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{{Short description|Protein-coding gene in the species Homo sapiens}}
{{PBB|geneid=51455}}
{{Infobox_gene}}
'''DNA repair protein REV1''' is a [[protein]] that in humans is encoded by the ''REV1'' [[gene]].<ref name="pmid10536157">{{cite journal | author = Lin W, Xin H, Zhang Y, Wu X, Yuan F, Wang Z | title = The human REV1 gene codes for a DNA template-dependent dCMP transferase | journal = Nucleic Acids Res | volume = 27 | issue = 22 | pages = 4468–75 |date=Dec 1999 | pmid = 10536157 | pmc = 148731 | doi =10.1093/nar/27.22.4468 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: REV1 REV1 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51455| accessdate = }}</ref> <!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
'''DNA repair protein REV1''' is a [[protein]] that in humans is encoded by the ''REV1'' [[gene]].<ref name="pmid10536157">{{cite journal |vauthors=Lin W, Xin H, Zhang Y, Wu X, Yuan F, Wang Z | title = The human REV1 gene codes for a DNA template-dependent dCMP transferase | journal = Nucleic Acids Res | volume = 27 | issue = 22 | pages = 4468–75 |date=Dec 1999 | pmid = 10536157 | pmc = 148731 | doi =10.1093/nar/27.22.4468 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: REV1 REV1 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51455| accessdate = }}</ref>
{{PBB_Summary

| section_title =
| summary_text = This gene encodes a protein with similarity to the S. cerevisiae mutagenesis protein Rev1. The Rev1 proteins contain a BRCT domain, which is important in protein-protein interactions. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.<ref name="entrez"/>
This gene encodes a protein with similarity to the [[S. cerevisiae]] [[mutagenesis]] protein Rev1. The Rev1 proteins contain a [[BRCT domain]], which is important in [[protein-protein interactions]]. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA [[polymerase]]s involved in [[translesion synthesis]] (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.<ref name="entrez"/>

}} Rev1 is a [[DNA polymerase#Family Y|Y family DNA polymerase]]; it is sometimes referred to as a ''deoxycytidyl transferase'' because it only inserts [[deoxycytidine]] (dC) across from lesions. Whether [[Guanine|G]], [[Adenine|A]], [[Thymine|T]], [[Cytidine|C]], or an [[AP site|abasic site]], Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an [[arginine]] as a template which complements well with C. Yet it is believed{{By whom|date=May 2011}} that Rev1 rarely uses its polymerase activity, rather it is thought that Rev1's primary role is as a protein landing pad, whereby it helps direct the recruitment of TLS proteins, especially Pol ζ ([[REV3L|Rev3]]/Rev7).
Rev1 is a [[DNA polymerase#Family Y|Y family DNA polymerase]]; it is sometimes referred to as a ''deoxycytidyl transferase'' because it only inserts [[deoxycytidine]] (dC) across from lesions. Whether [[Guanine|G]], [[Adenine|A]], [[Thymine|T]], [[Cytidine|C]], or an [[AP site|abasic site]], Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an [[arginine]] as a template which complements well with C.<ref>{{Cite journal|title = Rev1 employs a novel mechanism of DNA synthesis using a protein template|last = Nair|first = DT|date = Sep 30, 2005|journal = Science|doi = 10.1126/science.1116336|pmid = 16195463|volume=309|issue = 5744|pages=2219–22|bibcode = 2005Sci...309.2219N|s2cid = 35378034}}</ref> Yet it is believed{{By whom|date=May 2011}} that Rev1 rarely uses its polymerase activity; rather it is thought that Rev1's primary role is as a protein landing pad, whereby it helps direct the recruitment of TLS proteins, especially Pol ζ ([[REV3L|Rev3]]/Rev7).


==Interactions==
==Interactions==
REV1 has been shown to [[Protein-protein interaction|interact]] with [[MAD2L2]].<ref name=pmid11485998>{{cite journal |last=Murakumo |first=Y |authorlink= |coauthors=Ogura Y, Ishii H, Numata S, Ichihara M, Croce C M, Fishel R, Takahashi M |date=September 2001 |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7 |journal=J. Biol. Chem. |volume=276 |issue=38 |pages=35644–51 |publisher= |location = United States| issn = 0021-9258| pmid = 11485998 |doi = 10.1074/jbc.M102051200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> It is believed that Rev1 may interact with PCNA, once ubiquitylated due to a lesion, and help recruit Pol ζ ([[REV3L|Rev3]]/Rev7) a B family polymerase involved in TLS.
REV1 has been shown to [[Protein-protein interaction|interact]] with [[MAD2L2]].<ref name=pmid11485998>{{cite journal |last=Murakumo |first=Y |author2=Ogura Y |author3=Ishii H |author4=Numata S |author5=Ichihara M |author6=Croce C M |author7=Fishel R |author8=Takahashi M |date=September 2001 |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7 |journal=J. Biol. Chem. |volume=276 |issue=38 |pages=35644–51 |location = United States| issn = 0021-9258| pmid = 11485998 |doi = 10.1074/jbc.M102051200 |doi-access=free }}</ref> It is believed that Rev1 may interact with PCNA, once [[ubiquitylated]] due to a lesion, and help recruit Pol ζ ([[REV3L|Rev3]]/Rev7) a B family polymerase involved in TLS.

== See also ==

* [[REV3L]]


==References==
==References==
Line 14: Line 19:
==Further reading==
==Further reading==
{{Refbegin | 2}}
{{Refbegin | 2}}
*{{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 |doi-access=free }}
{{PBB_Further_reading
*{{cite journal |vauthors=Wixler V, Laplantine E, Geerts D, etal |title=Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains. |journal=FEBS Lett. |volume=445 |issue= 2–3 |pages= 351–5 |year= 1999 |pmid= 10094488 |doi=10.1016/S0014-5793(99)00151-9 |s2cid=9218762 |doi-access= }}
| citations =
*{{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=10.1101/gr.6.9.791 }}
*{{cite journal |vauthors=Gibbs PE, Wang XD, Li Z, etal |title=The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4186–91 |year= 2000 |pmid= 10760286 |doi=10.1073/pnas.97.8.4186 | pmc=18191 |bibcode=2000PNAS...97.4186G |doi-access=free }}
*{{cite journal | author=Wixler V, Laplantine E, Geerts D, ''et al.'' |title=Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains. |journal=FEBS Lett. |volume=445 |issue= 2-3 |pages= 351–5 |year= 1999 |pmid= 10094488 |doi=10.1016/S0014-5793(99)00151-9 }}
*{{cite journal |vauthors=Wixler V, Geerts D, Laplantine E, etal |title=The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33669–78 |year= 2000 |pmid= 10906324 |doi= 10.1074/jbc.M002519200 |doi-access= free }}
*{{cite journal | author=Gibbs PE, Wang XD, Li Z, ''et al.'' |title=The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4186–91 |year= 2000 |pmid= 10760286 |doi=10.1073/pnas.97.8.4186 | pmc=18191 }}
*{{cite journal |vauthors=Masuda Y, Takahashi M, Tsunekuni N, etal |title=Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15051–8 |year= 2001 |pmid= 11278384 |doi= 10.1074/jbc.M008082200 |doi-access= free }}
*{{cite journal | author=Wixler V, Geerts D, Laplantine E, ''et al.'' |title=The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33669–78 |year= 2000 |pmid= 10906324 |doi= 10.1074/jbc.M002519200 }}
*{{cite journal |vauthors=Murakumo Y, Ogura Y, Ishii H, etal |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35644–51 |year= 2001 |pmid= 11485998 |doi= 10.1074/jbc.M102051200 |doi-access= free }}
*{{cite journal | author=Masuda Y, Takahashi M, Tsunekuni N, ''et al.'' |title=Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15051–8 |year= 2001 |pmid= 11278384 |doi= 10.1074/jbc.M008082200 }}
*{{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 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal | author=Murakumo Y, Ogura Y, Ishii H, ''et al.'' |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35644–51 |year= 2001 |pmid= 11485998 |doi= 10.1074/jbc.M102051200 }}
*{{cite journal |vauthors=Masuda Y, Ohmae M, Masuda K, Kamiya K |title=Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. |journal=J. Biol. Chem. |volume=278 |issue= 14 |pages= 12356–60 |year= 2003 |pmid= 12529368 |doi= 10.1074/jbc.M211765200 |doi-access= free }}
*{{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 | pmc=139241 }}
*{{cite journal |vauthors=Clark DR, Zacharias W, Panaitescu L, McGregor WG |title=Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene. |journal=Nucleic Acids Res. |volume=31 |issue= 17 |pages= 4981–8 |year= 2004 |pmid= 12930947 |doi=10.1093/nar/gkg725 | pmc=212819 }}
*{{cite journal | author=Masuda Y, Ohmae M, Masuda K, Kamiya K |title=Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. |journal=J. Biol. Chem. |volume=278 |issue= 14 |pages= 12356–60 |year= 2003 |pmid= 12529368 |doi= 10.1074/jbc.M211765200 }}
*{{cite journal |vauthors=Guo C, Fischhaber PL, Luk-Paszyc MJ, etal |title=Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6621–30 |year= 2004 |pmid= 14657033 |doi= 10.1093/emboj/cdg626 | pmc=291821 }}
*{{cite journal | author=Clark DR, Zacharias W, Panaitescu L, McGregor WG |title=Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene. |journal=Nucleic Acids Res. |volume=31 |issue= 17 |pages= 4981–8 |year= 2004 |pmid= 12930947 |doi=10.1093/nar/gkg725 | pmc=212819 }}
*{{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 |doi-access= free }}
*{{cite journal | author=Guo C, Fischhaber PL, Luk-Paszyc MJ, ''et al.'' |title=Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6621–30 |year= 2004 |pmid= 14657033 |doi= 10.1093/emboj/cdg626 | pmc=291821 }}
*{{cite journal |vauthors=Ohashi E, Murakumo Y, Kanjo N, etal |title=Interaction of hREV1 with three human Y-family DNA polymerases. |journal=Genes Cells |volume=9 |issue= 6 |pages= 523–31 |year= 2005 |pmid= 15189446 |doi= 10.1111/j.1356-9597.2004.00747.x |s2cid=24470762 |doi-access= }}
*{{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=Tissier A, Kannouche P, Reck MP, etal |title=Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein. |journal=DNA Repair (Amst.) |volume=3 |issue= 11 |pages= 1503–14 |year= 2005 |pmid= 15380106 |doi= 10.1016/j.dnarep.2004.06.015 }}
*{{cite journal | author=Ohashi E, Murakumo Y, Kanjo N, ''et al.'' |title=Interaction of hREV1 with three human Y-family DNA polymerases. |journal=Genes Cells |volume=9 |issue= 6 |pages= 523–31 |year= 2005 |pmid= 15189446 |doi= 10.1111/j.1356-9597.2004.00747.x }}
*{{cite journal |vauthors=Hillier LW, Graves TA, Fulton RS, etal |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 |bibcode=2005Natur.434..724H |doi-access=free }}
*{{cite journal | author=Tissier A, Kannouche P, Reck MP, ''et al.'' |title=Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein. |journal=DNA Repair (Amst.) |volume=3 |issue= 11 |pages= 1503–14 |year= 2005 |pmid= 15380106 |doi= 10.1016/j.dnarep.2004.06.015 }}
*{{cite journal |vauthors=Lin X, Okuda T, Trang J, Howell SB |title=Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells. |journal=Mol. Pharmacol. |volume=69 |issue= 5 |pages= 1748–54 |year= 2006 |pmid= 16495473 |doi= 10.1124/mol.105.020446 |s2cid=22316155 }}
*{{cite journal | author=Hillier LW, Graves TA, Fulton RS, ''et al.'' |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 }}
*{{cite journal |vauthors=Masuda Y, Kamiya K |title=Role of single-stranded DNA in targeting REV1 to primer termini. |journal=J. Biol. Chem. |volume=281 |issue= 34 |pages= 24314–21 |year= 2006 |pmid= 16803901 |doi= 10.1074/jbc.M602967200 |doi-access= free }}
*{{cite journal | author=Lin X, Okuda T, Trang J, Howell SB |title=Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells. |journal=Mol. Pharmacol. |volume=69 |issue= 5 |pages= 1748–54 |year= 2006 |pmid= 16495473 |doi= 10.1124/mol.105.020446 }}
*{{cite journal |vauthors=Yuasa MS, Masutani C, Hirano A, etal |title=A human DNA polymerase eta complex containing Rad18, Rad6 and Rev1; proteomic analysis and targeting of the complex to the chromatin-bound fraction of cells undergoing replication fork arrest. |journal=Genes Cells |volume=11 |issue= 7 |pages= 731–44 |year= 2006 |pmid= 16824193 |doi= 10.1111/j.1365-2443.2006.00974.x |s2cid=32695133 |doi-access= }}
*{{cite journal | author=Masuda Y, Kamiya K |title=Role of single-stranded DNA in targeting REV1 to primer termini. |journal=J. Biol. Chem. |volume=281 |issue= 34 |pages= 24314–21 |year= 2006 |pmid= 16803901 |doi= 10.1074/jbc.M602967200 }}
*{{cite journal | author=Yuasa MS, Masutani C, Hirano A, ''et al.'' |title=A human DNA polymerase eta complex containing Rad18, Rad6 and Rev1; proteomic analysis and targeting of the complex to the chromatin-bound fraction of cells undergoing replication fork arrest. |journal=Genes Cells |volume=11 |issue= 7 |pages= 731–44 |year= 2006 |pmid= 16824193 |doi= 10.1111/j.1365-2443.2006.00974.x }}
}}
{{Refend}}
{{Refend}}

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{{Gene-2-stub}}

Latest revision as of 13:00, 20 July 2024

REV1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesREV1, REV1L, AIBP80, DNA directed polymerase, REV1 DNA directed polymerase
External IDsOMIM: 606134; MGI: 1929074; HomoloGene: 32309; GeneCards: REV1; OMA:REV1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

51455

56210

Ensembl

ENSG00000135945

ENSMUSG00000026082

UniProt

Q9UBZ9

Q920Q2

RefSeq (mRNA)

NM_019570
NM_001359287
NM_001359288

RefSeq (protein)

NP_062516
NP_001346216
NP_001346217

Location (UCSC)Chr 2: 99.4 – 99.49 MbChr 1: 38.05 – 38.13 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DNA repair protein REV1 is a protein that in humans is encoded by the REV1 gene.[5][6]

This gene encodes a protein with similarity to the S. cerevisiae mutagenesis protein Rev1. The Rev1 proteins contain a BRCT domain, which is important in protein-protein interactions. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.[6]

Rev1 is a Y family DNA polymerase; it is sometimes referred to as a deoxycytidyl transferase because it only inserts deoxycytidine (dC) across from lesions. Whether G, A, T, C, or an abasic site, Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an arginine as a template which complements well with C.[7] Yet it is believed[by whom?] that Rev1 rarely uses its polymerase activity; rather it is thought that Rev1's primary role is as a protein landing pad, whereby it helps direct the recruitment of TLS proteins, especially Pol ζ (Rev3/Rev7).

Interactions

[edit]

REV1 has been shown to interact with MAD2L2.[8] It is believed that Rev1 may interact with PCNA, once ubiquitylated due to a lesion, and help recruit Pol ζ (Rev3/Rev7) a B family polymerase involved in TLS.

See also

[edit]

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000135945 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026082 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lin W, Xin H, Zhang Y, Wu X, Yuan F, Wang Z (Dec 1999). "The human REV1 gene codes for a DNA template-dependent dCMP transferase". Nucleic Acids Res. 27 (22): 4468–75. doi:10.1093/nar/27.22.4468. PMC 148731. PMID 10536157.
  6. ^ a b "Entrez Gene: REV1 REV1 homolog (S. cerevisiae)".
  7. ^ Nair, DT (Sep 30, 2005). "Rev1 employs a novel mechanism of DNA synthesis using a protein template". Science. 309 (5744): 2219–22. Bibcode:2005Sci...309.2219N. doi:10.1126/science.1116336. PMID 16195463. S2CID 35378034.
  8. ^ Murakumo, Y; Ogura Y; Ishii H; Numata S; Ichihara M; Croce C M; Fishel R; Takahashi M (September 2001). "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7". J. Biol. Chem. 276 (38). United States: 35644–51. doi:10.1074/jbc.M102051200. ISSN 0021-9258. PMID 11485998.

Further reading

[edit]
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