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P18858 (DNLI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA ligase 1

EC=6.5.1.1
Alternative name(s):
DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1
Gene names
Name:LIG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length919 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.

Catalytic activity

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).

Cofactor

Magnesium. Ref.17

Subcellular location

Nucleus.

Sequence similarities

Belongs to the ATP-dependent DNA ligase family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA recombination
DNA repair
DNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA ligation involved in DNA repair

Inferred from electronic annotation. Source: InterPro

DNA metabolic process

Traceable author statement Ref.1. Source: ProtInc

DNA repair

Traceable author statement. Source: Reactome

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

anatomical structure morphogenesis

Traceable author statement PubMed 8696349. Source: ProtInc

base-excision repair

Traceable author statement. Source: Reactome

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

double-strand break repair via nonhomologous end joining

Inferred from electronic annotation. Source: Ensembl

lagging strand elongation

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA gap filling

Traceable author statement. Source: Reactome

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

chromosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement PubMed 8696349. Source: ProtInc

DNA ligase (ATP) activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA ligase activity

Inferred from direct assay PubMed 9809069. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 919919DNA ligase 1
PRO_0000059570

Regions

Region449 – 45810Interaction with target DNA
Region642 – 6443Interaction with target DNA

Sites

Active site5681N6-AMP-lysine intermediate By similarity
Metal binding6211Magnesium 1 Probable
Metal binding7201Magnesium 2 Probable
Binding site5661ATP
Binding site5731ATP
Binding site5891ATP
Binding site7251ATP
Binding site7381ATP By similarity
Binding site7441ATP
Site3051Interaction with target DNA
Site5901Interaction with target DNA
Site7701Interaction with target DNA
Site7951Interaction with target DNA

Amino acid modifications

Modified residue471Phosphoserine Ref.14
Modified residue491Phosphoserine Ref.13 Ref.14
Modified residue511Phosphoserine Ref.8 Ref.10 Ref.13 Ref.14 Ref.16
Modified residue661Phosphoserine Ref.7 Ref.8 Ref.9 Ref.13 Ref.14 Ref.16
Modified residue761Phosphoserine Ref.7 Ref.8 Ref.9 Ref.13 Ref.14 Ref.16
Modified residue1411Phosphoserine Ref.7 Ref.10 Ref.13 Ref.14 Ref.16
Modified residue1951Phosphothreonine Ref.8 Ref.10 Ref.13 Ref.14 Ref.16
Modified residue2011Phosphoserine Ref.10 Ref.13 Ref.14
Modified residue2261N6-acetyllysine By similarity
Modified residue2331Phosphothreonine Ref.8 Ref.10
Modified residue9111Phosphoserine Ref.10 Ref.13 Ref.14 Ref.16
Modified residue9131Phosphoserine Ref.10 Ref.13 Ref.14 Ref.16
Cross-link422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Natural variations

Natural variant241A → V. Ref.2
Corresponds to variant rs3730855 [ dbSNP | Ensembl ].
VAR_018802
Natural variant521P → L.
Corresponds to variant rs4987181 [ dbSNP | Ensembl ].
VAR_020194
Natural variant621R → W. Ref.2
Corresponds to variant rs3730863 [ dbSNP | Ensembl ].
VAR_018803
Natural variant721D → G.
Corresponds to variant rs4987070 [ dbSNP | Ensembl ].
VAR_020195
Natural variant1521K → E in a colorectal cancer sample; somatic mutation. Ref.19
VAR_036511
Natural variant2491G → E. Ref.2
Corresponds to variant rs3730911 [ dbSNP | Ensembl ].
VAR_016766
Natural variant2671N → S. Ref.2
Corresponds to variant rs3730933 [ dbSNP | Ensembl ].
VAR_016767
Natural variant3491V → M. Ref.2
Corresponds to variant rs3730947 [ dbSNP | Ensembl ].
VAR_018804
Natural variant3691V → I. Ref.2
Corresponds to variant rs3730966 [ dbSNP | Ensembl ].
VAR_018805
Natural variant4091R → H.
Corresponds to variant rs4987068 [ dbSNP | Ensembl ].
VAR_016768
Natural variant4801M → V. Ref.2
Corresponds to variant rs3730980 [ dbSNP | Ensembl ].
VAR_016769
Natural variant5661E → K Found in a patient with a syndrome of immunodeficiency and increased cellular sensitivity to DNA-damaging agents due to LIG1 deficiency; compound heterozygote carrying W-771. Ref.18
VAR_002262
Natural variant6121S → L in a colorectal cancer sample; somatic mutation. Ref.19
VAR_036512
Natural variant6141T → I. Ref.2
Corresponds to variant rs3731003 [ dbSNP | Ensembl ].
VAR_016770
Natural variant6771R → L. Ref.2
Corresponds to variant rs3731008 [ dbSNP | Ensembl ].
VAR_018806
Natural variant7711R → W Found in a patient with a syndrome of immunodeficiency and increased cellular sensitivity to DNA-damaging agents due to LIG1 deficiency; compound heterozygote carrying K-566. Ref.18
VAR_002263

Secondary structure

.................................................................................................... 919
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18858 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: B2854DAE38A8D4AD

FASTA919101,736
        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 

« Hide

References

« Hide 'large scale' references
[1]"Human DNA ligase I cDNA: cloning and functional expression in Saccharomyces cerevisiae."
Barnes D.E., Johnston L.H., Kodama K., Tomkinson A.E., Lasko D.D., Lindahl T.
Proc. Natl. Acad. Sci. U.S.A. 87:6679-6683(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: T lymphoblast.
[2]NIEHS SNPs program
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-24; TRP-62; GLU-249; SER-267; MET-349; ILE-369; VAL-480; ILE-614 AND LEU-677.
[3]"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. expand/collapse author list , 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].
Tissue: Thymus.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[6]"A wild-type DNA ligase I gene is expressed in Bloom's syndrome cells."
Petrini J.H.J., Huwiler K.G., Weaver D.T.
Proc. Natl. Acad. Sci. U.S.A. 88:7615-7619(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 716-753.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-76 AND SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76; THR-195 AND THR-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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."
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.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-141; THR-195; SER-201; THR-233; SER-911 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells."
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.
Proteomics 8:2885-2896(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422.
Tissue: Cervix carcinoma.
[12]"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].
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51; SER-66; SER-76; SER-141; THR-195; SER-201; SER-911 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-51; SER-66; SER-76; SER-141; THR-195; SER-201; SER-911 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76; SER-141; THR-195; SER-911 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Human DNA ligase I completely encircles and partially unwinds nicked DNA."
Pascal J.M., O'Brien P.J., Tomkinson A.E., Ellenberger T.
Nature 432:473-478(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-919 IN COMPLEX WITH NICKED DNA AND AMP, COFACTOR, ACTIVE SITE.
[18]"Mutations in the DNA ligase I gene of an individual with immunodeficiencies and cellular hypersensitivity to DNA-damaging agents."
Barnes D.E., Tomkinson A.E., Lehmann A.R., Webster A.D.B., Lindahl T.
Cell 69:495-503(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-566 AND TRP-771.
[19]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-152 AND LEU-612.
+Additional computationally mapped references.

Web resources

LIG1base

LIG1 mutation db

NIEHS-SNPs
Wikipedia

DNA ligase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36067 mRNA. Translation: AAA59518.1.
AF527418 Genomic DNA. Translation: AAM77697.1.
AK314210 mRNA. Translation: BAG36885.1.
CH471177 Genomic DNA. Translation: EAW52316.1.
BC108318 mRNA. Translation: AAI08319.1.
CCDSCCDS12711.1.
PIRA41275. A36048.
RefSeqNP_000225.1. NM_000234.2.
NP_001275992.1. NM_001289063.1.
NP_001275993.1. NM_001289064.1.
XP_006723279.1. XM_006723216.1.
UniGeneHs.1770.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9NX-ray3.00A233-919[»]
ProteinModelPortalP18858.
SMRP18858. Positions 262-901.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110166. 6 interactions.
DIPDIP-24215N.
IntActP18858. 3 interactions.
MINTMINT-141868.
STRING9606.ENSP00000263274.

Chemistry

BindingDBP18858.
ChEMBLCHEMBL5694.
DrugBankDB00290. Bleomycin.

PTM databases

PhosphoSiteP18858.

Polymorphism databases

DMDM118773.

Proteomic databases

MaxQBP18858.
PaxDbP18858.
PeptideAtlasP18858.
PRIDEP18858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263274; ENSP00000263274; ENSG00000105486.
GeneID3978.
KEGGhsa:3978.
UCSCuc002pia.1. human.

Organism-specific databases

CTD3978.
GeneCardsGC19M048618.
HGNCHGNC:6598. LIG1.
HPACAB037015.
HPA041431.
HPA048071.
MIM126391. gene.
neXtProtNX_P18858.
PharmGKBPA30372.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1793.
HOGENOMHOG000036006.
HOVERGENHBG005514.
InParanoidP18858.
KOK10747.
OMALDPSGYN.
OrthoDBEOG7RFTGN.
PhylomeDBP18858.
TreeFamTF300342.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP18858.
BgeeP18858.
CleanExHS_LIG1.
GenevestigatorP18858.

Family and domain databases

Gene3D1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProIPR000977. DNA_ligase_ATP-dep.
IPR012309. DNA_ligase_ATP-dep_C.
IPR012310. DNA_ligase_ATP-dep_cent.
IPR016059. DNA_ligase_ATP-dep_CS.
IPR012308. DNA_ligase_ATP-dep_N.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]
SUPFAMSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00574. dnl1. 1 hit.
PROSITEPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLIG1. human.
EvolutionaryTraceP18858.
GeneWikiLIG1.
GenomeRNAi3978.
NextBio15592.
PROP18858.
SOURCESearch...

Entry information

Entry nameDNLI1_HUMAN
AccessionPrimary (citable) accession number: P18858
Secondary accession number(s): B2RAI8, Q32P23
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM