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REV1_HUMAN
ID   REV1_HUMAN              Reviewed;        1251 AA.
AC   Q9UBZ9; O95941; Q53SI7; Q9C0J4; Q9NUP2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=DNA repair protein REV1;
DE            EC=2.7.7.-;
DE   AltName: Full=Alpha integrin-binding protein 80;
DE            Short=AIBP80;
DE   AltName: Full=Rev1-like terminal deoxycytidyl transferase;
GN   Name=REV1; Synonyms=REV1L;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Bone marrow, Leukocyte, and T-cell;
RX   PubMed=10536157; DOI=10.1093/nar/27.22.4468;
RA   Lin W., Xin H., Zhang X., Wu X., Yuan F., Wang Z.;
RT   "The human REV1 gene codes for a DNA template-dependent dCMP transferase.";
RL   Nucleic Acids Res. 27:4468-4475(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ROLE IN UV-INDUCED MUTAGENESIS.
RC   TISSUE=Brain;
RX   PubMed=10760286; DOI=10.1073/pnas.97.8.4186;
RA   Gibbs P.E.M., Wang X.-D., Li Z., McManus T.P., McGregor W.G.,
RA   Lawrence C.W., Maher V.M.;
RT   "The function of the human homolog of Saccharomyces cerevisiae REV1 is
RT   required for mutagenesis induced by UV light.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:4186-4191(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, MUTAGENESIS OF
RP   ASP-570 AND GLU-571, AND TISSUE SPECIFICITY.
RC   TISSUE=Mammary cancer, and Testis;
RX   PubMed=11278384; DOI=10.1074/jbc.m008082200;
RA   Masuda Y., Takahashi M., Tsunekuni N., Minami T., Sumii M., Miyagawa K.,
RA   Kamiya K.;
RT   "Deoxycytidyl transferase activity of the human REV1 protein is closely
RT   associated with the conserved polymerase domain.";
RL   J. Biol. Chem. 276:15051-15058(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH REV3L AND MAD2L2.
RC   TISSUE=Testis;
RX   PubMed=11485998; DOI=10.1074/jbc.m102051200;
RA   Murakumo Y., Ogura Y., Ishii H., Numata S., Ichihara M., Croce C.M.,
RA   Fishel R., Takahashi M.;
RT   "Interactions in the error-prone postreplication repair proteins hREV1,
RT   hREV3, and hREV7.";
RL   J. Biol. Chem. 276:35644-35651(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 479-1251 (ISOFORM 2), AND INTERACTION WITH
RP   ITGA3.
RC   TISSUE=Placenta;
RX   PubMed=10094488; DOI=10.1016/s0014-5793(99)00151-9;
RA   Wixler V., Laplantine E., Geerts D., Sonnenberg A., Petersohn D., Eckes B.,
RA   Paulsson M., Aumailley M.;
RT   "Identification of novel interaction partners for the conserved membrane
RT   proximal region of alpha-integrin cytoplasmic domains.";
RL   FEBS Lett. 445:351-355(1999).
RN   [8]
RP   INTERACTION WITH MAD2L2.
RX   PubMed=12529368; DOI=10.1074/jbc.m211765200;
RA   Masuda Y., Ohmae M., Masuda K., Kamiya K.;
RT   "Structure and enzymatic properties of a stable complex of the human REV1
RT   and REV7 proteins.";
RL   J. Biol. Chem. 278:12356-12360(2003).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   INTERACTION WITH DNA POLYMERASE ZETA.
RX   PubMed=20164194; DOI=10.1074/jbc.m109.092403;
RA   Hara K., Hashimoto H., Murakumo Y., Kobayashi S., Kogame T., Unzai S.,
RA   Akashi S., Takeda S., Shimizu T., Sato M.;
RT   "Crystal structure of human REV7 in complex with a human REV3 fragment and
RT   structural implication of the interaction between DNA polymerase zeta and
RT   REV1.";
RL   J. Biol. Chem. 285:12299-12307(2010).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH C1ORF86.
RX   PubMed=22266823; DOI=10.1038/nsmb.2222;
RA   Kim H., Yang K., Dejsuphong D., D'Andrea A.D.;
RT   "Regulation of Rev1 by the Fanconi anemia core complex.";
RL   Nat. Struct. Mol. Biol. 19:164-170(2012).
RN   [12]
RP   STRUCTURE BY NMR OF 43-133.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the BRCT domain from human DNA repair protein
RT   REV1.";
RL   Submitted (AUG-2007) to the PDB data bank.
CC   -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a
CC       dCMP residue from dCTP to the 3'-end of a DNA primer in a template-
CC       dependent reaction. May assist in the first step in the bypass of
CC       abasic lesions by the insertion of a nucleotide opposite the lesion.
CC       Required for normal induction of mutations by physical and chemical
CC       agents. {ECO:0000269|PubMed:10536157, ECO:0000269|PubMed:10760286,
CC       ECO:0000269|PubMed:11278384, ECO:0000269|PubMed:11485998,
CC       ECO:0000269|PubMed:22266823}.
CC   -!- SUBUNIT: Monomer. Interacts with the DNA polymerase zeta which is
CC       composed of REV3L and MAD2L2; the interaction with MAD2L2 is direct and
CC       requires that REV3L is in its closed conformation. Interacts with POLH,
CC       POLI and POLK. May bind ITGA3. Interacts with FAAP20/C1orf86.
CC       {ECO:0000269|PubMed:10094488, ECO:0000269|PubMed:11485998,
CC       ECO:0000269|PubMed:12529368, ECO:0000269|PubMed:20164194,
CC       ECO:0000269|PubMed:22266823}.
CC   -!- INTERACTION:
CC       Q9UBZ9; Q6NZ36: FAAP20; NbExp=2; IntAct=EBI-7353917, EBI-2817693;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=REV1;
CC         IsoId=Q9UBZ9-1; Sequence=Displayed;
CC       Name=2; Synonyms=REV1S;
CC         IsoId=Q9UBZ9-2; Sequence=VSP_012812;
CC       Name=3;
CC         IsoId=Q9UBZ9-3; Sequence=VSP_012809, VSP_012810, VSP_012811;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10536157,
CC       ECO:0000269|PubMed:11278384, ECO:0000269|PubMed:11485998}.
CC   -!- DOMAIN: The C-terminal domain is necessary for protein interactions.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK43708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF151538; AAF06731.1; -; mRNA.
DR   EMBL; AF206019; AAF18986.1; -; mRNA.
DR   EMBL; AB047646; BAB21441.1; -; mRNA.
DR   EMBL; AF357886; AAK43708.1; ALT_INIT; mRNA.
DR   EMBL; AK002087; BAA92079.1; -; mRNA.
DR   EMBL; AC018690; AAY24314.1; -; Genomic_DNA.
DR   EMBL; AJ131720; CAB38231.1; -; mRNA.
DR   CCDS; CCDS2045.1; -. [Q9UBZ9-1]
DR   CCDS; CCDS42722.1; -. [Q9UBZ9-2]
DR   RefSeq; NP_001032961.1; NM_001037872.2. [Q9UBZ9-2]
DR   RefSeq; NP_001308383.1; NM_001321454.1.
DR   RefSeq; NP_001308384.1; NM_001321455.1.
DR   RefSeq; NP_001308387.1; NM_001321458.1.
DR   RefSeq; NP_001308388.1; NM_001321459.1.
DR   RefSeq; NP_001308389.1; NM_001321460.1.
DR   RefSeq; NP_057400.1; NM_016316.3. [Q9UBZ9-1]
DR   PDB; 2EBW; NMR; -; A=44-133.
DR   PDB; 2LSI; NMR; -; A=1156-1251.
DR   PDB; 2LSK; NMR; -; A=1158-1251.
DR   PDB; 2LSY; NMR; -; A=1158-1251.
DR   PDB; 2N1G; NMR; -; A=1158-1251.
DR   PDB; 3GQC; X-ray; 2.50 A; A/B/C/D=330-833.
DR   PDB; 3VU7; X-ray; 2.80 A; H=1140-1251.
DR   PDB; 4BA9; X-ray; 2.73 A; A/B/C/D/E/F=1158-1242.
DR   PDB; 4EXT; X-ray; 1.90 A; A=1156-1251.
DR   PDB; 4GK0; X-ray; 2.70 A; E/F=1117-1251.
DR   PDB; 4GK5; X-ray; 3.21 A; E/F=1117-1251.
DR   PDB; 5VZM; NMR; -; B=933-1040.
DR   PDB; 6ASR; X-ray; 2.36 A; B=998-1040.
DR   PDB; 6AXD; NMR; -; A=998-1040.
DR   PDB; 6WS0; X-ray; 2.24 A; HHH=1158-1251.
DR   PDB; 6WS5; X-ray; 2.47 A; HHH=1158-1251.
DR   PDBsum; 2EBW; -.
DR   PDBsum; 2LSI; -.
DR   PDBsum; 2LSK; -.
DR   PDBsum; 2LSY; -.
DR   PDBsum; 2N1G; -.
DR   PDBsum; 3GQC; -.
DR   PDBsum; 3VU7; -.
DR   PDBsum; 4BA9; -.
DR   PDBsum; 4EXT; -.
DR   PDBsum; 4GK0; -.
DR   PDBsum; 4GK5; -.
DR   PDBsum; 5VZM; -.
DR   PDBsum; 6ASR; -.
DR   PDBsum; 6AXD; -.
DR   PDBsum; 6WS0; -.
DR   PDBsum; 6WS5; -.
DR   AlphaFoldDB; Q9UBZ9; -.
DR   BMRB; Q9UBZ9; -.
DR   SMR; Q9UBZ9; -.
DR   BioGRID; 119551; 32.
DR   CORUM; Q9UBZ9; -.
DR   IntAct; Q9UBZ9; 7.
DR   MINT; Q9UBZ9; -.
DR   STRING; 9606.ENSP00000258428; -.
DR   BindingDB; Q9UBZ9; -.
DR   ChEMBL; CHEMBL4295973; -.
DR   CarbonylDB; Q9UBZ9; -.
DR   iPTMnet; Q9UBZ9; -.
DR   PhosphoSitePlus; Q9UBZ9; -.
DR   BioMuta; REV1; -.
DR   DMDM; 59798439; -.
DR   EPD; Q9UBZ9; -.
DR   jPOST; Q9UBZ9; -.
DR   MassIVE; Q9UBZ9; -.
DR   MaxQB; Q9UBZ9; -.
DR   PaxDb; Q9UBZ9; -.
DR   PeptideAtlas; Q9UBZ9; -.
DR   PRIDE; Q9UBZ9; -.
DR   ProteomicsDB; 84105; -. [Q9UBZ9-1]
DR   ProteomicsDB; 84106; -. [Q9UBZ9-2]
DR   ProteomicsDB; 84107; -. [Q9UBZ9-3]
DR   Antibodypedia; 32824; 171 antibodies from 29 providers.
DR   DNASU; 51455; -.
DR   Ensembl; ENST00000258428.8; ENSP00000258428.3; ENSG00000135945.10. [Q9UBZ9-1]
DR   Ensembl; ENST00000393445.7; ENSP00000377091.3; ENSG00000135945.10. [Q9UBZ9-2]
DR   GeneID; 51455; -.
DR   KEGG; hsa:51455; -.
DR   MANE-Select; ENST00000258428.8; ENSP00000258428.3; NM_016316.4; NP_057400.1.
DR   UCSC; uc002tac.4; human. [Q9UBZ9-1]
DR   CTD; 51455; -.
DR   DisGeNET; 51455; -.
DR   GeneCards; REV1; -.
DR   HGNC; HGNC:14060; REV1.
DR   HPA; ENSG00000135945; Low tissue specificity.
DR   MIM; 606134; gene.
DR   neXtProt; NX_Q9UBZ9; -.
DR   OpenTargets; ENSG00000135945; -.
DR   PharmGKB; PA162401120; -.
DR   VEuPathDB; HostDB:ENSG00000135945; -.
DR   eggNOG; KOG2093; Eukaryota.
DR   GeneTree; ENSGT00940000156374; -.
DR   HOGENOM; CLU_003901_0_1_1; -.
DR   InParanoid; Q9UBZ9; -.
DR   OMA; PVKHLGH; -.
DR   OrthoDB; 299766at2759; -.
DR   PhylomeDB; Q9UBZ9; -.
DR   TreeFam; TF314488; -.
DR   PathwayCommons; Q9UBZ9; -.
DR   Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR   Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR   Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR   Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR   SignaLink; Q9UBZ9; -.
DR   BioGRID-ORCS; 51455; 71 hits in 1078 CRISPR screens.
DR   ChiTaRS; REV1; human.
DR   EvolutionaryTrace; Q9UBZ9; -.
DR   GeneWiki; REV1; -.
DR   GenomeRNAi; 51455; -.
DR   Pharos; Q9UBZ9; Tbio.
DR   PRO; PR:Q9UBZ9; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9UBZ9; protein.
DR   Bgee; ENSG00000135945; Expressed in secondary oocyte and 193 other tissues.
DR   ExpressionAtlas; Q9UBZ9; baseline and differential.
DR   Genevisible; Q9UBZ9; HS.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR   GO; GO:0017125; F:deoxycytidyl transferase activity; IBA:GO_Central.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR   GO; GO:0070987; P:error-free translesion synthesis; IBA:GO_Central.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR   Gene3D; 1.20.58.1280; -; 1.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   IDEAL; IID00284; -.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR025527; HUWE1/Rev1_UBM.
DR   InterPro; IPR012112; REV1.
DR   InterPro; IPR031991; Rev1_C.
DR   InterPro; IPR038401; Rev1_C_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF16727; REV1_C; 1.
DR   Pfam; PF14377; UBM; 2.
DR   PIRSF; PIRSF036573; REV1; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA damage; DNA repair; DNA synthesis;
KW   DNA-binding; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1251
FT                   /note="DNA repair protein REV1"
FT                   /id="PRO_0000173992"
FT   DOMAIN          44..131
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          419..653
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   REGION          206..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..362
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          653..656
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          709..717
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          1035..1096
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1119..1147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1150..1249
FT                   /note="Protein interaction domain; mediates interaction
FT                   with DNA polymerase zeta"
FT   MOTIF           1071..1078
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1039..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1082
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         357
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         423..427
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         423
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         423
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         510..516
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         522
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         570
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         570
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         571
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   SITE            770
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            783
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..21
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_012809"
FT   VAR_SEQ         406..413
FT                   /note="DMSVLNSP -> RYLLKLSS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_012810"
FT   VAR_SEQ         414..1251
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_012811"
FT   VAR_SEQ         479
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10094488,
FT                   ECO:0000303|PubMed:11278384"
FT                   /id="VSP_012812"
FT   VARIANT         138
FT                   /note="V -> M (in dbSNP:rs3087403)"
FT                   /id="VAR_021249"
FT   VARIANT         257
FT                   /note="F -> S (in dbSNP:rs3087386)"
FT                   /id="VAR_021250"
FT   VARIANT         306
FT                   /note="N -> D (in dbSNP:rs28382882)"
FT                   /id="VAR_029193"
FT   VARIANT         373
FT                   /note="N -> S (in dbSNP:rs3087399)"
FT                   /id="VAR_021251"
FT   VARIANT         656
FT                   /note="M -> V (in dbSNP:rs3087394)"
FT                   /id="VAR_029194"
FT   VARIANT         660
FT                   /note="L -> W (in dbSNP:rs3087398)"
FT                   /id="VAR_029195"
FT   VARIANT         700
FT                   /note="D -> N (in dbSNP:rs28382941)"
FT                   /id="VAR_029196"
FT   VARIANT         704
FT                   /note="R -> Q (in dbSNP:rs28382942)"
FT                   /id="VAR_029197"
FT   VARIANT         902
FT                   /note="P -> H (in dbSNP:rs28382961)"
FT                   /id="VAR_029199"
FT   VARIANT         902
FT                   /note="P -> S (in dbSNP:rs28382960)"
FT                   /id="VAR_029198"
FT   VARIANT         921
FT                   /note="S -> I (in dbSNP:rs3087396)"
FT                   /id="VAR_029200"
FT   VARIANT         1003
FT                   /note="A -> T (in dbSNP:rs3087401)"
FT                   /id="VAR_024436"
FT   VARIANT         1060
FT                   /note="P -> T (in dbSNP:rs3087388)"
FT                   /id="VAR_029201"
FT   VARIANT         1074
FT                   /note="N -> K (in dbSNP:rs3087393)"
FT                   /id="VAR_029202"
FT   VARIANT         1091
FT                   /note="N -> T (in dbSNP:rs3087392)"
FT                   /id="VAR_029203"
FT   VARIANT         1102
FT                   /note="L -> P (in dbSNP:rs3087400)"
FT                   /id="VAR_029204"
FT   MUTAGEN         570
FT                   /note="D->A: Abolishes transferase activity; when
FT                   associated with A-571."
FT                   /evidence="ECO:0000269|PubMed:11278384"
FT   MUTAGEN         571
FT                   /note="E->A: Abolishes transferase activity; when
FT                   associated with A-570."
FT                   /evidence="ECO:0000269|PubMed:11278384"
FT   TURN            48..51
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   HELIX           64..73
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   HELIX           99..102
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   HELIX           112..120
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:2EBW"
FT   HELIX           345..355
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           357..375
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           384..387
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          419..424
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           427..432
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   TURN            433..435
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   TURN            437..441
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          444..446
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           463..471
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   TURN            472..475
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           500..502
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          509..511
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           513..516
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   TURN            517..519
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           526..532
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          537..539
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           543..558
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          564..568
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          571..575
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           577..583
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           587..602
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          606..613
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           614..624
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          629..631
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           634..636
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           637..643
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           646..648
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           654..662
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           668..671
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           676..683
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           685..694
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   TURN            695..697
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          712..716
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           725..745
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          748..760
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          776..790
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           793..805
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   HELIX           811..813
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          814..826
FT                   /evidence="ECO:0007829|PDB:3GQC"
FT   STRAND          936..939
FT                   /evidence="ECO:0007829|PDB:5VZM"
FT   HELIX           940..943
FT                   /evidence="ECO:0007829|PDB:5VZM"
FT   HELIX           948..955
FT                   /evidence="ECO:0007829|PDB:5VZM"
FT   HELIX           960..963
FT                   /evidence="ECO:0007829|PDB:5VZM"
FT   TURN            973..979
FT                   /evidence="ECO:0007829|PDB:5VZM"
FT   HELIX           985..987
FT                   /evidence="ECO:0007829|PDB:5VZM"
FT   HELIX           1004..1009
FT                   /evidence="ECO:0007829|PDB:6ASR"
FT   HELIX           1013..1015
FT                   /evidence="ECO:0007829|PDB:6ASR"
FT   HELIX           1018..1022
FT                   /evidence="ECO:0007829|PDB:6ASR"
FT   HELIX           1026..1037
FT                   /evidence="ECO:0007829|PDB:6ASR"
FT   STRAND          1160..1162
FT                   /evidence="ECO:0007829|PDB:3VU7"
FT   HELIX           1165..1178
FT                   /evidence="ECO:0007829|PDB:4EXT"
FT   HELIX           1184..1199
FT                   /evidence="ECO:0007829|PDB:4EXT"
FT   HELIX           1203..1218
FT                   /evidence="ECO:0007829|PDB:4EXT"
FT   HELIX           1223..1243
FT                   /evidence="ECO:0007829|PDB:4EXT"
FT   STRAND          1245..1248
FT                   /evidence="ECO:0007829|PDB:4EXT"
SQ   SEQUENCE   1251 AA;  138248 MW;  010E261D537DBA80 CRC64;
     MRRGGWRKRA ENDGWETWGG YMAAKVQKLE EQFRSDAAMQ KDGTSSTIFS GVAIYVNGYT
     DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA
     GRLLSYIPYQ LYTKQSSVQK GLSFNPVCRP EDPLPGPSNI AKQLNNRVNH IVKKIETENE
     VKVNGMNSWN EEDENNDFSF VDLEQTSPGR KQNGIPHPRG STAIFNGHTP SSNGALKTQD
     CLVPMVNSVA SRLSPAFSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSFSL
     SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TFSKAAPSVP SKPSDCNFIS NFYSHSRLHH
     ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV VTDTGDMSVL NSPRHQSCIM
     HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR GTGRAPLRPG ANPQLEWQYY QNKILKGKAA
     DIPDSSLWEN PDSAQANGID SVLSRAEIAS CSYEARQLGI KNGMFFGHAK QLCPNLQAVP
     YDFHAYKEVA QTLYETLASY THNIEAVSCD EALVDITEIL AETKLTPDEF ANAVRMEIKD
     QTKCAASVGI GSNILLARMA TRKAKPDGQY HLKPEEVDDF IRGQLVTNLP GVGHSMESKL
     ASLGIKTCGD LQYMTMAKLQ KEFGPKTGQM LYRFCRGLDD RPVRTEKERK SVSAEINYGI
     RFTQPKEAEA FLLSLSEEIQ RRLEATGMKG KRLTLKIMVR KPGAPVETAK FGGHGICDNI
     ARTVTLDQAT DNAKIIGKAM LNMFHTMKLN ISDMRGVGIH VNQLVPTNLN PSTCPSRPSV
     QSSHFPSGSY SVRDVFQVQK AKKSTEEEHK EVFRAAVDLE ISSASRTCTF LPPFPAHLPT
     SPDTNKAESS GKWNGLHTPV SVQSRLNLSI EVPSPSQLDQ SVLEALPPDL REQVEQVCAV
     QQAESHGDKK KEPVNGCNTG ILPQPVGTVL LQIPEPQESN SDAGINLIAL PAFSQVDPEV
     FAALPAELQR ELKAAYDQRQ RQGENSTHQQ SASASVPKNP LLHLKAAVKE KKRNKKKKTI
     GSPKRIQSPL NNKLLNSPAK TLPGACGSPQ KLIDGFLKHE GPPAEKPLEE LSASTSGVPG
     LSSLQSDPAG CVRPPAPNLA GAVEFNDVKT LLREWITTIS DPMEEDILQV VKYCTDLIEE
     KDLEKLDLVI KYMKRLMQQS VESVWNMAFD FILDNVQVVL QQTYGSTLKV T
 
 
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