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O35955

- PSB10_MOUSE

UniProt

O35955 - PSB10_MOUSE

Protein

Proteasome subunit beta type-10

Gene

Psmb10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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. This subunit is involved in antigen processing to generate class I binding peptides. Plays a role in determining the T-cell repertoire for an antiviral T-cell response.1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei39 – 402Cleavage; by autocatalysis
    Active sitei40 – 401Nucleophile

    GO - Molecular functioni

    1. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cell morphogenesis Source: MGI
    2. proteolysis involved in cellular protein catabolic process Source: InterPro
    3. T cell proliferation Source: MGI

    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

    MEROPSiT01.014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-10 (EC:3.4.25.1)
    Alternative name(s):
    Low molecular mass protein 10
    Macropain subunit MECl-1
    Multicatalytic endopeptidase complex subunit MECl-1
    Proteasome MECl-1
    Proteasome subunit beta-2i
    Gene namesi
    Name:Psmb10
    Synonyms:Lmp10, Mecl1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1096380. Psmb10.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex Source: UniProtKB
    4. spermatoproteasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Disruption phenotypei

    Impaired response of cytotoxic T-lymphocyte (CTL) to dominant epitopes of lymphocytic choriomeningitis virus (LCMV).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401T → A: Prevents the correct removal of the propeptide. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 3939Removed in mature formPRO_0000026653Add
    BLAST
    Chaini40 – 273234Proteasome subunit beta type-10PRO_0000026654Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Post-translational modificationi

    Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity.

    Keywords - PTMi

    Acetylation, Zymogen

    Proteomic databases

    MaxQBiO35955.
    PaxDbiO35955.
    PRIDEiO35955.

    PTM databases

    PhosphoSiteiO35955.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Inductioni

    Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1.1 Publication

    Gene expression databases

    ArrayExpressiO35955.
    BgeeiO35955.
    GenevestigatoriO35955.

    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. Component of the immunoproteasome, where it displaces the equivalent houskeeping subunit PSMB7. Component of the spermatoproteasome, a form of the proteasome specifically found in testis.3 Publications

    Protein-protein interaction databases

    IntActiO35955. 5 interactions.
    MINTiMINT-4108870.

    Structurei

    Secondary structure

    1
    273
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi41 – 466
    Beta strandi48 – 558
    Beta strandi59 – 613
    Beta strandi64 – 696
    Beta strandi73 – 775
    Beta strandi80 – 878
    Helixi88 – 10922
    Helixi115 – 12814
    Turni129 – 1313
    Beta strandi135 – 1439
    Beta strandi146 – 1527
    Beta strandi158 – 1603
    Beta strandi162 – 1676
    Helixi170 – 18011
    Helixi187 – 20418
    Beta strandi205 – 2073
    Beta strandi212 – 2209
    Beta strandi222 – 2298
    Beta strandi250 – 2578

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNFX-ray2.90H/V40-273[»]
    3UNHX-ray3.20H/V40-273[»]
    ProteinModelPortaliO35955.
    SMRiO35955. Positions 40-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046533.
    HOGENOMiHOG000182856.
    HOVERGENiHBG093416.
    InParanoidiO35955.
    KOiK02733.
    OMAiQYRFAPG.
    OrthoDBiEOG7CRTQJ.
    PhylomeDBiO35955.
    TreeFamiTF106222.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR024689. Proteasome_bsu_C.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF12465. Pr_beta_C. 1 hit.
    PF00227. Proteasome. 1 hit.
    [Graphical view]
    PRINTSiPR00141. PROTEASOME.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O35955-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKQAVEPTG GFSFENCQRN ASLEHVLPGL RVPHARKTGT TIAGLVFRDG    50
    VILGADTRAT NDSVVADKSC EKIHFIAPKI YCCGAGVAAD TEMTTRMAAS 100
    KMELHALSTG REPRVATVTR ILRQTLFRYQ GHVGASLVVG GVDLNGPQLY 150
    EVHPHGSYSR LPFTALGSGQ GAAVALLEDR FQPNMTLEAA QELLVEAITA 200
    GILSDLGSGG NVDACVITAG GAKLQRALST PTEPVQRAGR YRFAPGTTPV 250
    LTREVRPLTL ELLEETVQAM EVE 273
    Length:273
    Mass (Da):29,063
    Last modified:January 1, 1998 - v1
    Checksum:i9A1AAE55888FA905
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41Q → E in AAH04730. (PubMed:15489334)Curated
    Sequence conflicti9 – 91T → R in AAH04730. (PubMed:15489334)Curated
    Sequence conflicti189 – 1891A → L in CAA71825. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77784 mRNA. Translation: AAB86994.1.
    U77785 Genomic DNA. Translation: AAB87637.1.
    D85561 mRNA. Translation: BAA22855.1.
    D85562 Genomic DNA. Translation: BAA22856.1.
    Y10875 mRNA. Translation: CAA71825.1.
    BC004730 mRNA. Translation: AAH04730.1.
    CCDSiCCDS22621.1.
    RefSeqiNP_038668.2. NM_013640.3.
    UniGeneiMm.787.

    Genome annotation databases

    EnsembliENSMUST00000034369; ENSMUSP00000034369; ENSMUSG00000031897.
    GeneIDi19171.
    KEGGimmu:19171.
    UCSCiuc009nep.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U77784 mRNA. Translation: AAB86994.1 .
    U77785 Genomic DNA. Translation: AAB87637.1 .
    D85561 mRNA. Translation: BAA22855.1 .
    D85562 Genomic DNA. Translation: BAA22856.1 .
    Y10875 mRNA. Translation: CAA71825.1 .
    BC004730 mRNA. Translation: AAH04730.1 .
    CCDSi CCDS22621.1.
    RefSeqi NP_038668.2. NM_013640.3.
    UniGenei Mm.787.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3UNF X-ray 2.90 H/V 40-273 [» ]
    3UNH X-ray 3.20 H/V 40-273 [» ]
    ProteinModelPortali O35955.
    SMRi O35955. Positions 40-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O35955. 5 interactions.
    MINTi MINT-4108870.

    Protein family/group databases

    MEROPSi T01.014.

    PTM databases

    PhosphoSitei O35955.

    Proteomic databases

    MaxQBi O35955.
    PaxDbi O35955.
    PRIDEi O35955.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034369 ; ENSMUSP00000034369 ; ENSMUSG00000031897 .
    GeneIDi 19171.
    KEGGi mmu:19171.
    UCSCi uc009nep.2. mouse.

    Organism-specific databases

    CTDi 5699.
    MGIi MGI:1096380. Psmb10.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046533.
    HOGENOMi HOG000182856.
    HOVERGENi HBG093416.
    InParanoidi O35955.
    KOi K02733.
    OMAi QYRFAPG.
    OrthoDBi EOG7CRTQJ.
    PhylomeDBi O35955.
    TreeFami TF106222.

    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

    ChiTaRSi PSMB10. mouse.
    NextBioi 295842.
    PROi O35955.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35955.
    Bgeei O35955.
    Genevestigatori O35955.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR024689. Proteasome_bsu_C.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF12465. Pr_beta_C. 1 hit.
    PF00227. Proteasome. 1 hit.
    [Graphical view ]
    PRINTSi PR00141. PROTEASOME.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence, chromosomal localization, and tissue expression of the mouse proteasome subunit lmp10 (Psmb10) gene."
      Cruz M., Elenich L.A., Smolarek T.A., Menon A.G., Monaco J.J.
      Genomics 45:618-622(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: 129/SvJ and BALB/c.
      Tissue: Liver.
    2. "The mouse genes encoding the third pair of beta-type proteasome subunits regulated reciprocally by IFN-gamma: structural comparison, chromosomal localization, and analysis of the promoter."
      Hayashi M., Ishibashi T., Tanaka K., Kasahara M.
      J. Immunol. 159:2760-2770(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: BALB/c and C57BL/6.
    3. "Molecular cloning of the mouse proteasome subunits MC14 and MECL-1: reciprocally regulated tisue expression of interferon-gamma-modulated proteasome subunits."
      Stohwasser R., Standera S., Peters I., Kloetzel P.-M., Groettrup M.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Spleen.
    4. "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].
    5. "Mutational analysis of subunit i beta2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes."
      Salzmann U., Kral S., Braun B., Standera S., Schmidt M., Kloetzel P.M., Sijts A.
      FEBS Lett. 454:11-15(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-40, AUTOCATALYTIC CLEAVAGE.
    6. "IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression of immunosubunits of the proteasome."
      Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y., Tsuchiya K., Okamoto R., Kanai T., Watanabe M.
      FEBS Lett. 579:2781-2787(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY INTERFERON GAMMA AND IRF1.
    7. "An altered T cell repertoire in MECL-1-deficient mice."
      Basler M., Moebius J., Elenich L., Groettrup M., Monaco J.J.
      J. Immunol. 176:6665-6672(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    8. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
    9. Cited for: IDENTIFICATION IN THE SPERMATOPROTEASOME.
    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 nameiPSB10_MOUSE
    AccessioniPrimary (citable) accession number: O35955
    Secondary accession number(s): O08687, Q99KC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 123 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, 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