Proteasome subunit alpha type-4
Details
- Name
- Proteasome subunit alpha type-4
- 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
- ComponentsP-body
- 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
Resource Link UniProtKB ID P25789 UniProtKB Entry Name PSA4_HUMAN GenBank Protein ID 220030 GenBank Gene ID D00763 GeneCard ID PSMA4 HGNC ID HGNC: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 ID hsa:5685 NCBI Gene ID 5685 - General References
- 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]
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- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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
- Bio-Entities
Bio-Entity Type Proteasome subunit alpha type-4 (Humans) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE experimental unknown target Details