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Q9R1P3

- PSB2_MOUSE

UniProt

Q9R1P3 - PSB2_MOUSE

Protein

Proteasome subunit beta type-2

Gene

Psmb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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. This subunit has a chymotrypsin-like activity.1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    GO - Molecular functioni

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

    GO - Biological processi

    1. proteolysis involved in cellular protein catabolic process Source: InterPro
    2. response to organic cyclic compound Source: Ensembl
    3. response to organonitrogen compound Source: Ensembl

    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

    MEROPSiT01.984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-2 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C7-I
    Multicatalytic endopeptidase complex subunit C7-I
    Proteasome component C7-I
    Gene namesi
    Name:Psmb2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1347045. Psmb2.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201Proteasome subunit beta type-2PRO_0000148044Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9R1P3.
    PaxDbiQ9R1P3.
    PRIDEiQ9R1P3.

    2D gel databases

    REPRODUCTION-2DPAGEQ9R1P3.

    PTM databases

    PhosphoSiteiQ9R1P3.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9R1P3.
    GenevestigatoriQ9R1P3.

    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.2 Publications

    Protein-protein interaction databases

    BioGridi204996. 2 interactions.
    IntActiQ9R1P3. 7 interactions.
    MINTiMINT-1856775.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi13 – 186
    Beta strandi21 – 233
    Beta strandi26 – 316
    Beta strandi35 – 373
    Beta strandi39 – 4911
    Helixi52 – 7120
    Helixi77 – 9216
    Beta strandi94 – 963
    Beta strandi100 – 1089
    Turni109 – 1113
    Beta strandi112 – 1187
    Beta strandi124 – 1263
    Beta strandi128 – 1336
    Helixi136 – 14510
    Helixi153 – 16917
    Beta strandi171 – 1733
    Beta strandi178 – 1847
    Beta strandi187 – 1904

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.90J/X/l/z1-201[»]
    3UNEX-ray3.20J/X/l/z1-201[»]
    3UNFX-ray2.90J/X1-201[»]
    3UNHX-ray3.20J/X1-201[»]
    ProteinModelPortaliQ9R1P3.
    SMRiQ9R1P3. Positions 1-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00640000091536.
    HOGENOMiHOG000188743.
    HOVERGENiHBG000815.
    InParanoidiQ9R1P3.
    KOiK02734.
    OMAiHFVRGEL.
    OrthoDBiEOG7N63NQ.
    PhylomeDBiQ9R1P3.
    TreeFamiTF106219.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9R1P3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA    50
    GDTVQFAEYI QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV 100
    NLLLAGYDEH EGPALYYMDY LAALAKAPFA AHGYGAFLTL SILDRYYTPT 150
    ISRERAVELL RKCLEELQKR FILNLPTFSV RVIDKDGIHN LENIAFPKRD 200
    S 201
    Length:201
    Mass (Da):22,906
    Last modified:May 1, 2000 - v1
    Checksum:iE9B3121974777958
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060090 mRNA. Translation: AAD50535.1.
    BC008265 mRNA. Translation: AAH08265.1.
    CCDSiCCDS18657.1.
    RefSeqiNP_036100.3. NM_011970.4.
    UniGeneiMm.22233.

    Genome annotation databases

    EnsembliENSMUST00000030642; ENSMUSP00000030642; ENSMUSG00000028837.
    GeneIDi26445.
    KEGGimmu:26445.
    UCSCiuc008utr.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060090 mRNA. Translation: AAD50535.1 .
    BC008265 mRNA. Translation: AAH08265.1 .
    CCDSi CCDS18657.1.
    RefSeqi NP_036100.3. NM_011970.4.
    UniGenei Mm.22233.

    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 J/X/l/z 1-201 [» ]
    3UNE X-ray 3.20 J/X/l/z 1-201 [» ]
    3UNF X-ray 2.90 J/X 1-201 [» ]
    3UNH X-ray 3.20 J/X 1-201 [» ]
    ProteinModelPortali Q9R1P3.
    SMRi Q9R1P3. Positions 1-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204996. 2 interactions.
    IntActi Q9R1P3. 7 interactions.
    MINTi MINT-1856775.

    Protein family/group databases

    MEROPSi T01.984.

    PTM databases

    PhosphoSitei Q9R1P3.

    2D gel databases

    REPRODUCTION-2DPAGE Q9R1P3.

    Proteomic databases

    MaxQBi Q9R1P3.
    PaxDbi Q9R1P3.
    PRIDEi Q9R1P3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030642 ; ENSMUSP00000030642 ; ENSMUSG00000028837 .
    GeneIDi 26445.
    KEGGi mmu:26445.
    UCSCi uc008utr.2. mouse.

    Organism-specific databases

    CTDi 5690.
    MGIi MGI:1347045. Psmb2.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00640000091536.
    HOGENOMi HOG000188743.
    HOVERGENi HBG000815.
    InParanoidi Q9R1P3.
    KOi K02734.
    OMAi HFVRGEL.
    OrthoDBi EOG7N63NQ.
    PhylomeDBi Q9R1P3.
    TreeFami TF106219.

    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 PSMB2. mouse.
    NextBioi 304537.
    PROi Q9R1P3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R1P3.
    Genevestigatori Q9R1P3.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
    PS51476. PROTEASOME_BETA_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: C57BL/6J.
      Tissue: Mammary gland.
    3. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 71-85; 127-145 AND 171-198, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    4. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
    5. "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 nameiPSB2_MOUSE
    AccessioniPrimary (citable) accession number: Q9R1P3
    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