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Protein

DNA ligase 4

Gene

LIG4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.PROSITE-ProRule annotation

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei271ATPBy similarity1
Active sitei273N6-AMP-lysine intermediatePROSITE-ProRule annotation1
Binding sitei278ATPBy similarity1
Binding sitei293ATPBy similarity1
Metal bindingi331Magnesium 1Sequence analysis1
Metal bindingi427Magnesium 2Sequence analysis1
Binding sitei432ATPBy similarity1
Binding sitei443ATPBy similarity1
Binding sitei449ATPBy similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB
  • DNA ligase (ATP) activity Source: UniProtKB
  • DNA ligase activity Source: UniProtKB
  • ligase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein C-terminus binding Source: UniProtKB

GO - Biological processi

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

BioCyciZFISH:HS10794-MONOMER.
BRENDAi6.5.1.1. 2681.
ReactomeiR-HSA-164843. 2-LTR circle formation.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
SignaLinkiP49917.
SIGNORiP49917.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligase 4 (EC:6.5.1.1PROSITE-ProRule annotation)
Alternative name(s):
DNA ligase IV
Polydeoxyribonucleotide synthase [ATP] 4
Gene namesi
Name:LIG4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:6601. LIG4.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome Source: UniProtKB
  • cytoplasm Source: HPA
  • DNA-dependent protein kinase-DNA ligase 4 complex Source: UniProtKB
  • DNA ligase IV complex Source: UniProtKB
  • focal adhesion Source: HPA
  • nonhomologous end joining complex Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

LIG4 syndrome (LIG4S)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by immunodeficiency and developmental and growth delay. Patients display unusual facial features, microcephaly, growth and/or developmental delay, pancytopenia, and various skin abnormalities.
See also OMIM:606593
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012774278R → H in LIG4S and leukemia; impairs activity. 3 PublicationsCorresponds to variant rs104894421dbSNPEnsembl.1
Natural variantiVAR_012775469G → E in LIG4S. 1 PublicationCorresponds to variant rs104894420dbSNPEnsembl.1
Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing radiation (RSSCID)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:602450
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_044123433Missing in RSSCID. 1 Publication1

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

DisGeNETi3981.
MalaCardsiLIG4.
MIMi602450. phenotype.
606593. phenotype.
OpenTargetsiENSG00000174405.
Orphaneti235. Dubowitz syndrome.
99812. LIG4 syndrome.
39041. Omenn syndrome.
PharmGKBiPA30375.

Polymorphism and mutation databases

BioMutaiLIG4.
DMDMi88911290.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000595761 – 911DNA ligase 4Add BLAST911

Proteomic databases

EPDiP49917.
MaxQBiP49917.
PaxDbiP49917.
PeptideAtlasiP49917.
PRIDEiP49917.

PTM databases

iPTMnetiP49917.
PhosphoSitePlusiP49917.

Expressioni

Tissue specificityi

Testis, thymus, prostate and heart.

Gene expression databases

BgeeiENSG00000174405.
CleanExiHS_LIG4.
ExpressionAtlasiP49917. baseline and differential.
GenevisibleiP49917. HS.

Organism-specific databases

HPAiHPA001334.

Interactioni

Subunit structurei

Interacts with XRCC4. The LIG4-XRCC4 complex has probably a 1:2 stoichiometry. The LIG4-XRCC4 complex associates in a DNA-dependent manner with the DNA-PK complex composed of PRKDC, XRCC6/Ku70 and XRCC5/Ku86 to form the core non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and C9orf142/PAXX. Interacts with APLF.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APLFQ8IW192EBI-847896,EBI-1256044
DCLRE1CQ96SD111EBI-847896,EBI-11694104
NHEJ1Q9H9Q44EBI-847896,EBI-847807
XRCC4Q134267EBI-847896,EBI-717592

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110169. 129 interactors.
DIPiDIP-37958N.
IntActiP49917. 11 interactors.
MINTiMINT-3018022.
STRINGi9606.ENSP00000349393.

Structurei

Secondary structure

1911
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Helixi16 – 28Combined sources13
Helixi32 – 53Combined sources22
Turni54 – 56Combined sources3
Helixi65 – 71Combined sources7
Helixi73 – 75Combined sources3
Helixi86 – 96Combined sources11
Helixi104 – 110Combined sources7
Helixi125 – 133Combined sources9
Turni134 – 136Combined sources3
Helixi145 – 160Combined sources16
Helixi164 – 176Combined sources13
Helixi180 – 191Combined sources12
Helixi200 – 207Combined sources8
Helixi211 – 218Combined sources8
Helixi221 – 227Combined sources7
Beta strandi250 – 253Combined sources4
Helixi256 – 258Combined sources3
Helixi259 – 262Combined sources4
Turni263 – 265Combined sources3
Beta strandi268 – 272Combined sources5
Beta strandi276 – 284Combined sources9
Beta strandi287 – 292Combined sources6
Helixi299 – 302Combined sources4
Beta strandi308 – 311Combined sources4
Helixi312 – 315Combined sources4
Helixi316 – 318Combined sources3
Beta strandi324 – 336Combined sources13
Turni337 – 340Combined sources4
Beta strandi341 – 343Combined sources3
Helixi351 – 356Combined sources6
Beta strandi359 – 372Combined sources14
Beta strandi378 – 380Combined sources3
Helixi382 – 392Combined sources11
Turni397 – 399Combined sources3
Beta strandi400 – 402Combined sources3
Beta strandi405 – 408Combined sources4
Helixi411 – 423Combined sources13
Beta strandi429 – 432Combined sources4
Beta strandi443 – 450Combined sources8
Helixi458 – 460Combined sources3
Beta strandi462 – 471Combined sources10
Helixi474 – 478Combined sources5
Beta strandi479 – 488Combined sources10
Beta strandi500 – 507Combined sources8
Helixi513 – 522Combined sources10
Helixi523 – 525Combined sources3
Beta strandi536 – 539Combined sources4
Beta strandi546 – 548Combined sources3
Helixi551 – 553Combined sources3
Beta strandi556 – 560Combined sources5
Beta strandi562 – 566Combined sources5
Beta strandi568 – 570Combined sources3
Beta strandi573 – 578Combined sources6
Beta strandi580 – 584Combined sources5
Helixi590 – 592Combined sources3
Helixi596 – 603Combined sources8
Turni658 – 661Combined sources4
Beta strandi663 – 666Combined sources4
Beta strandi671 – 673Combined sources3
Helixi675 – 684Combined sources10
Beta strandi687 – 692Combined sources6
Beta strandi697 – 701Combined sources5
Helixi707 – 714Combined sources8
Helixi723 – 732Combined sources10
Helixi740 – 742Combined sources3
Beta strandi743 – 745Combined sources3
Helixi748 – 753Combined sources6
Turni754 – 757Combined sources4
Beta strandi764 – 767Combined sources4
Helixi771 – 779Combined sources9
Helixi789 – 802Combined sources14
Helixi809 – 811Combined sources3
Turni812 – 815Combined sources4
Beta strandi817 – 820Combined sources4
Beta strandi823 – 825Combined sources3
Helixi829 – 831Combined sources3
Helixi837 – 847Combined sources11
Beta strandi851 – 855Combined sources5
Beta strandi862 – 865Combined sources4
Helixi872 – 880Combined sources9
Beta strandi887 – 890Combined sources4
Helixi892 – 899Combined sources8
Helixi906 – 908Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49917.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini654 – 743BRCT 1PROSITE-ProRule annotationAdd BLAST90
Domaini808 – 911BRCT 2PROSITE-ProRule annotationAdd BLAST104

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0966. Eukaryota.
COG1793. LUCA.
GeneTreeiENSGT00860000133881.
HOGENOMiHOG000007831.
HOVERGENiHBG005516.
InParanoidiP49917.
KOiK10777.
OMAiIGEDHSR.
OrthoDBiEOG091G03K0.
PhylomeDBiP49917.
TreeFamiTF312980.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
Gene3Di1.10.3260.10. 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 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA58467 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti246F → S in CAA58467 (PubMed:7760816).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0293523A → V Associated with resistance to multiple myeloma. 1 PublicationCorresponds to variant rs1805389dbSNPEnsembl.1
Natural variantiVAR_0338849T → I Associated with resistance to multiple myeloma. 1 PublicationCorresponds to variant rs1805388dbSNPEnsembl.1
Natural variantiVAR_02935362D → H.Corresponds to variant rs3093763dbSNPEnsembl.1
Natural variantiVAR_018808231P → S.1 PublicationCorresponds to variant rs3093765dbSNPEnsembl.1
Natural variantiVAR_012774278R → H in LIG4S and leukemia; impairs activity. 3 PublicationsCorresponds to variant rs104894421dbSNPEnsembl.1
Natural variantiVAR_044123433Missing in RSSCID. 1 Publication1
Natural variantiVAR_044124461E → G.Corresponds to variant rs2232640dbSNPEnsembl.1
Natural variantiVAR_012775469G → E in LIG4S. 1 PublicationCorresponds to variant rs104894420dbSNPEnsembl.1
Natural variantiVAR_016771539L → F.Corresponds to variant rs3742212dbSNPEnsembl.1
Natural variantiVAR_016772658I → V.Corresponds to variant rs2232641dbSNPEnsembl.1
Natural variantiVAR_075826774L → P Found in a patient with microcephalic primordial dwarfism; unknown pathological significance. 1 Publication1
Natural variantiVAR_016773857A → T.1 PublicationCorresponds to variant rs2232642dbSNPEnsembl.1

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_001317524.1. NM_001330595.1.
NP_002303.2. NM_002312.3.
NP_996820.1. NM_206937.1.
XP_005254113.1. XM_005254056.1.
XP_005254114.1. XM_005254057.4.
XP_005254115.1. XM_005254058.3.
XP_006720014.1. XM_006719951.3.
XP_006720015.1. XM_006719952.1.
XP_011519393.1. XM_011521091.2.
XP_011519394.1. XM_011521092.2.
XP_016876058.1. XM_017020569.1.
XP_016876059.1. XM_017020570.1.
XP_016876060.1. XM_017020571.1.
XP_016876062.1. XM_017020573.1.
UniGeneiHs.166091.

Genome annotation databases

EnsembliENST00000356922; ENSP00000349393; ENSG00000174405.
ENST00000405925; ENSP00000385955; ENSG00000174405.
ENST00000442234; ENSP00000402030; ENSG00000174405.
ENST00000611712; ENSP00000484288; ENSG00000174405.
GeneIDi3981.
KEGGihsa:3981.
UCSCiuc001vqn.4. human.

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.
CCDSiCCDS9508.1.
PIRiI37079.
RefSeqiNP_001091738.1. NM_001098268.1.
NP_001317524.1. NM_001330595.1.
NP_002303.2. NM_002312.3.
NP_996820.1. NM_206937.1.
XP_005254113.1. XM_005254056.1.
XP_005254114.1. XM_005254057.4.
XP_005254115.1. XM_005254058.3.
XP_006720014.1. XM_006719951.3.
XP_006720015.1. XM_006719952.1.
XP_011519393.1. XM_011521091.2.
XP_011519394.1. XM_011521092.2.
XP_016876058.1. XM_017020569.1.
XP_016876059.1. XM_017020570.1.
XP_016876060.1. XM_017020571.1.
XP_016876062.1. XM_017020573.1.
UniGeneiHs.166091.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110169. 129 interactors.
DIPiDIP-37958N.
IntActiP49917. 11 interactors.
MINTiMINT-3018022.
STRINGi9606.ENSP00000349393.

PTM databases

iPTMnetiP49917.
PhosphoSitePlusiP49917.

Polymorphism and mutation databases

BioMutaiLIG4.
DMDMi88911290.

Proteomic databases

EPDiP49917.
MaxQBiP49917.
PaxDbiP49917.
PeptideAtlasiP49917.
PRIDEiP49917.

Protocols and materials databases

DNASUi3981.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356922; ENSP00000349393; ENSG00000174405.
ENST00000405925; ENSP00000385955; ENSG00000174405.
ENST00000442234; ENSP00000402030; ENSG00000174405.
ENST00000611712; ENSP00000484288; ENSG00000174405.
GeneIDi3981.
KEGGihsa:3981.
UCSCiuc001vqn.4. human.

Organism-specific databases

CTDi3981.
DisGeNETi3981.
GeneCardsiLIG4.
HGNCiHGNC:6601. LIG4.
HPAiHPA001334.
MalaCardsiLIG4.
MIMi601837. gene.
602450. phenotype.
606593. phenotype.
neXtProtiNX_P49917.
OpenTargetsiENSG00000174405.
Orphaneti235. Dubowitz syndrome.
99812. LIG4 syndrome.
39041. Omenn syndrome.
PharmGKBiPA30375.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0966. Eukaryota.
COG1793. LUCA.
GeneTreeiENSGT00860000133881.
HOGENOMiHOG000007831.
HOVERGENiHBG005516.
InParanoidiP49917.
KOiK10777.
OMAiIGEDHSR.
OrthoDBiEOG091G03K0.
PhylomeDBiP49917.
TreeFamiTF312980.

Enzyme and pathway databases

BioCyciZFISH:HS10794-MONOMER.
BRENDAi6.5.1.1. 2681.
ReactomeiR-HSA-164843. 2-LTR circle formation.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
SignaLinkiP49917.
SIGNORiP49917.

Miscellaneous databases

ChiTaRSiLIG4. human.
EvolutionaryTraceiP49917.
GeneWikiiLIG4.
GenomeRNAii3981.
PROiP49917.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000174405.
CleanExiHS_LIG4.
ExpressionAtlasiP49917. baseline and differential.
GenevisibleiP49917. HS.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
Gene3Di1.10.3260.10. 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]
ProtoNetiSearch...

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 30, 2016
This is version 189 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.