UBE2L3: Difference between revisions

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{{Infobox_gene}}
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'''Ubiquitin-conjugating enzyme E2 L3''' (UBE2L3), also called UBCH7, is a [[protein]] that in humans is encoded by the ''UBE2L3'' [[gene]].<ref name="pmid8672131">{{cite journal | vauthors = Moynihan TP, Ardley HC, Leek JP, Thompson J, Brindle NS, Markham AF, Robinson PA | title = Characterization of a human ubiquitin-conjugating enzyme gene UBE2L3 | journal = Mamm. Genome | volume = 7 | issue = 7 | pages = 520–5  | date = October 1996 | pmid = 8672131 | pmc =  | doi = 10.1007/s003359900155 }}</ref><ref name="pmid9693040">{{cite journal | vauthors = Moynihan TP, Cole CG, Dunham I, O'Neil L, Markham AF, Robinson PA | title = Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3 | journal = Genomics | volume = 51 | issue = 1 | pages = 124–7  | date = September 1998 | pmid = 9693040 | pmc =  | doi = 10.1006/geno.1998.5257 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBE2L3 ubiquitin-conjugating enzyme E2L 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7332| accessdate = }}</ref> As an E2 enzyme, UBE2L3 participates in [[ubiquitination]] to target proteins for degradation.<ref name="entrez"/> The role of UBE2L3 in the ubiquitination of the NF-κB precursor implicated it in various major autoimmune diseases, including [[rheumatoid arthritis]] (RA), [[celiac disease]], [[Crohn's disease]](CD), and [[systemic lupus erythematosus]].<ref name = "pmid24162738">{{cite journal | vauthors = Hu Z, Liu Y, Zhai X, Dai J, Jin G, Wang L, Zhu L, Yang Y, Liu J, Chu M, Wen J, Xie K, Du G, Wang Q, Zhou Y, Cao M, Liu L, He Y, Wang Y, Zhou G, Jia W, Lu J, Li S, Liu J, Yang H, Shi Y, Zhou W, Shen H | display-authors = 6 | title = New loci associated with chronic hepatitis B virus infection in Han Chinese | journal = Nature Genetics | volume = 45 | issue = 12 | pages = 1499–503 | date = Dec 2013 | pmid = 24162738 | doi = 10.1038/ng.2809 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Structure==
{{GNF_Protein_box
| image = PBB_Protein_UBE2L3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c4z.
| PDB = {{PDB2|1c4z}}, {{PDB2|1fbv}}
| Name = Ubiquitin-conjugating enzyme E2L 3
| HGNCid = 12488
| Symbol = UBE2L3
| AltSymbols =; L-UBC; E2-F1; UBCH7; UbcM4
| OMIM = 603721
| ECnumber = 
| Homologene = 43226
| MGIid = 109240
| GeneAtlas_image1 = PBB_GE_UBE2L3_200682_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_UBE2L3_200676_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_UBE2L3_200683_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}}
| Component = {{GNF_GO|id=GO:0000151 |text = ubiquitin ligase complex}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7332
    | Hs_Ensembl = ENSG00000185651
    | Hs_RefseqProtein = NP_003338
    | Hs_RefseqmRNA = NM_003347
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 22
    | Hs_GenLoc_start = 20251957
    | Hs_GenLoc_end = 20308323
    | Hs_Uniprot = P68036
    | Mm_EntrezGene = 22195
    | Mm_Ensembl = ENSMUSG00000038965
    | Mm_RefseqmRNA = NM_009456
    | Mm_RefseqProtein = NP_033482
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 17065576
    | Mm_GenLoc_end = 17115055
    | Mm_Uniprot = Q3TIH9
  }}
}}
'''Ubiquitin-conjugating enzyme E2L 3''', also known as '''UBE2L3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBE2L3 ubiquitin-conjugating enzyme E2L 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7332| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
===Gene===
{{PBB_Summary
The ''UBE2L3'' gene is located at [[chromosome 22]]q11.21, consisting of 6 [[exons]].Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez"/>
| section_title =  
| summary_text = The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2L3 ubiquitin-conjugating enzyme E2L 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7332| accessdate = }}</ref>
}}


==References==
===Protein===
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Blumenfeld N, Gonen H, Mayer A, ''et al.'' |title=Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates. |journal=J. Biol. Chem. |volume=269 |issue= 13 |pages= 9574-81 |year= 1994 |pmid= 8144544 |doi=  }}
*{{cite journal  | author=Robinson PA, Leek JP, Thompson J, ''et al.'' |title=A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3. |journal=Mamm. Genome |volume=6 |issue= 10 |pages= 725-31 |year= 1996 |pmid= 8563171 |doi=  }}
*{{cite journal  | author=Nuber U, Schwarz S, Kaiser P, ''et al.'' |title=Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2795-800 |year= 1996 |pmid= 8576257 |doi=  }}
*{{cite journal  | author=Moynihan TP, Ardley HC, Leek JP, ''et al.'' |title=Characterization of a human ubiquitin-conjugating enzyme gene UBE2L3. |journal=Mamm. Genome |volume=7 |issue= 7 |pages= 520-5 |year= 1996 |pmid= 8672131 |doi=  }}
*{{cite journal  | author=Kumar S, Kao WH, Howley PM |title=Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13548-54 |year= 1997 |pmid= 9153201 |doi=  }}
*{{cite journal  | author=Moynihan TP, Cole CG, Dunham I, ''et al.'' |title=Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3. |journal=Genomics |volume=51 |issue= 1 |pages= 124-7 |year= 1998 |pmid= 9693040 |doi= 10.1006/geno.1998.5257 }}
*{{cite journal  | author=Anan T, Nagata Y, Koga H, ''et al.'' |title=Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes. |journal=Genes Cells |volume=3 |issue= 11 |pages= 751-63 |year= 1999 |pmid= 9990509 |doi=  }}
*{{cite journal  | author=Martinez-Noel G, Niedenthal R, Tamura T, Harbers K |title=A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4. |journal=FEBS Lett. |volume=454 |issue= 3 |pages= 257-61 |year= 1999 |pmid= 10431818 |doi=  }}
*{{cite journal  | author=Moynihan TP, Ardley HC, Nuber U, ''et al.'' |title=The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30963-8 |year= 1999 |pmid= 10521492 |doi=  }}
*{{cite journal  | author=Yokouchi M, Kondo T, Houghton A, ''et al.'' |title=Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. |journal=J. Biol. Chem. |volume=274 |issue= 44 |pages= 31707-12 |year= 1999 |pmid= 10531381 |doi=  }}
*{{cite journal  | author=Huang L, Kinnucan E, Wang G, ''et al.'' |title=Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. |journal=Science |volume=286 |issue= 5443 |pages= 1321-6 |year= 1999 |pmid= 10558980 |doi=  }}
*{{cite journal  | author=Ardley HC, Moynihan TP, Markham AF, Robinson PA |title=Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7. |journal=Biochim. Biophys. Acta |volume=1491 |issue= 1-3 |pages= 57-64 |year= 2000 |pmid= 10760570 |doi=  }}
*{{cite journal  | author=Zheng N, Wang P, Jeffrey PD, Pavletich NP |title=Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. |journal=Cell |volume=102 |issue= 4 |pages= 533-9 |year= 2000 |pmid= 10966114 |doi=  }}
*{{cite journal  | author=Zhang Y, Gao J, Chung KK, ''et al.'' |title=Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 24 |pages= 13354-9 |year= 2001 |pmid= 11078524 |doi= 10.1073/pnas.240347797 }}
*{{cite journal  | author=Niwa  J, Ishigaki S, Doyu M, ''et al.'' |title=A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity. |journal=Biochem. Biophys. Res. Commun. |volume=281 |issue= 3 |pages= 706-13 |year= 2001 |pmid= 11237715 |doi= 10.1006/bbrc.2001.4414 }}
*{{cite journal  | author=Pringa E, Martinez-Noel G, Muller U, Harbers K |title=Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19617-23 |year= 2001 |pmid= 11274149 |doi= 10.1074/jbc.M100192200 }}
*{{cite journal  | author=Ardley HC, Tan NG, Rose SA, ''et al.'' |title=Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19640-7 |year= 2001 |pmid= 11278816 |doi= 10.1074/jbc.M011028200 }}
*{{cite journal  | author=Obin M, Lee BY, Meinke G, ''et al.'' |title=Ubiquitylation of the transducin betagamma subunit complex. Regulation by phosducin. |journal=J. Biol. Chem. |volume=277 |issue= 46 |pages= 44566-75 |year= 2003 |pmid= 12215439 |doi= 10.1074/jbc.M205308200 }}
*{{cite journal  | author=Wong ES, Fong CW, Lim J, ''et al.'' |title=Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. |journal=EMBO J. |volume=21 |issue= 18 |pages= 4796-808 |year= 2002 |pmid= 12234920 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}


{{gene-22-stub}}
There are 38 E2 enzymes in humans.<ref name="pmid19489725">{{cite journal | vauthors = Deshaies RJ, Joazeiro CA | title = RING domain E3 ubiquitin ligases | journal = Annual Review of Biochemistry | volume = 78 | pages = 399–434 | date = 2009 | pmid = 19489725 | doi = 10.1146/annurev.biochem.78.101807.093809 }}</ref> They all contain a conserved catalytic core [[Protein domain|domain]] that interacts with E1 and E3 and many E2s possess additional N- and/or [[C-terminal]] protein sequences.<ref name="pmid16142244">{{cite journal | vauthors = Eletr ZM, Huang DT, Duda DM, Schulman BA, Kuhlman B | title = E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer | journal = Nature Structural & Molecular Biology | volume = 12 | issue = 10 | pages = 933–4 | date = October 2005 | pmid = 16142244 | doi = 10.1038/nsmb984 }}</ref><ref name="pmid21158740">{{cite journal | vauthors = Wenzel DM, Stoll KE, Klevit RE | title = E2s: structurally economical and functionally replete | journal = The Biochemical Journal | volume = 433 | issue = 1 | pages = 31–42 | date = January 2011 | pmid = 21158740 | doi = 10.1042/BJ20100985 | pmc=3118098}}</ref> In contrast to other E2s, residues necessary for [[lysine]] reactivity are absent: the D87 and D117 residues (in [[UBCH5C]] numbering) are replaced by [[Proline|Pro]] and [[Histidine|His]] residues.<ref name="pmid21532592">{{cite journal | vauthors = Wenzel DM, Lissounov A, Brzovic PS, Klevit RE | title = UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids | journal = Nature | volume = 474 | issue = 7349 | pages = 105–8 | date = June 2011 | pmid = 21532592 | doi = 10.1038/nature09966 | pmc=3444301}}</ref>
{{WikiDoc Sources}}
 
== Function ==
 
The modification of proteins with [[ubiquitin]] is an important cellular mechanism for targeting abnormal or short-lived proteins for [[Biodegradation|degradation]]. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). E2s play a key role in the whole ubiquitin (Ub) transfer pathway and are responsible for Ub [[cellular signaling]]. Unlike many E2s that transfer Ub with RINGs, UBE2L3 has E3-independent reactivity with lysine.<ref name="pmid21532592"/> This enzyme is demonstrated to participate in the ubiquitination of [[p53]], [[c-Fos]], and the [[NF-κB]] precursor p105 in vitro. UBE2L3 is primarily known for its role in the [[cell cycle]]. Specifically, UBE2L3 manages cell cycle regulatory protein levels via the ubiquitin proteolytic pathway (UPP) during the G1/S transition and during the actual [[S phase]].<ref name = "pmid22476155">{{cite journal | vauthors = Wang S, Adrianto I, Wiley GB, Lessard CJ, Kelly JA, Adler AJ, Glenn SB, Williams AH, Ziegler JT, Comeau ME, Marion MC, Wakeland BE, Liang C, Kaufman KM, Guthridge JM, Alarcón-Riquelme ME, Alarcón GS, Anaya JM, Bae SC, Kim JH, Joo YB, Boackle SA, Brown EE, Petri MA, Ramsey-Goldman R, Reveille JD, Vilá LM, Criswell LA, Edberg JC, Freedman BI, Gilkeson GS, Jacob CO, James JA, Kamen DL, Kimberly RP, Martin J, Merrill JT, Niewold TB, Pons-Estel BA, Scofield RH, Stevens AM, Tsao BP, Vyse TJ, Langefeld CD, Harley JB, Wakeland EK, Moser KL, Montgomery CG, Gaffney PM | display-authors = 6 | title = A functional haplotype of UBE2L3 confers risk for systemic lupus erythematosus | journal = Genes and Immunity | volume = 13 | issue = 5 | pages = 380–7 | date = Jul 2012 | pmid = 22476155 | doi = 10.1038/gene.2012.6 | pmc=3411915}}</ref>
 
== Clinical significance ==
 
Through [[genome-wide association studies]] (GWAS), UBE2L3 has been associated with several autoimmune diseases, including [[Rheumatoid arthritis|RA]], [[celiac disease]], [[CD]], and [[Systemic lupus erythematosus|SLE]] via the ubiquitination of the NK-κB precursor.<ref name = "pmid22476155"/><ref name = "pmid24091983">{{cite journal | vauthors = Morlacchi F, Armenise D, Losacco V, Trapani G | title = [Quantitative microbiologic determination of organophosphorus compounds] | journal = Bollettino Chimico Farmaceutico | volume = 124 | issue = 9 | pages = 387–92 | date = September 1985 | pmid = 4091983 }}</ref><ref name="pmid20601676">{{cite journal | vauthors = Fransen K, Visschedijk MC, van Sommeren S, Fu JY, Franke L, Festen EA, Stokkers PC, van Bodegraven AA, Crusius JB, Hommes DW, Zanen P, de Jong DJ, Wijmenga C, van Diemen CC, Weersma RK | title = Analysis of SNPs with an effect on gene expression identifies UBE2L3 and BCL3 as potential new risk genes for Crohn's disease | journal = Human Molecular Genetics | volume = 19 | issue = 17 | pages = 3482–8 | date = September 2010 | pmid = 20601676 | doi = 10.1093/hmg/ddq264 }}</ref> This association was observed in European, Asian, and African-American populations.<ref name = "pmid22476155"/> UBE2L3 has been linked to natural killer cell cytotoxic function, and high UBE2L3 levels had contributed to clearing chronic HBV infection.<ref name = "pmid24162738"/><ref name = "pmid20601676"/> UBE2L3 controls the protein stability of [[53BP1]] and determines the DNA [[double-strand break]] repair choice. Loss of UBE2L3 stabilizes 53BP1 and force cells to choose [[NHEJ]] to repair DNA double-strand break. Repair by NHEJ leads to radial chromosomes and cell death.<ref name="pmid20453858">{{cite journal | vauthors = Bouwman P, Aly A, Escandell JM, Pieterse M, Bartkova J, van der Gulden H, Hiddingh S, Thanasoula M, Kulkarni A, Yang Q, Haffty BG, Tommiska J, Blomqvist C, Drapkin R, Adams DJ, Nevanlinna H, Bartek J, Tarsounas M, Ganesan S, Jonkers J | title = 53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers | journal = Nature Structural & Molecular Biology | volume = 17 | issue = 6 | pages = 688–95 | date = June 2010 | pmid = 20453858 | doi = 10.1038/nsmb.1831 | pmc=2912507}}</ref><ref name="pmid19716796">{{cite journal | vauthors = Cao L, Xu X, Bunting SF, Liu J, Wang RH, Cao LL, Wu JJ, Peng TN, Chen J, Nussenzweig A, Deng CX, Finkel T | title = A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency | journal = Molecular Cell | volume = 35 | issue = 4 | pages = 534–41 | date = August 2009 | pmid = 19716796 | doi = 10.1016/j.molcel.2009.06.037 | pmc=3392030}}</ref> UBE2L3 depletion may become a novel strategy in enhancing the effect of anticancer therapies.<ref name="pmid25322456">{{cite journal | vauthors = Mitchell LJ, Moody CJ | title = Solar photochemical oxidation of alcohols using catalytic hydroquinone and copper nanoparticles under oxygen: oxidative cleavage of lignin models | journal = The Journal of Organic Chemistry | volume = 79 | issue = 22 | pages = 11091–100 | date = November 2014 | pmid = 25322456 | doi = 10.1021/jo5020917 }}</ref> The haplotype of ''UBE2L3'' gene is also reported associated with [[Hashimoto's thyroiditis]] in a Chinese Han population.<ref name="pmid27094594">{{cite journal | vauthors = Wang Y, Zhu YF, Wang Q, Xu J, Yan N, Xu J, Shi LF, He ST, Zhang JA | title = The haplotype of UBE2L3 gene is associated with Hashimoto's thyroiditis in a Chinese Han population | journal = BMC Endocrine Disorders | volume = 16 | pages = 18 | date = 19 April 2016 | pmid = 27094594 | doi = 10.1186/s12902-016-0098-6 | pmc=4837539}}</ref>(27094594)
 
== Interactions ==
 
UBE2L3 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[ARIH1]],<ref name = pmid14623119>{{cite journal | vauthors = Tan NG, Ardley HC, Scott GB, Rose SA, Markham AF, Robinson PA | title = Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP | journal = FEBS Lett. | volume = 554 | issue = 3 | pages = 501–4  | date = November 2003 | pmid = 14623119 | doi =  10.1016/s0014-5793(03)01235-3}}</ref><ref name = pmid10521492>{{cite journal | vauthors = Moynihan TP, Ardley HC, Nuber U, Rose SA, Jones PF, Markham AF, Scheffner M, Robinson PA | title = The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1 | journal = J. Biol. Chem. | volume = 274 | issue = 43 | pages = 30963–8  | date = October 1999 | pmid = 10521492 | doi =  10.1074/jbc.274.43.30963}}</ref><ref name = pmid11278816>{{cite journal | vauthors = Ardley HC, Tan NG, Rose SA, Markham AF, Robinson PA | title = Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7 | journal = J. Biol. Chem. | volume = 276 | issue = 22 | pages = 19640–7  | date = June 2001 | pmid = 11278816 | doi = 10.1074/jbc.M011028200 }}</ref>
* [[ARIH2]],<ref name = "pmid18946090"/>
* [[Cbl gene|CBL]],<ref name = pmid10531381>{{cite journal | vauthors = Yokouchi M, Kondo T, Houghton A, Bartkiewicz M, Horne WC, Zhang H, Yoshimura A, Baron R | title = Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7 | journal = J. Biol. Chem. | volume = 274 | issue = 44 | pages = 31707–12  | date = October 1999 | pmid = 10531381 | doi =  10.1074/jbc.274.44.31707}}</ref><ref name = pmid10966114>{{cite journal | vauthors = Zheng N, Wang P, Jeffrey PD, Pavletich NP | title = Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases | journal = Cell | volume = 102 | issue = 4 | pages = 533–9  | date = August 2000 | pmid = 10966114 | doi =  10.1016/S0092-8674(00)00057-X}}</ref><ref name = pmid12234920>{{cite journal | vauthors = Wong ES, Fong CW, Lim J, Yusoff P, Low BC, Langdon WY, Guy GR | title = Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling | journal = EMBO J. | volume = 21 | issue = 18 | pages = 4796–808  | date = September 2002 | pmid = 12234920 | pmc = 126289 | doi =  10.1093/emboj/cdf493}}</ref>
* [[CHEK1]],<ref name = "pmid18946090">{{cite journal | vauthors = Whitcomb EA, Dudek EJ, Liu Q, Taylor A | title = Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7 | journal = Molecular Biology of the Cell | volume = 20 | issue = 1 | pages = 1–9 | date = Jan 2009 | pmid = 18946090 | doi = 10.1091/mbc.E08-01-0036 | pmc=2613108}}</ref>
* [[NEDD4]],<ref name = pmid9990509/><ref name = pmid18498246>{{cite journal | vauthors = Bruce MC, Kanelis V, Fouladkou F, Debonneville A, Staub O, Rotin D | title = Regulation of Nedd4-2 self-ubiquitination and stability by a PY motif located within its HECT-domain | journal = Biochem. J. | volume = 415 | issue = 1 | pages = 155–63  | date = October 2008 | pmid = 18498246 | doi = 10.1042/BJ20071708 }}</ref>
* [[Parkin (ligase)|PARK2]],<ref name = "pmid18946090"/>
* [[SMURF2]],<ref name = "pmid18946090"/>
* [[TNFAIP3]],<ref name = "pmid24091983"/>
* [[TNFSF4]],<ref name = "pmid24091983"/>
* [[TNIP1]],<ref name = "pmid24091983"/>
* [[TRAF6]],<ref name = "pmid18946090"/>
* [[UBE3A]],<ref name = "pmid18946090"/>
* [[UBE3A]],<ref name = pmid9990509>{{cite journal | vauthors = Anan T, Nagata Y, Koga H, Honda Y, Yabuki N, Miyamoto C, Kuwano A, Matsuda I, Endo F, Saya H, Nakao M | title = Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes | journal = Genes Cells | volume = 3 | issue = 11 | pages = 751–63  | date = November 1998 | pmid = 9990509 | doi =  10.1046/j.1365-2443.1998.00227.x}}</ref><ref name = pmid8576257>{{cite journal | vauthors = Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M | title = Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5 | journal = J. Biol. Chem. | volume = 271 | issue = 5 | pages = 2795–800  | date = February 1996 | pmid = 8576257 | doi =  10.1074/jbc.271.5.2795}}</ref><ref name = pmid10558980>{{cite journal | vauthors = Huang L, Kinnucan E, Wang G, Beaudenon S, Howley PM, Huibregtse JM, Pavletich NP | title = Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade | journal = Science | volume = 286 | issue = 5443 | pages = 1321–6  | date = November 1999 | pmid = 10558980 | doi =  10.1126/science.286.5443.1321}}</ref>  and
* [[UBOX5]].<ref name = pmid11274149>{{cite journal | vauthors = Pringa E, Martinez-Noel G, Muller U, Harbers K | title = Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes | journal = J. Biol. Chem. | volume = 276 | issue = 22 | pages = 19617–23  | date = June 2001 | pmid = 11274149 | doi = 10.1074/jbc.M100192200 }}</ref>
{{Div col end}}
 
{{Clear}}
 
== References ==
{{Reflist|33em}}
 
== Further reading ==
{{Refbegin|33em}}
* {{cite journal | vauthors = Blumenfeld N, Gonen H, Mayer A, Smith CE, Siegel NR, Schwartz AL, Ciechanover A | title = Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates | journal = J. Biol. Chem. | volume = 269 | issue = 13 | pages = 9574–81 | year = 1994 | pmid = 8144544 | doi =  }}
* {{cite journal | vauthors = Robinson PA, Leek JP, Thompson J, Carr IM, Bailey A, Moynihan TP, Coletta PL, Lench NJ, Markham AF | title = A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3 | journal = Mamm. Genome | volume = 6 | issue = 10 | pages = 725–31 | year = 1995 | pmid = 8563171 | doi = 10.1007/BF00354295 }}
* {{cite journal | vauthors = Kumar S, Kao WH, Howley PM | title = Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity | journal = J. Biol. Chem. | volume = 272 | issue = 21 | pages = 13548–54 | year = 1997 | pmid = 9153201 | doi = 10.1074/jbc.272.21.13548 }}
* {{cite journal | vauthors = Martinez-Noel G, Niedenthal R, Tamura T, Harbers K | title = A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4 | journal = FEBS Lett. | volume = 454 | issue = 3 | pages = 257–61 | year = 1999 | pmid = 10431818 | doi = 10.1016/S0014-5793(99)00823-6 }}
* {{cite journal | vauthors = Ardley HC, Moynihan TP, Markham AF, Robinson PA | title = Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7 | journal = Biochim. Biophys. Acta | volume = 1491 | issue = 1–3 | pages = 57–64 | year = 2000 | pmid = 10760570 | doi = 10.1016/s0167-4781(00)00024-5 }}
* {{cite journal | vauthors = Zhang Y, Gao J, Chung KK, Huang H, Dawson VL, Dawson TM | title = Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 24 | pages = 13354–9 | year = 2000 | pmid = 11078524 | pmc = 27228 | doi = 10.1073/pnas.240347797 }}
* {{cite journal | vauthors = Niwa J, Ishigaki S, Doyu M, Suzuki T, Tanaka K, Sobue G | title = A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity | journal = Biochem. Biophys. Res. Commun. | volume = 281 | issue = 3 | pages = 706–13 | year = 2001 | pmid = 11237715 | doi = 10.1006/bbrc.2001.4414 }}
* {{cite journal | vauthors = Obin M, Lee BY, Meinke G, Bohm A, Lee RH, Gaudet R, Hopp JA, Arshavsky VY, Willardson BM, Taylor A | title = Ubiquitylation of the transducin betagamma subunit complex. Regulation by phosducin | journal = J. Biol. Chem. | volume = 277 | issue = 46 | pages = 44566–75 | year = 2002 | pmid = 12215439 | doi = 10.1074/jbc.M205308200 }}
{{Refend}}
 
{{PDB Gallery|geneid=7332}}
{{Ubiquitin-conjugating enzymes}}

Latest revision as of 09:31, 17 September 2017

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Ubiquitin-conjugating enzyme E2 L3 (UBE2L3), also called UBCH7, is a protein that in humans is encoded by the UBE2L3 gene.[1][2][3] As an E2 enzyme, UBE2L3 participates in ubiquitination to target proteins for degradation.[3] The role of UBE2L3 in the ubiquitination of the NF-κB precursor implicated it in various major autoimmune diseases, including rheumatoid arthritis (RA), celiac disease, Crohn's disease(CD), and systemic lupus erythematosus.[4]

Structure

Gene

The UBE2L3 gene is located at chromosome 22q11.21, consisting of 6 exons.Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.[3]

Protein

There are 38 E2 enzymes in humans.[5] They all contain a conserved catalytic core domain that interacts with E1 and E3 and many E2s possess additional N- and/or C-terminal protein sequences.[6][7] In contrast to other E2s, residues necessary for lysine reactivity are absent: the D87 and D117 residues (in UBCH5C numbering) are replaced by Pro and His residues.[8]

Function

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). E2s play a key role in the whole ubiquitin (Ub) transfer pathway and are responsible for Ub cellular signaling. Unlike many E2s that transfer Ub with RINGs, UBE2L3 has E3-independent reactivity with lysine.[8] This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-κB precursor p105 in vitro. UBE2L3 is primarily known for its role in the cell cycle. Specifically, UBE2L3 manages cell cycle regulatory protein levels via the ubiquitin proteolytic pathway (UPP) during the G1/S transition and during the actual S phase.[9]

Clinical significance

Through genome-wide association studies (GWAS), UBE2L3 has been associated with several autoimmune diseases, including RA, celiac disease, CD, and SLE via the ubiquitination of the NK-κB precursor.[9][10][11] This association was observed in European, Asian, and African-American populations.[9] UBE2L3 has been linked to natural killer cell cytotoxic function, and high UBE2L3 levels had contributed to clearing chronic HBV infection.[4][11] UBE2L3 controls the protein stability of 53BP1 and determines the DNA double-strand break repair choice. Loss of UBE2L3 stabilizes 53BP1 and force cells to choose NHEJ to repair DNA double-strand break. Repair by NHEJ leads to radial chromosomes and cell death.[12][13] UBE2L3 depletion may become a novel strategy in enhancing the effect of anticancer therapies.[14] The haplotype of UBE2L3 gene is also reported associated with Hashimoto's thyroiditis in a Chinese Han population.[15](27094594)

Interactions

UBE2L3 has been shown to interact with:

References

  1. ↑ Moynihan TP, Ardley HC, Leek JP, Thompson J, Brindle NS, Markham AF, Robinson PA (October 1996). "Characterization of a human ubiquitin-conjugating enzyme gene UBE2L3". Mamm. Genome. 7 (7): 520–5. doi:10.1007/s003359900155. PMID 8672131.
  2. ↑ Moynihan TP, Cole CG, Dunham I, O'Neil L, Markham AF, Robinson PA (September 1998). "Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3". Genomics. 51 (1): 124–7. doi:10.1006/geno.1998.5257. PMID 9693040.
  3. ↑ 3.0 3.1 3.2 "Entrez Gene: UBE2L3 ubiquitin-conjugating enzyme E2L 3".
  4. ↑ 4.0 4.1 Hu Z, Liu Y, Zhai X, Dai J, Jin G, Wang L, et al. (Dec 2013). "New loci associated with chronic hepatitis B virus infection in Han Chinese". Nature Genetics. 45 (12): 1499–503. doi:10.1038/ng.2809. PMID 24162738.
  5. ↑ Deshaies RJ, Joazeiro CA (2009). "RING domain E3 ubiquitin ligases". Annual Review of Biochemistry. 78: 399–434. doi:10.1146/annurev.biochem.78.101807.093809. PMID 19489725.
  6. ↑ Eletr ZM, Huang DT, Duda DM, Schulman BA, Kuhlman B (October 2005). "E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer". Nature Structural & Molecular Biology. 12 (10): 933–4. doi:10.1038/nsmb984. PMID 16142244.
  7. ↑ Wenzel DM, Stoll KE, Klevit RE (January 2011). "E2s: structurally economical and functionally replete". The Biochemical Journal. 433 (1): 31–42. doi:10.1042/BJ20100985. PMC 3118098. PMID 21158740.
  8. ↑ 8.0 8.1 Wenzel DM, Lissounov A, Brzovic PS, Klevit RE (June 2011). "UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids". Nature. 474 (7349): 105–8. doi:10.1038/nature09966. PMC 3444301. PMID 21532592.
  9. ↑ 9.0 9.1 9.2 Wang S, Adrianto I, Wiley GB, Lessard CJ, Kelly JA, Adler AJ, et al. (Jul 2012). "A functional haplotype of UBE2L3 confers risk for systemic lupus erythematosus". Genes and Immunity. 13 (5): 380–7. doi:10.1038/gene.2012.6. PMC 3411915. PMID 22476155.
  10. ↑ 10.0 10.1 10.2 10.3 Morlacchi F, Armenise D, Losacco V, Trapani G (September 1985). "[Quantitative microbiologic determination of organophosphorus compounds]". Bollettino Chimico Farmaceutico. 124 (9): 387–92. PMID 4091983.
  11. ↑ 11.0 11.1 Fransen K, Visschedijk MC, van Sommeren S, Fu JY, Franke L, Festen EA, Stokkers PC, van Bodegraven AA, Crusius JB, Hommes DW, Zanen P, de Jong DJ, Wijmenga C, van Diemen CC, Weersma RK (September 2010). "Analysis of SNPs with an effect on gene expression identifies UBE2L3 and BCL3 as potential new risk genes for Crohn's disease". Human Molecular Genetics. 19 (17): 3482–8. doi:10.1093/hmg/ddq264. PMID 20601676.
  12. ↑ Bouwman P, Aly A, Escandell JM, Pieterse M, Bartkova J, van der Gulden H, Hiddingh S, Thanasoula M, Kulkarni A, Yang Q, Haffty BG, Tommiska J, Blomqvist C, Drapkin R, Adams DJ, Nevanlinna H, Bartek J, Tarsounas M, Ganesan S, Jonkers J (June 2010). "53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers". Nature Structural & Molecular Biology. 17 (6): 688–95. doi:10.1038/nsmb.1831. PMC 2912507. PMID 20453858.
  13. ↑ Cao L, Xu X, Bunting SF, Liu J, Wang RH, Cao LL, Wu JJ, Peng TN, Chen J, Nussenzweig A, Deng CX, Finkel T (August 2009). "A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency". Molecular Cell. 35 (4): 534–41. doi:10.1016/j.molcel.2009.06.037. PMC 3392030. PMID 19716796.
  14. ↑ Mitchell LJ, Moody CJ (November 2014). "Solar photochemical oxidation of alcohols using catalytic hydroquinone and copper nanoparticles under oxygen: oxidative cleavage of lignin models". The Journal of Organic Chemistry. 79 (22): 11091–100. doi:10.1021/jo5020917. PMID 25322456.
  15. ↑ Wang Y, Zhu YF, Wang Q, Xu J, Yan N, Xu J, Shi LF, He ST, Zhang JA (19 April 2016). "The haplotype of UBE2L3 gene is associated with Hashimoto's thyroiditis in a Chinese Han population". BMC Endocrine Disorders. 16: 18. doi:10.1186/s12902-016-0098-6. PMC 4837539. PMID 27094594.
  16. ↑ Tan NG, Ardley HC, Scott GB, Rose SA, Markham AF, Robinson PA (November 2003). "Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP". FEBS Lett. 554 (3): 501–4. doi:10.1016/s0014-5793(03)01235-3. PMID 14623119.
  17. ↑ Moynihan TP, Ardley HC, Nuber U, Rose SA, Jones PF, Markham AF, Scheffner M, Robinson PA (October 1999). "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1". J. Biol. Chem. 274 (43): 30963–8. doi:10.1074/jbc.274.43.30963. PMID 10521492.
  18. ↑ Ardley HC, Tan NG, Rose SA, Markham AF, Robinson PA (June 2001). "Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7". J. Biol. Chem. 276 (22): 19640–7. doi:10.1074/jbc.M011028200. PMID 11278816.
  19. ↑ 19.0 19.1 19.2 19.3 19.4 19.5 Whitcomb EA, Dudek EJ, Liu Q, Taylor A (Jan 2009). "Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7". Molecular Biology of the Cell. 20 (1): 1–9. doi:10.1091/mbc.E08-01-0036. PMC 2613108. PMID 18946090.
  20. ↑ Yokouchi M, Kondo T, Houghton A, Bartkiewicz M, Horne WC, Zhang H, Yoshimura A, Baron R (October 1999). "Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7". J. Biol. Chem. 274 (44): 31707–12. doi:10.1074/jbc.274.44.31707. PMID 10531381.
  21. ↑ Zheng N, Wang P, Jeffrey PD, Pavletich NP (August 2000). "Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases". Cell. 102 (4): 533–9. doi:10.1016/S0092-8674(00)00057-X. PMID 10966114.
  22. ↑ Wong ES, Fong CW, Lim J, Yusoff P, Low BC, Langdon WY, Guy GR (September 2002). "Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling". EMBO J. 21 (18): 4796–808. doi:10.1093/emboj/cdf493. PMC 126289. PMID 12234920.
  23. ↑ 23.0 23.1 Anan T, Nagata Y, Koga H, Honda Y, Yabuki N, Miyamoto C, Kuwano A, Matsuda I, Endo F, Saya H, Nakao M (November 1998). "Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes". Genes Cells. 3 (11): 751–63. doi:10.1046/j.1365-2443.1998.00227.x. PMID 9990509.
  24. ↑ Bruce MC, Kanelis V, Fouladkou F, Debonneville A, Staub O, Rotin D (October 2008). "Regulation of Nedd4-2 self-ubiquitination and stability by a PY motif located within its HECT-domain". Biochem. J. 415 (1): 155–63. doi:10.1042/BJ20071708. PMID 18498246.
  25. ↑ Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M (February 1996). "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5". J. Biol. Chem. 271 (5): 2795–800. doi:10.1074/jbc.271.5.2795. PMID 8576257.
  26. ↑ Huang L, Kinnucan E, Wang G, Beaudenon S, Howley PM, Huibregtse JM, Pavletich NP (November 1999). "Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade". Science. 286 (5443): 1321–6. doi:10.1126/science.286.5443.1321. PMID 10558980.
  27. ↑ Pringa E, Martinez-Noel G, Muller U, Harbers K (June 2001). "Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes". J. Biol. Chem. 276 (22): 19617–23. doi:10.1074/jbc.M100192200. PMID 11274149.

Further reading

  • Blumenfeld N, Gonen H, Mayer A, Smith CE, Siegel NR, Schwartz AL, Ciechanover A (1994). "Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates". J. Biol. Chem. 269 (13): 9574–81. PMID 8144544.
  • Robinson PA, Leek JP, Thompson J, Carr IM, Bailey A, Moynihan TP, Coletta PL, Lench NJ, Markham AF (1995). "A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3". Mamm. Genome. 6 (10): 725–31. doi:10.1007/BF00354295. PMID 8563171.
  • Kumar S, Kao WH, Howley PM (1997). "Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity". J. Biol. Chem. 272 (21): 13548–54. doi:10.1074/jbc.272.21.13548. PMID 9153201.
  • Martinez-Noel G, Niedenthal R, Tamura T, Harbers K (1999). "A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4". FEBS Lett. 454 (3): 257–61. doi:10.1016/S0014-5793(99)00823-6. PMID 10431818.
  • Ardley HC, Moynihan TP, Markham AF, Robinson PA (2000). "Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7". Biochim. Biophys. Acta. 1491 (1–3): 57–64. doi:10.1016/s0167-4781(00)00024-5. PMID 10760570.
  • Zhang Y, Gao J, Chung KK, Huang H, Dawson VL, Dawson TM (2000). "Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1". Proc. Natl. Acad. Sci. U.S.A. 97 (24): 13354–9. doi:10.1073/pnas.240347797. PMC 27228. PMID 11078524.
  • Niwa J, Ishigaki S, Doyu M, Suzuki T, Tanaka K, Sobue G (2001). "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity". Biochem. Biophys. Res. Commun. 281 (3): 706–13. doi:10.1006/bbrc.2001.4414. PMID 11237715.
  • Obin M, Lee BY, Meinke G, Bohm A, Lee RH, Gaudet R, Hopp JA, Arshavsky VY, Willardson BM, Taylor A (2002). "Ubiquitylation of the transducin betagamma subunit complex. Regulation by phosducin". J. Biol. Chem. 277 (46): 44566–75. doi:10.1074/jbc.M205308200. PMID 12215439.
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