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P28076

- PSB9_MOUSE

UniProt

P28076 - PSB9_MOUSE

Protein

Proteasome subunit beta type-9

Gene

Psmb9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      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. Contributes to NFKBIA degradation and subsequently NFKB1 generation.2 Publications

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei20 – 212Cleavage; by autocatalysisBy similarity
    Active sitei21 – 211NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. antigen processing and presentation Source: MGI
    2. proteolysis involved in cellular 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

    MEROPSiT01.013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-9 (EC:3.4.25.1)
    Alternative name(s):
    LMP-2d
    Low molecular mass protein 2
    Macropain chain 7
    Multicatalytic endopeptidase complex chain 7
    Proteasome chain 7
    Proteasome subunit beta-1i
    Really interesting new gene 12 protein
    Gene namesi
    Name:Psmb9
    Synonyms:Lmp2, Ring12
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1346526. Psmb9.

    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

    Depletion of LMP2 by RNAi suppresses expression and activities of the matrix metalloproteinase MMP2 and MMP9 by blocking the transfer of active NF-kappa-B heterodimers into the nucleus.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 2020Removed in mature formBy similarityPRO_0000026621Add
    BLAST
    Chaini21 – 219199Proteasome subunit beta type-9PRO_0000026622Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531N6-acetyllysineBy similarity
    Modified residuei109 – 1091N6-acetyllysineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Zymogen

    Proteomic databases

    PaxDbiP28076.
    PRIDEiP28076.

    PTM databases

    PhosphoSiteiP28076.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level). Expressed at high levels in the thymus, spleen, lung, heart and liver. Expressed at moderate levels in the kidney.2 Publications

    Inductioni

    Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Up-regulated by heat shock treatment. Down-regulated by EGR1 in neuronal cells.3 Publications

    Gene expression databases

    ArrayExpressiP28076.
    BgeeiP28076.
    GenevestigatoriP28076.

    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 PSMB6. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Interacts with NCOA1, NCOA2 and NCOA3.3 Publications

    Protein-protein interaction databases

    IntActiP28076. 7 interactions.
    MINTiMINT-4108888.

    Structurei

    Secondary structure

    1
    219
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 276
    Beta strandi32 – 365
    Beta strandi40 – 423
    Beta strandi45 – 506
    Beta strandi54 – 585
    Beta strandi61 – 655
    Helixi69 – 8921
    Helixi96 – 10914
    Turni110 – 1134
    Beta strandi118 – 1247
    Turni125 – 1273
    Beta strandi128 – 1336
    Helixi135 – 1373
    Beta strandi143 – 1486
    Helixi149 – 1546
    Helixi155 – 1617
    Helixi168 – 18518
    Beta strandi193 – 1986
    Beta strandi203 – 2086
    Helixi210 – 2123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNFX-ray2.90N/b21-219[»]
    3UNHX-ray3.20N/b21-219[»]
    ProteinModelPortaliP28076.
    SMRiP28076. Positions 21-219.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG291022.
    GeneTreeiENSGT00510000046484.
    HOGENOMiHOG000091079.
    HOVERGENiHBG000123.
    InParanoidiP28076.
    KOiK02741.
    OrthoDBiEOG79GT80.
    PhylomeDBiP28076.
    TreeFamiTF106221.

    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.

    P28076-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRAGAPTAG SFRTEEVHTG TTIMAVEFDG GVVVGSDSRV SAGTAVVNRV    50
    FDKLSPLHQR IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA 100
    NVVKNISYKY REDLLAHLIV AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG 150
    SSYIYGYVDA AYKPGMTPEE CRRFTTNAIT LAMNRDGSSG GVIYLVTITA 200
    AGVDHRVILG DELPKFYDE 219
    Length:219
    Mass (Da):23,397
    Last modified:August 1, 1992 - v1
    Checksum:i036BC558E770BD3E
    GO

    Sequence cautioni

    The sequence AAA39439.1 differs from that shown. Reason: Frameshift at positions 10 and 130.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601R → H in LMP-2b.
    Natural varianti126 – 1261R → C in LMP-2b.
    Natural varianti177 – 1771N → D in LMP-2b and LMP-2q.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S59862 mRNA. Translation: AAB20105.1.
    U22448 mRNA. Translation: AAA75305.1.
    U22447 mRNA. Translation: AAA75304.1.
    S58203 mRNA. Translation: AAP13903.1.
    L11613 Genomic DNA. Translation: AAA39439.1. Frameshift.
    U22919 mRNA. Translation: AAA75306.1.
    U22920 mRNA. Translation: AAA75307.1.
    U35323 Genomic DNA. Translation: AAA98932.1.
    D14566 Genomic DNA. Translation: BAA40680.1.
    D44454 mRNA. Translation: BAA22575.1.
    D44457 mRNA. Translation: BAA22578.1.
    D44458 mRNA. Translation: BAA22579.1.
    D44460 mRNA. Translation: BAA22581.1.
    D44461 mRNA. Translation: BAA22582.1.
    D44462 mRNA. Translation: BAA22583.1.
    D43620 Genomic DNA. Translation: BAA19855.1.
    AF027865 Genomic DNA. Translation: AAB81528.1.
    AF100956 Genomic DNA. Translation: AAC69911.1.
    AK008429 mRNA. Translation: BAB25664.1.
    CCDSiCCDS28642.1.
    PIRiJC2019.
    RefSeqiNP_038613.1. NM_013585.2.
    UniGeneiMm.390983.

    Genome annotation databases

    EnsembliENSMUST00000174576; ENSMUSP00000133499; ENSMUSG00000096727.
    GeneIDi16912.
    KEGGimmu:16912.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S59862 mRNA. Translation: AAB20105.1 .
    U22448 mRNA. Translation: AAA75305.1 .
    U22447 mRNA. Translation: AAA75304.1 .
    S58203 mRNA. Translation: AAP13903.1 .
    L11613 Genomic DNA. Translation: AAA39439.1 . Frameshift.
    U22919 mRNA. Translation: AAA75306.1 .
    U22920 mRNA. Translation: AAA75307.1 .
    U35323 Genomic DNA. Translation: AAA98932.1 .
    D14566 Genomic DNA. Translation: BAA40680.1 .
    D44454 mRNA. Translation: BAA22575.1 .
    D44457 mRNA. Translation: BAA22578.1 .
    D44458 mRNA. Translation: BAA22579.1 .
    D44460 mRNA. Translation: BAA22581.1 .
    D44461 mRNA. Translation: BAA22582.1 .
    D44462 mRNA. Translation: BAA22583.1 .
    D43620 Genomic DNA. Translation: BAA19855.1 .
    AF027865 Genomic DNA. Translation: AAB81528.1 .
    AF100956 Genomic DNA. Translation: AAC69911.1 .
    AK008429 mRNA. Translation: BAB25664.1 .
    CCDSi CCDS28642.1.
    PIRi JC2019.
    RefSeqi NP_038613.1. NM_013585.2.
    UniGenei Mm.390983.

    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 N/b 21-219 [» ]
    3UNH X-ray 3.20 N/b 21-219 [» ]
    ProteinModelPortali P28076.
    SMRi P28076. Positions 21-219.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P28076. 7 interactions.
    MINTi MINT-4108888.

    Chemistry

    ChEMBLi CHEMBL1944491.

    Protein family/group databases

    MEROPSi T01.013.

    PTM databases

    PhosphoSitei P28076.

    Proteomic databases

    PaxDbi P28076.
    PRIDEi P28076.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000174576 ; ENSMUSP00000133499 ; ENSMUSG00000096727 .
    GeneIDi 16912.
    KEGGi mmu:16912.

    Organism-specific databases

    CTDi 5698.
    MGIi MGI:1346526. Psmb9.

    Phylogenomic databases

    eggNOGi NOG291022.
    GeneTreei ENSGT00510000046484.
    HOGENOMi HOG000091079.
    HOVERGENi HBG000123.
    InParanoidi P28076.
    KOi K02741.
    OrthoDBi EOG79GT80.
    PhylomeDBi P28076.
    TreeFami TF106221.

    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 290956.
    PROi P28076.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28076.
    Bgeei P28076.
    Genevestigatori P28076.

    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. "Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene."
      Martinez C.K., Monaco J.J.
      Nature 353:664-667(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Various strains.
    2. "Genomic organization of the mouse Lmp-2 gene and characteristic structure of its promoter."
      Kishi F., Suminami Y., Monaco J.J.
      Gene 133:243-248(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NOD.
    3. "Molecular basis of genetic polymorphism in major histocompatibility complex-linked proteasome gene (Lmp-2)."
      Zhou P., Cao H., Smart M., David C.
      Proc. Natl. Acad. Sci. U.S.A. 90:2681-2684(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LMP-2B AND LMP-2Q.
    4. "Genomic organization and tissue expression of mouse proteasome gene Lmp-2."
      Zhou P., Zanelli E., Smart M., David C.
      Genomics 16:664-668(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: BALB/c.
    5. "Molecular and serological analysis of polymorphisms in the murine major histocompatibility complex-encoded proteasome subunits, LMP-2 and LMP-7."
      Nandi D., Iyer M.N., Monaco J.J.
      Exp. Clin. Immunogenet. 13:20-29(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: B10.RIII, C57BL/6 and R37.
    6. "Genomic organization of a mouse MHC class II region including the H2-M and Lmp2 loci."
      Peleraux A., Karlsson L., Chambers J., Peterson P.A.
      Immunogenetics 43:204-214(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
    7. Mizuno K., Saitou N., Tsutiya K., Sagai T., Moriwaki K., Shiroishi T.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Various strains.
      Tissue: Spleen.
    8. "Molecular analysis of a recombinational hotspot adjacent to Lmp2 gene in the mouse MHC: fine location and chromatin structure."
      Mizuno K., Koide T., Sagai T., Moriwaki K., Shiroishi T.
      Mamm. Genome 7:490-496(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: B10.MOL-SGR.
    9. "Sequence of the mouse major histocomaptibility locus class II region."
      Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J., Lasky S., Hood L.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 129/SvJ.
    10. "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: Small intestine.
    11. "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.
    12. "Proteasome subunit LMP2 is required for matrix metalloproteinase-2 and -9 expression and activities in human invasive extravillous trophoblast cell line."
      Wang H.X., Wang H.M., Lin H.Y., Yang Q., Zhang H., Tsang B.K., Zhu C.
      J. Cell. Physiol. 206:616-623(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    13. "Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes."
      Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.
      J. Immunol. 177:8393-8399(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY HEAT SHOCK.
    14. "Regulation of the neuronal proteasome by Zif268 (Egr1)."
      James A.B., Conway A.M., Morris B.J.
      J. Neurosci. 26:1624-1634(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY EGR1.
    15. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
    16. Cited for: IDENTIFICATION IN THE SPERMATOPROTEASOME.
    17. "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 nameiPSB9_MOUSE
    AccessioniPrimary (citable) accession number: P28076
    Secondary accession number(s): O09085
    , O09151, Q07704, Q60827, Q64278
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 141 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

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