26S protease regulatory subunit 6A

Details

Name
26S protease regulatory subunit 6A
Synonyms
  • 26S proteasome AAA-ATPase subunit RPT5
  • Proteasome 26S subunit ATPase 3
  • Proteasome subunit P50
  • Tat-binding protein 1
  • TBP-1
  • TBP1
Gene Name
PSMC3
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049777|26S protease regulatory subunit 6A
MNLLPNIESPVTRQEKMATVWDEAEQDGIGEEVLKMSTEEIIQRTRLLDSEIKIMKSEVL
RVTHELQAMKDKIKENSEKIKVNKTLPYLVSNVIELLDVDPNDQEEDGANIDLDSQRKGK
CAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDER
PTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARAC
AAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEK
AGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNEE
ARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDY
MEGILEVQAKKKANLQYYA
Number of residues
439
Molecular Weight
49203.11
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / ATPase activity / identical protein binding / proteasome-activating ATPase activity / TBP-class protein binding
Processes
anaphase-promoting complex-dependent catabolic process / antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent / blastocyst development / Fc-epsilon receptor signaling pathway / MAPK cascade / modulation by host of viral transcription / negative regulation of canonical Wnt signaling pathway / negative regulation of G2/M transition of mitotic cell cycle / negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle / neutrophil degranulation / NIK/NF-kappaB signaling / positive regulation of canonical Wnt signaling pathway / positive regulation of RNA polymerase II transcriptional preinitiation complex assembly / positive regulation of transcription from RNA polymerase II promoter / positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition / proteasome-mediated ubiquitin-dependent protein catabolic process / protein deubiquitination / protein polyubiquitination / regulation of cellular amino acid metabolic process / regulation of mRNA stability / regulation of transcription from RNA polymerase II promoter in response to hypoxia / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / stimulatory C-type lectin receptor signaling pathway / T cell receptor signaling pathway / transmembrane transport / tumor necrosis factor-mediated signaling pathway / ubiquitin-dependent ERAD pathway / viral process / Wnt signaling pathway, planar cell polarity pathway
Components
cytosol / cytosolic proteasome complex / extracellular region / ficolin-1-rich granule lumen / membrane / nuclear proteasome complex / nucleoplasm / nucleus / P-body / proteasome accessory complex / proteasome complex / proteasome regulatory particle, base subcomplex / secretory granule lumen
General Function
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC3 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Specific Function
Atp binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0049778|26S protease regulatory subunit 6A (PSMC3)
ATGAATCTGCTGCCGAATATTGAGAGTCCAGTGACTCGGCAGGAGAAGATGGCGACCGTG
TGGGATGAGGCCGAGCAAGATGGAATTGGGGAGGAGGTGCTCAAGATGTCCACGGAGGAG
ATCATCCAGCGCACACGGCTGCTGGACAGTGAGATCAAGATCATGAAGAGTGAAGTGTTG
AGAGTCACCCATGAGCTCCAAGCCATGAAGGACAAGATAAAAGAGAACAGTGAGAAAATC
AAAGTGAACAAGACCCTGCCGTACCTTGTCTCCAACGTCATCGAGCTCCTGGATGTTGAT
CCTAATGACCAAGAGGAGGATGGTGCCAATATTGACCTGGACTCCCAGAGGAAGGGCAAG
TGTGCTGTGATCAAAACCTCTACACGACAGACGTACTTCCTTCCTGTGATTGGGTTGGTG
GATGCTGAAAAGCTAAAGCCAGGAGACCTGGTGGGTGTGAACAAAGACTCCTATCTGATC
CTGGAGACGCTGCCCACAGAGTATGACTCGCGGGTGAAGGCCATGGAGGTAGACGAGAGG
CCCACGGAGCAATACAGTGACATTGGGGGTTTGGACAAGCAGATCCAGGAGCTGGTGGAG
GCCATTGTCTTGCCAATGAACCACAAGGAGAAGTTTGAGAACTTGGGGATCCAACCTCCA
AAAGGGGTGCTGATGTATGGGCCCCCAGGGACGGGGAAGACCCTCCTGGCCCGGGCCTGT
GCCGCACAGACTAAGGCCACCTTCCTAAAGCTGGCTGGCCCCCAGCTGGTGCAGATGTTC
ATTGGAGATGGTGCCAAGCTAGTCCGGGATGCCTTTGCCCTGGCCAAGGAGAAAGCGCCC
TCTATCATCTTCATTGATGAGTTGGATGCCATCGGCACCAAGCGCTTTGACAGTGAGAAG
GCTGGGGACCGGGAGGTGCAGAGGACAATGCTGGAGCTTCTGAACCAGCTGGATGGCTTC
CAGCCCAACACCCAAGTTAAGGTAATTGCAGCCACAAACAGGGTGGACATCCTGGACCCC
GCCCTCCTCCGCTCGGGCCGCCTTGACCGCAAGATAGAGTTCCCGATGCCCAATGAGGAG
GCCCGGGCCAGAATCATGCAGATCCACTCCCGAAAGATGAATGTCAGTCCTGACGTGAAC
TACGAGGAGCTGGCCCGCTGCACAGATGACTTCAATGGGGCCCAGTGCAAGGCTGTGTGT
GTGGAGGCGGGCATGATCGCACTGCGCAGGGGTGCCACGGAGCTCACCCACGAGGACTAC
ATGGAAGGCATCCTGGAGGTGCAGGCCAAGAAGAAAGCCAACCTACAATACTACGCCTAG
Chromosome Location
11
Locus
11p11.2
External Identifiers
ResourceLink
UniProtKB IDP17980
UniProtKB Entry NamePRS6A_HUMAN
HGNC IDHGNC:9549
General References
  1. Ohana B, Moore PA, Ruben SM, Southgate CD, Green MR, Rosen CA: The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes. Proc Natl Acad Sci U S A. 1993 Jan 1;90(1):138-42. [Article]
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  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. Nelbock P, Dillon PJ, Perkins A, Rosen CA: A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator. Science. 1990 Jun 29;248(4963):1650-3. [Article]
  5. DeMartino GN, Proske RJ, Moomaw CR, Strong AA, Song X, Hisamatsu H, Tanaka K, Slaughter CA: Identification, purification, and characterization of a PA700-dependent activator of the proteasome. J Biol Chem. 1996 Feb 9;271(6):3112-8. [Article]
  6. Kanayama HO, Tamura T, Ugai S, Kagawa S, Tanahashi N, Yoshimura T, Tanaka K, Ichihara A: Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms. Eur J Biochem. 1992 Jun 1;206(2):567-78. [Article]
  7. Park Y, Hwang YP, Lee JS, Seo SH, Yoon SK, Yoon JB: Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases. Mol Cell Biol. 2005 May;25(9):3842-53. [Article]
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  9. Jakobs A, Himstedt F, Funk M, Korn B, Gaestel M, Niedenthal R: Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation. Nucleic Acids Res. 2007;35(17):e109. Epub 2007 Aug 20. [Article]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
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  13. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
  14. 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]
  15. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [Article]
  16. 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]
  17. Huang X, Luan B, Wu J, Shi Y: An atomic structure of the human 26S proteasome. Nat Struct Mol Biol. 2016 Sep;23(9):778-85. doi: 10.1038/nsmb.3273. Epub 2016 Jul 18. [Article]
  18. Schweitzer A, Aufderheide A, Rudack T, Beck F, Pfeifer G, Plitzko JM, Sakata E, Schulten K, Forster F, Baumeister W: Structure of the human 26S proteasome at a resolution of 3.9 A. Proc Natl Acad Sci U S A. 2016 Jul 12;113(28):7816-21. doi: 10.1073/pnas.1608050113. Epub 2016 Jun 24. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB12695Phenethyl IsothiocyanateinvestigationalunknownDetails