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Q920Q2 (REV1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein REV1

EC=2.7.7.-
Alternative name(s):
Rev1-like terminal deoxycytidyl transferase
Gene names
Name:Rev1
Synonyms:Rev1l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Ref.1

Subunit structure

Interacts with FAAP20 By similarity. Monomer. Interacts with the DNA polymerase zeta which is composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct and requires that REV3L is in its closed conformation. Interacts with POLH, POLI and POLK. Ref.1 Ref.4

Subcellular location

Nucleus Probable.

Tissue specificity

Ubiquitous. Ref.1

Domain

The C-terminal domain is necessary for protein interactions.

Sequence similarities

Belongs to the DNA polymerase type-Y family.

Contains 1 BRCT domain.

Contains 1 umuC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12491249DNA repair protein REV1
PRO_0000173993

Regions

Domain44 – 13188BRCT
Domain417 – 651235UmuC
Nucleotide binding421 – 4255dCTP binding By similarity
Nucleotide binding508 – 5147dCTP binding By similarity
Region350 – 36011Interaction with target DNA By similarity
Region651 – 6544Interaction with target DNA By similarity
Region707 – 7159Interaction with target DNA By similarity
Region1150 – 1249100Protein interaction domain; mediates interaction with DNA polymerase zeta
Motif1072 – 10787Nuclear localization signal Potential

Sites

Metal binding4211Magnesium 1 By similarity
Metal binding4211Magnesium 2 By similarity
Metal binding5681Magnesium 1 By similarity
Metal binding5691Magnesium 1 By similarity
Binding site3551dCTP By similarity
Binding site5201dCTP By similarity
Binding site5681dCTP By similarity
Site7681Interaction with target DNA By similarity
Site7811Interaction with target DNA By similarity

Experimental info

Sequence conflict4381K → T in AAF23323. Ref.2
Sequence conflict5551L → W in AAF23323. Ref.2
Sequence conflict6381F → S in AAF23323. Ref.2
Sequence conflict6611L → S in AAF23323. Ref.2
Sequence conflict6841K → R in AAF23323. Ref.2

Secondary structure

.......... 1249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q920Q2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F82E0B6171AA3F75

FASTA1,249137,341
        10         20         30         40         50         60 
MRRGGWRKRT ENDGWEKWGG YMAAKVQKLE EQFRTDAANQ KDGTASAIFS GVAIYVNGYT 

        70         80         90        100        110        120 
DPSAEELRNL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA 

       130        140        150        160        170        180 
GRLLSSAPYQ LYTKPSAAQK SLNFNPVCKP EDPGPGPSNR AKQLNNRVNH IIKKIETESE 

       190        200        210        220        230        240 
VKANGLSSWN EDGVNDDFSF EDLEHTFPGR KQNGVMHPRD TAVIFNGHTH SSNGALKTQD 

       250        260        270        280        290        300 
CLVPVGNSVA SRLSLDSTQE EKRAEKSNAD FRDCTVQHLQ HSTRSADALR SPHRTNSLSP 

       310        320        330        340        350        360 
SLHSNTKING AHHSTVQGPS STKSTSVLTL SKVAPSVPSK PSDCNFISDF YSRSRLHHIS 

       370        380        390        400        410        420 
TWKCELTEFV NTLQRQSSGI FPGREKLKKV KTGRSSLVVT DTGTMSVLSS PRHQSCVMHV 

       430        440        450        460        470        480 
DMDCFFVSVG IRNRPDLKGK PVAVTSNRGT GTAPLRPGAN PQLEWQYYQN RALRGKAADI 

       490        500        510        520        530        540 
PDSSVWENQD STQTNGIDSV LSKAEIASCS YEARQVGIKN GMFFGYAKQL CPNLQAVPYD 

       550        560        570        580        590        600 
FHACREVAQA MYETLASYTH SIEAVSCDEA LIDVTDILAE TKLSPEEFAA ALRIEIKDKT 

       610        620        630        640        650        660 
KCAASVGIGS NILLARMATK KAKPDGQYHL QPDEVDDFIR GQLVTNLPGV GRSMESKLAS 

       670        680        690        700        710        720 
LGIKTCGDLQ CLTMAKLQKE FGPKTGQMLY RFCRGLDDRP VRTEKERKSV SAEINYGIRF 

       730        740        750        760        770        780 
TQPKEAEAFL LSLSEEIQRR LEAAGMKGKR LTLKIMVRKP GAPIETAKFG GHGICDNIAR 

       790        800        810        820        830        840 
TVTLDQATDS AKIIGKATLN MFHTMKLNIS DMRGVGIQVN QLVPANSNLS TCSSRPSAQS 

       850        860        870        880        890        900 
SLFSGRPHSV RDLFQLQKAK KPTEEEHKEV FLAAVDLEVS STSRACGLLS PLSAHLAASV 

       910        920        930        940        950        960 
SPDTNSGECS RKWNGLHSPV SGQSRLNLSI EVPSPSQIDQ SVLEALPLDL REQIEQVCAA 

       970        980        990       1000       1010       1020 
QQGEPRGKKK EPVNGCSSGV LPHPVGTVLL QIPEPQEPCN SDSKISVIAL PAFSQVDPDV 

      1030       1040       1050       1060       1070       1080 
FAALPAELQK ELKAAYDQRQ RQGEDTTHQQ PTSTSVPKNP LLQLKPPAMK DKRNKRKNLI 

      1090       1100       1110       1120       1130       1140 
GSPRKSPLKN KLLSSPAKTL PGAYGSPQKL MDGFLQHEGM ASERPLEEVS ASTPGAQDLS 

      1150       1160       1170       1180       1190       1200 
SLLPGQSSCF RPAAPNLAGA VEFSDVKTLL KEWITTISDP MEEDILQVVR YCTDLIEEKD 

      1210       1220       1230       1240 
LEKLDLVIKY MKRLMQQSVE SVWNMAFDFI LDNVQVVLQQ TYGSTLKVT 

« Hide

References

« Hide 'large scale' references
[1]"Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein."
Masuda Y., Takahashi M., Fukuda S., Sumii M., Kamiya K.
J. Biol. Chem. 277:3040-3046(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
Strain: C3H/He.
Tissue: Liver.
[2]"Mus musculus REV1 protein (Rev1) mRNA, complete cds."
Poltoratsky V.P., Scharff M.D.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis."
Guo C., Fischhaber P.L., Luk-Paszyc M.J., Masuda Y., Zhou J., Kamiya K., Kisker C., Friedberg E.C.
EMBO J. 22:6621-6630(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAD2L2; POLH; POLI AND POLK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB057418 mRNA. Translation: BAB64933.1.
AF179302 mRNA. Translation: AAF23323.1.
BC058093 mRNA. Translation: AAH58093.1.
RefSeqNP_062516.2. NM_019570.3.
XP_006496221.1. XM_006496158.1.
XP_006496222.1. XM_006496159.1.
XP_006496223.1. XM_006496160.1.
UniGeneMm.389103.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LSGNMR-A1150-1249[»]
2LSJNMR-A1135-1249[»]
4FJOX-ray2.72A1153-1249[»]
ProteinModelPortalQ920Q2.
SMRQ920Q2. Positions 48-133, 342-826, 1153-1249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207845. 7 interactions.
DIPDIP-41772N.
IntActQ920Q2. 4 interactions.
MINTMINT-1031694.
STRING10090.ENSMUSP00000027251.

PTM databases

PhosphoSiteQ920Q2.

Proteomic databases

PRIDEQ920Q2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027251; ENSMUSP00000027251; ENSMUSG00000026082.
GeneID56210.
KEGGmmu:56210.
UCSCuc007asp.1. mouse.

Organism-specific databases

CTD51455.
MGIMGI:1929074. Rev1.

Phylogenomic databases

eggNOGCOG0389.
GeneTreeENSGT00530000062942.
HOGENOMHOG000154094.
HOVERGENHBG054140.
InParanoidQ920Q2.
KOK03515.
OMAYRFCRGL.
OrthoDBEOG761BTT.
PhylomeDBQ920Q2.
TreeFamTF314488.

Gene expression databases

ArrayExpressQ920Q2.
BgeeQ920Q2.
CleanExMM_REV1.
GenevestigatorQ920Q2.

Family and domain databases

Gene3D3.30.1490.100. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
IPR012112. REV1.
[Graphical view]
PfamPF00533. BRCT. 1 hit.
PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
PIRSFPIRSF036573. REV1. 1 hit.
SMARTSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMSSF100879. SSF100879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSREV1. mouse.
NextBio312050.
PROQ920Q2.
SOURCESearch...

Entry information

Entry nameREV1_MOUSE
AccessionPrimary (citable) accession number: Q920Q2
Secondary accession number(s): Q9QXV2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot