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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 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 = Mol. Cell. Biol. | volume = 18 | issue = 1 | pages = 576–89  | date = Jan 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 = Biochem. Biophys. Res. Commun. | volume = 235 | issue = 2 | pages = 407–12  | date = Jul 1997 | pmid = 9199207 | pmc = | doi = 10.1006/bbrc.1997.6798 }}</ref><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| 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_UBE2V2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1j74.
| PDB = {{PDB2|1j74}}, {{PDB2|1j7d}}, {{PDB2|1zgu}}, {{PDB2|2a4d}}, {{PDB2|2c2v}}, {{PDB2|2hlw}}
| Name = Ubiquitin-conjugating enzyme E2 variant 2
| HGNCid = 12495
| Symbol = UBE2V2
| AltSymbols =; DDVIT1; DDVit-1; EDAF-1; EDPF-1; EDPF1; MMS2; UEV-2; UEV2
| OMIM = 603001
| ECnumber = 
| Homologene = 55739
| MGIid = 1917870
| GeneAtlas_image1 = PBB_GE_UBE2V2_209096_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein 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:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000209 |text = protein polyubiquitination}} {{GNF_GO|id=GO:0006282 |text = regulation of DNA repair}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7336
    | Hs_Ensembl = ENSG00000169139
    | Hs_RefseqProtein = NP_003341
    | Hs_RefseqmRNA = NM_003350
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 49116860
    | Hs_GenLoc_end = 49136683
    | Hs_Uniprot = Q15819
    | Mm_EntrezGene = 70620
    | Mm_Ensembl = ENSMUSG00000068964
    | Mm_RefseqmRNA = NM_023585
    | Mm_RefseqProtein = NP_076074
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 100570771
    | Mm_GenLoc_end = 100571939
    | Mm_Uniprot = Q4VBX4
  }}
}}
'''Ubiquitin-conjugating enzyme E2 variant 2''', also known as '''UBE2V2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBE2V2 ubiquitin-conjugating enzyme E2 variant 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7336| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family. They have 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. It may be involved in the differentiation of monocytes and enterocytes.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family. They have 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. It may be involved in the differentiation of monocytes and enterocytes.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2V2 ubiquitin-conjugating enzyme E2 variant 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7336| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
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 = Proc. Natl. Acad. Sci. U.S.A. | volume = 105 | issue = 10 | pages = 3768–73  | date = Mar 2008 | pmid = 18316726 | pmc = 2268824 | doi = 10.1073/pnas.0800563105 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{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 Res. | volume = 26 | issue = 17 | pages = 3908–14 | year = 1998 | pmid = 9705497 | pmc = 147796 | doi = 10.1093/nar/26.17.3908 }}
| 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=Fritsche J, Rehli M, Krause SW, ''et al.'' |title=Molecular cloning of a 1alpha,25-dihydroxyvitamin D3-inducible transcript (DDVit 1) in human blood monocytes. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 2 |pages= 407-12 |year= 1997 |pmid= 9199207 |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=Sancho E, Vilá MR, Sánchez-Pulido L, ''et al.'' |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=Mol. Cell. Biol. |volume=18 |issue= 1 |pages= 576-89 |year= 1998 |pmid= 9418904 |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=Xiao W, Lin SL, Broomfield S, ''et al.'' |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 Res. |volume=26 |issue= 17 |pages= 3908-14 |year= 1998 |pmid= 9705497 |doi= }}
* {{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 = Nat. Biotechnol. | volume = 21 | issue = 5 | pages = 566–9 | year = 2003 | pmid = 12665801 | doi = 10.1038/nbt810 }}
*{{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 = 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=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 = 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=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 = Simpson LJ, Sale JE | title = UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40 | journal = DNA Repair (Amst.) | volume = 4 | issue = 4 | pages = 503–10 | year = 2005 | pmid = 15725630 | doi = 10.1016/j.dnarep.2004.12.002 }}
*{{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 = 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=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
* {{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 | year = 2005 | pmid = 15952783 | doi = 10.1021/bi050065k }}
*{{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 = 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 = J. Cell Biol. | volume = 170 | issue = 5 | pages = 745–55 | year = 2005 | pmid = 16129784 | pmc = 2171356 | doi = 10.1083/jcb.200502113 }}
*{{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 = 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 | year = 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }}
*{{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 = 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 Mol. Biol. | volume = 61 | issue = 1-2 | pages = 241–53 | year = 2006 | pmid = 16786304 | doi = 10.1007/s11103-006-0007-x }}
*{{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 | 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 = Mol. Cell | volume = 25 | issue = 5 | pages = 663–75 | year = 2007 | pmid = 17349954 | doi = 10.1016/j.molcel.2007.01.029 }}
*{{cite journal  | author=Simpson LJ, Sale JE |title=UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40. |journal=DNA Repair (Amst.) |volume=4 |issue= 4 |pages= 503-10 |year= 2005 |pmid= 15725630 |doi= 10.1016/j.dnarep.2004.12.002 }}
*{{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=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 |year= 2005 |pmid= 15952783 |doi= 10.1021/bi050065k }}
*{{cite journal | author=Andersen PL, Zhou H, Pastushok L, ''et al.'' |title=Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. |journal=J. Cell Biol. |volume=170 |issue= 5 |pages= 745-55 |year= 2005 |pmid= 16129784 |doi= 10.1083/jcb.200502113 }}
*{{cite journal | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal | author=Wen R, Newton L, Li G, ''et al.'' |title=Arabidopsis thaliana UBC13: implication of error-free DNA damage tolerance and Lys63-linked polyubiquitylation in plants. |journal=Plant Mol. Biol. |volume=61 |issue= 1-2 |pages= 241-53 |year= 2006 |pmid= 16786304 |doi= 10.1007/s11103-006-0007-x }}
*{{cite journal | author=Zhao GY, Sonoda E, Barber LJ, ''et al.'' |title=A critical role for the ubiquitin-conjugating enzyme Ubc13 in initiating homologous recombination. |journal=Mol. Cell |volume=25 |issue= 5 |pages= 663-75 |year= 2007 |pmid= 17349954 |doi= 10.1016/j.molcel.2007.01.029 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=7336}}
{{WikiDoc Sources}}
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{{gene-8-stub}}

Revision as of 09:32, 17 September 2017

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

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Ensembl

n/a

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UniProt

n/a

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RefSeq (mRNA)

n/a

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RefSeq (protein)

n/a

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

Ubiquitin-conjugating enzyme E2 variant 2 is a protein that in humans is encoded by the UBE2V2 gene.[1][2][3]

Function

Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family. They have 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. It may be involved in the differentiation of monocytes and enterocytes.[3]

Interactions

UBE2V2 has been shown to interact with HLTF.[4]

References

  1. ↑ 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 (Jan 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". Mol. Cell. Biol. 18 (1): 576–89. doi:10.1128/mcb.18.1.576. PMC 121525. PMID 9418904.
  2. ↑ Fritsche J, Rehli M, Krause SW, Andreesen R, Kreutz M (Jul 1997). "Molecular cloning of a 1alpha,25-dihydroxyvitamin D3-inducible transcript (DDVit 1) in human blood monocytes". Biochem. Biophys. Res. Commun. 235 (2): 407–12. doi:10.1006/bbrc.1997.6798. PMID 9199207.
  3. ↑ 3.0 3.1 "Entrez Gene: UBE2V2 ubiquitin-conjugating enzyme E2 variant 2".
  4. ↑ Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L (Mar 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.

Further reading


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