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P49917

- DNLI4_HUMAN

UniProt

P49917 - DNLI4_HUMAN

Protein

DNA ligase 4

Gene

LIG4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (07 Feb 2006)
      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 non-homologous 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.2 Publications

    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: UniProtKB-KW
    2. DNA binding Source: UniProtKB
    3. DNA ligase (ATP) activity Source: UniProtKB
    4. DNA ligase activity Source: UniProtKB
    5. ligase activity Source: UniProtKB
    6. metal ion binding Source: UniProtKB-KW
    7. protein binding Source: UniProtKB
    8. protein C-terminus binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. cell proliferation Source: UniProtKB
    4. cellular response to lithium ion Source: Ensembl
    5. central nervous system development Source: UniProtKB
    6. chromosome organization Source: UniProtKB
    7. DNA ligation Source: UniProtKB
    8. DNA ligation involved in DNA recombination Source: UniProtKB
    9. DNA ligation involved in DNA repair Source: UniProtKB
    10. DNA repair Source: Reactome
    11. double-strand break repair Source: UniProtKB
    12. double-strand break repair via nonhomologous end joining Source: UniProtKB
    13. establishment of integrated proviral latency Source: Reactome
    14. immunoglobulin V(D)J recombination Source: Ensembl
    15. in utero embryonic development Source: UniProtKB
    16. isotype switching Source: UniProtKB
    17. lagging strand elongation Source: RefGenome
    18. negative regulation of neuron apoptotic process Source: UniProtKB
    19. neuron apoptotic process Source: UniProtKB
    20. nucleotide-excision repair, DNA gap filling Source: UniProtKB
    21. positive regulation of fibroblast proliferation Source: UniProtKB
    22. positive regulation of neurogenesis Source: UniProtKB
    23. pro-B cell differentiation Source: UniProtKB
    24. response to gamma radiation Source: UniProtKB
    25. response to X-ray Source: UniProtKB
    26. single strand break repair Source: UniProtKB
    27. somatic stem cell maintenance Source: UniProtKB
    28. T cell differentiation in thymus Source: UniProtKB
    29. T cell receptor V(D)J recombination Source: UniProtKB
    30. V(D)J recombination Source: UniProtKB
    31. viral process Source: Reactome

    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

    Enzyme and pathway databases

    BRENDAi6.5.1.1. 2681.
    ReactomeiREACT_1022. Nonhomologous End-joining (NHEJ).
    REACT_9058. 2-LTR circle formation.
    SignaLinkiP49917.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:6601. LIG4.

    Subcellular locationi

    GO - Cellular componenti

    1. condensed chromosome Source: UniProtKB
    2. cytoplasm Source: HPA
    3. DNA-dependent protein kinase-DNA ligase 4 complex Source: UniProtKB
    4. DNA ligase IV complex Source: UniProtKB
    5. focal adhesion Source: HPA
    6. nonhomologous end joining complex Source: UniProtKB
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProtKB
    9. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    LIG4 syndrome (LIG4S) [MIM:606593]: Characterized by immunodeficiency and developmental and growth delay. Patients display unusual facial features, microcephaly, growth and/or developmental delay, pancytopenia, and various skin abnormalities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti278 – 2781R → H in LIG4S and leukemia; impairs activity. 2 Publications
    VAR_012774
    Natural varianti469 – 4691G → E in LIG4S. 1 Publication
    VAR_012775
    Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing radiation (RSSCID) [MIM:602450]: A form of severe combined immunodeficiency, a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients present in infancy with recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. Individuals affected by RS-SCID show defects in the DNA repair machinery necessary for coding joint formation and the completion of V(D)J recombination. A subset of cells from such patients show increased radiosensitivity.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, SCID

    Organism-specific databases

    MIMi602450. phenotype.
    606593. phenotype.
    Orphaneti99812. LIG4 syndrome.
    39041. Omenn syndrome.
    PharmGKBiPA30375.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 911911DNA ligase 4PRO_0000059576Add
    BLAST

    Proteomic databases

    MaxQBiP49917.
    PaxDbiP49917.
    PRIDEiP49917.

    PTM databases

    PhosphoSiteiP49917.

    Expressioni

    Tissue specificityi

    Testis, thymus, prostate and heart.

    Gene expression databases

    BgeeiP49917.
    CleanExiHS_LIG4.
    GenevestigatoriP49917.

    Organism-specific databases

    HPAiHPA001334.

    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.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APLFQ8IW192EBI-847896,EBI-1256044
    NHEJ1Q9H9Q44EBI-847896,EBI-847807

    Protein-protein interaction databases

    BioGridi110169. 130 interactions.
    DIPiDIP-37958N.
    IntActiP49917. 7 interactions.
    MINTiMINT-3018022.
    STRINGi9606.ENSP00000349393.

    Structurei

    Secondary structure

    1
    911
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 123
    Helixi16 – 2813
    Helixi32 – 5322
    Turni54 – 563
    Helixi65 – 717
    Helixi73 – 753
    Helixi86 – 9611
    Helixi104 – 1107
    Helixi125 – 1339
    Turni134 – 1363
    Helixi145 – 16016
    Helixi164 – 17613
    Helixi180 – 19112
    Helixi200 – 2078
    Helixi211 – 2188
    Helixi221 – 2277
    Beta strandi250 – 2534
    Helixi256 – 2583
    Helixi259 – 2624
    Turni263 – 2653
    Beta strandi268 – 2725
    Beta strandi276 – 2849
    Beta strandi287 – 2926
    Helixi299 – 3024
    Beta strandi308 – 3114
    Helixi312 – 3154
    Helixi316 – 3183
    Beta strandi324 – 33613
    Turni337 – 3404
    Beta strandi341 – 3433
    Helixi351 – 3566
    Beta strandi359 – 37214
    Beta strandi378 – 3803
    Helixi382 – 39211
    Turni397 – 3993
    Beta strandi400 – 4023
    Beta strandi405 – 4084
    Helixi411 – 42313
    Beta strandi429 – 4324
    Beta strandi443 – 4508
    Helixi458 – 4603
    Beta strandi462 – 47110
    Helixi474 – 4785
    Beta strandi479 – 48810
    Beta strandi500 – 5078
    Helixi513 – 52210
    Helixi523 – 5253
    Beta strandi536 – 5394
    Beta strandi546 – 5483
    Helixi551 – 5533
    Beta strandi556 – 5605
    Beta strandi562 – 5665
    Beta strandi568 – 5703
    Beta strandi573 – 5786
    Beta strandi580 – 5845
    Helixi590 – 5923
    Helixi596 – 6038
    Turni658 – 6614
    Beta strandi663 – 6664
    Beta strandi671 – 6733
    Helixi675 – 68410
    Beta strandi687 – 6926
    Beta strandi697 – 7015
    Helixi707 – 7148
    Helixi723 – 73210
    Helixi740 – 7423
    Beta strandi743 – 7453
    Helixi748 – 7536
    Turni754 – 7574
    Beta strandi764 – 7674
    Helixi771 – 7799
    Helixi789 – 80214
    Helixi809 – 8113
    Turni812 – 8154
    Beta strandi817 – 8204
    Beta strandi823 – 8253
    Helixi829 – 8313
    Helixi837 – 84711
    Beta strandi851 – 8555
    Beta strandi862 – 8654
    Helixi872 – 8809
    Beta strandi887 – 8904
    Helixi892 – 8998
    Helixi906 – 9083

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IK9X-ray2.30C748-784[»]
    2E2WNMR-A654-759[»]
    3II6X-ray2.40X/Y654-911[»]
    3VNNX-ray2.90A268-406[»]
    3W1BX-ray2.40A1-609[»]
    3W1GX-ray2.55A1-609[»]
    3W5OX-ray2.84A/B1-609[»]
    4HTOX-ray2.81A1-240[»]
    4HTPX-ray2.25A/B1-240[»]
    ProteinModelPortaliP49917.
    SMRiP49917. Positions 6-605, 654-911.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49917.

    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.
    HOGENOMiHOG000007831.
    HOVERGENiHBG005516.
    InParanoidiP49917.
    KOiK10777.
    OMAiHMCPSTK.
    OrthoDBiEOG7BKCT2.
    PhylomeDBiP49917.
    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.

    P49917-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASQTSQTV ASHVPFADLC STLERIQKSK GRAEKIRHFR EFLDSWRKFH    50
    DALHKNHKDV TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP 100
    RDGKDALKLL NYRTPTGTHG DAGDFAMIAY FVLKPRCLQK GSLTIQQVND 150
    LLDSIASNNS AKRKDLIKKS LLQLITQSSA LEQKWLIRMI IKDLKLGVSQ 200
    QTIFSVFHND AAELHNVTTD LEKVCRQLHD PSVGLSDISI TLFSAFKPML 250
    AAIADIEHIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYKY FSRNGYNYTD 300
    QFGASPTEGS LTPFIHNAFK ADIQICILDG EMMAYNPNTQ TFMQKGTKFD 350
    IKRMVEDSDL QTCYCVFDVL MVNNKKLGHE TLRKRYEILS SIFTPIPGRI 400
    EIVQKTQAHT KNEVIDALNE AIDKREEGIM VKQPLSIYKP DKRGEGWLKI 450
    KPEYVSGLMD ELDILIVGGY WGKGSRGGMM SHFLCAVAEK PPPGEKPSVF 500
    HTLSRVGSGC TMKELYDLGL KLAKYWKPFH RKAPPSSILC GTEKPEVYIE 550
    PCNSVIVQIK AAEIVPSDMY KTGCTLRFPR IEKIRDDKEW HECMTLDDLE 600
    QLRGKASGKL ASKHLYIGGD DEPQEKKRKA APKMKKVIGI IEHLKAPNLT 650
    NVNKISNIFE DVEFCVMSGT DSQPKPDLEN RIAEFGGYIV QNPGPDTYCV 700
    IAGSENIRVK NIILSNKHDV VKPAWLLECF KTKSFVPWQP RFMIHMCPST 750
    KEHFAREYDC YGDSYFIDTD LNQLKEVFSG IKNSNEQTPE EMASLIADLE 800
    YRYSWDCSPL SMFRRHTVYL DSYAVINDLS TKNEGTRLAI KALELRFHGA 850
    KVVSCLAEGV SHVIIGEDHS RVADFKAFRR TFKRKFKILK ESWVTDSIDK 900
    CELQEENQYL I 911
    Length:911
    Mass (Da):103,971
    Last modified:February 7, 2006 - v2
    Checksum:i2122813E1EFA63B9
    GO

    Sequence cautioni

    The sequence AAL77435.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA58467.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti246 – 2461F → S in CAA58467. (PubMed:7760816)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31A → V Associated with resistance to multiple myeloma. 1 Publication
    Corresponds to variant rs1805389 [ dbSNP | Ensembl ].
    VAR_029352
    Natural varianti9 – 91T → I Associated with resistance to multiple myeloma. 1 Publication
    Corresponds to variant rs1805388 [ dbSNP | Ensembl ].
    VAR_033884
    Natural varianti62 – 621D → H.
    Corresponds to variant rs3093763 [ dbSNP | Ensembl ].
    VAR_029353
    Natural varianti231 – 2311P → S.1 Publication
    Corresponds to variant rs3093765 [ dbSNP | Ensembl ].
    VAR_018808
    Natural varianti278 – 2781R → H in LIG4S and leukemia; impairs activity. 2 Publications
    VAR_012774
    Natural varianti433 – 4331Missing in RS-SCID. 1 Publication
    VAR_044123
    Natural varianti461 – 4611E → G.
    Corresponds to variant rs2232640 [ dbSNP | Ensembl ].
    VAR_044124
    Natural varianti469 – 4691G → E in LIG4S. 1 Publication
    VAR_012775
    Natural varianti539 – 5391L → F.
    Corresponds to variant rs3742212 [ dbSNP | Ensembl ].
    VAR_016771
    Natural varianti658 – 6581I → V.
    Corresponds to variant rs2232641 [ dbSNP | Ensembl ].
    VAR_016772
    Natural varianti857 – 8571A → T.1 Publication
    Corresponds to variant rs2232642 [ dbSNP | Ensembl ].
    VAR_016773

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83441 mRNA. Translation: CAA58467.1. Different initiation.
    AF479264 Genomic DNA. Translation: AAL77435.1. Different initiation.
    AL157762 Genomic DNA. Translation: CAH70629.1.
    BC037491 mRNA. Translation: AAH37491.1.
    CCDSiCCDS9508.1.
    PIRiI37079.
    RefSeqiNP_001091738.1. NM_001098268.1.
    NP_002303.2. NM_002312.3.
    NP_996820.1. NM_206937.1.
    XP_005254113.1. XM_005254056.1.
    XP_005254114.1. XM_005254057.2.
    XP_005254115.1. XM_005254058.1.
    XP_006720013.1. XM_006719950.1.
    XP_006720014.1. XM_006719951.1.
    XP_006720015.1. XM_006719952.1.
    UniGeneiHs.166091.

    Genome annotation databases

    EnsembliENST00000356922; ENSP00000349393; ENSG00000174405.
    ENST00000405925; ENSP00000385955; ENSG00000174405.
    ENST00000442234; ENSP00000402030; ENSG00000174405.
    GeneIDi3981.
    KEGGihsa:3981.
    UCSCiuc001vqn.3. human.

    Polymorphism databases

    DMDMi88911290.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    LIG4base

    LIG4 mutation db

    NIEHS-SNPs
    Wikipedia

    DNA ligase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83441 mRNA. Translation: CAA58467.1 . Different initiation.
    AF479264 Genomic DNA. Translation: AAL77435.1 . Different initiation.
    AL157762 Genomic DNA. Translation: CAH70629.1 .
    BC037491 mRNA. Translation: AAH37491.1 .
    CCDSi CCDS9508.1.
    PIRi I37079.
    RefSeqi NP_001091738.1. NM_001098268.1.
    NP_002303.2. NM_002312.3.
    NP_996820.1. NM_206937.1.
    XP_005254113.1. XM_005254056.1.
    XP_005254114.1. XM_005254057.2.
    XP_005254115.1. XM_005254058.1.
    XP_006720013.1. XM_006719950.1.
    XP_006720014.1. XM_006719951.1.
    XP_006720015.1. XM_006719952.1.
    UniGenei Hs.166091.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IK9 X-ray 2.30 C 748-784 [» ]
    2E2W NMR - A 654-759 [» ]
    3II6 X-ray 2.40 X/Y 654-911 [» ]
    3VNN X-ray 2.90 A 268-406 [» ]
    3W1B X-ray 2.40 A 1-609 [» ]
    3W1G X-ray 2.55 A 1-609 [» ]
    3W5O X-ray 2.84 A/B 1-609 [» ]
    4HTO X-ray 2.81 A 1-240 [» ]
    4HTP X-ray 2.25 A/B 1-240 [» ]
    ProteinModelPortali P49917.
    SMRi P49917. Positions 6-605, 654-911.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110169. 130 interactions.
    DIPi DIP-37958N.
    IntActi P49917. 7 interactions.
    MINTi MINT-3018022.
    STRINGi 9606.ENSP00000349393.

    PTM databases

    PhosphoSitei P49917.

    Polymorphism databases

    DMDMi 88911290.

    Proteomic databases

    MaxQBi P49917.
    PaxDbi P49917.
    PRIDEi P49917.

    Protocols and materials databases

    DNASUi 3981.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356922 ; ENSP00000349393 ; ENSG00000174405 .
    ENST00000405925 ; ENSP00000385955 ; ENSG00000174405 .
    ENST00000442234 ; ENSP00000402030 ; ENSG00000174405 .
    GeneIDi 3981.
    KEGGi hsa:3981.
    UCSCi uc001vqn.3. human.

    Organism-specific databases

    CTDi 3981.
    GeneCardsi GC13M108859.
    HGNCi HGNC:6601. LIG4.
    HPAi HPA001334.
    MIMi 601837. gene.
    602450. phenotype.
    606593. phenotype.
    neXtProti NX_P49917.
    Orphaneti 99812. LIG4 syndrome.
    39041. Omenn syndrome.
    PharmGKBi PA30375.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1793.
    HOGENOMi HOG000007831.
    HOVERGENi HBG005516.
    InParanoidi P49917.
    KOi K10777.
    OMAi HMCPSTK.
    OrthoDBi EOG7BKCT2.
    PhylomeDBi P49917.
    TreeFami TF312980.

    Enzyme and pathway databases

    BRENDAi 6.5.1.1. 2681.
    Reactomei REACT_1022. Nonhomologous End-joining (NHEJ).
    REACT_9058. 2-LTR circle formation.
    SignaLinki P49917.

    Miscellaneous databases

    ChiTaRSi LIG4. human.
    EvolutionaryTracei P49917.
    GeneWikii LIG4.
    GenomeRNAii 3981.
    NextBioi 15604.
    PROi P49917.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49917.
    CleanExi HS_LIG4.
    Genevestigatori P49917.

    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. "Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination."
      Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C., Yu G.-L., Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E., Haseltine W.A., Lindahl T.
      Mol. Cell. Biol. 15:3206-3216(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Prostate.
    2. NIEHS SNPs program
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-231 AND THR-857.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. Cited for: CHARACTERIZATION.
    6. "DNA ligase IV is essential for V(D)J recombination and DNA double-strand break repair in human precursor lymphocytes."
      Grawunder U., Zimmer D., Fugmann S., Schwarz K., Lieber M.R.
      Mol. Cell 2:477-484(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH XRCC4.
    7. "Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV."
      Critchlow S.E., Bowater R.P., Jackson S.P.
      Curr. Biol. 7:588-598(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XRCC4.
    8. "Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase."
      Chen L., Trujillo K., Sung P., Tomkinson A.E.
      J. Biol. Chem. 275:26196-26205(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH XRCC4; G22P1; G22P2 AND PRKDC.
    9. "Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment."
      Calsou P., Delteil C., Frit P., Drouet J., Salles B.
      J. Mol. Biol. 326:93-103(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH G22P1; G22P2 AND PRKDC.
    10. "A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses."
      Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A.
      EMBO J. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APLF.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 748-784 IN COMPLEX WITH XRCC4.
    13. "Solution structure of the first BRCT domain of human DNA ligase IV."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 654-759.
    14. Cited for: VARIANT LEUKEMIA HIS-278.
    15. "Cellular and biochemical impact of a mutation in DNA ligase IV conferring clinical radiosensitivity."
      Riballo E., Doherty A.J., Dai Y., Stiff T., Oettinger M.A., Jeggo P.A., Kysela B.
      J. Biol. Chem. 276:31124-31132(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT HIS-278.
    16. Cited for: VARIANTS LIG4S HIS-278 AND GLU-469.
    17. "Genetic variants of NHEJ DNA ligase IV can affect the risk of developing multiple myeloma, a tumour characterised by aberrant class switch recombination."
      Roddam P.L., Rollinson S., O'Driscoll M., Jeggo P.A., Jack A., Morgan G.J.
      J. Med. Genet. 39:900-905(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-3 AND ILE-9, ASSOCIATION WITH RESISTANCE TO MULTIPLE MYELOMA.
    18. Cited for: VARIANT RS-SCID GLN-433 DEL.

    Entry informationi

    Entry nameiDNLI4_HUMAN
    AccessioniPrimary (citable) accession number: P49917
    Secondary accession number(s): Q8IY66, Q8TEU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 166 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3