Proteasome subunit beta type-6

Details

Name
Proteasome subunit beta type-6
Kind
protein
Synonyms
  • 3.4.25.1
  • LMPY
  • Macropain delta chain
  • Multicatalytic endopeptidase complex delta chain
  • Proteasome delta chain
  • Proteasome subunit Y
  • Y
Gene Name
PSMB6
UniProtKB Entry
P28072Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
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
proteasome-mediated ubiquitin-dependent protein catabolic process
Components
cytoplasm / cytosol / extracellular exosome / nucleoplasm / nucleus / proteasome complex / proteasome core complex
General Function
Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB6 displays a peptidylglutamyl-hydrolizing activity also termed postacidic or caspase-like activity, meaning that the peptides bond hydrolysis occurs directly after acidic residues
Specific Function
cadherin binding
Pfam Domain Function
Signal Regions
Not Available
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
17
Locus
17p13.2
External Identifiers
ResourceLink
UniProtKB IDP28072
UniProtKB Entry NamePSB6_HUMAN
GenBank Protein ID558528
GenBank Gene IDD29012
GeneCard IDPSMB6
HGNC IDHGNC:9543
PDB ID(s)4R3O, 4R67, 5A0Q, 5GJQ, 5GJR, 5L4G, 5LE5, 5LEX, 5LEY, 5LEZ, 5LF0, 5LF1, 5LF3, 5LF4, 5LF6, 5LF7, 5LN3, 5M32, 5T0C, 5T0G, 5T0H, 5T0I, 5T0J, 5VFO, 5VFP, 5VFQ, 5VFR, 5VFS, 5VFT, 5VFU, 6KWY, 6MSB, 6MSD, 6MSE, 6MSG, 6MSH, 6MSJ, 6MSK, 6R70, 6REY, 6RGQ, 6WJD, 6WJN, 6XMJ, 7LXV, 7NAN, 7NAO, 7NAP, 7NAQ, 7NHT, 7PG9, 7QXN, 7QXP, 7QXU, 7QXW, 7QXX, 7QY7, 7QYA, 7QYB, 7V5G, 7V5M, 7W37, 7W38, 7W39, 7W3A, 7W3B, 7W3C, 7W3F, 7W3G, 7W3H, 7W3I, 7W3J, 7W3K, 7W3M, 8BZL, 8CVR, 8CVS, 8CVT, 8CXB, 8QYN, 8QYO, 8QYS, 8UD9
KEGG IDhsa:5694
NCBI Gene ID5694
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]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
(3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDEexperimentalunknowntargetDetails