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Database: UniProt
Entry: Q3U4X8_MOUSE
LinkDB: Q3U4X8_MOUSE
Original site: Q3U4X8_MOUSE 
ID   Q3U4X8_MOUSE            Unreviewed;       932 AA.
AC   Q3U4X8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   28-MAR-2018, entry version 117.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=Lig1 {ECO:0000313|EMBL:AAI38542.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000096411, ECO:0000313|MGI:MGI:101789};
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 {ECO:0000313|EMBL:BAE32302.1};
RN   [1] {ECO:0000313|EMBL:BAE32302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE32302.1};
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAE32302.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE32302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE32302.1};
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAE32302.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE32302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE32302.1};
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAE32302.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE32302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE32302.1};
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAE32302.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE32302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE32302.1};
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAE32302.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:AAI38542.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI38542.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M.,
RA   Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S.,
RA   Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F.,
RA   Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J.,
RA   Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N.,
RA   Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B.,
RA   Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B.,
RA   Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S.,
RA   Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R.,
RA   Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L.,
RA   Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E.,
RA   Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D.,
RA   Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G.,
RA   Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J.,
RA   Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L.,
RA   Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D.,
RA   Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A.,
RA   Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S.,
RA   Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7] {ECO:0000313|EMBL:BAE32302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE32302.1};
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAE32302.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:BAE32302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE32302.1};
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAE32302.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9] {ECO:0000313|EMBL:BAE32302.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD {ECO:0000313|EMBL:BAE32302.1};
RC   TISSUE=Thymus {ECO:0000313|EMBL:BAE32302.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [10] {ECO:0000213|PubMed:17242355}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [11] {ECO:0000213|PubMed:19144319}
RP   IDENTIFICATION 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   [12] {ECO:0000213|PubMed:19131326}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [13] {ECO:0000313|Ensembl:ENSMUSP00000096411, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000096411,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [14] {ECO:0000213|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [15] {ECO:0000313|Ensembl:ENSMUSP00000096411}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000096411};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [16] {ECO:0000313|Ensembl:ENSMUSP00000136972}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000136972};
RG   Ensembl;
RL   Submitted (AUG-2012) to UniProtKB.
RN   [17] {ECO:0000213|PubMed:23806337}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; AC161792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC138541; AAI38542.1; -; mRNA.
DR   EMBL; BC138542; AAI38543.1; -; mRNA.
DR   EMBL; AK153993; BAE32302.1; -; mRNA.
DR   RefSeq; NP_001076657.1; NM_001083188.1.
DR   RefSeq; NP_001186239.1; NM_001199310.1.
DR   RefSeq; NP_034845.2; NM_010715.2.
DR   UniGene; Mm.288179; -.
DR   UniGene; Mm.421129; -.
DR   Ensembl; ENSMUST00000098814; ENSMUSP00000096411; ENSMUSG00000056394.
DR   Ensembl; ENSMUST00000165964; ENSMUSP00000126525; ENSMUSG00000056394.
DR   Ensembl; ENSMUST00000177588; ENSMUSP00000136972; ENSMUSG00000056394.
DR   GeneID; 16881; -.
DR   KEGG; mmu:16881; -.
DR   UCSC; uc009ffq.1; mouse.
DR   CTD; 3978; -.
DR   MGI; MGI:101789; Lig1.
DR   eggNOG; KOG0967; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   GeneTree; ENSGT00860000133792; -.
DR   HOGENOM; HOG000036006; -.
DR   HOVERGEN; HBG005514; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; EOG091G06OS; -.
DR   TreeFam; TF300342; -.
DR   Reactome; R-MMU-110362; POLB-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-MMU-174414; Processive synthesis on the C-strand of the telomere.
DR   Reactome; R-MMU-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-MMU-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-MMU-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-MMU-69183; Processive synthesis on the lagging strand.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000056394; -.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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   ATP-binding {ECO:0000256|RuleBase:RU000617};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000589};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Proteomics identification {ECO:0000213|EPD:Q3U4X8,
KW   ECO:0000213|MaxQB:Q3U4X8, ECO:0000213|PeptideAtlas:Q3U4X8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN      662    798       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   COILED      153    173       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   932 AA;  104093 MW;  BAC3966B2D3D523A CRC64;
     MRKKEQERKG ETSAANMQRS IMSFFQPTKE GKAKKPEKET PSSIREKEPP PKVALKERNQ
     VVPESDSPVK RTGRKVAQVL SCEGEDEDEA PGTPKVQKPV SDSEQSSPPS PDTCPENSPV
     FNCSSPMDIS PSGFPKRRTA RKQLPKRTIQ DTLEEQNEDK TKTAKKRKKE EETPKESLAE
     AEDVKQKEEK EGDQLIVPSE PTKSPESVTL TKTENIPVCK AGVKLKPQEE EQSKPPARGA
     KTLSSFFTPR KPAVKTEVKQ EESGTLRKEE TKGTLDPANY NPSKNNYHPI EDACWKHGQK
     VPFLAVARTF EKIEEVSARL KMVETLSNLL RSVVALSPPD LLPVLYLSLN RLGPPQQGLE
     LGVGDGVLLK AVAQATGRQL ESIRAEVAEK GDVGLVAENS RSTQRLMLPP PPLTISGVFT
     KFCDIARLTG SASMAKKMDI IKGLFVACRH SEARYIARSL SGRLRLGLAE QSVLAALAQA
     VSLTPPGQEF PTAVVDAGKG KTAEARKMWL EEQGMILKQT FCEVPDLDRI IPVLLEHGLE
     RLPEHCKLSP GVPLKPMLAH PTRGVSEVLK RFEEVDFTCE YKYDGQRAQI HVLEGGEVKI
     FSRNQEDNTG KYPDIISRIP KIKHPSVTSF ILDTEAVAWD REKKQIQPFQ VLTTRKRKEV
     DASEIQVQVC LYAFDLIYLN GESLVRQPLS RRRQLLRENF VETEGEFVFT TSLDTKDTEQ
     IAEFLEQSVK DSCEGLMVKT LDVDATYEIA KRSHNWLKLK KDYLDGVGDT LDLVVIGAYL
     GRGKRAGRYG GFLLAAYDEE SEELQAICKL GTGFSDEELE EHHQSLQALV LPTPRPYVRI
     DGAVAPDHWL DPSIVWEVKC ADLSLSPIYP AARGLVDKEK GISLRFPRFI RVRKDKQPEQ
     ATTSNQVASL YRKQSQIQNQ QSSDLDSDVE DY
//
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