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Q920Q2

- REV1_MOUSE

UniProt

Q920Q2 - REV1_MOUSE

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Protein

DNA repair protein REV1

Gene

Rev1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei355 – 3551dCTPBy similarity
Metal bindingi421 – 4211Magnesium 1PROSITE-ProRule annotation
Metal bindingi421 – 4211Magnesium 2PROSITE-ProRule annotation
Binding sitei520 – 5201dCTPBy similarity
Metal bindingi568 – 5681Magnesium 1PROSITE-ProRule annotation
Binding sitei568 – 5681dCTPBy similarity
Metal bindingi569 – 5691Magnesium 1PROSITE-ProRule annotation
Sitei768 – 7681Interaction with target DNABy similarity
Sitei781 – 7811Interaction with target DNABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi421 – 4255dCTP bindingBy similarity
Nucleotide bindingi508 – 5147dCTP bindingBy similarity

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. deoxycytidyl transferase activity Source: MGI
  3. DNA-directed DNA polymerase activity Source: InterPro
  4. magnesium ion binding Source: InterPro

GO - Biological processi

  1. error-prone translesion synthesis Source: MGI
  2. response to UV Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA synthesis

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_216200. Translesion synthesis by HREV1.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein REV1 (EC:2.7.7.-)
Alternative name(s):
Rev1-like terminal deoxycytidyl transferase
Gene namesi
Name:Rev1
Synonyms:Rev1l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1929074. Rev1.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12491249DNA repair protein REV1PRO_0000173993Add
BLAST

Proteomic databases

PRIDEiQ920Q2.

PTM databases

PhosphoSiteiQ920Q2.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ920Q2.
CleanExiMM_REV1.
ExpressionAtlasiQ920Q2. baseline and differential.
GenevestigatoriQ920Q2.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi207845. 7 interactions.
DIPiDIP-41772N.
IntActiQ920Q2. 4 interactions.
MINTiMINT-1031694.
STRINGi10090.ENSMUSP00000027251.

Structurei

Secondary structure

1
1249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1163 – 117614Combined sources
Helixi1182 – 119716Combined sources
Helixi1201 – 121717Combined sources
Helixi1221 – 124222Combined sources
Beta strandi1243 – 12464Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LSGNMR-A1150-1249[»]
2LSJNMR-A1135-1249[»]
4FJOX-ray2.72A1153-1249[»]
ProteinModelPortaliQ920Q2.
SMRiQ920Q2. Positions 48-133, 342-826, 1153-1249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 13188BRCTPROSITE-ProRule annotationAdd
BLAST
Domaini417 – 651235UmuCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni350 – 36011Interaction with target DNABy similarityAdd
BLAST
Regioni651 – 6544Interaction with target DNABy similarity
Regioni707 – 7159Interaction with target DNABy similarity
Regioni1150 – 1249100Protein interaction domain; mediates interaction with DNA polymerase zetaAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1072 – 10787Nuclear localization signalSequence Analysis

Domaini

The C-terminal domain is necessary for protein interactions.

Sequence similaritiesi

Belongs to the DNA polymerase type-Y family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation
Contains 1 umuC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0389.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000154094.
HOVERGENiHBG054140.
InParanoidiQ920Q2.
KOiK03515.
OMAiYRFCRGL.
OrthoDBiEOG761BTT.
PhylomeDBiQ920Q2.
TreeFamiTF314488.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. 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]
PfamiPF00533. BRCT. 1 hit.
PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036573. REV1. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50173. UMUC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q920Q2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRRGGWRKRT ENDGWEKWGG YMAAKVQKLE EQFRTDAANQ KDGTASAIFS
60 70 80 90 100
GVAIYVNGYT DPSAEELRNL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI
110 120 130 140 150
KELKGEKVIR PEWIVESIKA GRLLSSAPYQ LYTKPSAAQK SLNFNPVCKP
160 170 180 190 200
EDPGPGPSNR AKQLNNRVNH IIKKIETESE VKANGLSSWN EDGVNDDFSF
210 220 230 240 250
EDLEHTFPGR KQNGVMHPRD TAVIFNGHTH SSNGALKTQD CLVPVGNSVA
260 270 280 290 300
SRLSLDSTQE EKRAEKSNAD FRDCTVQHLQ HSTRSADALR SPHRTNSLSP
310 320 330 340 350
SLHSNTKING AHHSTVQGPS STKSTSVLTL SKVAPSVPSK PSDCNFISDF
360 370 380 390 400
YSRSRLHHIS TWKCELTEFV NTLQRQSSGI FPGREKLKKV KTGRSSLVVT
410 420 430 440 450
DTGTMSVLSS PRHQSCVMHV DMDCFFVSVG IRNRPDLKGK PVAVTSNRGT
460 470 480 490 500
GTAPLRPGAN PQLEWQYYQN RALRGKAADI PDSSVWENQD STQTNGIDSV
510 520 530 540 550
LSKAEIASCS YEARQVGIKN GMFFGYAKQL CPNLQAVPYD FHACREVAQA
560 570 580 590 600
MYETLASYTH SIEAVSCDEA LIDVTDILAE TKLSPEEFAA ALRIEIKDKT
610 620 630 640 650
KCAASVGIGS NILLARMATK KAKPDGQYHL QPDEVDDFIR GQLVTNLPGV
660 670 680 690 700
GRSMESKLAS LGIKTCGDLQ CLTMAKLQKE FGPKTGQMLY RFCRGLDDRP
710 720 730 740 750
VRTEKERKSV SAEINYGIRF TQPKEAEAFL LSLSEEIQRR LEAAGMKGKR
760 770 780 790 800
LTLKIMVRKP GAPIETAKFG GHGICDNIAR TVTLDQATDS AKIIGKATLN
810 820 830 840 850
MFHTMKLNIS DMRGVGIQVN QLVPANSNLS TCSSRPSAQS SLFSGRPHSV
860 870 880 890 900
RDLFQLQKAK KPTEEEHKEV FLAAVDLEVS STSRACGLLS PLSAHLAASV
910 920 930 940 950
SPDTNSGECS RKWNGLHSPV SGQSRLNLSI EVPSPSQIDQ SVLEALPLDL
960 970 980 990 1000
REQIEQVCAA QQGEPRGKKK EPVNGCSSGV LPHPVGTVLL QIPEPQEPCN
1010 1020 1030 1040 1050
SDSKISVIAL PAFSQVDPDV FAALPAELQK ELKAAYDQRQ RQGEDTTHQQ
1060 1070 1080 1090 1100
PTSTSVPKNP LLQLKPPAMK DKRNKRKNLI GSPRKSPLKN KLLSSPAKTL
1110 1120 1130 1140 1150
PGAYGSPQKL MDGFLQHEGM ASERPLEEVS ASTPGAQDLS SLLPGQSSCF
1160 1170 1180 1190 1200
RPAAPNLAGA VEFSDVKTLL KEWITTISDP MEEDILQVVR YCTDLIEEKD
1210 1220 1230 1240
LEKLDLVIKY MKRLMQQSVE SVWNMAFDFI LDNVQVVLQQ TYGSTLKVT
Length:1,249
Mass (Da):137,341
Last modified:December 1, 2001 - v1
Checksum:iF82E0B6171AA3F75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti438 – 4381K → T in AAF23323. 1 PublicationCurated
Sequence conflicti555 – 5551L → W in AAF23323. 1 PublicationCurated
Sequence conflicti638 – 6381F → S in AAF23323. 1 PublicationCurated
Sequence conflicti661 – 6611L → S in AAF23323. 1 PublicationCurated
Sequence conflicti684 – 6841K → R in AAF23323. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB057418 mRNA. Translation: BAB64933.1.
AF179302 mRNA. Translation: AAF23323.1.
BC058093 mRNA. Translation: AAH58093.1.
CCDSiCCDS14899.1.
RefSeqiNP_062516.2. NM_019570.3.
XP_006496221.1. XM_006496158.1.
XP_006496222.1. XM_006496159.1.
XP_006496223.1. XM_006496160.1.
UniGeneiMm.389103.

Genome annotation databases

EnsembliENSMUST00000027251; ENSMUSP00000027251; ENSMUSG00000026082.
GeneIDi56210.
KEGGimmu:56210.
UCSCiuc007asp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB057418 mRNA. Translation: BAB64933.1 .
AF179302 mRNA. Translation: AAF23323.1 .
BC058093 mRNA. Translation: AAH58093.1 .
CCDSi CCDS14899.1.
RefSeqi NP_062516.2. NM_019570.3.
XP_006496221.1. XM_006496158.1.
XP_006496222.1. XM_006496159.1.
XP_006496223.1. XM_006496160.1.
UniGenei Mm.389103.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LSG NMR - A 1150-1249 [» ]
2LSJ NMR - A 1135-1249 [» ]
4FJO X-ray 2.72 A 1153-1249 [» ]
ProteinModelPortali Q920Q2.
SMRi Q920Q2. Positions 48-133, 342-826, 1153-1249.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207845. 7 interactions.
DIPi DIP-41772N.
IntActi Q920Q2. 4 interactions.
MINTi MINT-1031694.
STRINGi 10090.ENSMUSP00000027251.

PTM databases

PhosphoSitei Q920Q2.

Proteomic databases

PRIDEi Q920Q2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027251 ; ENSMUSP00000027251 ; ENSMUSG00000026082 .
GeneIDi 56210.
KEGGi mmu:56210.
UCSCi uc007asp.1. mouse.

Organism-specific databases

CTDi 51455.
MGIi MGI:1929074. Rev1.

Phylogenomic databases

eggNOGi COG0389.
GeneTreei ENSGT00530000062942.
HOGENOMi HOG000154094.
HOVERGENi HBG054140.
InParanoidi Q920Q2.
KOi K03515.
OMAi YRFCRGL.
OrthoDBi EOG761BTT.
PhylomeDBi Q920Q2.
TreeFami TF314488.

Enzyme and pathway databases

Reactomei REACT_216200. Translesion synthesis by HREV1.

Miscellaneous databases

ChiTaRSi Rev1. mouse.
NextBioi 312050.
PROi Q920Q2.
SOURCEi Search...

Gene expression databases

Bgeei Q920Q2.
CleanExi MM_REV1.
ExpressionAtlasi Q920Q2. baseline and differential.
Genevestigatori Q920Q2.

Family and domain databases

Gene3Di 3.30.1490.100. 1 hit.
3.40.50.10190. 1 hit.
InterProi IPR001357. 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 ]
Pfami PF00533. BRCT. 1 hit.
PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF036573. REV1. 1 hit.
SMARTi SM00292. BRCT. 1 hit.
[Graphical view ]
SUPFAMi SSF100879. SSF100879. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. BRCT. 1 hit.
PS50173. UMUC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiREV1_MOUSE
AccessioniPrimary (citable) accession number: Q920Q2
Secondary accession number(s): Q9QXV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3