UBE2L6: Difference between revisions

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'''Ubiquitin/ISG15-conjugating enzyme E2 L6''' is a [[protein]] that in humans is encoded by the ''UBE2L6'' [[gene]].<ref name="pmid9153201">{{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 |date=Jul 1997 | pmid = 9153201 | pmc =  | doi =10.1074/jbc.272.21.13548 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBE2L6 ubiquitin-conjugating enzyme E2L 6| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9246| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_UBE2L6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wzv.
| PDB = {{PDB2|1wzv}}, {{PDB2|1wzw}}
| Name = Ubiquitin-conjugating enzyme E2L 6
| HGNCid = 12490
| Symbol = UBE2L6
| AltSymbols =; UBCH8; MGC40331; RIG-B
| OMIM = 603890
| ECnumber =
| Homologene = 3112
| MGIid = 1914500
  | GeneAtlas_image1 = PBB_GE_UBE2L6_201649_at_tn.png
| GeneAtlas_image2 = PBB_GE_UBE2L6_gnf1h10137_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:0042296 |text = ISG15 conjugating enzyme activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0019941 |text = modification-dependent protein catabolic process}} {{GNF_GO|id=GO:0032020 |text = ISG15-protein conjugation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9246
    | Hs_Ensembl = ENSG00000156587
    | Hs_RefseqProtein = NP_004214
    | Hs_RefseqmRNA = NM_004223
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 57075705
    | Hs_GenLoc_end = 57092333
    | Hs_Uniprot = O14933
    | Mm_EntrezGene = 56791
    | Mm_Ensembl = ENSMUSG00000027078
    | Mm_RefseqmRNA = NM_019949
    | Mm_RefseqProtein = NP_064333
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 84599678
    | Mm_GenLoc_end = 84611015
    | Mm_Uniprot = Q3U8R0
  }}
}}
'''Ubiquitin-conjugating enzyme E2L 6''', also known as '''UBE2L6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBE2L6 ubiquitin-conjugating enzyme E2L 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9246| accessdate = }}</ref>


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{{PBB_Summary
| section_title =  
| 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 highly similar in primary structure to the enzyme encoded by UBE2L3 gene. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2L6 ubiquitin-conjugating enzyme E2L 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9246| accessdate = }}</ref>
| 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 highly similar in primary structure to the enzyme encoded by UBE2L3 gene. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2L6 ubiquitin-conjugating enzyme E2L 6| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9246| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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  | vauthors=Kang HY, Yeh S, Fujimoto N, Chang C |title=Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8570–6 |year= 1999 |pmid= 10085091 |doi=10.1074/jbc.274.13.8570 }}
*{{cite journal  | author=Kang HY, Yeh S, Fujimoto N, Chang C |title=Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8570-6 |year= 1999 |pmid= 10085091 |doi=  }}
*{{cite journal   |vauthors=Moynihan TP, Ardley HC, Nuber U, etal |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=10.1074/jbc.274.43.30963 }}
*{{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   |vauthors=Huang L, Kinnucan E, Wang G, etal |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=10.1126/science.286.5443.1321 }}
*{{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   |vauthors=Nyman TA, Matikainen S, Sareneva T, etal |title=Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-alpha-regulated genes. |journal=Eur. J. Biochem. |volume=267 |issue= 13 |pages= 4011–9 |year= 2000 |pmid= 10866800 |doi=10.1046/j.1432-1327.2000.01433.x }}
*{{cite journal | author=Nyman TA, Matikainen S, Sareneva T, ''et al.'' |title=Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-alpha-regulated genes. |journal=Eur. J. Biochem. |volume=267 |issue= 13 |pages= 4011-9 |year= 2000 |pmid= 10866800 |doi=  }}
*{{cite journal   |vauthors=Ardley HC, Rose SA, Tan N, etal |title=Genomic organization of the human ubiquitin-conjugating enzyme gene, UBE2L6 on chromosome 11q12. |journal=Cytogenet. Cell Genet. |volume=89 |issue= 1–2 |pages= 137–40 |year= 2000 |pmid= 10894956 |doi=10.1159/000015593 }}
*{{cite journal | author=Ardley HC, Rose SA, Tan N, ''et al.'' |title=Genomic organization of the human ubiquitin-conjugating enzyme gene, UBE2L6 on chromosome 11q12. |journal=Cytogenet. Cell Genet. |volume=89 |issue= 1-2 |pages= 137-40 |year= 2000 |pmid= 10894956 |doi=  }}
*{{cite journal   |vauthors=Zhang Y, Gao J, Chung KK, etal |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 | pmc=27228 }}
*{{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   |vauthors=Niwa  J, Ishigaki S, Doyu M, etal |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=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   |vauthors=Wheeler TC, Chin LS, Li Y, etal |title=Regulation of synaptophysin degradation by mammalian homologues of seven in absentia |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10273–82 |year= 2002 |pmid= 11786535 |doi= 10.1074/jbc.M107857200 }}
*{{cite journal | author=Wheeler TC, Chin LS, Li Y, ''et al.'' |title=Regulation of synaptophysin degradation by mammalian homologues of seven in absentia. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10273-82 |year= 2002 |pmid= 11786535 |doi= 10.1074/jbc.M107857200 }}
*{{cite journal   |vauthors=Urano T, Saito T, Tsukui T, etal |title=Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth |journal=Nature |volume=417 |issue= 6891 |pages= 871–5 |year= 2002 |pmid= 12075357 |doi= 10.1038/nature00826 }}
*{{cite journal | author=Urano T, Saito T, Tsukui T, ''et al.'' |title=Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth. |journal=Nature |volume=417 |issue= 6891 |pages= 871-5 |year= 2002 |pmid= 12075357 |doi= 10.1038/nature00826 }}
*{{cite journal  | vauthors=Chin LS, Vavalle JP, Li L |title=Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35071–9 |year= 2002 |pmid= 12121982 |doi= 10.1074/jbc.M203300200 }}
*{{cite journal  | author=Chin LS, Vavalle JP, Li L |title=Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35071-9 |year= 2002 |pmid= 12121982 |doi= 10.1074/jbc.M203300200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
*{{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=Ota T, Suzuki Y, Nishikawa T, etal |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=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=Chuang TH, Ulevitch RJ |title=Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors |journal=Nat. Immunol. |volume=5 |issue= 5 |pages= 495–502 |year= 2004 |pmid= 15107846 |doi= 10.1038/ni1066 }}
*{{cite journal  | author=Chuang TH, Ulevitch RJ |title=Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors. |journal=Nat. Immunol. |volume=5 |issue= 5 |pages= 495-502 |year= 2004 |pmid= 15107846 |doi= 10.1038/ni1066 }}
*{{cite journal   |vauthors=Zhao C, Beaudenon SL, Kelley ML, etal |title=The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 20 |pages= 7578–82 |year= 2004 |pmid= 15131269 |doi= 10.1073/pnas.0402528101 | pmc=419648 }}
*{{cite journal | author=Zhao C, Beaudenon SL, Kelley ML, ''et al.'' |title=The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 20 |pages= 7578-82 |year= 2004 |pmid= 15131269 |doi= 10.1073/pnas.0402528101 }}
*{{cite journal  | vauthors=Tripathi MK, Chaudhuri G |title=Down-regulation of UCRP and UBE2L6 in BRCA2 knocked-down human breast cells |journal=Biochem. Biophys. Res. Commun. |volume=328 |issue= 1 |pages= 43–8 |year= 2005 |pmid= 15670748 |doi= 10.1016/j.bbrc.2004.12.142 |pmc=3085986}}
*{{cite journal  | author=Tripathi MK, Chaudhuri G |title=Down-regulation of UCRP and UBE2L6 in BRCA2 knocked-down human breast cells. |journal=Biochem. Biophys. Res. Commun. |volume=328 |issue= 1 |pages= 43-8 |year= 2005 |pmid= 15670748 |doi= 10.1016/j.bbrc.2004.12.142 }}
*{{cite journal   |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal   |vauthors=Li J, Wang J, Yang X, etal |title=The Spen homolog Msx2-interacting nuclear target protein interacts with the E2 ubiquitin-conjugating enzyme UbcH8 |journal=Mol. Cell. Biochem. |volume=288 |issue= 1–2 |pages= 151–7 |year= 2007 |pmid= 16583136 |doi= 10.1007/s11010-006-9131-9 }}
*{{cite journal | author=Li J, Wang J, Yang X, ''et al.'' |title=The Spen homolog Msx2-interacting nuclear target protein interacts with the E2 ubiquitin-conjugating enzyme UbcH8. |journal=Mol. Cell. Biochem. |volume=288 |issue= 1-2 |pages= 151-7 |year= 2007 |pmid= 16583136 |doi= 10.1007/s11010-006-9131-9 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=9246}}
{{Ubiquitin-conjugating enzymes}}
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Latest revision as of 09:32, 17 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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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/ISG15-conjugating enzyme E2 L6 is a protein that in humans is encoded by the UBE2L6 gene.[1][2]

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 highly similar in primary structure to the enzyme encoded by UBE2L3 gene. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.[2]

References

  1. ↑ Kumar S, Kao WH, Howley PM (Jul 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.
  2. ↑ 2.0 2.1 "Entrez Gene: UBE2L6 ubiquitin-conjugating enzyme E2L 6".

Further reading



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