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O55234

- PSB5_MOUSE

UniProt

O55234 - PSB5_MOUSE

Protein

Proteasome subunit beta type-5

Gene

Psmb5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 3 (29 Apr 2008)
      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 unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib By similarity. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway.By similarity1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei60 – 601NucleophileBy similarity
    Binding sitei108 – 1081Bortezomib; via amide nitrogenBy similarity

    GO - Molecular functioni

    1. peptidase activity Source: MGI
    2. threonine-type endopeptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
    2. response to oxidative stress 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.P01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-5 (EC:3.4.25.1)
    Alternative name(s):
    Macropain epsilon chain
    Multicatalytic endopeptidase complex epsilon chain
    Proteasome chain 6
    Proteasome epsilon chain
    Proteasome subunit X
    Gene namesi
    Name:Psmb5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1194513. Psmb5.

    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
    Propeptidei1 – 5959Removed in mature formBy similarityPRO_0000026591Add
    BLAST
    Chaini60 – 264205Proteasome subunit beta type-5PRO_0000026592Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiO55234.
    PaxDbiO55234.
    PRIDEiO55234.

    PTM databases

    PhosphoSiteiO55234.

    Expressioni

    Tissue specificityi

    Expressed in uterus at the embryo implantation site.1 Publication

    Inductioni

    Up-regulated in embryonic fibroblasts and neuroblastoma cells by antioxidants through the Nrf2-ARE pathway (at protein level). Up-regulated by the antioxidant dithiolethione (D3T) in liver, small intestine and brain (at protein level). Down-regulated under lithium treatment.4 Publications

    Gene expression databases

    BgeeiO55234.
    GenevestigatoriO55234.

    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. This subunit can be displaced by the equivalent immune-specific subunit PSMB8. Directly interacts with POMP. Interacts with ABCB1 and TAP1.1 Publication

    Protein-protein interaction databases

    BioGridi202421. 4 interactions.
    IntActiO55234. 7 interactions.
    MINTiMINT-4125600.

    Structurei

    Secondary structure

    1
    264
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 677
    Beta strandi70 – 756
    Beta strandi79 – 813
    Beta strandi84 – 885
    Beta strandi93 – 975
    Beta strandi100 – 1034
    Helixi108 – 12922
    Helixi135 – 14713
    Turni148 – 1536
    Beta strandi156 – 1649
    Beta strandi167 – 1748
    Beta strandi179 – 1813
    Beta strandi183 – 1886
    Helixi191 – 20010
    Helixi208 – 22518
    Beta strandi226 – 2283
    Beta strandi231 – 2399
    Beta strandi242 – 2509
    Helixi251 – 2588

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNBX-ray2.901/K/Y/m60-264[»]
    3UNEX-ray3.201/K/Y/m60-264[»]
    ProteinModelPortaliO55234.
    SMRiO55234. Positions 60-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046395.
    HOGENOMiHOG000091082.
    HOVERGENiHBG108297.
    InParanoidiO55234.
    KOiK02737.
    OMAiLRAIMHA.
    OrthoDBiEOG7FNC86.
    PhylomeDBiO55234.
    TreeFamiTF106223.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view]
    PfamiPF00227. 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.

    O55234-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALASVLQRP MPVNQHGFFG LGGGADLLDL GPGSPGDGLS LAAPSWGVPE    50
    EPRIEMLHGT TTLAFKFLHG VIVAADSRAT AGAYIASQTV KKVIEINPYL 100
    LGTMAGGAAD CSFWERLLAR QCRIYELRNK ERISVAAASK LLANMVYQYK 150
    GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGTAFSVGSG SVYAYGVMDR 200
    GYSYDLKVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE DGWIRVSSDN 250
    VADLHDKYSS VSVP 264
    Length:264
    Mass (Da):28,532
    Last modified:April 29, 2008 - v3
    Checksum:iFCCD619734EF3C57
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101D → N in BAB26942. (PubMed:16141072)Curated
    Sequence conflicti248 – 2481S → N in AAH12246. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB003304 mRNA. Translation: BAA24916.1.
    AB003306 Genomic DNA. Translation: BAA24917.1.
    AF060091 mRNA. Translation: AAD50536.1.
    AK010441 mRNA. Translation: BAB26942.1.
    AK133839 mRNA. Translation: BAE21876.1.
    BC012246 mRNA. Translation: AAH12246.1.
    BC106144 mRNA. Translation: AAI06145.1.
    CCDSiCCDS27095.1.
    RefSeqiNP_035316.1. NM_011186.1.
    UniGeneiMm.8911.

    Genome annotation databases

    EnsembliENSMUST00000022803; ENSMUSP00000022803; ENSMUSG00000022193.
    GeneIDi19173.
    KEGGimmu:19173.
    UCSCiuc007twl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB003304 mRNA. Translation: BAA24916.1 .
    AB003306 Genomic DNA. Translation: BAA24917.1 .
    AF060091 mRNA. Translation: AAD50536.1 .
    AK010441 mRNA. Translation: BAB26942.1 .
    AK133839 mRNA. Translation: BAE21876.1 .
    BC012246 mRNA. Translation: AAH12246.1 .
    BC106144 mRNA. Translation: AAI06145.1 .
    CCDSi CCDS27095.1.
    RefSeqi NP_035316.1. NM_011186.1.
    UniGenei Mm.8911.

    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 1/K/Y/m 60-264 [» ]
    3UNE X-ray 3.20 1/K/Y/m 60-264 [» ]
    ProteinModelPortali O55234.
    SMRi O55234. Positions 60-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202421. 4 interactions.
    IntActi O55234. 7 interactions.
    MINTi MINT-4125600.

    Chemistry

    ChEMBLi CHEMBL1944494.

    Protein family/group databases

    MEROPSi T01.P01.

    PTM databases

    PhosphoSitei O55234.

    Proteomic databases

    MaxQBi O55234.
    PaxDbi O55234.
    PRIDEi O55234.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022803 ; ENSMUSP00000022803 ; ENSMUSG00000022193 .
    GeneIDi 19173.
    KEGGi mmu:19173.
    UCSCi uc007twl.1. mouse.

    Organism-specific databases

    CTDi 5693.
    MGIi MGI:1194513. Psmb5.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046395.
    HOGENOMi HOG000091082.
    HOVERGENi HBG108297.
    InParanoidi O55234.
    KOi K02737.
    OMAi LRAIMHA.
    OrthoDBi EOG7FNC86.
    PhylomeDBi O55234.
    TreeFami TF106223.

    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 295850.
    PROi O55234.
    SOURCEi Search...

    Gene expression databases

    Bgeei O55234.
    Genevestigatori O55234.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000243. Pept_T1A_subB.
    IPR016050. Proteasome_bsu_CS.
    IPR001353. Proteasome_sua/b.
    IPR023333. Proteasome_suB-type.
    [Graphical view ]
    Pfami 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. "Structural analysis and chromosomal localization of the mouse Psmb5 gene coding for the constitutively expressed beta-type proteasome subunit."
      Kohda K., Matsuda Y., Ishibashi T., Tanaka K., Kasahara M.
      Immunogenetics 47:77-87(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: 129/SvJ and C57BL/6.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: B10.A.
      Tissue: Macrophage.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo and Embryonic stem cell.
    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].
      Strain: FVB/N.
      Tissue: Mammary tumor and Salivary gland.
    5. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 79-91; 141-150 AND 167-179, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway."
      Kwak M.K., Wakabayashi N., Greenlaw J.L., Yamamoto M., Kensler T.W.
      Mol. Cell. Biol. 23:8786-8794(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ANTIOXIDANTS.
    7. "Induction of 26S proteasome subunit PSMB5 by the bifunctional inducer 3-methylcholanthrene through the Nrf2-ARE, but not the AhR/Arnt-XRE, pathway."
      Kwak M.K., Kensler T.W.
      Biochem. Biophys. Res. Commun. 345:1350-1357(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ANTIOXIDANTS.
    8. "Serial analysis of gene expression in mouse uterus at the implantation site."
      Ma X.H., Hu S.J., Ni H., Zhao Y.C., Tian Z., Liu J.L., Ren G., Liang X.H., Yu H., Wan P., Yang Z.M.
      J. Biol. Chem. 281:9351-9360(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "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.
    10. "Microarray gene expression profiling of mouse brain mRNA in a model of lithium treatment."
      Chetcuti A., Adams L.J., Mitchell P.B., Schofield P.R.
      Psychiatr. Genet. 18:64-72(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY LITHIUM.
    11. "Protection against amyloid beta cytotoxicity by sulforaphane: role of the proteasome."
      Park H.M., Kim J.A., Kwak M.K.
      Arch. Pharm. Res. 32:109-115(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.

    Entry informationi

    Entry nameiPSB5_MOUSE
    AccessioniPrimary (citable) accession number: O55234
    Secondary accession number(s): Q3UZI1
    , Q91X53, Q9CWR4, Q9R1P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 124 of the entry and version 3 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