Proteasome subunit beta type-5

Details

Name
Proteasome subunit beta type-5
Synonyms
  • 3.4.25.1
  • LMPX
  • Macropain epsilon chain
  • MB1
  • Multicatalytic endopeptidase complex epsilon chain
  • Proteasome chain 6
  • Proteasome epsilon chain
  • Proteasome subunit MB1
  • Proteasome subunit X
  • X
Gene Name
PSMB5
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037858|Proteasome subunit beta type-5
MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGT
TTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLAR
QCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRI
SGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVRE
DGWIRVSSDNVADLHEKYSGSTP
Number of residues
263
Molecular Weight
28480.01
Theoretical pI
8.68
GO Classification
Functions
endopeptidase activity / threonine-type endopeptidase activity
Processes
activation of MAPKK activity / anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process / antigen processing and presentation of exogenous peptide antigen via MHC class I / antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent / antigen processing and presentation of peptide antigen via MHC class I / apoptotic process / axon guidance / cellular nitrogen compound metabolic process / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / epidermal growth factor receptor signaling pathway / Fc-epsilon receptor signaling pathway / fibroblast growth factor receptor signaling pathway / G1/S transition of mitotic cell cycle / gene expression / innate immune response / insulin receptor signaling pathway / MAPK cascade / mitotic cell cycle / negative regulation of apoptotic process / negative regulation of canonical Wnt signaling pathway / negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle / neurotrophin TRK receptor signaling pathway / NIK/NF-kappaB signaling / polyamine metabolic process / positive regulation of canonical Wnt signaling pathway / positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition / programmed cell death / proteasomal ubiquitin-independent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / protein polyubiquitination / Ras protein signal transduction / regulation of apoptotic process / regulation of cellular amino acid metabolic process / regulation of mRNA stability / regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle / response to oxidative stress / small GTPase mediated signal transduction / small molecule metabolic process / stimulatory C-type lectin receptor signaling pathway / T cell receptor signaling pathway / tumor necrosis factor-mediated signaling pathway / vascular endothelial growth factor receptor signaling pathway / viral process
Components
centrosome / cytoplasm / cytosol / extracellular exosome / nucleoplasm / nucleus / proteasome complex / proteasome core complex
General Function
Threonine-type endopeptidase activity
Specific Function
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. May catalyze basal processing of intracellular antigens. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway (By similarity).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019273|Proteasome subunit beta type-5 (PSMB5)
ATGGCTGGGGGCGCAGCGGATTGCAGCTTCTGGGAACGGCTGTTGGCTCGGCAATGTCGA
ATCTATGAGCTTCGAAATAAGGAACGCATCTCTGTAGCAGCTGCCTCCAAACTGCTTGCC
AACATGGTGTATCAGTACAAAGGCATGGGGCTGTCCATGGGCACCATGATCTGTGGCTGG
GATAAGAGAGGCCCTGGCCTCTACTACGTGGACAGTGAAGGGAACCGGATTTCAGGGGCC
ACCTTCTCTGTAGGTTCTGGCTCTGTGTATGCATATGGGGTCATGGATCGGGGCTATTCC
TATGACCTGGAAGTGGAGCAGGCCTATGATCTGGCCCGTCGAGCCATCTACCAAGCCACC
TACAGAGATGCCTACTCAGGAGGTGCAGTCAACCTCTACCACGTGCGGGAGGATGGCTGG
ATCCGAGTCTCCAGTGACAATGTGGCTGATCTACATGAGAAGTATAGTGGCTCTACCCCC
TGA
Chromosome Location
14
Locus
14q11.2
External Identifiers
ResourceLink
UniProtKB IDP28074
UniProtKB Entry NamePSB5_HUMAN
GenBank Protein ID558526
GenBank Gene IDD29011
GenAtlas IDPSMB5
HGNC IDHGNC:9542
General References
  1. Abdulla S, Beck S, Belich M, Jackson A, Nakamura T, Trowsdale J: Divergent intron arrangement in the MB1/LMP7 proteasome gene pair. Immunogenetics. 1996;44(4):254-8. [Article]
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  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [Article]
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  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  6. Akiyama K, Yokota K, Kagawa S, Shimbara N, Tamura T, Akioka H, Nothwang HG, Noda C, Tanaka K, Ichihara A: cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y. Science. 1994 Aug 26;265(5176):1231-4. [Article]
  7. Belich MP, Glynne RJ, Senger G, Sheer D, Trowsdale J: Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins. Curr Biol. 1994 Sep 1;4(9):769-76. [Article]
  8. Lee LW, Moomaw CR, Orth K, McGuire MJ, DeMartino GN, Slaughter CA: Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome). Biochim Biophys Acta. 1990 Feb 9;1037(2):178-85. [Article]
  9. Kristensen P, Johnsen AH, Uerkvitz W, Tanaka K, Hendil KB: Human proteasome subunits from 2-dimensional gels identified by partial sequencing. Biochem Biophys Res Commun. 1994 Dec 30;205(3):1785-9. [Article]
  10. Akiyama K, Kagawa S, Tamura T, Shimbara N, Takashina M, Kristensen P, Hendil KB, Tanaka K, Ichihara A: Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing. FEBS Lett. 1994 Apr 18;343(1):85-8. [Article]
  11. Kristensen P, Johnsen AH, Uerkvitz W, Tanaka K, Hendil KB: Human proteasome subunits from 2-dimensional gels identified by partial sequencing. Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. [Article]
  12. Gaczynska M, Goldberg AL, Tanaka K, Hendil KB, Rock KL: Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-gamma-induced subunits LMP2 and LMP7. J Biol Chem. 1996 Jul 19;271(29):17275-80. [Article]
  13. Apcher GS, Heink S, Zantopf D, Kloetzel PM, Schmid HP, Mayer RJ, Kruger E: Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits. FEBS Lett. 2003 Oct 9;553(1-2):200-4. [Article]
  14. Begley GS, Horvath AR, Taylor JC, Higgins CF: Cytoplasmic domains of the transporter associated with antigen processing and P-glycoprotein interact with subunits of the proteasome. Mol Immunol. 2005 Jan;42(1):137-41. [Article]
  15. Heink S, Ludwig D, Kloetzel PM, Kruger E: IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9241-6. Epub 2005 Jun 8. [Article]
  16. Wang X, Chen CF, Baker PR, Chen PL, Kaiser P, Huang L: Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry. 2007 Mar 20;46(11):3553-65. Epub 2007 Feb 27. [Article]
  17. Deng S, Zhou H, Xiong R, Lu Y, Yan D, Xing T, Dong L, Tang E, Yang H: Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics. Breast Cancer Res Treat. 2007 Jul;104(1):21-30. Epub 2006 Sep 27. [Article]
  18. Oerlemans R, Franke NE, Assaraf YG, Cloos J, van Zantwijk I, Berkers CR, Scheffer GL, Debipersad K, Vojtekova K, Lemos C, van der Heijden JW, Ylstra B, Peters GJ, Kaspers GL, Dijkmans BA, Scheper RJ, Jansen G: Molecular basis of bortezomib resistance: proteasome subunit beta5 (PSMB5) gene mutation and overexpression of PSMB5 protein. Blood. 2008 Sep 15;112(6):2489-99. doi: 10.1182/blood-2007-08-104950. Epub 2008 Jun 18. [Article]
  19. Lu S, Yang J, Song X, Gong S, Zhou H, Guo L, Song N, Bao X, Chen P, Wang J: Point mutation of the proteasome beta5 subunit gene is an important mechanism of bortezomib resistance in bortezomib-selected variants of Jurkat T cell lymphoblastic lymphoma/leukemia line. J Pharmacol Exp Ther. 2008 Aug;326(2):423-31. doi: 10.1124/jpet.108.138131. Epub 2008 May 23. [Article]
  20. Lu S, Yang J, Chen Z, Gong S, Zhou H, Xu X, Wang J: Different mutants of PSMB5 confer varying bortezomib resistance in T lymphoblastic lymphoma/leukemia cells derived from the Jurkat cell line. Exp Hematol. 2009 Jul;37(7):831-7. doi: 10.1016/j.exphem.2009.04.001. Epub 2009 May 6. [Article]
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  22. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  23. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08515(3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDEexperimentalunknownDetails
DB08889Carfilzomibapproved, investigationalyesinhibitorDetails
DB00188Bortezomibapproved, investigationalyesinhibitorDetails