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'''Ubiquitin-conjugating enzyme E2 variant 2''' is a [[protein]] that in humans is encoded by the ''UBE2V2'' [[gene]].<ref name="pmid9418904">{{cite journal | vauthors = Sancho E, Vilá MR, Sánchez-Pulido L, Lozano JJ, Paciucci R, Nadal M, Fox M, Harvey C, Bercovich B, Loukili N, Ciechanover A, Lin SL, Sanz F, Estivill X, Valencia A, Thomson TM | title = Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells | journal = | '''Ubiquitin-conjugating enzyme E2 variant 2''' is a [[protein]] that in humans is encoded by the ''UBE2V2'' [[gene]].<ref name="pmid9418904">{{cite journal | vauthors = Sancho E, Vilá MR, Sánchez-Pulido L, Lozano JJ, Paciucci R, Nadal M, Fox M, Harvey C, Bercovich B, Loukili N, Ciechanover A, Lin SL, Sanz F, Estivill X, Valencia A, Thomson TM | title = Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells | journal = Molecular and Cellular Biology | volume = 18 | issue = 1 | pages = 576–89 | date = January 1998 | pmid = 9418904 | pmc = 121525 | doi = 10.1128/mcb.18.1.576 }}</ref><ref name="pmid9199207">{{cite journal | vauthors = Fritsche J, Rehli M, Krause SW, Andreesen R, Kreutz M | title = Molecular cloning of a 1alpha,25-dihydroxyvitamin D3-inducible transcript (DDVit 1) in human blood monocytes | journal = Biochemical and Biophysical Research Communications | volume = 235 | issue = 2 | pages = 407–12 | date = June 1997 | pmid = 9199207 | pmc = | doi = 10.1006/bbrc.1997.6798 }}</ref> Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family. | ||
== Structure == | |||
UBE2V2 has sequence similarity to other [[Ubiquitin-conjugating enzyme|ubiquitin-conjugating enzymes]] but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene also shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2V2 ubiquitin-conjugating enzyme E2 variant 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7336| access-date = }}</ref> | |||
== Function == | == Function == | ||
UBE2V2 has also been implicated as an intracellular sensor of reactive electrophilic species, which are present in high levels during periods of pathogenic and/or environmental stress.<ref>{{cite journal | vauthors = Farmer EE, Davoine C | title = Reactive electrophile species | journal = Current Opinion in Plant Biology | volume = 10 | issue = 4 | pages = 380–6 | date = August 2007 | pmid = 17646124 | doi = 10.1016/j.pbi.2007.04.019 }}</ref> The C69 residue of UBE2V2 is capable of binding with various RES. It has been shown that binding of RES to UBE2V2 promotes UBE2V2-mediated activation of Ube2N, another E2 protein that complexes with UBE2V2. Activated Ube2N has been shown to play a major role in promoting DNA-damage responses. Thus, UBE2V2 may promote genome integrity by directly sensing RES and effecting DNA damage responses.<ref>{{cite journal | vauthors = Zhao Y, Long MJ, Wang Y, Zhang S, Aye Y | title = Ube2V2 Is a Rosetta Stone Bridging Redox and Ubiquitin Codes, Coordinating DNA Damage Responses | journal = ACS Central Science | volume = 4 | issue = 2 | pages = 246–259 | date = February 2018 | pmid = 29532025 | pmc = 5833000 | doi = 10.1021/acscentsci.7b00556 }}</ref> It may also be involved in the differentiation of monocytes and enterocytes.<ref name="entrez" /> | |||
== Interactions == | == Interactions == | ||
UBE2V2 has been shown to [[Protein-protein interaction|interact]] with [[HLTF]].<ref name=pmid18316726>{{cite journal | vauthors = Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L | title = Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination | journal = | UBE2V2 has been shown to [[Protein-protein interaction|interact]] with [[HLTF]].<ref name=pmid18316726>{{cite journal | vauthors = Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L | title = Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 105 | issue = 10 | pages = 3768–73 | date = March 2008 | pmid = 18316726 | pmc = 2268824 | doi = 10.1073/pnas.0800563105 }}</ref> Although UBE2V2 itself lacks ubiquitin-conjugating activity, it can interact with different [[Ubiquitin-conjugating enzyme|Ubiquitin-conjugating enzymes]] to facilitate their catalytic activities.<ref>{{cite journal | vauthors = Stewart MD, Ritterhoff T, Klevit RE, Brzovic PS | title = E2 enzymes: more than just middle men | journal = Cell Research | volume = 26 | issue = 4 | pages = 423–40 | date = April 2016 | pmid = 27002219 | pmc = 4822130 | doi = 10.1038/cr.2016.35 }}</ref> For instance, UBE2V2 can complex with [[UBE2N]] to form a heterodimer capable of synthesizing Lys-63 linked polyubiquitin chains.<ref>{{cite journal | vauthors = Fletcher AJ, Christensen DE, Nelson C, Tan CP, Schaller T, Lehner PJ, Sundquist WI, Towers GJ | title = TRIM5α requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription | journal = The EMBO Journal | volume = 34 | issue = 15 | pages = 2078–95 | date = August 2015 | pmid = 26101372 | pmc = 4551353 | doi = 10.15252/embj.201490361 }}</ref> UBE2V2 may facilitate UBE2N activity by coordinating UBE2N's positioning to promote ubiquitin chain formation specifically at Lys-63, as the ubiquitin molecule has multiple potential Lysine binding sites.<ref>{{cite journal | vauthors = Eddins MJ, Carlile CM, Gomez KM, Pickart CM, Wolberger C | title = Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation | journal = Nature Structural & Molecular Biology | volume = 13 | issue = 10 | pages = 915–20 | date = October 2006 | pmid = 16980971 | doi = 10.1038/nsmb1148 }}</ref> Similarly, it has been shown that UBE2V2 interact with the ubiquitin-conjugating enzyme, Ubc13, to induce Ubc13 to adopt an active conformation that can create Lys-63 polyubituitin chains on various substrates.<ref>{{cite journal | vauthors = Branigan E, Plechanovová A, Jaffray EG, Naismith JH, Hay RT | title = Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains | journal = Nature Structural & Molecular Biology | volume = 22 | issue = 8 | pages = 597–602 | date = August 2015 | pmid = 26148049 | pmc = 4529489 | doi = 10.1038/nsmb.3052 }}</ref> | ||
Addition of Lys-63 polyubiquitin chains to intracellular targets is distinct from the canonical Lys-48 polyubiquitin chains in that Lys-63 chains do not mediate proteasomal degradation of its substrate.<ref>{{cite journal | vauthors = Fletcher AJ, Christensen DE, Nelson C, Tan CP, Schaller T, Lehner PJ, Sundquist WI, Towers GJ | title = TRIM5α requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription | journal = The EMBO Journal | volume = 34 | issue = 15 | pages = 2078–95 | date = August 2015 | pmid = 26101372 | pmc = 4551353 | doi = 10.15252/embj.201490361 }}</ref> Although their function remains poorly characterized, Lys-63 chains have been shown to regulate signaling pathways by either activating or inhibiting its target protein function.<ref>{{Cite web|url=https://www.uniprot.org/uniprot/P61088|title=UBE2N - Ubiquitin-conjugating enzyme E2 N - Homo sapiens (Human) - UBE2N gene & protein|website=www.uniprot.org|language=en|access-date=2018-04-06}}</ref> For example, [[TRIM5alpha]] restriction of retroviral reverse-transcription is dependent on UBE2V2/UBE2N-mediated poly-ubiquitination.<ref>{{cite journal | vauthors = Fletcher AJ, Christensen DE, Nelson C, Tan CP, Schaller T, Lehner PJ, Sundquist WI, Towers GJ | title = TRIM5α requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription | journal = The EMBO Journal | volume = 34 | issue = 15 | pages = 2078–95 | date = August 2015 | pmid = 26101372 | pmc = 4551353 | doi = 10.15252/embj.201490361 }}</ref> UBE2V2 has been shown to regulate [[TRIM21]] antiviral activity in an analogous manner.<ref>{{cite journal | vauthors = Fletcher AJ, Mallery DL, Watkinson RE, Dickson CF, James LC | title = Sequential ubiquitination and deubiquitination enzymes synchronize the dual sensor and effector functions of TRIM21 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 112 | issue = 32 | pages = 10014–9 | date = August 2015 | pmid = 26150489 | pmc = 4538650 | doi = 10.1073/pnas.1507534112 }}</ref> | |||
== References == | == References == | ||
| Line 15: | Line 21: | ||
== Further reading == | == Further reading == | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
* {{cite journal | vauthors = Xiao W, Lin SL, Broomfield S, Chow BL, Wei YF | title = The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family | journal = Nucleic Acids | * {{cite journal | vauthors = Xiao W, Lin SL, Broomfield S, Chow BL, Wei YF | title = The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family | journal = Nucleic Acids Research | volume = 26 | issue = 17 | pages = 3908–14 | date = September 1998 | pmid = 9705497 | pmc = 147796 | doi = 10.1093/nar/26.17.3908 }} | ||
* {{cite journal | vauthors = Hofmann RM, Pickart CM | title = Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair | journal = Cell | volume = 96 | issue = 5 | pages = 645–53 | | * {{cite journal | vauthors = Hofmann RM, Pickart CM | title = Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair | journal = Cell | volume = 96 | issue = 5 | pages = 645–53 | date = March 1999 | pmid = 10089880 | doi = 10.1016/S0092-8674(00)80575-9 }} | ||
* {{cite journal | vauthors = Chan NL, Hill CP | title = Defining polyubiquitin chain topology | journal = | * {{cite journal | vauthors = Chan NL, Hill CP | title = Defining polyubiquitin chain topology | journal = Nature Structural Biology | volume = 8 | issue = 8 | pages = 650–2 | date = August 2001 | pmid = 11473244 | doi = 10.1038/90337 }} | ||
* {{cite journal | vauthors = Moraes TF, Edwards RA, McKenna S, Pastushok L, Xiao W, Glover JN, Ellison MJ | title = Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13 | journal = | * {{cite journal | vauthors = Moraes TF, Edwards RA, McKenna S, Pastushok L, Xiao W, Glover JN, Ellison MJ | title = Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13 | journal = Nature Structural Biology | volume = 8 | issue = 8 | pages = 669–73 | date = August 2001 | pmid = 11473255 | doi = 10.1038/90373 }} | ||
* {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = | * {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nature Biotechnology | volume = 21 | issue = 5 | pages = 566–9 | date = May 2003 | pmid = 12665801 | doi = 10.1038/nbt810 }} | ||
* {{cite journal | vauthors = Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD | title = The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains | journal = Oncogene | volume = 22 | issue = 46 | pages = 7101–7 | | * {{cite journal | vauthors = Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD | title = The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains | journal = Oncogene | volume = 22 | issue = 46 | pages = 7101–7 | date = October 2003 | pmid = 14562038 | doi = 10.1038/sj.onc.1206831 }} | ||
* {{cite journal | vauthors = Zhou H, Wertz I, O'Rourke K, Ultsch M, Seshagiri S, Eby M, Xiao W, Dixit VM | title = Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO | journal = Nature | volume = 427 | issue = 6970 | pages = 167–71 | | * {{cite journal | vauthors = Zhou H, Wertz I, O'Rourke K, Ultsch M, Seshagiri S, Eby M, Xiao W, Dixit VM | title = Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO | journal = Nature | volume = 427 | issue = 6970 | pages = 167–71 | date = January 2004 | pmid = 14695475 | doi = 10.1038/nature02273 }} | ||
* {{cite journal | vauthors = Simpson LJ, Sale JE | title = UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40 | journal = DNA Repair | * {{cite journal | vauthors = Simpson LJ, Sale JE | title = UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40 | journal = DNA Repair | volume = 4 | issue = 4 | pages = 503–10 | date = April 2005 | pmid = 15725630 | doi = 10.1016/j.dnarep.2004.12.002 }} | ||
* {{cite journal | vauthors = Pastushok L, Moraes TF, Ellison MJ, Xiao W | title = A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex | journal = | * {{cite journal | vauthors = Pastushok L, Moraes TF, Ellison MJ, Xiao W | title = A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex | journal = The Journal of Biological Chemistry | volume = 280 | issue = 18 | pages = 17891–900 | date = May 2005 | pmid = 15749714 | doi = 10.1074/jbc.M410469200 }} | ||
* {{cite journal | vauthors = Spyracopoulos L, Lewis MJ, Saltibus LF | title = Main chain and side chain dynamics of the ubiquitin conjugating enzyme variant human Mms2 in the free and ubiquitin-bound States | journal = Biochemistry | volume = 44 | issue = 24 | pages = 8770–81 | | * {{cite journal | vauthors = Spyracopoulos L, Lewis MJ, Saltibus LF | title = Main chain and side chain dynamics of the ubiquitin conjugating enzyme variant human Mms2 in the free and ubiquitin-bound States | journal = Biochemistry | volume = 44 | issue = 24 | pages = 8770–81 | date = June 2005 | pmid = 15952783 | doi = 10.1021/bi050065k }} | ||
* {{cite journal | vauthors = Andersen PL, Zhou H, Pastushok L, Moraes T, McKenna S, Ziola B, Ellison MJ, Dixit VM, Xiao W | title = Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A | journal = | * {{cite journal | vauthors = Andersen PL, Zhou H, Pastushok L, Moraes T, McKenna S, Ziola B, Ellison MJ, Dixit VM, Xiao W | title = Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A | journal = The Journal of Cell Biology | volume = 170 | issue = 5 | pages = 745–55 | date = August 2005 | pmid = 16129784 | pmc = 2171356 | doi = 10.1083/jcb.200502113 }} | ||
* {{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | | * {{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | date = September 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }} | ||
* {{cite journal | vauthors = Wen R, Newton L, Li G, Wang H, Xiao W | title = Arabidopsis thaliana UBC13: implication of error-free DNA damage tolerance and Lys63-linked polyubiquitylation in plants | journal = Plant | * {{cite journal | vauthors = Wen R, Newton L, Li G, Wang H, Xiao W | title = Arabidopsis thaliana UBC13: implication of error-free DNA damage tolerance and Lys63-linked polyubiquitylation in plants | journal = Plant Molecular Biology | volume = 61 | issue = 1-2 | pages = 241–53 | date = May 2006 | pmid = 16786304 | doi = 10.1007/s11103-006-0007-x }} | ||
* {{cite journal | vauthors = Zhao GY, Sonoda E, Barber LJ, Oka H, Murakawa Y, Yamada K, Ikura T, Wang X, Kobayashi M, Yamamoto K, Boulton SJ, Takeda S | title = A critical role for the ubiquitin-conjugating enzyme Ubc13 in initiating homologous recombination | journal = | * {{cite journal | vauthors = Zhao GY, Sonoda E, Barber LJ, Oka H, Murakawa Y, Yamada K, Ikura T, Wang X, Kobayashi M, Yamamoto K, Boulton SJ, Takeda S | title = A critical role for the ubiquitin-conjugating enzyme Ubc13 in initiating homologous recombination | journal = Molecular Cell | volume = 25 | issue = 5 | pages = 663–75 | date = March 2007 | pmid = 17349954 | doi = 10.1016/j.molcel.2007.01.029 }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=7336}} | {{PDB Gallery|geneid=7336}} | ||
{{Ubiquitin-conjugating enzymes}} | {{Ubiquitin-conjugating enzymes}} | ||
{{gene-8-stub}} | {{gene-8-stub}} | ||
Revision as of 21:22, 10 April 2018
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Ubiquitin-conjugating enzyme E2 variant 2 is a protein that in humans is encoded by the UBE2V2 gene.[1][2] Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family.
Structure
UBE2V2 has sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene also shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product.[3]
Function
UBE2V2 has also been implicated as an intracellular sensor of reactive electrophilic species, which are present in high levels during periods of pathogenic and/or environmental stress.[4] The C69 residue of UBE2V2 is capable of binding with various RES. It has been shown that binding of RES to UBE2V2 promotes UBE2V2-mediated activation of Ube2N, another E2 protein that complexes with UBE2V2. Activated Ube2N has been shown to play a major role in promoting DNA-damage responses. Thus, UBE2V2 may promote genome integrity by directly sensing RES and effecting DNA damage responses.[5] It may also be involved in the differentiation of monocytes and enterocytes.[3]
Interactions
UBE2V2 has been shown to interact with HLTF.[6] Although UBE2V2 itself lacks ubiquitin-conjugating activity, it can interact with different Ubiquitin-conjugating enzymes to facilitate their catalytic activities.[7] For instance, UBE2V2 can complex with UBE2N to form a heterodimer capable of synthesizing Lys-63 linked polyubiquitin chains.[8] UBE2V2 may facilitate UBE2N activity by coordinating UBE2N's positioning to promote ubiquitin chain formation specifically at Lys-63, as the ubiquitin molecule has multiple potential Lysine binding sites.[9] Similarly, it has been shown that UBE2V2 interact with the ubiquitin-conjugating enzyme, Ubc13, to induce Ubc13 to adopt an active conformation that can create Lys-63 polyubituitin chains on various substrates.[10]
Addition of Lys-63 polyubiquitin chains to intracellular targets is distinct from the canonical Lys-48 polyubiquitin chains in that Lys-63 chains do not mediate proteasomal degradation of its substrate.[11] Although their function remains poorly characterized, Lys-63 chains have been shown to regulate signaling pathways by either activating or inhibiting its target protein function.[12] For example, TRIM5alpha restriction of retroviral reverse-transcription is dependent on UBE2V2/UBE2N-mediated poly-ubiquitination.[13] UBE2V2 has been shown to regulate TRIM21 antiviral activity in an analogous manner.[14]
References
- ↑ Sancho E, Vilá MR, Sánchez-Pulido L, Lozano JJ, Paciucci R, Nadal M, Fox M, Harvey C, Bercovich B, Loukili N, Ciechanover A, Lin SL, Sanz F, Estivill X, Valencia A, Thomson TM (January 1998). "Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells". Molecular and Cellular Biology. 18 (1): 576–89. doi:10.1128/mcb.18.1.576. PMC 121525. PMID 9418904.
- ↑ Fritsche J, Rehli M, Krause SW, Andreesen R, Kreutz M (June 1997). "Molecular cloning of a 1alpha,25-dihydroxyvitamin D3-inducible transcript (DDVit 1) in human blood monocytes". Biochemical and Biophysical Research Communications. 235 (2): 407–12. doi:10.1006/bbrc.1997.6798. PMID 9199207.
- ↑ 3.0 3.1 "Entrez Gene: UBE2V2 ubiquitin-conjugating enzyme E2 variant 2".
- ↑ Farmer EE, Davoine C (August 2007). "Reactive electrophile species". Current Opinion in Plant Biology. 10 (4): 380–6. doi:10.1016/j.pbi.2007.04.019. PMID 17646124.
- ↑ Zhao Y, Long MJ, Wang Y, Zhang S, Aye Y (February 2018). "Ube2V2 Is a Rosetta Stone Bridging Redox and Ubiquitin Codes, Coordinating DNA Damage Responses". ACS Central Science. 4 (2): 246–259. doi:10.1021/acscentsci.7b00556. PMC 5833000. PMID 29532025.
- ↑ Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L (March 2008). "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination". Proceedings of the National Academy of Sciences of the United States of America. 105 (10): 3768–73. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726.
- ↑ Stewart MD, Ritterhoff T, Klevit RE, Brzovic PS (April 2016). "E2 enzymes: more than just middle men". Cell Research. 26 (4): 423–40. doi:10.1038/cr.2016.35. PMC 4822130. PMID 27002219.
- ↑ Fletcher AJ, Christensen DE, Nelson C, Tan CP, Schaller T, Lehner PJ, Sundquist WI, Towers GJ (August 2015). "TRIM5α requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription". The EMBO Journal. 34 (15): 2078–95. doi:10.15252/embj.201490361. PMC 4551353. PMID 26101372.
- ↑ Eddins MJ, Carlile CM, Gomez KM, Pickart CM, Wolberger C (October 2006). "Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation". Nature Structural & Molecular Biology. 13 (10): 915–20. doi:10.1038/nsmb1148. PMID 16980971.
- ↑ Branigan E, Plechanovová A, Jaffray EG, Naismith JH, Hay RT (August 2015). "Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains". Nature Structural & Molecular Biology. 22 (8): 597–602. doi:10.1038/nsmb.3052. PMC 4529489. PMID 26148049.
- ↑ Fletcher AJ, Christensen DE, Nelson C, Tan CP, Schaller T, Lehner PJ, Sundquist WI, Towers GJ (August 2015). "TRIM5α requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription". The EMBO Journal. 34 (15): 2078–95. doi:10.15252/embj.201490361. PMC 4551353. PMID 26101372.
- ↑ "UBE2N - Ubiquitin-conjugating enzyme E2 N - Homo sapiens (Human) - UBE2N gene & protein". www.uniprot.org. Retrieved 2018-04-06.
- ↑ Fletcher AJ, Christensen DE, Nelson C, Tan CP, Schaller T, Lehner PJ, Sundquist WI, Towers GJ (August 2015). "TRIM5α requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription". The EMBO Journal. 34 (15): 2078–95. doi:10.15252/embj.201490361. PMC 4551353. PMID 26101372.
- ↑ Fletcher AJ, Mallery DL, Watkinson RE, Dickson CF, James LC (August 2015). "Sequential ubiquitination and deubiquitination enzymes synchronize the dual sensor and effector functions of TRIM21". Proceedings of the National Academy of Sciences of the United States of America. 112 (32): 10014–9. doi:10.1073/pnas.1507534112. PMC 4538650. PMID 26150489.
Further reading
- Xiao W, Lin SL, Broomfield S, Chow BL, Wei YF (September 1998). "The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family". Nucleic Acids Research. 26 (17): 3908–14. doi:10.1093/nar/26.17.3908. PMC 147796. PMID 9705497.
- Hofmann RM, Pickart CM (March 1999). "Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair". Cell. 96 (5): 645–53. doi:10.1016/S0092-8674(00)80575-9. PMID 10089880.
- Chan NL, Hill CP (August 2001). "Defining polyubiquitin chain topology". Nature Structural Biology. 8 (8): 650–2. doi:10.1038/90337. PMID 11473244.
- Moraes TF, Edwards RA, McKenna S, Pastushok L, Xiao W, Glover JN, Ellison MJ (August 2001). "Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13". Nature Structural Biology. 8 (8): 669–73. doi:10.1038/90373. PMID 11473255.
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
- Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD (October 2003). "The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains". Oncogene. 22 (46): 7101–7. doi:10.1038/sj.onc.1206831. PMID 14562038.
- Zhou H, Wertz I, O'Rourke K, Ultsch M, Seshagiri S, Eby M, Xiao W, Dixit VM (January 2004). "Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO". Nature. 427 (6970): 167–71. doi:10.1038/nature02273. PMID 14695475.
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