UBE2B: Difference between revisions
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{{ | '''Ubiquitin-conjugating enzyme E2 B''' is a [[protein]] that in humans is encoded by the ''UBE2B'' [[gene]].<ref name="pmid1559696">{{cite journal |vauthors=Koken MH, Smit EM, Jaspers-Dekker I, Oostra BA, Hagemeijer A, Bootsma D, Hoeijmakers JH | title = Localization of two human homologs, HHR6A and HHR6B, of the yeast DNA repair gene RAD6 to chromosomes Xq24-q25 and 5q23-q31 | journal = Genomics | volume = 12 | issue = 3 | pages = 447–53 |date=May 1992 | pmid = 1559696 | pmc = | doi =10.1016/0888-7543(92)90433-S }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBE2B ubiquitin-conjugating enzyme E2B (RAD6 homolog)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7320| accessdate = }}</ref> | ||
}} | |||
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| 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. This enzyme is required for post-replicative DNA damage repair. Its protein sequence is 100% identical to the mouse, rat, and rabbit homologs, which indicates that this enzyme is highly conserved in eukaryotic evolution.<ref name="entrez" | | 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. This enzyme is required for post-replicative DNA damage repair. Its protein sequence is 100% identical to the mouse, rat, and rabbit homologs, which indicates that this enzyme is highly conserved in eukaryotic evolution.<ref name="entrez"/> | ||
}} | }} | ||
==Interactions== | |||
UBE2B has been shown to [[Protein-protein interaction|interact]] with [[RAD18]].<ref name=pmid10908344>{{cite journal |doi=10.1093/nar/28.14.2847 |last=Xin |first=H |authorlink= |author2=Lin W |author3=Sumanasekera W |author4=Zhang Y |author5=Wu X |author6=Wang Z |date=July 2000 |title=The human RAD18 gene product interacts with HHR6A and HHR6B |journal=Nucleic Acids Res. |volume=28 |issue=14 |pages=2847–54 |publisher= |location = ENGLAND| issn = | pmid = 10908344 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=102657 }}</ref><ref name=pmid10884424>{{cite journal |doi=10.1073/pnas.97.14.7927 |last=Tateishi |first=S |authorlink= |author2=Sakuraba Y |author3=Masuyama S |author4=Inoue H |author5=Yamaizumi M |date=July 2000 |title=Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens |journal=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=97 |issue=14 |pages=7927–32 |publisher= |location = UNITED STATES| issn = 0027-8424| pmid = 10884424 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=16647 }}</ref> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | *{{cite journal |vauthors=Koken MH, Reynolds P, Jaspers-Dekker I, etal |title=Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 20 |pages= 8865–9 |year= 1991 |pmid= 1717990 |doi=10.1073/pnas.88.20.8865 | pmc=52611 }} | ||
*{{cite journal |vauthors=Woffendin C, Chen ZY, Staskus K, etal |title=Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating enzyme encoded by yeast DNA repair gene RAD6. |journal=Biochim. Biophys. Acta |volume=1090 |issue= 1 |pages= 81–5 |year= 1991 |pmid= 1883845 |doi= 10.1016/0167-4781(91)90039-o}} | |||
*{{cite journal | *{{cite journal |vauthors=Schneider R, Eckerskorn C, Lottspeich F, Schweiger M |title=The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the yeast DNA repair gene RAD6. |journal=EMBO J. |volume=9 |issue= 5 |pages= 1431–5 |year= 1990 |pmid= 2158443 |doi= | pmc=551831 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Koken MH, Hoogerbrugge JW, Jasper-Dekker I, etal |title=Expression of the ubiquitin-conjugating DNA repair enzymes HHR6A and B suggests a role in spermatogenesis and chromatin modification. |journal=Dev. Biol. |volume=173 |issue= 1 |pages= 119–32 |year= 1996 |pmid= 8575614 |doi=10.1006/dbio.1996.0011 }} | ||
*{{cite journal | *{{cite journal |vauthors=Tateishi S, Sakuraba Y, Masuyama S, etal |title=Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 14 |pages= 7927–32 |year= 2000 |pmid= 10884424 |doi=10.1073/pnas.97.14.7927 | pmc=16647 }} | ||
*{{cite journal | *{{cite journal |vauthors=Xin H, Lin W, Sumanasekera W, etal |title=The human RAD18 gene product interacts with HHR6A and HHR6B. |journal=Nucleic Acids Res. |volume=28 |issue= 14 |pages= 2847–54 |year= 2000 |pmid= 10908344 |doi=10.1093/nar/28.14.2847 | pmc=102657 }} | ||
*{{cite journal | *{{cite journal |vauthors=Miura T, Klaus W, Ross A, etal |title=The NMR structure of the class I human ubiquitin-conjugating enzyme 2b. |journal=J. Biomol. NMR |volume=22 |issue= 1 |pages= 89–92 |year= 2003 |pmid= 11885984 |doi=10.1023/A:1013807519703 }} | ||
*{{cite journal | *{{cite journal |vauthors=Shekhar MP, Lyakhovich A, Visscher DW, etal |title=Rad6 overexpression induces multinucleation, centrosome amplification, abnormal mitosis, aneuploidy, and transformation. |journal=Cancer Res. |volume=62 |issue= 7 |pages= 2115–24 |year= 2002 |pmid= 11929833 |doi= }} | ||
*{{cite journal | *{{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 | *{{cite journal |vauthors=Kwon YT, Xia Z, An JY, etal |title=Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway. |journal=Mol. Cell. Biol. |volume=23 |issue= 22 |pages= 8255–71 |year= 2003 |pmid= 14585983 |doi=10.1128/MCB.23.22.8255-8271.2003 | pmc=262401 }} | ||
*{{cite journal | *{{cite journal |vauthors=Lyakhovich A, Shekhar MP |title=RAD6B overexpression confers chemoresistance: RAD6 expression during cell cycle and its redistribution to chromatin during DNA damage-induced response. |journal=Oncogene |volume=23 |issue= 17 |pages= 3097–106 |year= 2004 |pmid= 14981545 |doi= 10.1038/sj.onc.1207449 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Watanabe K, Tateishi S, Kawasuji M, etal |title=Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination. |journal=EMBO J. |volume=23 |issue= 19 |pages= 3886–96 |year= 2005 |pmid= 15359278 |doi= 10.1038/sj.emboj.7600383 | pmc=522788 }} | ||
*{{cite journal | *{{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 | pmc=528928 }} | ||
*{{cite journal | *{{cite journal |vauthors=Stelzl U, Worm U, Lalowski M, etal |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 | *{{cite journal |vauthors=Shekhar MP, Tait L, Gerard B |title=Essential role of T-cell factor/beta-catenin in regulation of Rad6B: a potential mechanism for Rad6B overexpression in breast cancer cells. |journal=Mol. Cancer Res. |volume=4 |issue= 10 |pages= 729–45 |year= 2007 |pmid= 17050667 |doi= 10.1158/1541-7786.MCR-06-0136 }} | ||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=7320}} | |||
{{Ubiquitin-conjugating enzymes}} | |||
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Revision as of 09:30, 17 September 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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Ubiquitin-conjugating enzyme E2 B is a protein that in humans is encoded by the UBE2B 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, 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. This enzyme is required for post-replicative DNA damage repair. Its protein sequence is 100% identical to the mouse, rat, and rabbit homologs, which indicates that this enzyme is highly conserved in eukaryotic evolution.[2]
Interactions
UBE2B has been shown to interact with RAD18.[3][4]
References
- ↑ Koken MH, Smit EM, Jaspers-Dekker I, Oostra BA, Hagemeijer A, Bootsma D, Hoeijmakers JH (May 1992). "Localization of two human homologs, HHR6A and HHR6B, of the yeast DNA repair gene RAD6 to chromosomes Xq24-q25 and 5q23-q31". Genomics. 12 (3): 447–53. doi:10.1016/0888-7543(92)90433-S. PMID 1559696.
- ↑ 2.0 2.1 "Entrez Gene: UBE2B ubiquitin-conjugating enzyme E2B (RAD6 homolog)".
- ↑ Xin, H; Lin W; Sumanasekera W; Zhang Y; Wu X; Wang Z (July 2000). "The human RAD18 gene product interacts with HHR6A and HHR6B". Nucleic Acids Res. ENGLAND. 28 (14): 2847–54. doi:10.1093/nar/28.14.2847. PMC 102657. PMID 10908344.
- ↑ Tateishi, S; Sakuraba Y; Masuyama S; Inoue H; Yamaizumi M (July 2000). "Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens". Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 97 (14): 7927–32. doi:10.1073/pnas.97.14.7927. ISSN 0027-8424. PMC 16647. PMID 10884424.
Further reading
- Koken MH, Reynolds P, Jaspers-Dekker I, et al. (1991). "Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6". Proc. Natl. Acad. Sci. U.S.A. 88 (20): 8865–9. doi:10.1073/pnas.88.20.8865. PMC 52611. PMID 1717990.
- Woffendin C, Chen ZY, Staskus K, et al. (1991). "Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating enzyme encoded by yeast DNA repair gene RAD6". Biochim. Biophys. Acta. 1090 (1): 81–5. doi:10.1016/0167-4781(91)90039-o. PMID 1883845.
- Schneider R, Eckerskorn C, Lottspeich F, Schweiger M (1990). "The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the yeast DNA repair gene RAD6". EMBO J. 9 (5): 1431–5. PMC 551831. PMID 2158443.
- Koken MH, Hoogerbrugge JW, Jasper-Dekker I, et al. (1996). "Expression of the ubiquitin-conjugating DNA repair enzymes HHR6A and B suggests a role in spermatogenesis and chromatin modification". Dev. Biol. 173 (1): 119–32. doi:10.1006/dbio.1996.0011. PMID 8575614.
- Tateishi S, Sakuraba Y, Masuyama S, et al. (2000). "Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens". Proc. Natl. Acad. Sci. U.S.A. 97 (14): 7927–32. doi:10.1073/pnas.97.14.7927. PMC 16647. PMID 10884424.
- Xin H, Lin W, Sumanasekera W, et al. (2000). "The human RAD18 gene product interacts with HHR6A and HHR6B". Nucleic Acids Res. 28 (14): 2847–54. doi:10.1093/nar/28.14.2847. PMC 102657. PMID 10908344.
- Miura T, Klaus W, Ross A, et al. (2003). "The NMR structure of the class I human ubiquitin-conjugating enzyme 2b". J. Biomol. NMR. 22 (1): 89–92. doi:10.1023/A:1013807519703. PMID 11885984.
- Shekhar MP, Lyakhovich A, Visscher DW, et al. (2002). "Rad6 overexpression induces multinucleation, centrosome amplification, abnormal mitosis, aneuploidy, and transformation". Cancer Res. 62 (7): 2115–24. PMID 11929833.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Kwon YT, Xia Z, An JY, et al. (2003). "Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway". Mol. Cell. Biol. 23 (22): 8255–71. doi:10.1128/MCB.23.22.8255-8271.2003. PMC 262401. PMID 14585983.
- Lyakhovich A, Shekhar MP (2004). "RAD6B overexpression confers chemoresistance: RAD6 expression during cell cycle and its redistribution to chromatin during DNA damage-induced response". Oncogene. 23 (17): 3097–106. doi:10.1038/sj.onc.1207449. PMID 14981545.
- Watanabe K, Tateishi S, Kawasuji M, et al. (2005). "Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination". EMBO J. 23 (19): 3886–96. doi:10.1038/sj.emboj.7600383. PMC 522788. PMID 15359278.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
- Shekhar MP, Tait L, Gerard B (2007). "Essential role of T-cell factor/beta-catenin in regulation of Rad6B: a potential mechanism for Rad6B overexpression in breast cancer cells". Mol. Cancer Res. 4 (10): 729–45. doi:10.1158/1541-7786.MCR-06-0136. PMID 17050667.
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