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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 1''' is a [[protein]] that in humans is encoded by the ''UBE2V1'' [[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 = January 1998 | pmid = 9418904 | pmc = 121525 | doi =  10.1128/mcb.18.1.576}}</ref><ref name="pmid9305758">{{cite journal | vauthors = Rothofsky ML, Lin SL | title = CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter | journal = Gene | volume = 195 | issue = 2 | pages = 141–9 | date = October 1997 | pmid = 9305758 | pmc = | doi = 10.1016/S0378-1119(97)00097-8 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBE2V1 ubiquitin-conjugating enzyme E2 variant 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7335| 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_UBE2V1_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 1
| HGNCid = 12494
| Symbol = UBE2V1
| AltSymbols =; CIR1; CROC-1; CROC1; UBE2V; UEV-1; UEV1; UEV1A
| OMIM = 602995
| ECnumber = 
| Homologene = 81888
| MGIid = 1913839
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0031371 |text = ubiquitin conjugating enzyme 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:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0051092 |text = activation of NF-kappaB transcription factor}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7335
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_001027459
    | Hs_RefseqmRNA = NM_001032288
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 66589
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_023230
    | Mm_RefseqProtein = NP_075719
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Ubiquitin-conjugating enzyme E2 variant 1''', also known as '''UBE2V1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBE2V1 ubiquitin-conjugating enzyme E2 variant 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7335| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Ubiquitin-conjugating E2 enzyme 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 is located in the nucleus and can cause transcriptional activation of the human FOS proto-oncogene. It is thought to be involved in the control of differentiation by altering cell cycle behavior. Multiple alternatively spliced transcripts encoding different isoforms have been described for this gene. A pseudogene has been identified which is also located on chromosome 20. Co-transcription of this gene and the neighboring upstream gene generates a rare transcript (Kua-UEV), which encodes a fusion protein consisting of sequence sharing identity with each individual gene product.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Ubiquitin-conjugating E2 enzyme 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 is located in the nucleus and can cause transcriptional activation of the human FOS proto-oncogene. It is thought to be involved in the control of differentiation by altering cell cycle behavior. Multiple alternatively spliced transcripts encoding different isoforms have been described for this gene. A pseudogene has been identified which is also located on chromosome 20. Co-transcription of this gene and the neighboring upstream gene generates a rare transcript (Kua-UEV), which encodes a fusion protein comprised of sequence sharing identity with each individual gene product.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2V1 ubiquitin-conjugating enzyme E2 variant 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7335| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
UBE2V1 has been shown to [[Protein-protein interaction|interact]] with [[UBE2N]].<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 | language =  | journal = Cell | volume = 103 | issue = 2 | pages = 351–61 | date = October 2000 | pmid = 11057907 | doi = 10.1016/S0092-8674(00)00126-4 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Long M | title = A new function evolved from gene fusion. | journal = Genome Res. | volume = 10 | issue = 11 | pages = 1655–7 | year = 2001 | pmid = 11076848 | doi = 10.1101/gr.165700 }}
| citations =
* {{cite journal | vauthors = Thomson TM, Khalid H, Lozano JJ, Sancho E, Ariño J | title = Role of UEV-1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage. | journal = FEBS Lett. | volume = 423 | issue = 1 | pages = 49–52 | year = 1998 | pmid = 9580084 | doi = 10.1016/S0014-5793(98)00060-X }}
*{{cite journal | author=Long M |title=A new function evolved from gene fusion. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1655-7 |year= 2001 |pmid= 11076848 |doi= }}
* {{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 }}
*{{cite journal  | author=Rothofsky ML, Lin SL |title=CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter. |journal=Gene |volume=195 |issue= 2 |pages= 141-9 |year= 1997 |pmid= 9305758 |doi=  }}
* {{cite journal | vauthors = Ma L, Broomfield S, Lavery C, Lin SL, Xiao W, Bacchetti S | title = Up-regulation of CIR1/CROC1 expression upon cell immortalization and in tumor-derived human cell lines. | journal = Oncogene | volume = 17 | issue = 10 | pages = 1321–6 | year = 1998 | pmid = 9771976 | doi = 10.1038/sj.onc.1202058 }}
*{{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 = 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=Thomson TM, Khalid H, Lozano JJ, ''et al.'' |title=Role of UEV-1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage. |journal=FEBS Lett. |volume=423 |issue= 1 |pages= 49-52 |year= 1998 |pmid= 9580084 |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=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 = Thomson TM, Lozano JJ, Loukili N, Carrió R, Serras F, Cormand B, Valeri M, Díaz VM, Abril J, Burset M, Merino J, Macaya A, Corominas M, Guigó R | title = Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene. | journal = Genome Res. | volume = 10 | issue = 11 | pages = 1743–56 | year = 2001 | pmid = 11076860 | pmc = 310942 | doi = 10.1101/gr.GR-1405R }}
*{{cite journal | author=Ma L, Broomfield S, Lavery C, ''et al.'' |title=Up-regulation of CIR1/CROC1 expression upon cell immortalization and in tumor-derived human cell lines. |journal=Oncogene |volume=17 |issue= 10 |pages= 1321-6 |year= 1998 |pmid= 9771976 |doi= 10.1038/sj.onc.1202058 }}
* {{cite journal | vauthors = Ito M, Shichijo S, Tsuda N, Ochi M, Harashima N, Saito N, Itoh K | title = Molecular basis of T cell-mediated recognition of pancreatic cancer cells. | journal = Cancer Res. | volume = 61 | issue = 5 | pages = 2038–46 | year = 2001 | pmid = 11280764 | doi =  }}
*{{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 = 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=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 = Hau DD, Lewis MJ, Saltibus LF, Pastushok L, Xiao W, Spyracopoulos L | title = Structure and interactions of the ubiquitin-conjugating enzyme variant human Uev1a: implications for enzymatic synthesis of polyubiquitin chains. | journal = Biochemistry | volume = 45 | issue = 32 | pages = 9866–77 | year = 2006 | pmid = 16893187 | doi = 10.1021/bi060631r }}
*{{cite journal | author=Thomson TM, Lozano JJ, Loukili N, ''et al.'' |title=Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1743-56 |year= 2001 |pmid= 11076860 |doi= }}
* {{cite journal | vauthors = Syed NA, Andersen PL, Warrington RC, Xiao W | title = Uev1A, a ubiquitin conjugating enzyme variant, inhibits stress-induced apoptosis through NF-kappaB activation. | journal = Apoptosis | volume = 11 | issue = 12 | pages = 2147–57 | year = 2007 | pmid = 17041755 | doi = 10.1007/s10495-006-0197-3 }}
*{{cite journal | author=Ito M, Shichijo S, Tsuda N, ''et al.'' |title=Molecular basis of T cell-mediated recognition of pancreatic cancer cells. |journal=Cancer Res. |volume=61 |issue= 5 |pages= 2038-46 |year= 2001 |pmid= 11280764 |doi=  }}
* {{cite journal | vauthors = Petroski MD, Zhou X, Dong G, Daniel-Issakani S, Payan DG, Huang J | title = Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme. | journal = J. Biol. Chem. | volume = 282 | issue = 41 | pages = 29936–45 | year = 2007 | pmid = 17709375 | doi = 10.1074/jbc.M703911200 }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{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  | 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  | 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=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=Hau DD, Lewis MJ, Saltibus LF, ''et al.'' |title=Structure and interactions of the ubiquitin-conjugating enzyme variant human Uev1a: implications for enzymatic synthesis of polyubiquitin chains. |journal=Biochemistry |volume=45 |issue= 32 |pages= 9866-77 |year= 2006 |pmid= 16893187 |doi= 10.1021/bi060631r }}
*{{cite journal | author=Syed NA, Andersen PL, Warrington RC, Xiao W |title=Uev1A, a ubiquitin conjugating enzyme variant, inhibits stress-induced apoptosis through NF-kappaB activation. |journal=Apoptosis |volume=11 |issue= 12 |pages= 2147-57 |year= 2007 |pmid= 17041755 |doi= 10.1007/s10495-006-0197-3 }}
*{{cite journal | author=Petroski MD, Zhou X, Dong G, ''et al.'' |title=Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme. |journal=J. Biol. Chem. |volume=282 |issue= 41 |pages= 29936-45 |year= 2007 |pmid= 17709375 |doi= 10.1074/jbc.M703911200 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=7335}}
{{Ubiquitin-conjugating enzymes}}


{{protein-stub}}
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 09:32, 17 September 2017

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

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Ensembl

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UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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

Ubiquitin-conjugating enzyme E2 variant 1 is a protein that in humans is encoded by the UBE2V1 gene.[1][2][3]

Function

Ubiquitin-conjugating E2 enzyme 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 is located in the nucleus and can cause transcriptional activation of the human FOS proto-oncogene. It is thought to be involved in the control of differentiation by altering cell cycle behavior. Multiple alternatively spliced transcripts encoding different isoforms have been described for this gene. A pseudogene has been identified which is also located on chromosome 20. Co-transcription of this gene and the neighboring upstream gene generates a rare transcript (Kua-UEV), which encodes a fusion protein consisting of sequence sharing identity with each individual gene product.[3]

Interactions

UBE2V1 has been shown to interact with UBE2N.[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 (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". Mol Cell Biol. 18 (1): 576–89. doi:10.1128/mcb.18.1.576. PMC 121525. PMID 9418904.
  2. ↑ Rothofsky ML, Lin SL (October 1997). "CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter". Gene. 195 (2): 141–9. doi:10.1016/S0378-1119(97)00097-8. PMID 9305758.
  3. ↑ 3.0 3.1 "Entrez Gene: UBE2V1 ubiquitin-conjugating enzyme E2 variant 1".
  4. ↑ 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


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