UBE2N: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Ubiquitin-conjugating enzyme E2 N''' is a [[protein]] that in humans is encoded by the ''UBE2N'' [[gene]].<ref name="pmid8902611">{{cite journal | vauthors = Yamaguchi T, Kim NS, Sekine S, Seino H, Osaka F, Yamao F, Kato S | title = Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product | journal = J Biochem | volume = 120 | issue = 3 | pages = 494–97 | date = February 1997 | pmid = 8902611 | pmc = | doi = 10.1093/oxfordjournals.jbchem.a021440 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7334| accessdate = }}</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. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_UBE2N_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1j7d.
| PDB = {{PDB2|1j7d}}, {{PDB2|2c2v}}
| Name = Ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)
| HGNCid = 12492
| Symbol = UBE2N
| AltSymbols =; MGC131857; MGC8489; UBC13; UbcH-ben
| OMIM = 603679
| ECnumber = 
| Homologene = 2512
| MGIid = 1934835
| GeneAtlas_image1 = PBB_GE_UBE2N_212751_at_tn.png
| GeneAtlas_image2 = PBB_GE_UBE2N_201523_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_UBE2N_201524_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0043130 |text = ubiquitin binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0031372 |text = UBC13-MMS2 complex}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0016567 |text = protein ubiquitination}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0045739 |text = positive regulation of DNA repair}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}} {{GNF_GO|id=GO:0051092 |text = activation of NF-kappaB transcription factor}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7334
    | Hs_Ensembl = ENSG00000177889
    | Hs_RefseqProtein = NP_003339
    | Hs_RefseqmRNA = NM_003348
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 92326221
    | Hs_GenLoc_end = 92360157
    | Hs_Uniprot = P61088
    | Mm_EntrezGene = 93765
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_080560
    | Mm_RefseqProtein = NP_542127
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)''', also known as '''UBE2N''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7334| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Studies in mouse suggest that this protein plays a role in DNA postreplication repair.<ref name="entrez"/>
{{PBB_Summary
| 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, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Studies in mouse suggest that this protein plays a role in DNA postreplication repair.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7334| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
UBE2N has been shown to [[Protein-protein interaction|interact]] with:
* [[Aurora A kinase|AURKA]],<ref name = pmid12881723>{{cite journal | vauthors = Ewart-Toland A, Briassouli P, de Koning JP, Mao JH, Yuan J, Chan F, MacCarthy-Morrogh L, Ponder BA, Nagase H, Burn J, Ball S, Almeida M, Linardopoulos S, Balmain A | title = Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human | journal = Nat. Genet. | volume = 34 | issue = 4 | pages = 403–12 | date = August 2003 | pmid = 12881723 | doi = 10.1038/ng1220 }}</ref>
* [[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 = Proc. Natl. Acad. Sci. U.S.A. | volume = 105 | issue = 10 | pages = 3768–73 | date = March 2008 | pmid = 18316726 | pmc = 2268824 | doi = 10.1073/pnas.0800563105 }}</ref>
* [[TRAF2]],<ref name = pmid11057907>{{cite journal | vauthors = Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ | title = Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain | journal = Cell | volume = 103 | issue = 2 | pages = 351–61 | date = October 2000 | pmid = 11057907 | doi =  10.1016/s0092-8674(00)00126-4}}</ref>
* [[TRAF6]],<ref name = pmid11057907/>  and
* [[UBE2V1]].<ref name = pmid11057907/>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery. | journal = Genome Res. | volume = 6 | issue = 9 | pages = 791–806 | year = 1997 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
| citations =
* {{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 | year = 1999 | pmid = 10089880 | doi = 10.1016/S0092-8674(00)80575-9 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ | title = Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. | journal = Cell | volume = 103 | issue = 2 | pages = 351–61 | year = 2000 | pmid = 11057907 | doi = 10.1016/S0092-8674(00)00126-4 }}
*{{cite journal  | author=Yamaguchi T, Kim NS, Sekine S, ''et al.'' |title=Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product. |journal=J. Biochem. |volume=120 |issue= 3 |pages= 494-97 |year= 1997 |pmid= 8902611 |doi=  }}
* {{cite journal | vauthors = Chan NL, Hill CP | title = Defining polyubiquitin chain topology. | journal = Nat. Struct. Biol. | volume = 8 | issue = 8 | pages = 650–2 | year = 2001 | pmid = 11473244 | doi = 10.1038/90337 }}
*{{cite journal | author=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 |year= 1999 |pmid= 10089880 |doi= }}
* {{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 = Nat. Struct. Biol. | volume = 8 | issue = 8 | pages = 669–73 | year = 2001 | pmid = 11473255 | doi = 10.1038/90373 }}
*{{cite journal | author=Deng L, Wang C, Spencer E, ''et al.'' |title=Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. |journal=Cell |volume=103 |issue= 2 |pages= 351-61 |year= 2000 |pmid= 11057907 |doi= }}
* {{cite journal | vauthors = Ashley C, Pastushok L, McKenna S, Ellison MJ, Xiao W | title = Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked ubiquitination. | journal = Gene | volume = 285 | issue = 1-2 | pages = 183–91 | year = 2002 | pmid = 12039045 | doi = 10.1016/S0378-1119(02)00409-2 }}
*{{cite journal | author=Chan NL, Hill CP |title=Defining polyubiquitin chain topology. |journal=Nat. Struct. Biol. |volume=8 |issue= 8 |pages= 650-2 |year= 2001 |pmid= 11473244 |doi= 10.1038/90337 }}
* {{cite journal | vauthors = McKenna S, Moraes T, Pastushok L, Ptak C, Xiao W, Spyracopoulos L, Ellison MJ | title = An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis. | journal = J. Biol. Chem. | volume = 278 | issue = 15 | pages = 13151–8 | year = 2003 | pmid = 12569095 | doi = 10.1074/jbc.M212353200 }}
*{{cite journal | author=Moraes TF, Edwards RA, McKenna S, ''et al.'' |title=Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13. |journal=Nat. Struct. Biol. |volume=8 |issue= 8 |pages= 669-73 |year= 2001 |pmid= 11473255 |doi= 10.1038/90373 }}
* {{cite journal | vauthors = Anandasabapathy N, Ford GS, Bloom D, Holness C, Paragas V, Seroogy C, Skrenta H, Hollenhorst M, Fathman CG, Soares L | title = GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells. | journal = Immunity | volume = 18 | issue = 4 | pages = 535–47 | year = 2003 | pmid = 12705856 | doi = 10.1016/S1074-7613(03)00084-0 }}
*{{cite journal | author=Ashley C, Pastushok L, McKenna S, ''et al.'' |title=Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked ubiquitination. |journal=Gene |volume=285 |issue= 1-2 |pages= 183-91 |year= 2002 |pmid= 12039045 |doi= }}
* {{cite journal | vauthors = Ewart-Toland A, Briassouli P, de Koning JP, Mao JH, Yuan J, Chan F, MacCarthy-Morrogh L, Ponder BA, Nagase H, Burn J, Ball S, Almeida M, Linardopoulos S, Balmain A | title = Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human. | journal = Nat. Genet. | volume = 34 | issue = 4 | pages = 403–12 | year = 2003 | pmid = 12881723 | doi = 10.1038/ng1220 }}
*{{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 }}
* {{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 | year = 2003 | pmid = 14562038 | doi = 10.1038/sj.onc.1206831 }}
*{{cite journal | author=McKenna S, Moraes T, Pastushok L, ''et al.'' |title=An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis. |journal=J. Biol. Chem. |volume=278 |issue= 15 |pages= 13151-8 |year= 2003 |pmid= 12569095 |doi= 10.1074/jbc.M212353200 }}
* {{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 | year = 2004 | pmid = 14695475 | doi = 10.1038/nature02273 }}
*{{cite journal | author=Anandasabapathy N, Ford GS, Bloom D, ''et al.'' |title=GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells. |journal=Immunity |volume=18 |issue= 4 |pages= 535-47 |year= 2003 |pmid= 12705856 |doi= }}
* {{cite journal | vauthors = Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ | title = The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. | journal = Mol. Cell | volume = 14 | issue = 3 | pages = 289–301 | year = 2004 | pmid = 15125833 | doi = 10.1016/S1097-2765(04)00236-9 }}
*{{cite journal | author=Ewart-Toland A, Briassouli P, de Koning JP, ''et al.'' |title=Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human. |journal=Nat. Genet. |volume=34 |issue= 4 |pages= 403-12 |year= 2003 |pmid= 12881723 |doi= 10.1038/ng1220 }}
* {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional proteomics mapping of a human signaling pathway. | journal = Genome Res. | volume = 14 | issue = 7 | pages = 1324–32 | year = 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }}
*{{cite journal | author=Bothos J, Summers MK, Venere M, ''et al.'' |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 |year= 2003 |pmid= 14562038 |doi= 10.1038/sj.onc.1206831 }}
* {{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 = J. Biol. Chem. | volume = 280 | issue = 18 | pages = 17891–900 | year = 2005 | pmid = 15749714 | doi = 10.1074/jbc.M410469200 }}
*{{cite journal | author=Zhou H, Wertz I, O'Rourke K, ''et al.'' |title=Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO. |journal=Nature |volume=427 |issue= 6970 |pages= 167-71 |year= 2004 |pmid= 14695475 |doi= 10.1038/nature02273 }}
* {{cite journal | vauthors = Takeuchi T, Yokosawa H | title = ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity. | journal = Biochem. Biophys. Res. Commun. | volume = 336 | issue = 1 | pages = 9–13 | year = 2005 | pmid = 16112642 | doi = 10.1016/j.bbrc.2005.08.034 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Zou W, Papov V, Malakhova O, Kim KI, Dao C, Li J, Zhang DE | title = ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin. | journal = Biochem. Biophys. Res. Commun. | volume = 336 | issue = 1 | pages = 61–8 | year = 2005 | pmid = 16122702 | doi = 10.1016/j.bbrc.2005.08.038 }}
*{{cite journal  | author=Sun L, Deng L, Ea CK, ''et al.'' |title=The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. |journal=Mol. Cell |volume=14 |issue= 3 |pages= 289-301 |year= 2004 |pmid= 15125833 |doi= }}
*{{cite journal | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=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=J. Biol. Chem. |volume=280 |issue= 18 |pages= 17891-900 |year= 2005 |pmid= 15749714 |doi= 10.1074/jbc.M410469200 }}
*{{cite journal | author=Takeuchi T, Yokosawa H |title=ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity. |journal=Biochem. Biophys. Res. Commun. |volume=336 |issue= 1 |pages= 9-13 |year= 2005 |pmid= 16112642 |doi= 10.1016/j.bbrc.2005.08.034 }}
*{{cite journal | author=Zou W, Papov V, Malakhova O, ''et al.'' |title=ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin. |journal=Biochem. Biophys. Res. Commun. |volume=336 |issue= 1 |pages= 61-8 |year= 2005 |pmid= 16122702 |doi= 10.1016/j.bbrc.2005.08.038 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=7334}}
{{WikiDoc Sources}}
{{Ubiquitin-conjugating enzymes}}
 
 
{{gene-12-stub}}

Latest revision as of 01:58, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Ubiquitin-conjugating enzyme E2 N is a protein that in humans is encoded by the UBE2N gene.[1][2]

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, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Studies in mouse suggest that this protein plays a role in DNA postreplication repair.[2]

Interactions

UBE2N has been shown to interact with:

References

  1. ↑ Yamaguchi T, Kim NS, Sekine S, Seino H, Osaka F, Yamao F, Kato S (February 1997). "Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product". J Biochem. 120 (3): 494–97. doi:10.1093/oxfordjournals.jbchem.a021440. PMID 8902611.
  2. ↑ 2.0 2.1 "Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)".
  3. ↑ Ewart-Toland A, Briassouli P, de Koning JP, Mao JH, Yuan J, Chan F, MacCarthy-Morrogh L, Ponder BA, Nagase H, Burn J, Ball S, Almeida M, Linardopoulos S, Balmain A (August 2003). "Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human". Nat. Genet. 34 (4): 403–12. doi:10.1038/ng1220. PMID 12881723.
  4. ↑ 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". Proc. Natl. Acad. Sci. U.S.A. 105 (10): 3768–73. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726.
  5. ↑ 5.0 5.1 5.2 Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (October 2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell. 103 (2): 351–61. doi:10.1016/s0092-8674(00)00126-4. PMID 11057907.

Further reading

  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Hofmann RM, Pickart CM (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.
  • Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell. 103 (2): 351–61. doi:10.1016/S0092-8674(00)00126-4. PMID 11057907.
  • Chan NL, Hill CP (2001). "Defining polyubiquitin chain topology". Nat. Struct. Biol. 8 (8): 650–2. doi:10.1038/90337. PMID 11473244.
  • Moraes TF, Edwards RA, McKenna S, Pastushok L, Xiao W, Glover JN, Ellison MJ (2001). "Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13". Nat. Struct. Biol. 8 (8): 669–73. doi:10.1038/90373. PMID 11473255.
  • Ashley C, Pastushok L, McKenna S, Ellison MJ, Xiao W (2002). "Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked ubiquitination". Gene. 285 (1–2): 183–91. doi:10.1016/S0378-1119(02)00409-2. PMID 12039045.
  • McKenna S, Moraes T, Pastushok L, Ptak C, Xiao W, Spyracopoulos L, Ellison MJ (2003). "An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis". J. Biol. Chem. 278 (15): 13151–8. doi:10.1074/jbc.M212353200. PMID 12569095.
  • Anandasabapathy N, Ford GS, Bloom D, Holness C, Paragas V, Seroogy C, Skrenta H, Hollenhorst M, Fathman CG, Soares L (2003). "GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells". Immunity. 18 (4): 535–47. doi:10.1016/S1074-7613(03)00084-0. PMID 12705856.
  • Ewart-Toland A, Briassouli P, de Koning JP, Mao JH, Yuan J, Chan F, MacCarthy-Morrogh L, Ponder BA, Nagase H, Burn J, Ball S, Almeida M, Linardopoulos S, Balmain A (2003). "Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human". Nat. Genet. 34 (4): 403–12. doi:10.1038/ng1220. PMID 12881723.
  • Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD (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 (2004). "Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO". Nature. 427 (6970): 167–71. doi:10.1038/nature02273. PMID 14695475.
  • Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ (2004). "The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes". Mol. Cell. 14 (3): 289–301. doi:10.1016/S1097-2765(04)00236-9. PMID 15125833.
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