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P37913 (DNLI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
Synonyms:Lig-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length916 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 By similarity.

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
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA ligation

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from mutant phenotype PubMed 21390131. Source: MGI

DNA replication

Inferred from mutant phenotype PubMed 11896201. Source: MGI

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype PubMed 21655080. Source: MGI

lagging strand elongation

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to hydrogen peroxide

Inferred from mutant phenotype PubMed 21390131. Source: MGI

   Cellular_componentchromosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrion

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay PubMed 9001252. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: InterPro

DNA ligase (ATP) activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 – 916916DNA ligase 1
PRO_0000059571

Regions

Region447 – 45610Interaction with target DNA By similarity
Region640 – 6423Interaction with target DNA By similarity

Sites

Active site5661N6-AMP-lysine intermediate By similarity
Metal binding6191Magnesium 1 By similarity
Metal binding7181Magnesium 2 By similarity
Binding site5641ATP By similarity
Binding site5711ATP By similarity
Binding site5871ATP By similarity
Binding site7231ATP By similarity
Binding site7361ATP By similarity
Binding site7421ATP By similarity
Site3031Interaction with target DNA By similarity
Site5881Interaction with target DNA By similarity
Site7681Interaction with target DNA By similarity
Site7931Interaction with target DNA By similarity

Amino acid modifications

Modified residue491Phosphoserine By similarity
Modified residue511Phosphoserine Ref.4 Ref.5 Ref.6
Modified residue651Phosphoserine Ref.4
Modified residue771Phosphothreonine Ref.4
Modified residue1441N6-acetyllysine Ref.7
Modified residue1931Phosphothreonine By similarity
Modified residue2251N6-acetyllysine Ref.7
Modified residue2321Phosphothreonine By similarity
Modified residue9111Phosphoserine By similarity
Cross-link420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P37913 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 6310B044364FB0E7

FASTA916102,290
        10         20         30         40         50         60 
MQRSIMSFFQ PTKEGKAKKP EKETPSSIRE KEPPPKVALK ERNQVVPESD SPVKRTGRKV 

        70         80         90        100        110        120 
AQVLSCEGED EDEAPGTPKV QKPVSDSEQS SPPSPDTCPE NSPVFNCSSP MDISPSGFPK 

       130        140        150        160        170        180 
RRTARKQLPK RTIQDTLEEQ NEDKTKTAKK RKKEEETPKE SLAEAEDIKQ KEEKEGDQLI 

       190        200        210        220        230        240 
VPSEPTKSPE SVTLTKTENI PVCKAGVKLK PQEEEQSKPP ARGAKTLSSF FTPRKPAVKT 

       250        260        270        280        290        300 
EVKQEESGTL RKEETKGTLD PANYNPSKNN YHPIEDACWK HGQKVPFLAV ARTFEKIEEV 

       310        320        330        340        350        360 
SARLKMVETL SNLLRSVVAL SPPDLLPVLY LSLNRLGPPQ QGLELGVGDG VLLKAVAQAT 

       370        380        390        400        410        420 
GRQLESIRAE VAEKGDVGLV AENSRSTQRL MLPPPPLTIS GVFTKFCDIA RLTGSASMAK 

       430        440        450        460        470        480 
KMDIIKGLFV ACRHSEARYI ARSLSGRLRL GLAEQSVLAA LAQAVSLTPP GQEFPTVVVD 

       490        500        510        520        530        540 
AGKGKTAEAR KMWLEEQGMI LKQTFCEVPD LDRIIPVLLE HGLERLPEHC KLSPGVPLKP 

       550        560        570        580        590        600 
MLAHPTRGVS EVLKRFEEVD FTCEYKYDGQ RAQIHVLEGG EVKIFSRNQE DNTGKYPDII 

       610        620        630        640        650        660 
SRIPKIKHPS VTSFILDTEA VAWDREKKQI QPFQVLTTRK RKEVDASEIQ VQVCLYAFDL 

       670        680        690        700        710        720 
IYLNGESLVR QPLSRRRQLL RENFVETEGE FVFTTSLDTK DTEQIAEFLE QSVKDSCEGL 

       730        740        750        760        770        780 
MVKTLDVDAT YEIAKRSHNW LKLKKDYLDG VGDTLDLVVI GAYLGRGKRA GRYGGFLLAA 

       790        800        810        820        830        840 
YDEESEELQA ICKLGTGFSD EELEEHHQSL QALVLPTPRP YVRIDGAVAP DHWLDPSIVW 

       850        860        870        880        890        900 
EVKCADLSLS PIYPAARGLV DKEKGISLRF PRFIRVRKDK QPEQATTSNQ VASLYRKQSQ 

       910 
IQNQQSSDLD SDVEDY 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of a cDNA coding for the murine DNA ligase I enzyme."
Savini E., Biamonti G., Ciarrocchi G., Montecucco A.
Gene 144:253-257(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[2]Montecucco A.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Comparison between cDNA clones encoding murine DNA ligase I."
Jessop J.K., Melton D.W.
Gene 160:307-308(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/Ola.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-65 AND THR-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144 AND LYS-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04674 mRNA. Translation: AAA70403.1.
U19604 mRNA. Translation: AAB60500.1.
PIRI48921.
RefSeqNP_034845.2. NM_010715.2.
UniGeneMm.288179.
Mm.421129.

3D structure databases

ProteinModelPortalP37913.
SMRP37913. Positions 260-899.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201164. 1 interaction.

PTM databases

PhosphoSiteP37913.

Proteomic databases

MaxQBP37913.
PaxDbP37913.
PRIDEP37913.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID16881.
KEGGmmu:16881.

Organism-specific databases

CTD3978.
MGIMGI:101789. Lig1.

Phylogenomic databases

eggNOGCOG1793.
HOVERGENHBG005514.
InParanoidP37913.
KOK10747.

Gene expression databases

CleanExMM_LIG1.
GenevestigatorP37913.

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

NextBio290882.
PROP37913.
SOURCESearch...

Entry information

Entry nameDNLI1_MOUSE
AccessionPrimary (citable) accession number: P37913
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot