26S protease regulatory subunit 6A


Name26S 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 NamePSMC3
OrganismHuman
Amino acid sequence
>lcl|BSEQ0049777|26S protease regulatory subunit 6A
MNLLPNIESPVTRQEKMATVWDEAEQDGIGEEVLKMSTEEIIQRTRLLDSEIKIMKSEVL
RVTHELQAMKDKIKENSEKIKVNKTLPYLVSNVIELLDVDPNDQEEDGANIDLDSQRKGK
CAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDER
PTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARAC
AAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEK
AGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNEE
ARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDY
MEGILEVQAKKKANLQYYA
Number of residuesNone
Molecular Weight49203.11
Theoretical pINone
GO Classification
Functions
  • ATP binding
  • TBP-class protein binding
  • ATPase activity
  • proteasome-activating ATPase activity
  • identical protein binding
Processes
  • negative regulation of canonical Wnt signaling pathway
  • blastocyst development
  • MAPK cascade
  • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle
  • protein deubiquitination
  • positive regulation of transcription from RNA polymerase II promoter
  • NIK/NF-kappaB signaling
  • stimulatory C-type lectin receptor signaling pathway
  • modulation by host of viral transcription
  • positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition
  • T cell receptor signaling pathway
  • ubiquitin-dependent ERAD pathway
  • proteasome-mediated ubiquitin-dependent protein catabolic process
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly
  • regulation of cellular amino acid metabolic process
  • protein polyubiquitination
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
  • viral process
  • regulation of mRNA stability
  • tumor necrosis factor-mediated signaling pathway
  • Fc-epsilon receptor signaling pathway
  • anaphase-promoting complex-dependent catabolic process
  • transmembrane transport
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia
  • negative regulation of G2/M transition of mitotic cell cycle
  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent
  • neutrophil degranulation
  • positive regulation of canonical Wnt signaling pathway
  • Wnt signaling pathway, planar cell polarity pathway
Components
  • membrane
  • ficolin-1-rich granule lumen
  • P-body
  • extracellular region
  • nucleus
  • cytosolic proteasome complex
  • cytosol
  • nuclear proteasome complex
  • nucleoplasm
  • proteasome accessory complex
  • proteasome complex
  • secretory granule lumen
  • proteasome regulatory particle, base subcomplex
General FunctionComponent 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 FunctionAtp binding
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP17980
UniProtKB Entry Name
Cellular LocationCytoplasm
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
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome Location11
Locus11p11.2
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. [8419915 ]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [14702039 ]
  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. [15489334 ]
  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. [2194290 ]
  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. [8621709 ]
  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. [1317798 ]
  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. [15831487 ]
  8. 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. [17323924 ]
  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. [17709345 ]
  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. [19413330 ]
  11. 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. [20068231 ]
  12. 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. [21269460 ]
  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. [21406692 ]
  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. [22814378 ]
  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. [23186163 ]
  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. [24275569 ]
  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. [27428775 ]
  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. [27342858 ]

From www.t3db.ca