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Volumn 11, Issue 2 P.1199-1590, 2006, Pages 1500-1507

Cloning, characterization and subcellular localization of a gene encoding a human ubiquitin-conjugating enzyme (E2) homologous to the Arabidopsis thaliana UBC-16 gene product

Author keywords

8q13; 8q21.1; Chromosome; Class I; NLS; Nuclear Localization Signal; Polymerase chain reaction; Reverse transcription; RT PCR; Subcellular Localization; Ubiquitin Conjugating Enzyme (UBC OR E2)

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 32844459257     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1899     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • S. Jentsch: The ubiquitin-conjugation system. Annu Rev Genet 26, 179-207 (1992)
    • (1992) Annu Rev Genet , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 2
    • 0035955731 scopus 로고    scopus 로고
    • Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination
    • S. McKenna, L. Spyracopoulos, T. Moraes, L. Pastushok, C. Ptak, W. Xiao & M. J. Ellison: Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination. J Biol Chem. 276, 40120-40126 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 40120-40126
    • McKenna, S.1    Spyracopoulos, L.2    Moraes, T.3    Pastushok, L.4    Ptak, C.5    Xiao, W.6    Ellison, M.J.7
  • 4
    • 0030997067 scopus 로고    scopus 로고
    • Regulating protein degradation by ubiquitination
    • A. M. Weissman: Regulating protein degradation by ubiquitination. Immunol Today. 18, 189-198 (1997)
    • (1997) Immunol Today , vol.18 , pp. 189-198
    • Weissman, A.M.1
  • 6
    • 0035701458 scopus 로고    scopus 로고
    • Ubiquitin-activating enzyme (E1) isoforms in lens epithelial cells: Origin of translation, E2 specificity and cellular localization determined with novel site-specific antibodies
    • F. Shang, G. Deng, M. Obin, C. C. Wu, X. Gong, D. Smith, R. A. Laursen, U. P. Andley, J. R. Reddan & A. Taylor: Ubiquitin-activating enzyme (E1) isoforms in lens epithelial cells: origin of translation, E2 specificity and cellular localization determined with novel site-specific antibodies. Exp Eye Res. 73, 827-836 (2001)
    • (2001) Exp Eye Res , vol.73 , pp. 827-836
    • Shang, F.1    Deng, G.2    Obin, M.3    Wu, C.C.4    Gong, X.5    Smith, D.6    Laursen, R.A.7    Andley, U.P.8    Reddan, J.R.9    Taylor, A.10
  • 7
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • M. Hochstrasser: Ubiquitin-dependent protein degradation. Annu Rev Genet. 30,405-439 (1996)
    • (1996) Annu Rev Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 8
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • A. Varshavsky: The ubiquitin system. Trends Biochem Sci. 22, 383-387 (1997)
    • (1997) Trends Biochem Sci , vol.22 , pp. 383-387
    • Varshavsky, A.1
  • 9
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • A. Hershko & A. Ciechanover: The ubiquitin system for protein degradation. Annu Rev Biochem. 61, 761-807 (1992)
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 10
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • A. Ciechanover: The ubiquitin-proteasome proteolytic pathway. Cell 79, 13-21 (1994)
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 11
    • 0141704419 scopus 로고    scopus 로고
    • Non-traditional functions of ubiquitin and ubiquitin-binding proteins
    • J.D. Schnell & L. Hicke: Non-traditional functions of ubiquitin and ubiquitin-binding proteins. J Biol Chem. 278, 35857-35860 (2003)
    • (2003) J Biol Chem , vol.278 , pp. 35857-35860
    • Schnell, J.D.1    Hicke, L.2
  • 12
    • 0026701772 scopus 로고
    • A rabbit reticulocyte ubiquitin carrier protein that supports ubiquitin-dependent proteolysis (E214k) is homologous to the yeast DNA repair gene RAD6
    • S. S. Wing, F. Dumas & D. Banville: A rabbit reticulocyte ubiquitin carrier protein that supports ubiquitin-dependent proteolysis (E214k) is homologous to the yeast DNA repair gene RAD6. J Biol Chem. 267, 6495-6501 (1992)
    • (1992) J Biol Chem , vol.267 , pp. 6495-6501
    • Wing, S.S.1    Dumas, F.2    Banville, D.3
  • 13
    • 0035854796 scopus 로고    scopus 로고
    • Nuclear import/export of hRPF1/Nedd4 regulates the ubiquitin-dependent degradation of its nuclear substrates
    • M. H. Hamilton, I. Tcherepanova, J. M. Huibregtse & D. P. McDonnell: Nuclear import/export of hRPF1/Nedd4 regulates the ubiquitin-dependent degradation of its nuclear substrates. J. Biol. Chem. 276, 26324-26331 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 26324-26331
    • Hamilton, M.H.1    Tcherepanova, I.2    Huibregtse, J.M.3    McDonnell, D.P.4
  • 14
    • 0033536063 scopus 로고    scopus 로고
    • P19 (ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2
    • W. Tao & A. J. Levine: P19 (ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2. Proc. Natl Acad. Sci. USA 96, 6937-6941 (1999).
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 15
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • J. Roth, M. Dobbelstein, D. A. Freedman, T. Shenk & A. J. Levine: Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J. 17, 554-564 (1998)
    • (1998) EMBO J , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 16
    • 9444240315 scopus 로고    scopus 로고
    • Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import
    • S. M. Plafker, K. S. Plafker, A. M. Weissman & I. G. Macara: Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import. J Cell Biol. 167, 649-659 (2004)
    • (2004) J Cell Biol , vol.167 , pp. 649-659
    • Plafker, S.M.1    Plafker, K.S.2    Weissman, A.M.3    Macara, I.G.4
  • 17
    • 0031579648 scopus 로고    scopus 로고
    • Cloning, characterization and expression of a cDNA clone encoding rabbit ubiquitin-conjugating enzyme, E2(32k)
    • B. Sun, K. Jeyaseelan, M. C. Chung, T. W. Tan, P. B. Chock & T. S. Teo: Cloning, characterization and expression of a cDNA clone encoding rabbit ubiquitin-conjugating enzyme, E2(32k). Biochim Biophys Acta. 1351, 231-238 (1997)
    • (1997) Biochim Biophys Acta , vol.1351 , pp. 231-238
    • Sun, B.1    Jeyaseelan, K.2    Chung, M.C.3    Tan, T.W.4    Chock, P.B.5    Teo, T.S.6
  • 18
    • 0037013260 scopus 로고    scopus 로고
    • Activation of UBC5 ubiquitin-conjugating enzyme by the RING finger of ROC1 and assembly of active ubiquitin ligases by all cullins
    • M. Furukawa, T. Ohta & Y. Xiong: Activation of UBC5 ubiquitin-conjugating enzyme by the RING finger of ROC1 and assembly of active ubiquitin ligases by all cullins. J Biol Chem. 277, 15758-15765 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 15758-15765
    • Furukawa, M.1    Ohta, T.2    Xiong, Y.3
  • 19
    • 0025319223 scopus 로고
    • Mutation of cysteine-88 in the Saccharomyces cerevisiae RAD6 protein abolishes its ubiquitm-conjugating activity and its various biological functions
    • P. Sung, S. Prakash & L. Prakash: Mutation of cysteine-88 in the Saccharomyces cerevisiae RAD6 protein abolishes its ubiquitm-conjugating activity and its various biological functions. Proc Natl Acad Sci USA 87, 2695-2699 (1990)
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2695-2699
    • Sung, P.1    Prakash, S.2    Prakash, L.3
  • 20
    • 0035685516 scopus 로고    scopus 로고
    • Histone variants and histone modifications: A structural perspective
    • J. Ausio, D. W. Abbott, X. Wang & S. C. Moore: Histone variants and histone modifications: a structural perspective. Biochem Cell Biol. 79, 693-708 (2001)
    • (2001) Biochem Cell Biol , vol.79 , pp. 693-708
    • Ausio, J.1    Abbott, D.W.2    Wang, X.3    Moore, S.C.4
  • 21
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • E. M. Bradbury: Reversible histone modifications and the chromosome cell cycle. Bioessays. 14, 9-16 (1992)
    • (1992) Bioessays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 22
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • B. D. Strahl & C. D. Allis: The language of covalent histone modifications. Nature 403, 41-45 (2000)
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 23
    • 0034791090 scopus 로고    scopus 로고
    • Ubiquitin enters the new millennium
    • C. M. Pickart: Ubiquitin enters the new millennium. Mol Cell. 8, 499-504 (2001)
    • (2001) Mol Cell , vol.8 , pp. 499-504
    • Pickart, C.M.1
  • 24
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • C. M. Pickart: Mechanisms underlying ubiquitination. Annu Rev Biochem. 70, 503-533 (2001)
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 25
    • 12344275439 scopus 로고    scopus 로고
    • Ub in charge: Regulating E2 enzyme nuclear import
    • X. D. Zhang & M. J. Matunis: Ub in charge: regulating E2 enzyme nuclear import. Nat Cell Biol. 7, 12-14 (2005)
    • (2005) Nat Cell Biol , vol.7 , pp. 12-14
    • Zhang, X.D.1    Matunis, M.J.2
  • 26
    • 3242671372 scopus 로고    scopus 로고
    • A field guide to ubiquitylation
    • S. Fang & A. M. Weissman: A field guide to ubiquitylation. Cell Mol Life Sci. 61, 1546-1561 (2004)
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1546-1561
    • Fang, S.1    Weissman, A.M.2
  • 28
    • 0034676027 scopus 로고    scopus 로고
    • Importin-11, a nuclear import receptor for the ubiquitin-conjugating enzyme, UbcM2
    • S. M. Plafker & I. G. Macara: Importin-11, a nuclear import receptor for the ubiquitin-conjugating enzyme, UbcM2. EMBO J. 19, 5502-5513 (2000)
    • (2000) EMBO J , vol.19 , pp. 5502-5513
    • Plafker, S.M.1    Macara, I.G.2
  • 29
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • K. Weis: Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112, 441-451 (2003)
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1


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