Proteasome subunit beta type-7
Details
- Name
- Proteasome subunit beta type-7
- Kind
- protein
- Synonyms
- 3.4.25.1
- Macropain chain Z
- Multicatalytic endopeptidase complex chain Z
- Proteasome subunit Z
- Z
- Gene Name
- PSMB7
- UniProtKB Entry
- Q99436Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0007505|Proteasome subunit beta type-7 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGAD TRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVV TANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAV FEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGT RLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS
- Number of residues
- 277
- Molecular Weight
- 29965.16
- Theoretical pI
- 7.79
- GO Classification
- Functionsendopeptidase activity / threonine-type endopeptidase activityProcessesproteasome-mediated ubiquitin-dependent protein catabolic processComponentscytoplasm / cytosol / 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, PSMB7 displays a trypsin-like activity
- Specific Function
- endopeptidase activity
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0020726|Proteasome subunit beta type-7 (PSMB7) ATGGCGGCTGTGTCGGTGTATGCTCCACCAGTTGGAGGCTTCTCTTTTGATAACTGCCGC AGGAATGCCGTCTTGGAAGCCGATTTTGCAAAGAGGGGATACAAGCTTCCAAAGGTCCGG AAAACTGGCACGACCATCGCTGGGGTGGTCTATAAGGATGGCATAGTTCTTGGAGCAGAT ACAAGAGCAACTGAAGGGATGGTTGTTGCTGACAAGAACTGTTCAAAAATACACTTCATA TCTCCTAATATTTATTGTTGTGGTGCTGGGACAGCTGCAGACACAGACATGACAACCCAG CTCATTTCTTCCAACCTGGAGCTCCACTCCCTCTCCACTGGCCGTCTTCCCAGAGTTGTG ACAGCCAATCGGATGCTGAAGCAGATGCTTTTCAGGTATCAAGGTTACATTGGTGCAGCC CTAGTTTTAGGGGGAGTAGATGTTACTGGACCTCACCTCTACAGCATCTATCCTCATGGA TCAACTGATAAGTTGCCTTATGTCACCATGGGTTCTGGCTCCTTGGCAGCAATGGCTGTA TTTGAAGATAAGTTTAGGCCAGACATGGAGGAGGAGGAAGCCAAGAATCTGGTGAGCGAA GCCATCGCAGCTGGCATCTTCAACGACCTGGGCTCCGGAAGCAACATTGACCTCTGCGTC ATCAGCAAGAACAAGCTGGATTTTCTCCGCCCATACACAGTGCCCAACAAGAAGGGGACC AGGCTTGGCCGGTACAGGTGTGAGAAAGGGACTACTGCAGTCCTCACTGAGAAAATCACT CCTCTGGAGATTGAGGTGCTGGAAGAAACAGTCCAAACAATGGACACTTCCTGA
- Chromosome Location
- 9
- Locus
- 9q33.3
- External Identifiers
Resource Link UniProtKB ID Q99436 UniProtKB Entry Name PSB7_HUMAN GenBank Protein ID 1531533 GenBank Gene ID D38048 GeneCard ID PSMB7 HGNC ID HGNC:9544 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, 6HTB, 6HTC, 6HTD, 6HTP, 6HTR, 6HUB, 6HUC, 6HUQ, 6HUU, 6HUV, 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, 8QYJ, 8QYL, 8QYM, 8QYN, 8QYO, 8QYS, 8QZ9, 8UD9 KEGG ID hsa:5695 NCBI Gene ID 5695 - General References
- Hisamatsu H, Shimbara N, Saito Y, Kristensen P, Hendil KB, Fujiwara T, Takahashi E, Tanahashi N, Tamura T, Ichihara A, Tanaka K: Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma. J Exp Med. 1996 Apr 1;183(4):1807-16. [Article]
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- 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]
- 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]
- 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]
- Rho JH, Qin S, Wang JY, Roehrl MH: Proteomic expression analysis of surgical human colorectal cancer tissues: up-regulation of PSB7, PRDX1, and SRP9 and hypoxic adaptation in cancer. J Proteome Res. 2008 Jul;7(7):2959-72. doi: 10.1021/pr8000892. Epub 2008 Jun 13. [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
- 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