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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).PROSITE-ProRule annotation

Cofactori

Mg2+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 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. central nervous system development Source: UniProtKB
  5. chromosome organization Source: UniProtKB
  6. DNA biosynthetic process Source: InterPro
  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. in utero embryonic development Source: UniProtKB
  15. isotype switching Source: UniProtKB
  16. lagging strand elongation Source: RefGenome
  17. negative regulation of neuron apoptotic process Source: UniProtKB
  18. neuron apoptotic process Source: UniProtKB
  19. nucleotide-excision repair, DNA gap filling Source: UniProtKB
  20. positive regulation of fibroblast proliferation Source: UniProtKB
  21. positive regulation of neurogenesis Source: UniProtKB
  22. pro-B cell differentiation Source: UniProtKB
  23. response to gamma radiation Source: UniProtKB
  24. response to X-ray Source: UniProtKB
  25. single strand break repair Source: UniProtKB
  26. somatic stem cell maintenance Source: UniProtKB
  27. T cell differentiation in thymus Source: UniProtKB
  28. T cell receptor V(D)J recombination Source: UniProtKB
  29. V(D)J recombination Source: UniProtKB
  30. 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.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.
Orphaneti235. Dubowitz syndrome.
99812. 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 – 123Combined sources
Helixi16 – 2813Combined sources
Helixi32 – 5322Combined sources
Turni54 – 563Combined sources
Helixi65 – 717Combined sources
Helixi73 – 753Combined sources
Helixi86 – 9611Combined sources
Helixi104 – 1107Combined sources
Helixi125 – 1339Combined sources
Turni134 – 1363Combined sources
Helixi145 – 16016Combined sources
Helixi164 – 17613Combined sources
Helixi180 – 19112Combined sources
Helixi200 – 2078Combined sources
Helixi211 – 2188Combined sources
Helixi221 – 2277Combined sources
Beta strandi250 – 2534Combined sources
Helixi256 – 2583Combined sources
Helixi259 – 2624Combined sources
Turni263 – 2653Combined sources
Beta strandi268 – 2725Combined sources
Beta strandi276 – 2849Combined sources
Beta strandi287 – 2926Combined sources
Helixi299 – 3024Combined sources
Beta strandi308 – 3114Combined sources
Helixi312 – 3154Combined sources
Helixi316 – 3183Combined sources
Beta strandi324 – 33613Combined sources
Turni337 – 3404Combined sources
Beta strandi341 – 3433Combined sources
Helixi351 – 3566Combined sources
Beta strandi359 – 37214Combined sources
Beta strandi378 – 3803Combined sources
Helixi382 – 39211Combined sources
Turni397 – 3993Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi405 – 4084Combined sources
Helixi411 – 42313Combined sources
Beta strandi429 – 4324Combined sources
Beta strandi443 – 4508Combined sources
Helixi458 – 4603Combined sources
Beta strandi462 – 47110Combined sources
Helixi474 – 4785Combined sources
Beta strandi479 – 48810Combined sources
Beta strandi500 – 5078Combined sources
Helixi513 – 52210Combined sources
Helixi523 – 5253Combined sources
Beta strandi536 – 5394Combined sources
Beta strandi546 – 5483Combined sources
Helixi551 – 5533Combined sources
Beta strandi556 – 5605Combined sources
Beta strandi562 – 5665Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi573 – 5786Combined sources
Beta strandi580 – 5845Combined sources
Helixi590 – 5923Combined sources
Helixi596 – 6038Combined sources
Turni658 – 6614Combined sources
Beta strandi663 – 6664Combined sources
Beta strandi671 – 6733Combined sources
Helixi675 – 68410Combined sources
Beta strandi687 – 6926Combined sources
Beta strandi697 – 7015Combined sources
Helixi707 – 7148Combined sources
Helixi723 – 73210Combined sources
Helixi740 – 7423Combined sources
Beta strandi743 – 7453Combined sources
Helixi748 – 7536Combined sources
Turni754 – 7574Combined sources
Beta strandi764 – 7674Combined sources
Helixi771 – 7799Combined sources
Helixi789 – 80214Combined sources
Helixi809 – 8113Combined sources
Turni812 – 8154Combined sources
Beta strandi817 – 8204Combined sources
Beta strandi823 – 8253Combined sources
Helixi829 – 8313Combined sources
Helixi837 – 84711Combined sources
Beta strandi851 – 8555Combined sources
Beta strandi862 – 8654Combined sources
Helixi872 – 8809Combined sources
Beta strandi887 – 8904Combined sources
Helixi892 – 8998Combined sources
Helixi906 – 9083Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00750000117695.
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.
IPR029710. LIG4.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PANTHERiPTHR10459:SF7. PTHR10459:SF7. 1 hit.
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

        10         20         30         40         50
MAASQTSQTV ASHVPFADLC STLERIQKSK GRAEKIRHFR EFLDSWRKFH
60 70 80 90 100
DALHKNHKDV TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP
110 120 130 140 150
RDGKDALKLL NYRTPTGTHG DAGDFAMIAY FVLKPRCLQK GSLTIQQVND
160 170 180 190 200
LLDSIASNNS AKRKDLIKKS LLQLITQSSA LEQKWLIRMI IKDLKLGVSQ
210 220 230 240 250
QTIFSVFHND AAELHNVTTD LEKVCRQLHD PSVGLSDISI TLFSAFKPML
260 270 280 290 300
AAIADIEHIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYKY FSRNGYNYTD
310 320 330 340 350
QFGASPTEGS LTPFIHNAFK ADIQICILDG EMMAYNPNTQ TFMQKGTKFD
360 370 380 390 400
IKRMVEDSDL QTCYCVFDVL MVNNKKLGHE TLRKRYEILS SIFTPIPGRI
410 420 430 440 450
EIVQKTQAHT KNEVIDALNE AIDKREEGIM VKQPLSIYKP DKRGEGWLKI
460 470 480 490 500
KPEYVSGLMD ELDILIVGGY WGKGSRGGMM SHFLCAVAEK PPPGEKPSVF
510 520 530 540 550
HTLSRVGSGC TMKELYDLGL KLAKYWKPFH RKAPPSSILC GTEKPEVYIE
560 570 580 590 600
PCNSVIVQIK AAEIVPSDMY KTGCTLRFPR IEKIRDDKEW HECMTLDDLE
610 620 630 640 650
QLRGKASGKL ASKHLYIGGD DEPQEKKRKA APKMKKVIGI IEHLKAPNLT
660 670 680 690 700
NVNKISNIFE DVEFCVMSGT DSQPKPDLEN RIAEFGGYIV QNPGPDTYCV
710 720 730 740 750
IAGSENIRVK NIILSNKHDV VKPAWLLECF KTKSFVPWQP RFMIHMCPST
760 770 780 790 800
KEHFAREYDC YGDSYFIDTD LNQLKEVFSG IKNSNEQTPE EMASLIADLE
810 820 830 840 850
YRYSWDCSPL SMFRRHTVYL DSYAVINDLS TKNEGTRLAI KALELRFHGA
860 870 880 890 900
KVVSCLAEGV SHVIIGEDHS RVADFKAFRR TFKRKFKILK ESWVTDSIDK
910
CELQEENQYL I
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. Curated
The sequence CAA58467.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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.
ENST00000611712; ENSP00000484288; ENSG00000174405.
ENST00000614526; ENSP00000480814; 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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 .
ENST00000611712 ; ENSP00000484288 ; ENSG00000174405 .
ENST00000614526 ; ENSP00000480814 ; 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 235. Dubowitz syndrome.
99812. LIG4 syndrome.
39041. Omenn syndrome.
PharmGKBi PA30375.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1793.
GeneTreei ENSGT00750000117695.
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.
IPR029710. LIG4.
IPR012340. NA-bd_OB-fold.
[Graphical view ]
PANTHERi PTHR10459:SF7. PTHR10459:SF7. 1 hit.
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: November 26, 2014
This is version 168 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

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