263
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Helixi20 – 3112
    Beta strandi35 – 395
    Beta strandi41 – 499
    Beta strandi53 – 575
    Beta strandi63 – 653
    Beta strandi67 – 7610
    Helixi78 – 9821
    Beta strandi99 – 1013
    Helixi105 – 11713
    Helixi118 – 1203
    Beta strandi130 – 1389
    Beta strandi141 – 1477
    Beta strandi149 – 1513
    Beta strandi153 – 16311
    Helixi166 – 1749
    Turni176 – 1783
    Helixi179 – 1813
    Helixi184 – 19512
    Turni196 – 1983
    Turni207 – 2093
    Beta strandi210 – 21910
    Beta strandi222 – 2243
    Turni227 – 2293
    Helixi230 – 2334

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.90E/S/g/u1-263[»]
    3UNEX-ray3.20E/S/g/u1-263[»]
    3UNFX-ray2.90E/S1-263[»]
    3UNHX-ray3.20E/S1-263[»]
    ProteinModelPortaliQ9R1P4.
    SMRiQ9R1P4. Positions 4-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074855.
    HOGENOMiHOG000091080.
    HOVERGENiHBG105373.
    InParanoidiQ9R1P4.
    KOiK02725.
    OMAiFMKQQCL.
    OrthoDBiEOG7WQ7T1.
    PhylomeDBiQ9R1P4.
    TreeFamiTF106206.

    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.

    Q9R1P4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK    50
    RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD 100
    RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS 150
    ANYFDCRAMS IGARSQSART YLERHMSEFM ECNLDELVKH GLRALRETLP 200
    AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP QRKAQPSQAA 250
    EEPAEKADEP MEH 263
    Length:263
    Mass (Da):29,547
    Last modified:May 1, 2000 - v1
    Checksum:iCC791C56AFBA8043
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060088 mRNA. Translation: AAD50533.1.
    AJ272019 mRNA. Translation: CAB95966.1.
    AJ272272 Genomic DNA. Translation: CAB95969.1.
    BC005762 mRNA. Translation: AAH05762.1.
    CCDSiCCDS40094.1.
    RefSeqiNP_036095.1. NM_011965.2.
    UniGeneiMm.121265.

    Genome annotation databases

    EnsembliENSMUST00000033008; ENSMUSP00000033008; ENSMUSG00000030751.
    GeneIDi26440.
    KEGGimmu:26440.
    UCSCiuc009jhy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060088 mRNA. Translation: AAD50533.1 .
    AJ272019 mRNA. Translation: CAB95966.1 .
    AJ272272 Genomic DNA. Translation: CAB95969.1 .
    BC005762 mRNA. Translation: AAH05762.1 .
    CCDSi CCDS40094.1.
    RefSeqi NP_036095.1. NM_011965.2.
    UniGenei Mm.121265.

    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 E/S/g/u 1-263 [» ]
    3UNE X-ray 3.20 E/S/g/u 1-263 [» ]
    3UNF X-ray 2.90 E/S 1-263 [» ]
    3UNH X-ray 3.20 E/S 1-263 [» ]
    ProteinModelPortali Q9R1P4.
    SMRi Q9R1P4. Positions 4-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204991. 5 interactions.
    DIPi DIP-35147N.
    IntActi Q9R1P4. 20 interactions.
    MINTi MINT-1856889.

    Protein family/group databases

    MEROPSi T01.976.

    PTM databases

    PhosphoSitei Q9R1P4.

    2D gel databases

    COMPLUYEAST-2DPAGE Q9R1P4.
    REPRODUCTION-2DPAGE IPI00283862.
    Q9R1P4.

    Proteomic databases

    MaxQBi Q9R1P4.
    PaxDbi Q9R1P4.
    PRIDEi Q9R1P4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033008 ; ENSMUSP00000033008 ; ENSMUSG00000030751 .
    GeneIDi 26440.
    KEGGi mmu:26440.
    UCSCi uc009jhy.1. mouse.

    Organism-specific databases

    CTDi 5682.
    MGIi MGI:1347005. Psma1.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074855.
    HOGENOMi HOG000091080.
    HOVERGENi HBG105373.
    InParanoidi Q9R1P4.
    KOi K02725.
    OMAi FMKQQCL.
    OrthoDBi EOG7WQ7T1.
    PhylomeDBi Q9R1P4.
    TreeFami TF106206.

    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 304517.
    PROi Q9R1P4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R1P4.
    Bgeei Q9R1P4.
    Genevestigatori Q9R1P4.

    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 mouse Psma1 gene coding for the alpha-type C2 proteasome subunit: structural and functional analysis, mapping, and colocalization with Pde3b on mouse chromosome 7."
      Hopitzan A., Himmelbauer H., Spevak W., Castanon M.J.
      Genomics 66:313-323(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Skeletal muscle.
    3. "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-3.
      Tissue: Mammary gland.
    4. Lubec G., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 63-82 AND 97-107, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Hippocampus.
    5. "The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events."
      Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G., Morrison D.C., Vogel S.N.
      J. Immunol. 171:1515-1525(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LPS.
    6. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
    7. "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.
    8. "Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: enhanced activity for degradation of abnormal protein."
      Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.
      Life Sci. 80:2411-2420(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY DITHIOLETHIONE.
    9. "Proteomics of RAW 264.7 macrophages upon interaction with heat-inactivated Candida albicans cells unravel an anti-inflammatory response."
      Martinez-Solano L., Reales-Calderon J.A., Nombela C., Molero G., Gil C.
      Proteomics 9:2995-3010(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "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-110.
      Tissue: Brain and Spleen.
    11. "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 nameiPSA1_MOUSE
    AccessioniPrimary (citable) accession number: Q9R1P4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 125 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