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Q9UBZ9

- REV1_HUMAN

UniProt

Q9UBZ9 - REV1_HUMAN

Protein

DNA repair protein REV1

Gene

REV1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

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

    GO - Biological processi

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

    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 Curated

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    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 REV1PRO_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

    1
    1251
    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.
    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.
    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. 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:
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 118 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