REV1

Available structures

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

External IDs

MGI: 1929074 HomoloGene: 32309 GeneCards: REV1

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

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


51455


56210

Ensembl


ENSG00000135945


ENSMUSG00000026082

UniProt


Q9UBZ9


Q920Q2

RefSeq (mRNA)

NM_001037872 NM_016316 NM_001321454 NM_001321455 NM_001321458
NM_001321459 NM_001321460


NM_019570

RefSeq (protein)

NP_001032961.1 NP_057400.1 NP_001308383.1 NP_001308384.1 NP_001308387.1
NP_001308388.1 NP_001308389.1


NP_062516.2

Location (UCSC)

Chr 2: 99.4 – 99.49 Mb

Chr 1: 38.05 – 38.13 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

DNA repair protein REV1 is a protein that in humans is encoded by the REV1 gene.^[3]^[4] 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.^[4] 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.^[5] Yet it is believed 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.^[6] 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

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "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. doi:10.1126/science.1116336. PMID 16195463.
↑ 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. United States. 276 (38): 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.
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. 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. 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.
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. 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.
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.

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REV1

Interactions

References

Further reading