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Protein

DNA repair protein REV1

Gene

REV1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei357 – 3571dCTPBy similarity
Metal bindingi423 – 4231Magnesium 1PROSITE-ProRule annotation
Metal bindingi423 – 4231Magnesium 2PROSITE-ProRule annotation
Binding sitei522 – 5221dCTPBy similarity
Metal bindingi570 – 5701Magnesium 1PROSITE-ProRule annotation
Binding sitei570 – 5701dCTPBy similarity
Metal bindingi571 – 5711Magnesium 1PROSITE-ProRule annotation
Sitei770 – 7701Interaction with target DNABy similarity
Sitei783 – 7831Interaction with target DNABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi423 – 4275dCTP bindingBy similarity
Nucleotide bindingi510 – 5167dCTP bindingBy similarity

GO - Molecular functioni

GO - Biological processi

  • DNA repair Source: Reactome
  • DNA replication Source: ProtInc
  • error-prone translesion synthesis Source: UniProtKB
  • response to UV Source: UniProtKB
  • translesion synthesis Source: Reactome
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_355158. Translesion synthesis by POLK.
REACT_355250. Termination of translesion DNA synthesis.
REACT_355324. Translesion synthesis by POLI.
REACT_8. Translesion synthesis by REV1.
SignaLinkiQ9UBZ9.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein REV1 (EC:2.7.7.-)
Alternative name(s):
Alpha integrin-binding protein 80
Short name:
AIBP80
Rev1-like terminal deoxycytidyl transferase
Gene namesi
Name:REV1
Synonyms:REV1L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:14060. REV1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi570 – 5701D → A: Abolishes transferase activity; when associated with A-571. 1 Publication
Mutagenesisi571 – 5711E → A: Abolishes transferase activity; when associated with A-570. 1 Publication

Organism-specific databases

PharmGKBiPA162401120.

Polymorphism and mutation databases

BioMutaiREV1.
DMDMi59798439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12511251DNA repair protein REV1PRO_0000173992Add
BLAST

Proteomic databases

MaxQBiQ9UBZ9.
PaxDbiQ9UBZ9.
PRIDEiQ9UBZ9.

PTM databases

PhosphoSiteiQ9UBZ9.

Expressioni

Tissue specificityi

Ubiquitous.3 Publications

Gene expression databases

BgeeiQ9UBZ9.
CleanExiHS_REV1.
ExpressionAtlasiQ9UBZ9. baseline and differential.
GenevisibleiQ9UBZ9. HS.

Organism-specific databases

HPAiHPA044534.
HPA051036.

Interactioni

Subunit structurei

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. May bind ITGA3. Interacts with FAAP20/C1orf86.5 Publications

Protein-protein interaction databases

BioGridi119551. 20 interactions.
IntActiQ9UBZ9. 3 interactions.
MINTiMINT-140323.
STRINGi9606.ENSP00000258428.

Structurei

Secondary structure

1
1251
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni48 – 514Combined sources
Beta strandi53 – 564Combined sources
Helixi64 – 7310Combined sources
Beta strandi84 – 863Combined sources
Beta strandi89 – 913Combined sources
Helixi99 – 1024Combined sources
Beta strandi104 – 1063Combined sources
Helixi112 – 1209Combined sources
Helixi127 – 1293Combined sources
Helixi345 – 35511Combined sources
Helixi357 – 37519Combined sources
Helixi384 – 3874Combined sources
Beta strandi419 – 4246Combined sources
Helixi427 – 4326Combined sources
Turni433 – 4353Combined sources
Turni437 – 4415Combined sources
Beta strandi444 – 4463Combined sources
Helixi463 – 4719Combined sources
Turni472 – 4754Combined sources
Helixi500 – 5023Combined sources
Beta strandi509 – 5113Combined sources
Helixi513 – 5164Combined sources
Turni517 – 5193Combined sources
Helixi526 – 5327Combined sources
Beta strandi537 – 5393Combined sources
Helixi543 – 55816Combined sources
Beta strandi564 – 5685Combined sources
Beta strandi571 – 5755Combined sources
Helixi577 – 5837Combined sources
Helixi587 – 60216Combined sources
Beta strandi606 – 6138Combined sources
Helixi614 – 62411Combined sources
Beta strandi629 – 6313Combined sources
Helixi634 – 6363Combined sources
Helixi637 – 6437Combined sources
Helixi646 – 6483Combined sources
Helixi654 – 6629Combined sources
Helixi668 – 6714Combined sources
Helixi676 – 6838Combined sources
Helixi685 – 69410Combined sources
Turni695 – 6973Combined sources
Beta strandi712 – 7165Combined sources
Helixi725 – 74521Combined sources
Beta strandi748 – 76013Combined sources
Beta strandi776 – 79015Combined sources
Helixi793 – 80513Combined sources
Helixi811 – 8133Combined sources
Beta strandi814 – 82613Combined sources
Beta strandi1160 – 11623Combined sources
Helixi1165 – 117814Combined sources
Helixi1184 – 119916Combined sources
Helixi1203 – 121816Combined sources
Helixi1223 – 124321Combined sources
Beta strandi1245 – 12484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBWNMR-A44-133[»]
2LSINMR-A1156-1251[»]
2LSKNMR-A1158-1251[»]
2LSYNMR-A1158-1251[»]
3GQCX-ray2.50A/B/C/D330-833[»]
3VU7X-ray2.80H1140-1251[»]
4BA9X-ray2.73A/B/C/D/E/F1158-1242[»]
4EXTX-ray1.90A1156-1251[»]
4GK0X-ray2.70E/F1117-1251[»]
4GK5X-ray3.21E/F1117-1251[»]
ProteinModelPortaliQ9UBZ9.
SMRiQ9UBZ9. Positions 48-133, 344-828, 1156-1251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBZ9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 13188BRCTPROSITE-ProRule annotationAdd
BLAST
Domaini419 – 653235UmuCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni352 – 36211Interaction with target DNABy similarityAdd
BLAST
Regioni653 – 6564Interaction with target DNABy similarity
Regioni709 – 7179Interaction with target DNABy similarity
Regioni1150 – 1249100Protein interaction domain; mediates interaction with DNA polymerase zetaAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1071 – 10788Nuclear 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.
InParanoidiQ9UBZ9.
KOiK03515.
OMAiYRFCRGL.
OrthoDBiEOG761BTT.
PhylomeDBiQ9UBZ9.
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]
PANTHERiPTHR11076:SF13. PTHR11076:SF13. 1 hit.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBZ9-1) [UniParc]FASTAAdd to basket

Also known as: REV1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRRGGWRKRA ENDGWETWGG YMAAKVQKLE EQFRSDAAMQ KDGTSSTIFS
60 70 80 90 100
GVAIYVNGYT DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI
110 120 130 140 150
KELKGEKVIR PEWIVESIKA GRLLSYIPYQ LYTKQSSVQK GLSFNPVCRP
160 170 180 190 200
EDPLPGPSNI AKQLNNRVNH IVKKIETENE VKVNGMNSWN EEDENNDFSF
210 220 230 240 250
VDLEQTSPGR KQNGIPHPRG STAIFNGHTP SSNGALKTQD CLVPMVNSVA
260 270 280 290 300
SRLSPAFSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSFSL
310 320 330 340 350
SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TFSKAAPSVP SKPSDCNFIS
360 370 380 390 400
NFYSHSRLHH ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV
410 420 430 440 450
VTDTGDMSVL NSPRHQSCIM HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR
460 470 480 490 500
GTGRAPLRPG ANPQLEWQYY QNKILKGKAA DIPDSSLWEN PDSAQANGID
510 520 530 540 550
SVLSRAEIAS CSYEARQLGI KNGMFFGHAK QLCPNLQAVP YDFHAYKEVA
560 570 580 590 600
QTLYETLASY THNIEAVSCD EALVDITEIL AETKLTPDEF ANAVRMEIKD
610 620 630 640 650
QTKCAASVGI GSNILLARMA TRKAKPDGQY HLKPEEVDDF IRGQLVTNLP
660 670 680 690 700
GVGHSMESKL ASLGIKTCGD LQYMTMAKLQ KEFGPKTGQM LYRFCRGLDD
710 720 730 740 750
RPVRTEKERK SVSAEINYGI RFTQPKEAEA FLLSLSEEIQ RRLEATGMKG
760 770 780 790 800
KRLTLKIMVR KPGAPVETAK FGGHGICDNI ARTVTLDQAT DNAKIIGKAM
810 820 830 840 850
LNMFHTMKLN ISDMRGVGIH VNQLVPTNLN PSTCPSRPSV QSSHFPSGSY
860 870 880 890 900
SVRDVFQVQK AKKSTEEEHK EVFRAAVDLE ISSASRTCTF LPPFPAHLPT
910 920 930 940 950
SPDTNKAESS GKWNGLHTPV SVQSRLNLSI EVPSPSQLDQ SVLEALPPDL
960 970 980 990 1000
REQVEQVCAV QQAESHGDKK KEPVNGCNTG ILPQPVGTVL LQIPEPQESN
1010 1020 1030 1040 1050
SDAGINLIAL PAFSQVDPEV FAALPAELQR ELKAAYDQRQ RQGENSTHQQ
1060 1070 1080 1090 1100
SASASVPKNP LLHLKAAVKE KKRNKKKKTI GSPKRIQSPL NNKLLNSPAK
1110 1120 1130 1140 1150
TLPGACGSPQ KLIDGFLKHE GPPAEKPLEE LSASTSGVPG LSSLQSDPAG
1160 1170 1180 1190 1200
CVRPPAPNLA GAVEFNDVKT LLREWITTIS DPMEEDILQV VKYCTDLIEE
1210 1220 1230 1240 1250
KDLEKLDLVI KYMKRLMQQS VESVWNMAFD FILDNVQVVL QQTYGSTLKV

T
Length:1,251
Mass (Da):138,248
Last modified:May 1, 2000 - v1
Checksum:i010E261D537DBA80
GO
Isoform 2 (identifier: Q9UBZ9-2) [UniParc]FASTAAdd to basket

Also known as: REV1S

The sequence of this isoform differs from the canonical sequence as follows:
     479-479: Missing.

Show »
Length:1,250
Mass (Da):138,177
Checksum:iB4B1606DB6E866F2
GO
Isoform 3 (identifier: Q9UBZ9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     406-413: DMSVLNSP → RYLLKLSS
     414-1251: Missing.

Note: No experimental confirmation available.
Show »
Length:392
Mass (Da):43,649
Checksum:iA0EA83A568AD74F9
GO

Sequence cautioni

The sequence AAK43708.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381V → M.
Corresponds to variant rs3087403 [ dbSNP | Ensembl ].
VAR_021249
Natural varianti257 – 2571F → S.
Corresponds to variant rs3087386 [ dbSNP | Ensembl ].
VAR_021250
Natural varianti306 – 3061N → D.
Corresponds to variant rs28382882 [ dbSNP | Ensembl ].
VAR_029193
Natural varianti373 – 3731N → S.
Corresponds to variant rs3087399 [ dbSNP | Ensembl ].
VAR_021251
Natural varianti656 – 6561M → V.
Corresponds to variant rs3087394 [ dbSNP | Ensembl ].
VAR_029194
Natural varianti660 – 6601L → W.
Corresponds to variant rs3087398 [ dbSNP | Ensembl ].
VAR_029195
Natural varianti700 – 7001D → N.
Corresponds to variant rs28382941 [ dbSNP | Ensembl ].
VAR_029196
Natural varianti704 – 7041R → Q.
Corresponds to variant rs28382942 [ dbSNP | Ensembl ].
VAR_029197
Natural varianti902 – 9021P → H.
Corresponds to variant rs28382961 [ dbSNP | Ensembl ].
VAR_029199
Natural varianti902 – 9021P → S.
Corresponds to variant rs28382960 [ dbSNP | Ensembl ].
VAR_029198
Natural varianti921 – 9211S → I.
Corresponds to variant rs3087396 [ dbSNP | Ensembl ].
VAR_029200
Natural varianti1003 – 10031A → T.
Corresponds to variant rs3087401 [ dbSNP | Ensembl ].
VAR_024436
Natural varianti1060 – 10601P → T.
Corresponds to variant rs3087388 [ dbSNP | Ensembl ].
VAR_029201
Natural varianti1074 – 10741N → K.
Corresponds to variant rs3087393 [ dbSNP | Ensembl ].
VAR_029202
Natural varianti1091 – 10911N → T.
Corresponds to variant rs3087392 [ dbSNP | Ensembl ].
VAR_029203
Natural varianti1102 – 11021L → P.
Corresponds to variant rs3087400 [ dbSNP | Ensembl ].
VAR_029204

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform 3. 1 PublicationVSP_012809Add
BLAST
Alternative sequencei406 – 4138DMSVLNSP → RYLLKLSS in isoform 3. 1 PublicationVSP_012810
Alternative sequencei414 – 1251838Missing in isoform 3. 1 PublicationVSP_012811Add
BLAST
Alternative sequencei479 – 4791Missing in isoform 2. 2 PublicationsVSP_012812

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151538 mRNA. Translation: AAF06731.1.
AF206019 mRNA. Translation: AAF18986.1.
AB047646 mRNA. Translation: BAB21441.1.
AF357886 mRNA. Translation: AAK43708.1. Different initiation.
AK002087 mRNA. Translation: BAA92079.1.
AC018690 Genomic DNA. Translation: AAY24314.1.
AJ131720 mRNA. Translation: CAB38231.1.
CCDSiCCDS2045.1. [Q9UBZ9-1]
CCDS42722.1. [Q9UBZ9-2]
RefSeqiNP_001032961.1. NM_001037872.1. [Q9UBZ9-2]
NP_057400.1. NM_016316.2. [Q9UBZ9-1]
UniGeneiHs.443077.

Genome annotation databases

EnsembliENST00000258428; ENSP00000258428; ENSG00000135945. [Q9UBZ9-1]
ENST00000393445; ENSP00000377091; ENSG00000135945. [Q9UBZ9-2]
GeneIDi51455.
KEGGihsa:51455.
UCSCiuc002tac.3. human. [Q9UBZ9-2]
uc002tad.3. human. [Q9UBZ9-1]
uc002tae.1. human. [Q9UBZ9-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151538 mRNA. Translation: AAF06731.1.
AF206019 mRNA. Translation: AAF18986.1.
AB047646 mRNA. Translation: BAB21441.1.
AF357886 mRNA. Translation: AAK43708.1. Different initiation.
AK002087 mRNA. Translation: BAA92079.1.
AC018690 Genomic DNA. Translation: AAY24314.1.
AJ131720 mRNA. Translation: CAB38231.1.
CCDSiCCDS2045.1. [Q9UBZ9-1]
CCDS42722.1. [Q9UBZ9-2]
RefSeqiNP_001032961.1. NM_001037872.1. [Q9UBZ9-2]
NP_057400.1. NM_016316.2. [Q9UBZ9-1]
UniGeneiHs.443077.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBWNMR-A44-133[»]
2LSINMR-A1156-1251[»]
2LSKNMR-A1158-1251[»]
2LSYNMR-A1158-1251[»]
3GQCX-ray2.50A/B/C/D330-833[»]
3VU7X-ray2.80H1140-1251[»]
4BA9X-ray2.73A/B/C/D/E/F1158-1242[»]
4EXTX-ray1.90A1156-1251[»]
4GK0X-ray2.70E/F1117-1251[»]
4GK5X-ray3.21E/F1117-1251[»]
ProteinModelPortaliQ9UBZ9.
SMRiQ9UBZ9. Positions 48-133, 344-828, 1156-1251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119551. 20 interactions.
IntActiQ9UBZ9. 3 interactions.
MINTiMINT-140323.
STRINGi9606.ENSP00000258428.

PTM databases

PhosphoSiteiQ9UBZ9.

Polymorphism and mutation databases

BioMutaiREV1.
DMDMi59798439.

Proteomic databases

MaxQBiQ9UBZ9.
PaxDbiQ9UBZ9.
PRIDEiQ9UBZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258428; ENSP00000258428; ENSG00000135945. [Q9UBZ9-1]
ENST00000393445; ENSP00000377091; ENSG00000135945. [Q9UBZ9-2]
GeneIDi51455.
KEGGihsa:51455.
UCSCiuc002tac.3. human. [Q9UBZ9-2]
uc002tad.3. human. [Q9UBZ9-1]
uc002tae.1. human. [Q9UBZ9-3]

Organism-specific databases

CTDi51455.
GeneCardsiGC02M100016.
HGNCiHGNC:14060. REV1.
HPAiHPA044534.
HPA051036.
MIMi606134. gene.
neXtProtiNX_Q9UBZ9.
PharmGKBiPA162401120.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0389.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000154094.
HOVERGENiHBG054140.
InParanoidiQ9UBZ9.
KOiK03515.
OMAiYRFCRGL.
OrthoDBiEOG761BTT.
PhylomeDBiQ9UBZ9.
TreeFamiTF314488.

Enzyme and pathway databases

ReactomeiREACT_355158. Translesion synthesis by POLK.
REACT_355250. Termination of translesion DNA synthesis.
REACT_355324. Translesion synthesis by POLI.
REACT_8. Translesion synthesis by REV1.
SignaLinkiQ9UBZ9.

Miscellaneous databases

ChiTaRSiREV1. human.
EvolutionaryTraceiQ9UBZ9.
GeneWikiiREV1.
GenomeRNAii51455.
NextBioi55069.
PROiQ9UBZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBZ9.
CleanExiHS_REV1.
ExpressionAtlasiQ9UBZ9. baseline and differential.
GenevisibleiQ9UBZ9. HS.

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]
PANTHERiPTHR11076:SF13. PTHR11076:SF13. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human REV1 gene codes for a DNA template-dependent dCMP transferase."
    Lin W., Xin H., Zhang X., Wu X., Yuan F., Wang Z.
    Nucleic Acids Res. 27:4468-4475(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Bone marrow, Leukocyte and T-cell.
  2. "The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light."
    Gibbs P.E.M., Wang X.-D., Li Z., McManus T.P., McGregor W.G., Lawrence C.W., Maher V.M.
    Proc. Natl. Acad. Sci. U.S.A. 97:4186-4191(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ROLE IN UV-INDUCED MUTAGENESIS.
    Tissue: Brain.
  3. "Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain."
    Masuda Y., Takahashi M., Tsunekuni N., Minami T., Sumii M., Miyagawa K., Kamiya K.
    J. Biol. Chem. 276:15051-15058(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, MUTAGENESIS OF ASP-570 AND GLU-571, TISSUE SPECIFICITY.
    Tissue: Mammary cancer and Testis.
  4. "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7."
    Murakumo Y., Ogura Y., Ishii H., Numata S., Ichihara M., Croce C.M., Fishel R., Takahashi M.
    J. Biol. Chem. 276:35644-35651(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH REV3L AND MAD2L2.
    Tissue: Testis.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Placenta.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains."
    Wixler V., Laplantine E., Geerts D., Sonnenberg A., Petersohn D., Eckes B., Paulsson M., Aumailley M.
    FEBS Lett. 445:351-355(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 479-1251 (ISOFORM 2), INTERACTION WITH ITGA3.
    Tissue: Placenta.
  8. "Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins."
    Masuda Y., Ohmae M., Masuda K., Kamiya K.
    J. Biol. Chem. 278:12356-12360(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAD2L2.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1."
    Hara K., Hashimoto H., Murakumo Y., Kobayashi S., Kogame T., Unzai S., Akashi S., Takeda S., Shimizu T., Sato M.
    J. Biol. Chem. 285:12299-12307(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNA POLYMERASE ZETA.
  11. "Regulation of Rev1 by the Fanconi anemia core complex."
    Kim H., Yang K., Dejsuphong D., D'Andrea A.D.
    Nat. Struct. Mol. Biol. 19:164-170(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH C1ORF86.
  12. "Solution structure of the BRCT domain from human DNA repair protein REV1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 43-133.

Entry informationi

Entry nameiREV1_HUMAN
AccessioniPrimary (citable) accession number: Q9UBZ9
Secondary accession number(s): O95941
, Q53SI7, Q9C0J4, Q9NUP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.