REV1: Difference between revisions

REV1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2EBW, 2LSI, 2LSK, 2LSY, 3GQC, 3VU7, 4BA9, 4EXT, 4GK0, 4GK5, 2N1G
Identifiers
Aliases	REV1, REV1L, AIBP80, DNA directed polymerase, REV1 DNA directed polymerase
External IDs	OMIM: 606134; MGI: 1929074; HomoloGene: 32309; GeneCards: REV1; OMA:REV1 - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	99,490,035 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	38,129,801 bp
RNA expression pattern
	Top expressed in
	secondary oocyte; ; Achilles tendon; ; cerebellar hemisphere; ; right hemisphere of cerebellum; ; right uterine tube; ; ectocervix; ; gastric mucosa; ; body of uterus; ; skin of abdomen; ; left ovary;
	Top expressed in
	zygote; ; secondary oocyte; ; tail of embryo; ; superior cervical ganglion; ; Rostral migratory stream; ; spermatocyte; ; lobe of cerebellum; ; cerebellar vermis; ; primary oocyte; ; otic vesicle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; damaged DNA binding; DNA binding; nucleotidyltransferase activity; protein binding; metal ion binding; deoxycytidyl transferase activity;
Cellular component	nucleus; nucleoplasm;
Biological process	DNA replication; translesion synthesis; DNA biosynthetic process; response to UV; error-prone translesion synthesis; cellular response to DNA damage stimulus; DNA repair;
	Sources:Amigo / QuickGO
Orthologs
	51455
	56210
	ENSG00000135945
	ENSMUSG00000026082
	Q9UBZ9
	Q920Q2
NM_001037872; NM_016316; NM_001321454; NM_001321455; NM_001321458;
	NM_001321459; NM_001321460
	NM_019570; NM_001359287; NM_001359288
NP_001032961; NP_001308383; NP_001308384; NP_001308387; NP_001308388;
	NP_001308389; NP_057400
	NP_062516; NP_001346216; NP_001346217
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 13:00, 20 July 2024

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

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.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000135945 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026082 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "Entrez Gene: REV1 REV1 homolog (S. cerevisiae)".
^ 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.
^ 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.

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Wixler V, Laplantine E, Geerts D, et al. (1999). "Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains". FEBS Lett. 445 (2–3): 351–5. doi:10.1016/S0014-5793(99)00151-9. PMID 10094488. S2CID 9218762.
Gibbs PE, Wang XD, Li Z, et al. (2000). "The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light". Proc. Natl. Acad. Sci. U.S.A. 97 (8): 4186–91. Bibcode:2000PNAS...97.4186G. doi:10.1073/pnas.97.8.4186. PMC 18191. PMID 10760286.
Wixler V, Geerts D, Laplantine E, et al. (2000). "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes". J. Biol. Chem. 275 (43): 33669–78. doi:10.1074/jbc.M002519200. PMID 10906324.
Masuda Y, Takahashi M, Tsunekuni N, et al. (2001). "Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain". J. Biol. Chem. 276 (18): 15051–8. doi:10.1074/jbc.M008082200. PMID 11278384.
Murakumo Y, Ogura Y, Ishii H, et al. (2001). "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7". J. Biol. Chem. 276 (38): 35644–51. doi:10.1074/jbc.M102051200. PMID 11485998.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Masuda Y, Ohmae M, Masuda K, Kamiya K (2003). "Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins". J. Biol. Chem. 278 (14): 12356–60. doi:10.1074/jbc.M211765200. PMID 12529368.
Clark DR, Zacharias W, Panaitescu L, McGregor WG (2004). "Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene". Nucleic Acids Res. 31 (17): 4981–8. doi:10.1093/nar/gkg725. PMC 212819. PMID 12930947.
Guo C, Fischhaber PL, Luk-Paszyc MJ, et al. (2004). "Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis". EMBO J. 22 (24): 6621–30. doi:10.1093/emboj/cdg626. PMC 291821. PMID 14657033.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Ohashi E, Murakumo Y, Kanjo N, et al. (2005). "Interaction of hREV1 with three human Y-family DNA polymerases". Genes Cells. 9 (6): 523–31. doi:10.1111/j.1356-9597.2004.00747.x. PMID 15189446. S2CID 24470762.
Tissier A, Kannouche P, Reck MP, et al. (2005). "Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein". DNA Repair (Amst.). 3 (11): 1503–14. doi:10.1016/j.dnarep.2004.06.015. PMID 15380106.
Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
Lin X, Okuda T, Trang J, Howell SB (2006). "Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells". Mol. Pharmacol. 69 (5): 1748–54. doi:10.1124/mol.105.020446. PMID 16495473. S2CID 22316155.
Masuda Y, Kamiya K (2006). "Role of single-stranded DNA in targeting REV1 to primer termini". J. Biol. Chem. 281 (34): 24314–21. doi:10.1074/jbc.M602967200. PMID 16803901.
Yuasa MS, Masutani C, Hirano A, et al. (2006). "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". Genes Cells. 11 (7): 731–44. doi:10.1111/j.1365-2443.2006.00974.x. PMID 16824193. S2CID 32695133.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000135945 – Ensembl, May 2017

[refGRCm38Ensembl-2] 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.

[pmid10536157-5] 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.

[entrez-6] "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.

[pmid11485998-8] 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.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

@@ Line 1: / Line 1: @@
+{{Short description|Protein-coding gene in the species Homo sapiens}}
-{{Orphan|date=February 2009}}
+{{Infobox_gene}}
-{{PBB|geneid=51455}}
-'''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 | year = 1999 | month = Dec | 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">{{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>
-}} 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.
+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.<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==
-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 |year=[[2001]]|month=Sep. |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>
+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.
-==References==
+== See also ==
-{{reflist}}
-==Further reading==
-{{refbegin | 2}}
-{{PBB_Further_reading
-| 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  | 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  | 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  | 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  | 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  | 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  | 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  | 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  | 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  | 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  | 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=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  | 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  | 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  | 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  | 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}}
+* [[REV3L]]
-{{gene-2-stub}}
+==References==
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Reflist}}
-{{PBB_Controls
-| update_page = yes
+==Further reading==
-| require_manual_inspection = no
+{{Refbegin | 2}}
-| update_protein_box = yes
+*{{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 }}
-| update_summary = yes
+*{{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= }}
-| update_citations = yes
+*{{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   |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   |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   |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   |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  |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 }}
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