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P49917

- DNLI4_HUMAN

UniProt

P49917 - DNLI4_HUMAN

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Protein

DNA ligase 4

Gene
LIG4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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).

Cofactori

Magnesium By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei271 – 2711ATP By similarity
Active sitei273 – 2731N6-AMP-lysine intermediate By similarity
Binding sitei278 – 2781ATP By similarity
Binding sitei293 – 2931ATP By similarity
Metal bindingi331 – 3311Magnesium 1 Reviewed prediction
Metal bindingi427 – 4271Magnesium 2 Reviewed prediction
Binding sitei432 – 4321ATP By similarity
Binding sitei443 – 4431ATP By similarity
Binding sitei449 – 4491ATP By 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
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

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti278 – 2781R → H in LIG4S and leukemia; impairs activity. 3 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.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi110169. 129 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.

Miscellaneous databases

EvolutionaryTraceiP49917.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini654 – 74390BRCT 1Add
BLAST
Domaini808 – 911104BRCT 2Add
BLAST

Sequence similaritiesi

Contains 2 BRCT domains.

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.

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. 3 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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti246 – 2461F → S in CAA58467. 1 Publication

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. 129 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 165 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

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