Proteasome subunit beta type-6

Details

Name
Proteasome subunit beta type-6
Synonyms
  • 3.4.25.1
  • LMPY
  • Macropain delta chain
  • Multicatalytic endopeptidase complex delta chain
  • Proteasome delta chain
  • Proteasome subunit Y
  • Y
Gene Name
PSMB6
Organism
Humans
Amino acid sequence
>lcl|BSEQ0012732|Proteasome subunit beta type-6
MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYI
ANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEM
CYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREG
MTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA
Number of residues
239
Molecular Weight
25357.48
Theoretical pI
4.54
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 / 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
cytoplasm / cytosol / extracellular exosome / Golgi apparatus / 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 peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0007502|720 bp
ATGGCGGCTACCTTACTAGCTGCTCGGGGAGCCGGGCCAGCACCGGCTTGGGGGCCGGAG
GCATTCACTCCAGACTGGGAAAGCCGAGAAGTTTCCACTGGGACCACTATCATGGCCGTG
CAGTTTGACGGGGGCGTGGTTCTGGGGGCGGACTCCAGAACAACCACTGGGTCCTACATC
GCCAATCGAGTGACTGACAAGCTGACACCTATTCACGACCGCATTTTCTGCTGTCGCTCA
GGCTCAGCTGCTGATACCCAGGCAGTAGCTGATGCTGTCACCTACCAGCTCGGTTTCCAC
AGCATTGAACTGAATGAGCCTCCACTGGTCCACACAGCAGCCAGCCTCTTTAAGGAGATG
TGTTACCGATACCGGGAAGACCTGATGGCGGGAATCATCATCGCAGGCTGGGACCCTCAA
GAAGGAGGGCAGGGGTACTCAGTGCCTATGGGGGGTATGATGGTAAGGCAGTCCTTTGCC
ATTGGAGGCTCCGGGAGCTCCTACATCTATGGCTATGTTGATGCTACCTACCGGGAAGGC
ATGACCAAGGAAGAGTGTCTGCAATTCACTGCCAATGCTCTCGCTTTGGCCATGGAGCGG
GATGGCTCCAGTGGAGGAGTGATCCGCCTGGCAGCCATTGCAGAGTCAGGGGTAGAGCGG
CAAGTACTTTTGGGAGACCAGATACCCAAATTCGCCGTTGCCACTTTACCACCCGCCTGA
Chromosome Location
Not Available
Locus
17p13
External Identifiers
ResourceLink
UniProtKB IDP28072
UniProtKB Entry NamePSB6_HUMAN
GenBank Protein ID558528
GenBank Gene IDD29012
HGNC IDHGNC:9543
General References
  1. 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]
  2. 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]
  3. DeMartino GN, Orth K, McCullough ML, Lee LW, Munn TZ, Moomaw CR, Dawson PA, Slaughter CA: The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous. Biochim Biophys Acta. 1991 Aug 9;1079(1):29-38. [Article]
  4. 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]
  5. 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]
  6. 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]
  7. Onda M, Emi M, Yoshida A, Miyamoto S, Akaishi J, Asaka S, Mizutani K, Shimizu K, Nagahama M, Ito K, Tanaka T, Tsunoda T: Comprehensive gene expression profiling of anaplastic thyroid cancers with cDNA microarray of 25 344 genes. Endocr Relat Cancer. 2004 Dec;11(4):843-54. [Article]
  8. 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]
  9. 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]
  10. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [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