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P40306

- PSB10_HUMAN

UniProt

P40306 - PSB10_HUMAN

Protein

Proteasome subunit beta type-10

Gene

PSMB10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      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.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei39 – 402Cleavage; by autocatalysisBy similarity
    Active sitei40 – 401NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    5. apoptotic process Source: Reactome
    6. cell morphogenesis Source: Ensembl
    7. cellular nitrogen compound metabolic process Source: Reactome
    8. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    9. G1/S transition of mitotic cell cycle Source: Reactome
    10. gene expression Source: Reactome
    11. humoral immune response Source: ProtInc
    12. mitotic cell cycle Source: Reactome
    13. mRNA metabolic process Source: Reactome
    14. negative regulation of apoptotic process Source: Reactome
    15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    16. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    17. protein polyubiquitination Source: Reactome
    18. regulation of apoptotic process Source: Reactome
    19. regulation of cellular amino acid metabolic process Source: Reactome
    20. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    21. RNA metabolic process Source: Reactome
    22. small molecule metabolic process Source: Reactome
    23. T cell proliferation Source: Ensembl
    24. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9538. PSMB10.

    Subcellular locationi

    Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. proteasome complex Source: ProtInc
    4. proteasome core complex Source: UniProtKB
    5. spermatoproteasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33883.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 3939Removed in mature formBy similarityPRO_0000026651Add
    BLAST
    Chaini40 – 273234Proteasome subunit beta type-10PRO_0000026652Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    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

    MaxQBiP40306.
    PaxDbiP40306.
    PeptideAtlasiP40306.
    PRIDEiP40306.

    2D gel databases

    OGPiP40306.
    SWISS-2DPAGEP40306.

    PTM databases

    PhosphoSiteiP40306.

    Expressioni

    Developmental stagei

    Highly expressed in immature dendritic cells (at protein level).1 Publication

    Inductioni

    Up-regulated by IFNG/IFN-gamma (at protein level). Up-regulated by IRF1. Up-regulated by TNF (at protein level). Up-regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in Crohn's bowel disease (CD). Up-regulated by CD40L via the NFKB1 pathway in cancer cells.7 Publications

    Gene expression databases

    BgeeiP40306.
    CleanExiHS_PSMB10.
    GenevestigatoriP40306.

    Organism-specific databases

    HPAiHPA030225.

    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. Interacts with HIV-1 TAT protein.1 Publication

    Protein-protein interaction databases

    BioGridi111672. 17 interactions.
    IntActiP40306. 7 interactions.
    STRINGi9606.ENSP00000351314.

    Structurei

    3D structure databases

    ProteinModelPortaliP40306.
    SMRiP40306. Positions 40-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000182856.
    HOVERGENiHBG093416.
    InParanoidiP40306.
    KOiK02733.
    OMAiQYRFAPG.
    OrthoDBiEOG7CRTQJ.
    PhylomeDBiP40306.
    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.

    P40306-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKPALEPRG GFSFENCQRN ASLERVLPGL KVPHARKTGT TIAGLVFQDG    50
    VILGADTRAT NDSVVADKSC EKIHFIAPKI YCCGAGVAAD AEMTTRMVAS 100
    KMELHALSTG REPRVATVTR ILRQTLFRYQ GHVGASLIVG GVDLTGPQLY 150
    GVHPHGSYSR LPFTALGSGQ DAALAVLEDR FQPNMTLEAA QGLLVEAVTA 200
    GILGDLGSGG NVDACVITKT GAKLLRTLSS PTEPVKRSGR YHFVPGTTAV 250
    LTQTVKPLTL ELVEETVQAM EVE 273
    Length:273
    Mass (Da):28,936
    Last modified:February 1, 1995 - v1
    Checksum:iD6728E50513A45B9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71874 Genomic DNA. Translation: CAA50709.1.
    Y13640 mRNA. Translation: CAA73982.1.
    BT019723 mRNA. Translation: AAV38528.1.
    BT019724 mRNA. Translation: AAV38529.1.
    AK312208 mRNA. Translation: BAG35141.1.
    CH471092 Genomic DNA. Translation: EAW83187.1.
    BC017198 mRNA. Translation: AAH17198.1.
    BC052369 mRNA. Translation: AAH52369.1.
    CCDSiCCDS10853.1.
    PIRiI38135.
    RefSeqiNP_002792.1. NM_002801.3.
    UniGeneiHs.9661.

    Genome annotation databases

    EnsembliENST00000358514; ENSP00000351314; ENSG00000205220.
    GeneIDi5699.
    KEGGihsa:5699.
    UCSCiuc002eux.2. human.

    Polymorphism databases

    DMDMi730376.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71874 Genomic DNA. Translation: CAA50709.1 .
    Y13640 mRNA. Translation: CAA73982.1 .
    BT019723 mRNA. Translation: AAV38528.1 .
    BT019724 mRNA. Translation: AAV38529.1 .
    AK312208 mRNA. Translation: BAG35141.1 .
    CH471092 Genomic DNA. Translation: EAW83187.1 .
    BC017198 mRNA. Translation: AAH17198.1 .
    BC052369 mRNA. Translation: AAH52369.1 .
    CCDSi CCDS10853.1.
    PIRi I38135.
    RefSeqi NP_002792.1. NM_002801.3.
    UniGenei Hs.9661.

    3D structure databases

    ProteinModelPortali P40306.
    SMRi P40306. Positions 40-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111672. 17 interactions.
    IntActi P40306. 7 interactions.
    STRINGi 9606.ENSP00000351314.

    Chemistry

    ChEMBLi CHEMBL2364701.

    Protein family/group databases

    MEROPSi T01.014.

    PTM databases

    PhosphoSitei P40306.

    Polymorphism databases

    DMDMi 730376.

    2D gel databases

    OGPi P40306.
    SWISS-2DPAGE P40306.

    Proteomic databases

    MaxQBi P40306.
    PaxDbi P40306.
    PeptideAtlasi P40306.
    PRIDEi P40306.

    Protocols and materials databases

    DNASUi 5699.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358514 ; ENSP00000351314 ; ENSG00000205220 .
    GeneIDi 5699.
    KEGGi hsa:5699.
    UCSCi uc002eux.2. human.

    Organism-specific databases

    CTDi 5699.
    GeneCardsi GC16M067968.
    HGNCi HGNC:9538. PSMB10.
    HPAi HPA030225.
    MIMi 176847. gene.
    neXtProti NX_P40306.
    PharmGKBi PA33883.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000182856.
    HOVERGENi HBG093416.
    InParanoidi P40306.
    KOi K02733.
    OMAi QYRFAPG.
    OrthoDBi EOG7CRTQJ.
    PhylomeDBi P40306.
    TreeFami TF106222.

    Enzyme and pathway databases

    Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Miscellaneous databases

    ChiTaRSi PSMB10. human.
    GeneWikii PSMB10.
    GenomeRNAii 5699.
    NextBioi 22142.
    PROi P40306.
    SOURCEi Search...

    Gene expression databases

    Bgeei P40306.
    CleanExi HS_PSMB10.
    Genevestigatori P40306.

    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. "A tight cluster of five unrelated human genes on chromosome 16q22.1."
      Larsen F., Solheim J., Kristensen T., Kolstoe A.-B., Prydz H.
      Hum. Mol. Genet. 2:1589-1595(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Constitutive and interferon-gamma-induced expression of the human proteasome subunit multicatalytic endopeptidase complex-like 1."
      Foss G.S., Larsen F., Solheim J., Prydz H.
      Biochim. Biophys. Acta 1402:17-28(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Small intestine.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: B-cell and Lymph.
    7. "Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma."
      Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B., Fujiwara T., Takahashi E., Tanahashi N., Tamura T., Ichihara A., Tanaka K.
      J. Exp. Med. 183:1807-1816(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY IFNG.
    8. "Interferon regulatory factor 1 mediates the interferon-gamma induction of the human immunoproteasome subunit multicatalytic endopeptidase complex-like 1."
      Foss G.S., Prydz H.
      J. Biol. Chem. 274:35196-35202(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY IFNG AND IRF1.
    9. "Tumor necrosis factor-alpha induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface."
      Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L., Kiessling R., Levitskaya J.
      Blood 98:1108-1115(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY TNF AND IFNG.
    10. "Bipartite regulation of different components of the MHC class I antigen-processing machinery during dendritic cell maturation."
      Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.
      Int. Immunol. 13:1515-1523(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    11. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
      Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
      FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    12. "Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach."
      Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.
      Toxicon 44:597-608(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY TETRODOTOXIN.
    13. "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 IFNG AND IRF1.
    14. "Genome-wide gene expression differences in Crohn's disease and ulcerative colitis from endoscopic pinch biopsies: insights into distinctive pathogenesis."
      Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L., Bayless T.M., Parmigiani G., Chakravarti S.
      Inflamm. Bowel Dis. 13:807-821(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    15. "CD40 induces antigen transporter and immunoproteasome gene expression in carcinomas via the coordinated action of NF-kappaB and of NF-kappaB-mediated de novo synthesis of IRF-1."
      Moschonas A., Kouraki M., Knox P.G., Thymiakou E., Kardassis D., Eliopoulos A.G.
      Mol. Cell. Biol. 28:6208-6222(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY CD40L.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPSB10_HUMAN
    AccessioniPrimary (citable) accession number: P40306
    Secondary accession number(s): B2R5J4, Q5U098
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3