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Q8BTF7

- DNLI4_MOUSE

UniProt

Q8BTF7 - DNLI4_MOUSE

Protein

DNA ligase 4

Gene

Lig4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends By similarity.By similarity

    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
    Binding sitei271 – 2711ATPBy similarity
    Active sitei273 – 2731N6-AMP-lysine intermediatePROSITE-ProRule annotation
    Binding sitei278 – 2781ATPBy similarity
    Binding sitei293 – 2931ATPBy similarity
    Metal bindingi331 – 3311Magnesium 1Sequence Analysis
    Metal bindingi427 – 4271Magnesium 2Sequence Analysis
    Binding sitei432 – 4321ATPBy similarity
    Binding sitei443 – 4431ATPBy similarity
    Binding sitei449 – 4491ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: MGI
    2. DNA binding Source: Ensembl
    3. DNA ligase (ATP) activity Source: MGI
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. cell proliferation Source: MGI
    4. cellular response to lithium ion Source: Ensembl
    5. central nervous system development Source: MGI
    6. chromosome organization Source: MGI
    7. DNA ligation Source: MGI
    8. DNA ligation involved in DNA recombination Source: MGI
    9. DNA ligation involved in DNA repair Source: MGI
    10. DNA repair Source: MGI
    11. double-strand break repair Source: MGI
    12. double-strand break repair via nonhomologous end joining Source: MGI
    13. immunoglobulin V(D)J recombination Source: MGI
    14. in utero embryonic development Source: MGI
    15. isotype switching Source: MGI
    16. lagging strand elongation Source: RefGenome
    17. negative regulation of neuron apoptotic process Source: MGI
    18. neuron apoptotic process Source: MGI
    19. nucleotide-excision repair Source: RefGenome
    20. nucleotide-excision repair, DNA gap filling Source: Ensembl
    21. positive regulation of fibroblast proliferation Source: MGI
    22. positive regulation of neurogenesis Source: MGI
    23. pro-B cell differentiation Source: MGI
    24. response to gamma radiation Source: MGI
    25. response to ionizing radiation Source: MGI
    26. response to X-ray Source: Ensembl
    27. single strand break repair Source: Ensembl
    28. somatic stem cell maintenance Source: MGI
    29. T cell differentiation in thymus Source: MGI
    30. T cell receptor V(D)J recombination Source: MGI
    31. V(D)J recombination 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 4 (EC:6.5.1.1)
    Alternative name(s):
    DNA ligase IV
    Polydeoxyribonucleotide synthase [ATP] 4
    Gene namesi
    Name:Lig4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1335098. Lig4.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. chromosome Source: RefGenome
    2. condensed chromosome Source: Ensembl
    3. cytoplasm Source: Ensembl
    4. DNA-dependent protein kinase-DNA ligase 4 complex Source: MGI
    5. DNA ligase IV complex Source: RefGenome
    6. focal adhesion Source: Ensembl
    7. nonhomologous end joining complex Source: UniProtKB
    8. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 911911DNA ligase 4PRO_0000059577Add
    BLAST

    Proteomic databases

    PaxDbiQ8BTF7.
    PRIDEiQ8BTF7.

    PTM databases

    PhosphoSiteiQ8BTF7.

    Expressioni

    Gene expression databases

    CleanExiMM_LIG4.
    GenevestigatoriQ8BTF7.

    Interactioni

    Subunit structurei

    Binds to XRCC4. The LIG4-XRCC4 complex has probably a 1:2 stoichiometry. The LIG4-XRCC4 heteromer associates in a DNA-dependent manner with the DNA-dependent protein kinase complex DNA-PK, formed by the Ku p70/p86 dimer (G22P1/G22P2) and PRKDC. Interacts with APLF By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BTF7.
    SMRiQ8BTF7. Positions 6-605, 654-911.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini654 – 74390BRCT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini808 – 911104BRCT 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ATP-dependent DNA ligase family.Curated
    Contains 2 BRCT domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1793.
    GeneTreeiENSGT00750000117695.
    HOGENOMiHOG000007831.
    HOVERGENiHBG005516.
    InParanoidiQ8BTF7.
    KOiK10777.
    OMAiHMCPSTK.
    OrthoDBiEOG7BKCT2.
    TreeFamiTF312980.

    Family and domain databases

    Gene3Di1.10.3260.10. 1 hit.
    2.40.50.140. 1 hit.
    3.40.50.10190. 2 hits.
    InterProiIPR001357. BRCT_dom.
    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.
    IPR021536. DNA_ligase_IV_dom.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PfamiPF00533. BRCT. 2 hits.
    PF04679. DNA_ligase_A_C. 1 hit.
    PF01068. DNA_ligase_A_M. 1 hit.
    PF04675. DNA_ligase_A_N. 1 hit.
    PF11411. DNA_ligase_IV. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 2 hits.
    [Graphical view]
    SUPFAMiSSF117018. SSF117018. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF52113. SSF52113. 2 hits.
    TIGRFAMsiTIGR00574. dnl1. 1 hit.
    PROSITEiPS50172. BRCT. 2 hits.
    PS00697. DNA_LIGASE_A1. 1 hit.
    PS00333. DNA_LIGASE_A2. 1 hit.
    PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BTF7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSQTSQTV AAHVPFADLC STLERIQKGK DRAEKIRHFK EFLDSWRKFH    50
    DALHKNRKDV TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP 100
    REGKDAQKLL NYRTPSGART DAGDFAMIAY FVLKPRCLQK GSLTIQQVNE 150
    LLDLVASNNS GKKKDLVKKS LLQLITQSSA LEQKWLIRMI IKDLKLGISQ 200
    QTIFSIFHND AVELHNVTTD LEKVCRQLHD PSVGLSDISI TLFSAFKPML 250
    AAVADVERVE KDMKQQSFYI ETKLDGERMQ MHKDGALYRY FSRNGYNYTD 300
    QFGESPQEGS LTPFIHNAFG TDVQACILDG EMMAYNPTTQ TFMQKGVKFD 350
    IKRMVEDSGL QTCYSVFDVL MVNKKKLGRE TLRKRYEILS STFTPIQGRI 400
    EIVQKTQAHT KKEVVDALND AIDKREEGIM VKHPLSIYKP DKRGEGWLKI 450
    KPEYVSGLMD ELDVLIVGGY WGKGSRGGMM SHFLCAVAET PPPGDRPSVF 500
    HTLCRVGSGY TMKELYDLGL KLAKYWKPFH KKSPPSSILC GTEKPEVYIE 550
    PQNSVIVQIK AAEIVPSDMY KTGSTLRFPR IEKIRDDKEW HECMTLGDLE 600
    QLRGKASGKL ATKHLHVGDD DEPREKRRKP ISKTKKAIRI IEHLKAPNLS 650
    NVNKVSNVFE DVEFCVMSGL DGYPKADLEN RIAEFGGYIV QNPGPDTYCV 700
    IAGSENVRVK NIISSDKNDV VKPEWLLECF KTKTCVPWQP RFMIHMCPST 750
    KQHFAREYDC YGDSYFVDTD LDQLKEVFLG IKPSEQQTPE EMAPVIADLE 800
    CRYSWDHSPL SMFRHYTIYL DLYAVINDLS SRIEATRLGI TALELRFHGA 850
    KVVSCLSEGV SHVIIGEDQR RVTDFKIFRR MLKKKFKILQ ESWVSDSVDK 900
    GELQEENQYL L 911
    Length:911
    Mass (Da):104,120
    Last modified:October 3, 2012 - v2
    Checksum:i20CDD0F6465355A2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti268 – 2681F → L in BAC26747. (PubMed:16141072)Curated
    Sequence conflicti758 – 7581Y → C in BAE28333. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030029 mRNA. Translation: BAC26747.1.
    AK148081 mRNA. Translation: BAE28333.1.
    AC138397 Genomic DNA. No translation available.
    CH466566 Genomic DNA. Translation: EDL22038.1.
    CH466566 Genomic DNA. Translation: EDL22040.1.
    CCDSiCCDS22092.1.
    RefSeqiNP_795927.2. NM_176953.3.
    UniGeneiMm.80584.

    Genome annotation databases

    EnsembliENSMUST00000095476; ENSMUSP00000093130; ENSMUSG00000049717.
    ENSMUST00000170033; ENSMUSP00000130807; ENSMUSG00000049717.
    GeneIDi319583.
    KEGGimmu:319583.
    UCSCiuc009kul.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030029 mRNA. Translation: BAC26747.1 .
    AK148081 mRNA. Translation: BAE28333.1 .
    AC138397 Genomic DNA. No translation available.
    CH466566 Genomic DNA. Translation: EDL22038.1 .
    CH466566 Genomic DNA. Translation: EDL22040.1 .
    CCDSi CCDS22092.1.
    RefSeqi NP_795927.2. NM_176953.3.
    UniGenei Mm.80584.

    3D structure databases

    ProteinModelPortali Q8BTF7.
    SMRi Q8BTF7. Positions 6-605, 654-911.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8BTF7.

    Proteomic databases

    PaxDbi Q8BTF7.
    PRIDEi Q8BTF7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000095476 ; ENSMUSP00000093130 ; ENSMUSG00000049717 .
    ENSMUST00000170033 ; ENSMUSP00000130807 ; ENSMUSG00000049717 .
    GeneIDi 319583.
    KEGGi mmu:319583.
    UCSCi uc009kul.1. mouse.

    Organism-specific databases

    CTDi 3981.
    MGIi MGI:1335098. Lig4.

    Phylogenomic databases

    eggNOGi COG1793.
    GeneTreei ENSGT00750000117695.
    HOGENOMi HOG000007831.
    HOVERGENi HBG005516.
    InParanoidi Q8BTF7.
    KOi K10777.
    OMAi HMCPSTK.
    OrthoDBi EOG7BKCT2.
    TreeFami TF312980.

    Miscellaneous databases

    NextBioi 395028.
    PROi Q8BTF7.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_LIG4.
    Genevestigatori Q8BTF7.

    Family and domain databases

    Gene3Di 1.10.3260.10. 1 hit.
    2.40.50.140. 1 hit.
    3.40.50.10190. 2 hits.
    InterProi IPR001357. BRCT_dom.
    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.
    IPR021536. DNA_ligase_IV_dom.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    Pfami PF00533. BRCT. 2 hits.
    PF04679. DNA_ligase_A_C. 1 hit.
    PF01068. DNA_ligase_A_M. 1 hit.
    PF04675. DNA_ligase_A_N. 1 hit.
    PF11411. DNA_ligase_IV. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 2 hits.
    [Graphical view ]
    SUPFAMi SSF117018. SSF117018. 1 hit.
    SSF50249. SSF50249. 1 hit.
    SSF52113. SSF52113. 2 hits.
    TIGRFAMsi TIGR00574. dnl1. 1 hit.
    PROSITEi PS50172. BRCT. 2 hits.
    PS00697. DNA_LIGASE_A1. 1 hit.
    PS00333. DNA_LIGASE_A2. 1 hit.
    PS50160. DNA_LIGASE_A3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Testis.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiDNLI4_MOUSE
    AccessioniPrimary (citable) accession number: Q8BTF7
    Secondary accession number(s): G3UWC4, Q3UG76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 102 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