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Database: UniProt/SWISS-PROT
Entry: DNLI1_MOUSE
LinkDB: DNLI1_MOUSE
Original site: DNLI1_MOUSE 
ID   DNLI1_MOUSE             Reviewed;         916 AA.
AC   P37913;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   05-DEC-2018, entry version 146.
DE   RecName: Full=DNA ligase 1;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase I;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
GN   Name=Lig1; Synonyms=Lig-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fibroblast;
RX   PubMed=8039710; DOI=10.1016/0378-1119(94)90386-7;
RA   Savini E., Biamonti G., Ciarrocchi G., Montecucco A.;
RT   "Cloning and sequence analysis of a cDNA coding for the murine DNA
RT   ligase I enzyme.";
RL   Gene 144:253-257(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Montecucco A.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Ola;
RX   PubMed=7642116; DOI=10.1016/0378-1119(95)00222-R;
RA   Jessop J.K., Melton D.W.;
RT   "Comparison between cDNA clones encoding murine DNA ligase I.";
RL   Gene 160:307-308(1995).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-65, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-65; THR-77;
RP   SER-906; SER-907 AND SER-911, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144 AND LYS-225, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10135};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with PCNA. {ECO:0000250|UniProtKB:P12004}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; U04674; AAA70403.1; -; mRNA.
DR   EMBL; U19604; AAB60500.1; -; mRNA.
DR   PIR; I48921; I48921.
DR   RefSeq; NP_034845.2; NM_010715.2.
DR   UniGene; Mm.288179; -.
DR   UniGene; Mm.421129; -.
DR   ProteinModelPortal; P37913; -.
DR   SMR; P37913; -.
DR   BioGrid; 201164; 7.
DR   CORUM; P37913; -.
DR   STRING; 10090.ENSMUSP00000096411; -.
DR   iPTMnet; P37913; -.
DR   PhosphoSitePlus; P37913; -.
DR   SwissPalm; P37913; -.
DR   EPD; P37913; -.
DR   MaxQB; P37913; -.
DR   PaxDb; P37913; -.
DR   PeptideAtlas; P37913; -.
DR   PRIDE; P37913; -.
DR   GeneID; 16881; -.
DR   KEGG; mmu:16881; -.
DR   CTD; 3978; -.
DR   MGI; MGI:101789; Lig1.
DR   eggNOG; KOG0967; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   HOVERGEN; HBG005514; -.
DR   InParanoid; P37913; -.
DR   KO; K10747; -.
DR   PRO; PR:P37913; -.
DR   Proteomes; UP000000589; Unplaced.
DR   CleanEx; MM_LIG1; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0003909; F:DNA ligase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; ISO:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IMP:MGI.
DR   GO; GO:0006260; P:DNA replication; IMP:MGI.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:MGI.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell cycle; Cell division;
KW   Complete proteome; DNA damage; DNA recombination; DNA repair;
KW   DNA replication; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN         1    916       DNA ligase 1.
FT                                /FTId=PRO_0000059571.
FT   REGION      447    456       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   REGION      640    642       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   ACT_SITE    566    566       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       619    619       Magnesium 1. {ECO:0000250}.
FT   METAL       718    718       Magnesium 2. {ECO:0000250}.
FT   BINDING     564    564       ATP. {ECO:0000250}.
FT   BINDING     571    571       ATP. {ECO:0000250}.
FT   BINDING     587    587       ATP. {ECO:0000250}.
FT   BINDING     723    723       ATP. {ECO:0000250}.
FT   BINDING     736    736       ATP. {ECO:0000250}.
FT   BINDING     742    742       ATP. {ECO:0000250}.
FT   SITE        303    303       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        588    588       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        768    768       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   SITE        793    793       Interaction with target DNA.
FT                                {ECO:0000250}.
FT   MOD_RES      49     49       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P18858}.
FT   MOD_RES      51     51       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:19131326,
FT                                ECO:0000244|PubMed:19144319,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES      65     65       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES      77     77       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     144    144       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     193    193       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P18858}.
FT   MOD_RES     225    225       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     228    228       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P18858}.
FT   MOD_RES     229    229       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P18858}.
FT   MOD_RES     232    232       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P18858}.
FT   MOD_RES     796    796       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P18858}.
FT   MOD_RES     799    799       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P18858}.
FT   MOD_RES     906    906       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     907    907       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     911    911       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
SQ   SEQUENCE   916 AA;  102290 MW;  6310B044364FB0E7 CRC64;
     MQRSIMSFFQ PTKEGKAKKP EKETPSSIRE KEPPPKVALK ERNQVVPESD SPVKRTGRKV
     AQVLSCEGED EDEAPGTPKV QKPVSDSEQS SPPSPDTCPE NSPVFNCSSP MDISPSGFPK
     RRTARKQLPK RTIQDTLEEQ NEDKTKTAKK RKKEEETPKE SLAEAEDIKQ KEEKEGDQLI
     VPSEPTKSPE SVTLTKTENI PVCKAGVKLK PQEEEQSKPP ARGAKTLSSF FTPRKPAVKT
     EVKQEESGTL RKEETKGTLD PANYNPSKNN YHPIEDACWK HGQKVPFLAV ARTFEKIEEV
     SARLKMVETL SNLLRSVVAL SPPDLLPVLY LSLNRLGPPQ QGLELGVGDG VLLKAVAQAT
     GRQLESIRAE VAEKGDVGLV AENSRSTQRL MLPPPPLTIS GVFTKFCDIA RLTGSASMAK
     KMDIIKGLFV ACRHSEARYI ARSLSGRLRL GLAEQSVLAA LAQAVSLTPP GQEFPTVVVD
     AGKGKTAEAR KMWLEEQGMI LKQTFCEVPD LDRIIPVLLE HGLERLPEHC KLSPGVPLKP
     MLAHPTRGVS EVLKRFEEVD FTCEYKYDGQ RAQIHVLEGG EVKIFSRNQE DNTGKYPDII
     SRIPKIKHPS VTSFILDTEA VAWDREKKQI QPFQVLTTRK RKEVDASEIQ VQVCLYAFDL
     IYLNGESLVR QPLSRRRQLL RENFVETEGE FVFTTSLDTK DTEQIAEFLE QSVKDSCEGL
     MVKTLDVDAT YEIAKRSHNW LKLKKDYLDG VGDTLDLVVI GAYLGRGKRA GRYGGFLLAA
     YDEESEELQA ICKLGTGFSD EELEEHHQSL QALVLPTPRP YVRIDGAVAP DHWLDPSIVW
     EVKCADLSLS PIYPAARGLV DKEKGISLRF PRFIRVRKDK QPEQATTSNQ VASLYRKQSQ
     IQNQQSSDLD SDVEDY
//
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