Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P28063

- PSB8_MOUSE

UniProt

P28063 - PSB8_MOUSE

Protein

Proteasome subunit beta type-8

Gene

Psmb8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. May be involved in the inflammatory response pathway. Required for adipocyte differentiation.3 Publications

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei72 – 732Cleavage; by autocatalysis
    Active sitei73 – 731Nucleophile1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. antigen processing and presentation Source: MGI
    2. fat cell differentiation Source: UniProtKB
    3. proteolysis involved in cellular protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Differentiation, 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

    MEROPSiT01.015.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit beta type-8 (EC:3.4.25.1)
    Alternative name(s):
    Low molecular mass protein 7
    Macropain subunit C13
    Multicatalytic endopeptidase complex subunit C13
    Proteasome component C13
    Proteasome subunit beta-5i
    Gene namesi
    Name:Psmb8
    Synonyms:Lmp7, Mc13
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1346527. Psmb8.

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 7272Removed in mature formBy similarityPRO_0000026599Add
    BLAST
    Chaini73 – 276204Proteasome subunit beta type-8PRO_0000026600Add
    BLAST

    Post-translational modificationi

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

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiP28063.
    PaxDbiP28063.
    PRIDEiP28063.

    PTM databases

    PhosphoSiteiP28063.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level). Expressed in spleen, thymus, lung, liver, heart and, at a very low level, in kidney. Not expressed in brain nor testis.2 Publications

    Inductioni

    Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Down-regulated in spleen by deoxynivalenol (DON), a mycotoxin that alters immune functions. Down-regulated by the selective inhibitor PR-957. Up-regulated by heat shock treatment. Down-regulated by EGR1 in neuronal cells.5 Publications

    Gene expression databases

    ArrayExpressiP28063.
    BgeeiP28063.
    GenevestigatoriP28063.

    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 housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with TAP1.3 Publications

    Protein-protein interaction databases

    IntActiP28063. 4 interactions.
    MINTiMINT-1856641.

    Structurei

    Secondary structure

    1
    276
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi74 – 807
    Beta strandi83 – 886
    Beta strandi92 – 943
    Beta strandi97 – 1026
    Beta strandi106 – 1083
    Beta strandi113 – 1164
    Helixi121 – 14222
    Helixi148 – 16114
    Turni162 – 1643
    Beta strandi171 – 1777
    Beta strandi180 – 1867
    Beta strandi188 – 1903
    Beta strandi192 – 1943
    Beta strandi196 – 2016
    Helixi204 – 2129
    Helixi221 – 23818
    Beta strandi244 – 2529
    Beta strandi255 – 2639
    Helixi264 – 2718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UNFX-ray2.90K/Y73-276[»]
    3UNHX-ray3.20K/Y73-276[»]
    ProteinModelPortaliP28063.
    SMRiP28063. Positions 73-273.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00510000046395.
    HOGENOMiHOG000091082.
    HOVERGENiHBG108297.
    InParanoidiP28063.
    KOiK02740.
    OMAiSDLMHQY.
    PhylomeDBiP28063.
    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.

    P28063-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLDLCGAA RGQRPEWAAL DAGSGGRSDP GHYSFSAQAP ELALPRGMQP    50
    TAFLRSFGGD QERNVQIEMA HGTTTLAFKF QHGVIVAVDS RATAGSYISS 100
    LRMNKVIEIN PYLLGTMSGC AADCQYWERL LAKECRLYYL RNGERISVSA 150
    ASKLLSNMML QYRGMGLSMG SMICGWDKKG PGLYYVDDNG TRLSGQMFST 200
    GSGNTYAYGV MDSGYRQDLS PEEAYDLGRR AIAYATHRDN YSGGVVNMYH 250
    MKEDGWVKVE SSDVSDLLYK YGEAAL 276
    Length:276
    Mass (Da):30,260
    Last modified:November 1, 1995 - v2
    Checksum:iD9FCCF3EF83CD3C3
    GO

    Sequence cautioni

    The sequence CAA45780.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391A → R in CAB60065. (PubMed:8406612)Curated
    Sequence conflicti148 – 1481V → M in BAE26960. (PubMed:16141072)Curated
    Sequence conflicti199 – 1991S → P in AAH51450. (PubMed:15489334)Curated

    Polymorphismi

    The allele, LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7 found in strains NMRI, B10.BR, SJL, A.CA, B10.RIII, B10.cas4 and NOD may be post-translationally modified. Allele LMP7q is found in strain DBA/1J.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti272 – 2721G → R in LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7. 2 Publications
    Natural varianti275 – 2751A → S in LMP7q. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64449 mRNA. Translation: CAA45779.1.
    X64449 mRNA. Translation: CAA45780.1. Different initiation.
    L11145 mRNA. Translation: AAB46392.1.
    Z21847 Genomic DNA. Translation: CAB60065.1. Sequence problems.
    U22031 mRNA. Translation: AAA75033.1.
    U22032 mRNA. Translation: AAA75034.1.
    U22033 mRNA. Translation: AAA75035.1.
    U22034 mRNA. Translation: AAA75036.1.
    U22035 mRNA. Translation: AAA75037.1.
    AK031801 mRNA. Translation: BAC27555.1.
    AK050627 mRNA. Translation: BAE20682.1.
    AK146182 mRNA. Translation: BAE26960.1.
    AK150674 mRNA. Translation: BAE29756.1.
    AK159971 mRNA. Translation: BAE35524.1.
    AF027865 Genomic DNA. Translation: AAB81532.1.
    BC013785 mRNA. Translation: AAH13785.1.
    BC051450 mRNA. Translation: AAH51450.1.
    CCDSiCCDS50073.1.
    PIRiI54513.
    RefSeqiNP_034854.2. NM_010724.2.
    UniGeneiMm.180191.
    Mm.484878.

    Genome annotation databases

    EnsembliENSMUST00000025196; ENSMUSP00000025196; ENSMUSG00000024338.
    GeneIDi16913.
    KEGGimmu:16913.
    UCSCiuc012apv.1. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64449 mRNA. Translation: CAA45779.1 .
    X64449 mRNA. Translation: CAA45780.1 . Different initiation.
    L11145 mRNA. Translation: AAB46392.1 .
    Z21847 Genomic DNA. Translation: CAB60065.1 . Sequence problems.
    U22031 mRNA. Translation: AAA75033.1 .
    U22032 mRNA. Translation: AAA75034.1 .
    U22033 mRNA. Translation: AAA75035.1 .
    U22034 mRNA. Translation: AAA75036.1 .
    U22035 mRNA. Translation: AAA75037.1 .
    AK031801 mRNA. Translation: BAC27555.1 .
    AK050627 mRNA. Translation: BAE20682.1 .
    AK146182 mRNA. Translation: BAE26960.1 .
    AK150674 mRNA. Translation: BAE29756.1 .
    AK159971 mRNA. Translation: BAE35524.1 .
    AF027865 Genomic DNA. Translation: AAB81532.1 .
    BC013785 mRNA. Translation: AAH13785.1 .
    BC051450 mRNA. Translation: AAH51450.1 .
    CCDSi CCDS50073.1.
    PIRi I54513.
    RefSeqi NP_034854.2. NM_010724.2.
    UniGenei Mm.180191.
    Mm.484878.

    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 K/Y 73-276 [» ]
    3UNH X-ray 3.20 K/Y 73-276 [» ]
    ProteinModelPortali P28063.
    SMRi P28063. Positions 73-273.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P28063. 4 interactions.
    MINTi MINT-1856641.

    Chemistry

    ChEMBLi CHEMBL1944492.

    Protein family/group databases

    MEROPSi T01.015.

    PTM databases

    PhosphoSitei P28063.

    Proteomic databases

    MaxQBi P28063.
    PaxDbi P28063.
    PRIDEi P28063.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025196 ; ENSMUSP00000025196 ; ENSMUSG00000024338 .
    GeneIDi 16913.
    KEGGi mmu:16913.
    UCSCi uc012apv.1. mouse.

    Organism-specific databases

    CTDi 5696.
    MGIi MGI:1346527. Psmb8.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00510000046395.
    HOGENOMi HOG000091082.
    HOVERGENi HBG108297.
    InParanoidi P28063.
    KOi K02740.
    OMAi SDLMHQY.
    PhylomeDBi P28063.
    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 290960.
    PROi P28063.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28063.
    Bgeei P28063.
    Genevestigatori P28063.

    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. "Isolation and characterization of the MHC linked beta-type proteasome subunit MC13 cDNA."
      Frentzel S., Graef U., Haemmerling G., Kloetzel P.-M.
      FEBS Lett. 302:121-125(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Lymphoma.
    2. "Different genomic structure of mouse and human Lmp7 genes: characterization of MHC-encoded proteasome genes."
      Meinhardt T., Graf U., Hammerling G.J.
      Immunogenetics 38:373-379(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Lymphoma.
    3. "Genomic organization and tissue expression of the mouse proteasome gene Lmp-7."
      Zanelli E.H., Zhou P., Hong C., Smart M.K., David C.S.
      Immunogenetics 38:400-407(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: BALB/c.
    4. "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], VARIANTS LMP7K/LMP7S/LMPF/LMP7R/LMPCAS4/LMPG7 ARG-272 AND LMP7Q SER-275.
      Strain: A.CA, B10.BR, B10.CAS4, B10.RIII, BALB/c, DBA/1J, NOD and SJL.
      Tissue: Splenocyte and Thymocyte.
    5. "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 and DBA/2.
      Tissue: Bone marrow, Medulla oblongata and Thymus.
    6. "Sequence of the mouse major histocompatibility locus class II region."
      Rowen L., Qin S., Ahearn M.E., Loretz C., Faust J., Lasky S., Mahairas G., Hood L.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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], VARIANT LMP7K/LMP7S/LMPF/LMP7R/LMPCAS4/LMPG7 ARG-272.
      Strain: C57BL/6NCr and NMRI.
      Tissue: Hematopoietic stem cell and Mammary tumor.
    8. "MHC class I expression in mice lacking the proteasome subunit LMP-7."
      Fehling H.J., Swat W., Laplace C., Kuehn R., Rajewsky K., Mueller U., von Boehmer H.
      Science 265:1234-1237(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Gene expression profiling in spleens of deoxynivalenol-exposed mice: immediate early genes as primary targets."
      Kinser S., Jia Q., Li M., Laughter A., Cornwell P., Corton J.C., Pestka J.
      J. Toxicol. Environ. Health Part A 67:1423-1441(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY DEOXYNIVALENOL.
    10. "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.
    11. "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.
    12. "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.
    13. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
    14. "A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis."
      Muchamuel T., Basler M., Aujay M.A., Suzuki E., Kalim K.W., Lauer C., Sylvain C., Ring E.R., Shields J., Jiang J., Shwonek P., Parlati F., Demo S.D., Bennett M.K., Kirk C.J., Groettrup M.
      Nat. Med. 15:781-787(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY PR-957.
    15. Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION.
    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 IN COMPLEX WITH SYNTHETIC INHIBITOR, SUBUNIT, FUNCTION, TISSUE SPECIFICITY, ACTIVE SITE, AUTOCLEAVAGE.

    Entry informationi

    Entry nameiPSB8_MOUSE
    AccessioniPrimary (citable) accession number: P28063
    Secondary accession number(s): Q3UK42
    , Q64300, Q792S8, Q7TMX9, Q91VH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 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