Proteasome subunit alpha type-4

Details

Name
Proteasome subunit alpha type-4
Kind
protein
Synonyms
  • HC9
  • Macropain subunit C9
  • Multicatalytic endopeptidase complex subunit C9
  • Proteasome component C9
  • Proteasome subunit L
  • PSC9
Gene Name
PSMA4
UniProtKB Entry
P25789Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
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
Processes
proteasome-mediated ubiquitin-dependent protein catabolic process
Components
cytoplasm / cytosol / extracellular exosome / intracellular membrane-bounded organelle / nucleoplasm / nucleus / proteasome complex / proteasome core complex / proteasome core complex, alpha-subunit 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)
Specific Function
Not Available
Pfam Domain Function
Signal Regions
Not Available
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
GeneCard IDPSMA4
HGNC IDHGNC:9533
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, 6AVO, 6E5B, 6KWY, 6MSB, 6MSD, 6MSE, 6MSG, 6MSH, 6MSJ, 6MSK, 6R70, 6REY, 6RGQ, 6WJD, 6WJN, 6XMJ, 7AWE, 7B12, 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, 8QYJ, 8QYL, 8QYM, 8QYN, 8QYO, 8QYS, 8QZ9, 8UD9
KEGG IDhsa:5685
NCBI Gene ID5685
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]

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