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UniProtKB/Swiss-Prot entry P18858


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DNLI1_HUMAN
Primary accession number P18858
Secondary accession number Q32P23
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on November 1, 1990 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 107)
Name and origin of the protein
Protein name DNA ligase 1
Synonyms EC 6.5.1.1
DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1
Gene name
Name: LIG1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T lymphoblast;
DOI=10.1073/pnas.87.17.6679; PubMed=2204063 [NCBI, ExPASy, EBI, Israel, Japan]
Barnes D.E., Johnston L.H., Kodama K., Tomkinson A.E., Lasko D.D., Lindahl T.;
"Human DNA ligase I cDNA: cloning and functional expression in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 87:6679-6683(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-24; TRP-62; GLU-249; SER-267; MET-349; ILE-369; VAL-480; ILE-614 AND LEU-677.
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE OF 716-753.
DOI=10.1073/pnas.88.17.7615; PubMed=1881902 [NCBI, ExPASy, EBI, Israel, Japan]
Petrini J.H.J., Huwiler K.G., Weaver D.T.;
"A wild-type DNA ligase I gene is expressed in Bloom's syndrome cells.";
Proc. Natl. Acad. Sci. U.S.A. 88:7615-7619(1991).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-76; SER-141; THR-195 AND SER-911, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-66; SER-76; SER-141; THR-195; SER-201 AND THR-233, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76; THR-195 AND THR-233, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-76, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700120-MCP200; PubMed=17693683 [NCBI, ExPASy, EBI, Israel, Japan]
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51 AND SER-141, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76; SER-141; THR-195; SER-201; THR-233; SER-911 AND SER-913, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-919 IN COMPLEX WITH NICKED DNA AND AMP, COFACTOR, AND ACTIVE SITE.
DOI=10.1038/nature03082; PubMed=15565146 [NCBI, ExPASy, EBI, Israel, Japan]
Pascal J.M., O'Brien P.J., Tomkinson A.E., Ellenberger T.;
"Human DNA ligase I completely encircles and partially unwinds nicked DNA.";
Nature 432:473-478(2004).
[15]
VARIANTS LYS-566 AND TRP-771.
DOI=10.1016/0092-8674(92)90450-Q; PubMed=1581963 [NCBI, ExPASy, EBI, Israel, Japan]
Barnes D.E., Tomkinson A.E., Lehmann A.R., Webster A.D.B., Lindahl T.;
"Mutations in the DNA ligase I gene of an individual with immunodeficiencies and cellular hypersensitivity to DNA-damaging agents.";
Cell 69:495-503(1992).
[16]
VARIANTS [LARGE SCALE ANALYSIS] GLU-152 AND LEU-612.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M36067; AAA59518.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF527418; AAM77697.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC108318; AAI08319.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00219841; -.
PIR A36048; A41275.
RefSeq NP_000225.1; -.
UniGene Hs.1770
3D structure databases
PDB
1X9N; X-ray; 3.00 A; A=233-919.[ExPASy / RCSB / EBI]
PDBsum 1X9N; -.
ModBase P18858.
Protein-protein interaction databases
DIP DIP:24215N; -.
IntAct P18858; 2.
PTM databases
PhosphoSite P18858; -.
Enzyme and pathway databases
BRENDA 6.5.1.1; 247.
Reactome REACT_216; DNA Repair.
Organism-specific databases
GeneCards GC19M053310; -.
H-InvDB HIX0040136; -.
HGNC HGNC:6598; LIG1.
GenAtlas LIG1.
MIM 126391; gene. [NCBI / EBI]
PharmGKB PA30372; -.
Gene expression databases
ArrayExpress P18858; -.
Bgee P18858; -.
CleanEx HS_LIG1; -.
GermOnline ENSG00000105486; Homo sapiens.
Ontologies
GO
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0003910; Molecular function: DNA ligase (ATP) activity (inferred from electronic annotation from EC).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009653; Biological process: anatomical structure morphogenesis (traceable author statement from ProtInc).
GO:0007049; Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0006310; Biological process: DNA recombination (inferred from electronic annotation from UniProtKB-KW).
GO:0006260; Biological process: DNA replication (inferred from electronic annotation from UniProtKB-KW).
GO:0006297; Biological process: nucleotide-excision repair, DNA gap filling (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR000977; DNA_ligase.
IPR012309; DNA_ligase_A_C.
IPR012310; DNA_ligase_A_M.
IPR012308; DNA_ligase_A_N.
IPR016059; DNA_ligase_CS.
IPR012340; NA-bd_OB-fold.
Graphical view of domain structure.
Gene3D G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
Pfam PF04679; DNA_ligase_A_C; 1.
PF01068; DNA_ligase_A_M; 1.
PF04675; DNA_ligase_A_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00574; dnl1; 1.
PROSITE PS00697; DNA_LIGASE_A1; 1.
PS00333; DNA_LIGASE_A2; 1.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P18858; -.
PRIDE P18858; -.
Genome annotation databases
Ensembl ENSG00000105486; Homo sapiens. [Contig view]
GeneID 3978; -.
KEGG hsa:3978; -.
Phylogenomic databases
HOGENOM P18858; -.
HOVERGEN P18858; -.
OMA P18858; RNWLKLK.
Other
DrugBank DB00290; Bleomycin.
NextBio 15592; -.
SOURCE LIG1; Homo sapiens.
ProtoNet P18858.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cell cycle; Cell division; Disease mutation; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   919  919     DNA ligase 1. PRO_0000059570
REGION   449   458  10     Interaction with target DNA. 
REGION   642   644  3     Interaction with target DNA. 
ACT_SITE   568   568        N6-AMP-lysine intermediate (By similarity). 
METAL   621   621        Magnesium 1 (Probable). 
METAL   720   720        Magnesium 2 (Probable). 
BINDING   566   566        ATP. 
BINDING   573   573        ATP. 
BINDING   589   589        ATP. 
BINDING   725   725        ATP. 
BINDING   738   738        ATP (By similarity). 
BINDING   744   744        ATP. 
SITE   305   305  1     Interaction with target DNA. 
SITE   590   590  1     Interaction with target DNA. 
SITE   770   770  1     Interaction with target DNA. 
SITE   795   795  1     Interaction with target DNA. 
MOD_RES   49    49        Phosphoserine. 
MOD_RES   51    51        Phosphoserine. 
MOD_RES   66    66        Phosphoserine. 
MOD_RES   76    76        Phosphoserine. 
MOD_RES   141   141        Phosphoserine. 
MOD_RES   195   195        Phosphothreonine. 
MOD_RES   201   201        Phosphoserine. 
MOD_RES   230   230        Phosphoserine. 
MOD_RES   233   233        Phosphothreonine. 
MOD_RES   911   911        Phosphoserine. 
MOD_RES   913   913        Phosphoserine. 
VARIANT   24    24  1     A -> V (in dbSNP:rs3730855 [NCBI]). VAR_018802 
VARIANT   52    52  1     P -> L (in dbSNP:rs4987181 [NCBI]). VAR_020194 
VARIANT   62    62  1     R -> W (in dbSNP:rs3730863 [NCBI]). VAR_018803 
VARIANT   72    72  1     D -> G (in dbSNP:rs4987070 [NCBI]). VAR_020195 
VARIANT   152   152  1     K -> E (in a colorectal cancer sample; somatic mutation). VAR_036511 
VARIANT   249   249  1     G -> E (in dbSNP:rs3730911 [NCBI]). VAR_016766 
VARIANT   267   267  1     N -> S (in dbSNP:rs3730933 [NCBI]). VAR_016767 
VARIANT   349   349  1     V -> M (in dbSNP:rs3730947 [NCBI]). VAR_018804 
VARIANT   369   369  1     V -> I (in dbSNP:rs3730966 [NCBI]). VAR_018805 
VARIANT   409   409  1     R -> H (in dbSNP:rs4987068 [NCBI]). VAR_016768 
VARIANT   480   480  1     M -> V (in dbSNP:rs3730980 [NCBI]). VAR_016769 
VARIANT   566   566  1     E -> K (in LIG1 deficiency). VAR_002262 
VARIANT   612   612  1     S -> L (in a colorectal cancer sample; somatic mutation). VAR_036512 
VARIANT   614   614  1     T -> I (in dbSNP:rs3731003 [NCBI]). VAR_016770 
VARIANT   677   677  1     R -> L (in dbSNP:rs3731008 [NCBI]). VAR_018806 
VARIANT   771   771  1     R -> W (in LIG1 deficiency). VAR_002263 
HELIX   263   265  3      
HELIX   275   278  4      
HELIX   289   300  12      
HELIX   305   322  18      
HELIX   324   326  3      
HELIX   327   335  9      
HELIX   341   343  3      
HELIX   351   362  12      
HELIX   366   376  11      
HELIX   379   382  4      
HELIX   401   413  13      
HELIX   419   433  15      
HELIX   438   446  9      
HELIX   456   469  14      
TURN   483   486  4      
HELIX   489   509  21      
HELIX   513   527  15      
HELIX   529   531  3      
STRAND   544   550  7      
HELIX   551   557  7      
TURN   558   560  3      
STRAND   563   578  16      
STRAND   584   587  4      
TURN   595   597  3      
HELIX   599   603  5      
HELIX   606   608  3      
STRAND   616   625  10      
TURN   627   629  3      
HELIX   635   638  4      
HELIX   648   650  3      
STRAND   653   665  13      
HELIX   675   685  11      
TURN   690   692  3      
STRAND   693   695  3      
HELIX   704   716  13      
STRAND   718   730  13      
TURN   735   737  3      
STRAND   739   746  8      
HELIX   747   751  5      
STRAND   755   767  13      
STRAND   774   784  11      
TURN   785   788  4      
STRAND   789   796  8      
HELIX   802   814  13      
STRAND   816   819  4      
STRAND   827   829  3      
STRAND   833   836  4      
STRAND   841   854  14      
TURN   857   861  5      
STRAND   867   872  6      
STRAND   874   878  5      
HELIX   884   886  3      
HELIX   890   900  11      
Sequence information
Length: 919 AA [This is the length of the unprocessed precursor] Molecular weight: 101736 Da [This is the MW of the unprocessed precursor] CRC64: B2854DAE38A8D4AD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQRSIMSFFH PKKEGKAKKP EKEASNSSRE TEPPPKAALK EWNGVVSESD SPVKRPGRKA 

        70         80         90        100        110        120 
ARVLGSEGEE EDEALSPAKG QKPALDCSQV SPPRPATSPE NNASLSDTSP MDSSPSGIPK 

       130        140        150        160        170        180 
RRTARKQLPK RTIQEVLEEQ SEDEDREAKR KKEEEEEETP KESLTEAEVA TEKEGEDGDQ 

       190        200        210        220        230        240 
PTTPPKPLKT SKAETPTESV SEPEVATKQE LQEEEEQTKP PRRAPKTLSS FFTPRKPAVK 

       250        260        270        280        290        300 
KEVKEEEPGA PGKEGAAEGP LDPSGYNPAK NNYHPVEDAC WKPGQKVPYL AVARTFEKIE 

       310        320        330        340        350        360 
EVSARLRMVE TLSNLLRSVV ALSPPDLLPV LYLSLNHLGP PQQGLELGVG DGVLLKAVAQ 

       370        380        390        400        410        420 
ATGRQLESVR AEAAEKGDVG LVAENSRSTQ RLMLPPPPLT ASGVFSKFRD IARLTGSAST 

       430        440        450        460        470        480 
AKKIDIIKGL FVACRHSEAR FIARSLSGRL RLGLAEQSVL AALSQAVSLT PPGQEFPPAM 

       490        500        510        520        530        540 
VDAGKGKTAE ARKTWLEEQG MILKQTFCEV PDLDRIIPVL LEHGLERLPE HCKLSPGIPL 

       550        560        570        580        590        600 
KPMLAHPTRG ISEVLKRFEE AAFTCEYKYD GQRAQIHALE GGEVKIFSRN QEDNTGKYPD 

       610        620        630        640        650        660 
IISRIPKIKL PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE IQVQVCLYAF 

       670        680        690        700        710        720 
DLIYLNGESL VREPLSRRRQ LLRENFVETE GEFVFATSLD TKDIEQIAEF LEQSVKDSCE 

       730        740        750        760        770        780 
GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL DGVGDTLDLV VIGAYLGRGK RAGRYGGFLL 

       790        800        810        820        830        840 
ASYDEDSEEL QAICKLGTGF SDEELEEHHQ SLKALVLPSP RPYVRIDGAV IPDHWLDPSA 

       850        860        870        880        890        900 
VWEVKCADLS LSPIYPAARG LVDSDKGISL RFPRFIRVRE DKQPEQATTS AQVACLYRKQ 

       910 
SQIQNQQGED SGSDPEDTY 

P18858 in FASTA format

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