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P37913

- DNLI1_MOUSE

UniProt

P37913 - DNLI1_MOUSE

Protein

DNA ligase 1

Gene

Lig1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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

    Magnesium.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 ligation Source: RefGenome
    4. DNA recombination Source: UniProtKB-KW
    5. DNA repair Source: MGI
    6. DNA replication Source: MGI
    7. double-strand break repair via nonhomologous end joining Source: MGI
    8. lagging strand elongation Source: RefGenome
    9. response to hydrogen peroxide Source: MGI

    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

    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

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    MQRSIMSFFQ PTKEGKAKKP EKETPSSIRE KEPPPKVALK ERNQVVPESD    50
    SPVKRTGRKV AQVLSCEGED EDEAPGTPKV QKPVSDSEQS SPPSPDTCPE 100
    NSPVFNCSSP MDISPSGFPK RRTARKQLPK RTIQDTLEEQ NEDKTKTAKK 150
    RKKEEETPKE SLAEAEDIKQ KEEKEGDQLI VPSEPTKSPE SVTLTKTENI 200
    PVCKAGVKLK PQEEEQSKPP ARGAKTLSSF FTPRKPAVKT EVKQEESGTL 250
    RKEETKGTLD PANYNPSKNN YHPIEDACWK HGQKVPFLAV ARTFEKIEEV 300
    SARLKMVETL SNLLRSVVAL SPPDLLPVLY LSLNRLGPPQ QGLELGVGDG 350
    VLLKAVAQAT GRQLESIRAE VAEKGDVGLV AENSRSTQRL MLPPPPLTIS 400
    GVFTKFCDIA RLTGSASMAK KMDIIKGLFV ACRHSEARYI ARSLSGRLRL 450
    GLAEQSVLAA LAQAVSLTPP GQEFPTVVVD AGKGKTAEAR KMWLEEQGMI 500
    LKQTFCEVPD LDRIIPVLLE HGLERLPEHC KLSPGVPLKP MLAHPTRGVS 550
    EVLKRFEEVD FTCEYKYDGQ RAQIHVLEGG EVKIFSRNQE DNTGKYPDII 600
    SRIPKIKHPS VTSFILDTEA VAWDREKKQI QPFQVLTTRK RKEVDASEIQ 650
    VQVCLYAFDL IYLNGESLVR QPLSRRRQLL RENFVETEGE FVFTTSLDTK 700
    DTEQIAEFLE QSVKDSCEGL MVKTLDVDAT YEIAKRSHNW LKLKKDYLDG 750
    VGDTLDLVVI GAYLGRGKRA GRYGGFLLAA YDEESEELQA ICKLGTGFSD 800
    EELEEHHQSL QALVLPTPRP YVRIDGAVAP DHWLDPSIVW EVKCADLSLS 850
    PIYPAARGLV DKEKGISLRF PRFIRVRKDK QPEQATTSNQ VASLYRKQSQ 900
    IQNQQSSDLD SDVEDY 916
    Length:916
    Mass (Da):102,290
    Last modified:February 1, 1996 - v2
    Checksum:i6310B044364FB0E7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    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: October 1, 2014
    This is version 116 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