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Q9UBZ9

- REV1_HUMAN

UniProt

Q9UBZ9 - REV1_HUMAN

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Protein
DNA repair protein REV1
Gene
REV1, REV1L
Organism
Homo sapiens (Human)
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.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei357 – 3571dCTP By similarity
Metal bindingi423 – 4231Magnesium 1 By similarity
Metal bindingi423 – 4231Magnesium 2 By similarity
Binding sitei522 – 5221dCTP By similarity
Metal bindingi570 – 5701Magnesium 1 By similarity
Binding sitei570 – 5701dCTP By similarity
Metal bindingi571 – 5711Magnesium 1 By similarity
Sitei770 – 7701Interaction with target DNA By similarity
Sitei783 – 7831Interaction with target DNA By similarity

Regions

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

GO - Molecular functioni

  1. DNA-directed DNA polymerase activity Source: Reactome
  2. damaged DNA binding Source: ProtInc
  3. deoxycytidyl transferase activity Source: Ensembl
  4. magnesium ion binding Source: InterPro
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: Reactome
  2. DNA replication Source: ProtInc
  3. DNA-dependent DNA replication Source: GOC
  4. error-prone translesion synthesis Source: UniProtKB
  5. response to UV Source: UniProtKB
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_8. Translesion synthesis by HREV1.
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: Chromosome 2

Organism-specific databases

HGNCiHGNC:14060. REV1.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12511251DNA repair protein REV1
PRO_0000173992Add
BLAST

Proteomic databases

MaxQBiQ9UBZ9.
PaxDbiQ9UBZ9.
PRIDEiQ9UBZ9.

PTM databases

PhosphoSiteiQ9UBZ9.

Expressioni

Tissue specificityi

Ubiquitous.3 Publications

Gene expression databases

ArrayExpressiQ9UBZ9.
BgeeiQ9UBZ9.
CleanExiHS_REV1.
GenevestigatoriQ9UBZ9.

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. 16 interactions.
IntActiQ9UBZ9. 3 interactions.
MINTiMINT-140323.
STRINGi9606.ENSP00000258428.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ9UBZ9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 13188BRCT
Add
BLAST
Domaini419 – 653235UmuC
Add
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1071 – 10788Nuclear localization signal Reviewed prediction

Domaini

The C-terminal domain is necessary for protein interactions.

Sequence similaritiesi

Contains 1 BRCT domain.
Contains 1 umuC domain.

Phylogenomic databases

eggNOGiCOG0389.
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]
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. Align

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

MRRGGWRKRA ENDGWETWGG YMAAKVQKLE EQFRSDAAMQ KDGTSSTIFS     50
GVAIYVNGYT DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI 100
KELKGEKVIR PEWIVESIKA GRLLSYIPYQ LYTKQSSVQK GLSFNPVCRP 150
EDPLPGPSNI AKQLNNRVNH IVKKIETENE VKVNGMNSWN EEDENNDFSF 200
VDLEQTSPGR KQNGIPHPRG STAIFNGHTP SSNGALKTQD CLVPMVNSVA 250
SRLSPAFSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSFSL 300
SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TFSKAAPSVP SKPSDCNFIS 350
NFYSHSRLHH ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV 400
VTDTGDMSVL NSPRHQSCIM HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR 450
GTGRAPLRPG ANPQLEWQYY QNKILKGKAA DIPDSSLWEN PDSAQANGID 500
SVLSRAEIAS CSYEARQLGI KNGMFFGHAK QLCPNLQAVP YDFHAYKEVA 550
QTLYETLASY THNIEAVSCD EALVDITEIL AETKLTPDEF ANAVRMEIKD 600
QTKCAASVGI GSNILLARMA TRKAKPDGQY HLKPEEVDDF IRGQLVTNLP 650
GVGHSMESKL ASLGIKTCGD LQYMTMAKLQ KEFGPKTGQM LYRFCRGLDD 700
RPVRTEKERK SVSAEINYGI RFTQPKEAEA FLLSLSEEIQ RRLEATGMKG 750
KRLTLKIMVR KPGAPVETAK FGGHGICDNI ARTVTLDQAT DNAKIIGKAM 800
LNMFHTMKLN ISDMRGVGIH VNQLVPTNLN PSTCPSRPSV QSSHFPSGSY 850
SVRDVFQVQK AKKSTEEEHK EVFRAAVDLE ISSASRTCTF LPPFPAHLPT 900
SPDTNKAESS GKWNGLHTPV SVQSRLNLSI EVPSPSQLDQ SVLEALPPDL 950
REQVEQVCAV QQAESHGDKK KEPVNGCNTG ILPQPVGTVL LQIPEPQESN 1000
SDAGINLIAL PAFSQVDPEV FAALPAELQR ELKAAYDQRQ RQGENSTHQQ 1050
SASASVPKNP LLHLKAAVKE KKRNKKKKTI GSPKRIQSPL NNKLLNSPAK 1100
TLPGACGSPQ KLIDGFLKHE GPPAEKPLEE LSASTSGVPG LSSLQSDPAG 1150
CVRPPAPNLA GAVEFNDVKT LLREWITTIS DPMEEDILQV VKYCTDLIEE 1200
KDLEKLDLVI KYMKRLMQQS VESVWNMAFD FILDNVQVVL QQTYGSTLKV 1250
T 1251
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.

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.
VSP_012809Add
BLAST
Alternative sequencei406 – 4138DMSVLNSP → RYLLKLSS in isoform 3.
VSP_012810
Alternative sequencei414 – 1251838Missing in isoform 3.
VSP_012811Add
BLAST
Alternative sequencei479 – 4791Missing in isoform 2.
VSP_012812

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
XP_006712655.1. XM_006712592.1. [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]

Polymorphism databases

DMDMi59798439.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2045.1. [Q9UBZ9-1 ]
CCDS42722.1. [Q9UBZ9-2 ]
RefSeqi NP_001032961.1. NM_001037872.1. [Q9UBZ9-2 ]
NP_057400.1. NM_016316.2. [Q9UBZ9-1 ]
XP_006712655.1. XM_006712592.1. [Q9UBZ9-1 ]
UniGenei Hs.443077.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EBW NMR - A 44-133 [» ]
2LSI NMR - A 1156-1251 [» ]
2LSK NMR - A 1158-1251 [» ]
2LSY NMR - A 1158-1251 [» ]
3GQC X-ray 2.50 A/B/C/D 330-833 [» ]
3VU7 X-ray 2.80 H 1140-1251 [» ]
4BA9 X-ray 2.73 A/B/C/D/E/F 1158-1242 [» ]
4EXT X-ray 1.90 A 1156-1251 [» ]
4GK0 X-ray 2.70 E/F 1117-1251 [» ]
4GK5 X-ray 3.21 E/F 1117-1251 [» ]
ProteinModelPortali Q9UBZ9.
SMRi Q9UBZ9. Positions 48-133, 344-828, 1156-1251.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119551. 16 interactions.
IntActi Q9UBZ9. 3 interactions.
MINTi MINT-140323.
STRINGi 9606.ENSP00000258428.

PTM databases

PhosphoSitei Q9UBZ9.

Polymorphism databases

DMDMi 59798439.

Proteomic databases

MaxQBi Q9UBZ9.
PaxDbi Q9UBZ9.
PRIDEi Q9UBZ9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258428 ; ENSP00000258428 ; ENSG00000135945 . [Q9UBZ9-1 ]
ENST00000393445 ; ENSP00000377091 ; ENSG00000135945 . [Q9UBZ9-2 ]
GeneIDi 51455.
KEGGi hsa:51455.
UCSCi uc002tac.3. human. [Q9UBZ9-2 ]
uc002tad.3. human. [Q9UBZ9-1 ]
uc002tae.1. human. [Q9UBZ9-3 ]

Organism-specific databases

CTDi 51455.
GeneCardsi GC02M100016.
HGNCi HGNC:14060. REV1.
HPAi HPA044534.
HPA051036.
MIMi 606134. gene.
neXtProti NX_Q9UBZ9.
PharmGKBi PA162401120.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0389.
HOGENOMi HOG000154094.
HOVERGENi HBG054140.
InParanoidi Q9UBZ9.
KOi K03515.
OMAi YRFCRGL.
OrthoDBi EOG761BTT.
PhylomeDBi Q9UBZ9.
TreeFami TF314488.

Enzyme and pathway databases

Reactomei REACT_8. Translesion synthesis by HREV1.
SignaLinki Q9UBZ9.

Miscellaneous databases

ChiTaRSi REV1. human.
EvolutionaryTracei Q9UBZ9.
GeneWikii REV1.
GenomeRNAii 51455.
NextBioi 55069.
PROi Q9UBZ9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBZ9.
Bgeei Q9UBZ9.
CleanExi HS_REV1.
Genevestigatori Q9UBZ9.

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. "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: September 3, 2014
This is version 117 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

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