Proteasome subunit alpha type-4

Details

Name
Proteasome subunit alpha type-4
Synonyms
  • 3.4.25.1
  • HC9
  • Macropain subunit C9
  • Multicatalytic endopeptidase complex subunit C9
  • Proteasome component C9
  • Proteasome subunit L
  • PSC9
Gene Name
PSMA4
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007491|Proteasome subunit alpha type-4
MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVF
FSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQA
YTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYK
EGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKH
EEEEAKAEREKKEKEQKEKDK
Number of residues
261
Molecular Weight
29483.57
Theoretical pI
7.86
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 / cytoplasmic mRNA processing body / cytosol / extracellular exosome / intracellular membrane-bounded organelle / nucleoplasm / nucleus / proteasome complex / proteasome core complex / proteasome core complex, alpha-subunit 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0021697|Proteasome subunit alpha type-4 (PSMA4)
ATGTCTCGAAGATATGACTCCAGGACCACTATATTTTCTCCAGAAGGTCGCTTATACCAA
GTTGAATATGCCATGGAAGCTATTGGACATGCAGGCACCTGTTTGGGAATTTTAGCAAAT
GATGGTGTTTTGCTTGCAGCAGAGAGACGCAACATCCACAAGCTTCTTGATGAAGTCTTT
TTTTCTGAAAAAATTTATAAACTCAATGAGGACATGGCTTGCAGTGTGGCAGGCATAACT
TCTGATGCTAATGTTCTGACTAATGAACTAAGGCTCATTGCTCAAAGGTATTTATTACAG
TATCAGGAGCCAATACCTTGTGAGCAGTTGGTTACAGCGCTGTGTGATATCAAACAAGCT
TATACACAATTTGGAGGAAAACGTCCCTTTGGTGTTTCATTGCTGTACATTGGCTGGGAT
AAGCACTATGGCTTTCAGCTCTATCAGAGTGACCCTAGTGGAAATTACGGGGGATGGAAG
GCCACATGCATTGGAAATAATAGCGCTGCAGCTGTGTCAATGTTGAAACAAGACTATAAA
GAAGGAGAAATGACCTTGAAGTCAGCACTTGCTTTAGCTATCAAAGTACTAAATAAGACC
ATGGATGTTAGTAAACTCTCTGCTGAAAAAGTGGAAATTGCAACACTAACAAGAGAGAAT
GGAAAGACAGTAATCAGAGTTCTCAAACAAAAAGAAGTGGAGCAGTTGATCAAAAAACAT
GAGGAAGAAGAAGCCAAAGCTGAGCGTGAGAAGAAAGAAAAAGAACAGAAAGAAAAGGAT
AAATAG
Chromosome Location
15
Locus
15q25.1
External Identifiers
ResourceLink
UniProtKB IDP25789
UniProtKB Entry NamePSA4_HUMAN
GenBank Protein ID220030
GenBank Gene IDD00763
HGNC IDHGNC:9533
General References
  1. Tamura T, Lee DH, Osaka F, Fujiwara T, Shin S, Chung CH, Tanaka K, Ichihara A: Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes). Biochim Biophys Acta. 1991 May 2;1089(1):95-102. [Article]
  2. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [Article]
  3. 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]
  4. 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]
  5. Rousset R, Desbois C, Bantignies F, Jalinot P: Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome. Nature. 1996 May 23;381(6580):328-31. [Article]
  6. Takabe W, Mataki C, Wada Y, Ishii M, Izumi A, Aburatani H, Hamakubo T, Niki E, Kodama T, Noguchi N: Gene expression induced by BO-653, probucol and BHQ in human endothelial cells. J Atheroscler Thromb. 2000;7(4):223-30. [Article]
  7. 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]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
  10. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  11. 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]
  12. 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