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P37913

- DNLI1_MOUSE

UniProt

P37913 - DNLI1_MOUSE

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Protein

DNA ligase 1

Gene

Lig1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).PROSITE-ProRule annotation

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei303 – 3031Interaction with target DNABy similarity
Binding sitei564 – 5641ATPBy similarity
Active sitei566 – 5661N6-AMP-lysine intermediatePROSITE-ProRule annotation
Binding sitei571 – 5711ATPBy similarity
Binding sitei587 – 5871ATPBy similarity
Sitei588 – 5881Interaction with target DNABy similarity
Metal bindingi619 – 6191Magnesium 1By similarity
Metal bindingi718 – 7181Magnesium 2By similarity
Binding sitei723 – 7231ATPBy similarity
Binding sitei736 – 7361ATPBy similarity
Binding sitei742 – 7421ATPBy similarity
Sitei768 – 7681Interaction with target DNABy similarity
Sitei793 – 7931Interaction with target DNABy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: InterPro
  3. DNA ligase (ATP) activity Source: RefGenome
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. DNA biosynthetic process Source: InterPro
  4. DNA ligation Source: RefGenome
  5. DNA recombination Source: UniProtKB-KW
  6. DNA repair Source: MGI
  7. DNA replication Source: MGI
  8. double-strand break repair via nonhomologous end joining Source: MGI
  9. lagging strand elongation Source: RefGenome
  10. response to hydrogen peroxide Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, DNA replication

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligase 1 (EC:6.5.1.1)
Alternative name(s):
DNA ligase I
Polydeoxyribonucleotide synthase [ATP] 1
Gene namesi
Name:Lig1
Synonyms:Lig-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:101789. Lig1.

Subcellular locationi

GO - Cellular componenti

  1. chromosome Source: RefGenome
  2. mitochondrion Source: RefGenome
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 916916DNA ligase 1PRO_0000059571Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei51 – 511Phosphoserine3 Publications
Modified residuei65 – 651Phosphoserine1 Publication
Modified residuei77 – 771Phosphothreonine1 Publication
Modified residuei144 – 1441N6-acetyllysine1 Publication
Modified residuei193 – 1931PhosphothreonineBy similarity
Modified residuei225 – 2251N6-acetyllysine1 Publication
Modified residuei232 – 2321PhosphothreonineBy similarity
Cross-linki420 – 420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei911 – 9111PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP37913.
PaxDbiP37913.
PRIDEiP37913.

PTM databases

PhosphoSiteiP37913.

Expressioni

Gene expression databases

CleanExiMM_LIG1.
GenevestigatoriP37913.

Interactioni

Protein-protein interaction databases

BioGridi201164. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP37913.
SMRiP37913. Positions 260-899.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni447 – 45610Interaction with target DNABy similarity
Regioni640 – 6423Interaction with target DNABy similarity

Sequence similaritiesi

Belongs to the ATP-dependent DNA ligase family.Curated

Phylogenomic databases

eggNOGiCOG1793.
HOVERGENiHBG005514.
InParanoidiP37913.
KOiK10747.

Family and domain databases

Gene3Di1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR000977. 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]
PfamiPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00574. dnl1. 1 hit.
PROSITEiPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37913-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQRSIMSFFQ PTKEGKAKKP EKETPSSIRE KEPPPKVALK ERNQVVPESD
60 70 80 90 100
SPVKRTGRKV AQVLSCEGED EDEAPGTPKV QKPVSDSEQS SPPSPDTCPE
110 120 130 140 150
NSPVFNCSSP MDISPSGFPK RRTARKQLPK RTIQDTLEEQ NEDKTKTAKK
160 170 180 190 200
RKKEEETPKE SLAEAEDIKQ KEEKEGDQLI VPSEPTKSPE SVTLTKTENI
210 220 230 240 250
PVCKAGVKLK PQEEEQSKPP ARGAKTLSSF FTPRKPAVKT EVKQEESGTL
260 270 280 290 300
RKEETKGTLD PANYNPSKNN YHPIEDACWK HGQKVPFLAV ARTFEKIEEV
310 320 330 340 350
SARLKMVETL SNLLRSVVAL SPPDLLPVLY LSLNRLGPPQ QGLELGVGDG
360 370 380 390 400
VLLKAVAQAT GRQLESIRAE VAEKGDVGLV AENSRSTQRL MLPPPPLTIS
410 420 430 440 450
GVFTKFCDIA RLTGSASMAK KMDIIKGLFV ACRHSEARYI ARSLSGRLRL
460 470 480 490 500
GLAEQSVLAA LAQAVSLTPP GQEFPTVVVD AGKGKTAEAR KMWLEEQGMI
510 520 530 540 550
LKQTFCEVPD LDRIIPVLLE HGLERLPEHC KLSPGVPLKP MLAHPTRGVS
560 570 580 590 600
EVLKRFEEVD FTCEYKYDGQ RAQIHVLEGG EVKIFSRNQE DNTGKYPDII
610 620 630 640 650
SRIPKIKHPS VTSFILDTEA VAWDREKKQI QPFQVLTTRK RKEVDASEIQ
660 670 680 690 700
VQVCLYAFDL IYLNGESLVR QPLSRRRQLL RENFVETEGE FVFTTSLDTK
710 720 730 740 750
DTEQIAEFLE QSVKDSCEGL MVKTLDVDAT YEIAKRSHNW LKLKKDYLDG
760 770 780 790 800
VGDTLDLVVI GAYLGRGKRA GRYGGFLLAA YDEESEELQA ICKLGTGFSD
810 820 830 840 850
EELEEHHQSL QALVLPTPRP YVRIDGAVAP DHWLDPSIVW EVKCADLSLS
860 870 880 890 900
PIYPAARGLV DKEKGISLRF PRFIRVRKDK QPEQATTSNQ VASLYRKQSQ
910
IQNQQSSDLD SDVEDY
Length:916
Mass (Da):102,290
Last modified:February 1, 1996 - v2
Checksum:i6310B044364FB0E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04674 mRNA. Translation: AAA70403.1.
U19604 mRNA. Translation: AAB60500.1.
PIRiI48921.
RefSeqiNP_034845.2. NM_010715.2.
UniGeneiMm.288179.
Mm.421129.

Genome annotation databases

GeneIDi16881.
KEGGimmu:16881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04674 mRNA. Translation: AAA70403.1 .
U19604 mRNA. Translation: AAB60500.1 .
PIRi I48921.
RefSeqi NP_034845.2. NM_010715.2.
UniGenei Mm.288179.
Mm.421129.

3D structure databases

ProteinModelPortali P37913.
SMRi P37913. Positions 260-899.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201164. 1 interaction.

PTM databases

PhosphoSitei P37913.

Proteomic databases

MaxQBi P37913.
PaxDbi P37913.
PRIDEi P37913.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 16881.
KEGGi mmu:16881.

Organism-specific databases

CTDi 3978.
MGIi MGI:101789. Lig1.

Phylogenomic databases

eggNOGi COG1793.
HOVERGENi HBG005514.
InParanoidi P37913.
KOi K10747.

Miscellaneous databases

NextBioi 290882.
PROi P37913.
SOURCEi Search...

Gene expression databases

CleanExi MM_LIG1.
Genevestigatori P37913.

Family and domain databases

Gene3Di 1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProi IPR000977. 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 ]
Pfami PF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00574. dnl1. 1 hit.
PROSITEi PS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDNLI1_MOUSE
AccessioniPrimary (citable) accession number: P37913
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3