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P49917 (DNLI4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA ligase 4

EC=6.5.1.1
Alternative name(s):
DNA ligase IV
Polydeoxyribonucleotide synthase [ATP] 4
Gene names
Name:LIG4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8

Catalytic activity

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).

Cofactor

Magnesium By similarity.

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus.

Tissue specificity

Testis, thymus, prostate and heart.

Involvement in disease

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. Ref.16

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.

Sequence similarities

Belongs to the ATP-dependent DNA ligase family.

Contains 2 BRCT domains.

Sequence caution

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

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA recombination
DNA repair
DNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
SCID
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA ligation

Inferred from direct assay PubMed 12517771. Source: UniProtKB

DNA ligation involved in DNA recombination

Inferred from sequence or structural similarity. Source: UniProtKB

DNA ligation involved in DNA repair

Inferred from direct assay PubMed 12517771. Source: UniProtKB

DNA repair

Traceable author statement. Source: Reactome

T cell differentiation in thymus

Inferred from sequence or structural similarity. Source: UniProtKB

T cell receptor V(D)J recombination

Inferred from sequence or structural similarity. Source: UniProtKB

V(D)J recombination

Inferred from direct assay Ref.6. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Inferred from direct assay PubMed 9242410. Source: UniProtKB

double-strand break repair via nonhomologous end joining

Inferred from direct assay PubMed 12517771. Source: UniProtKB

establishment of integrated proviral latency

Traceable author statement. Source: Reactome

immunoglobulin V(D)J recombination

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from sequence or structural similarity. Source: UniProtKB

isotype switching

Inferred from sequence or structural similarity. Source: UniProtKB

lagging strand elongation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide-excision repair, DNA gap filling

Inferred from direct assay PubMed 12517771. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

pro-B cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

response to X-ray

Inferred from mutant phenotype Ref.6. Source: UniProtKB

response to gamma radiation

Inferred from sequence or structural similarity. Source: UniProtKB

single strand break repair

Inferred from direct assay Ref.5. Source: UniProtKB

somatic stem cell maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentDNA ligase IV complex

Inferred from mutant phenotype Ref.6. Source: UniProtKB

DNA-dependent protein kinase-DNA ligase 4 complex

Inferred from sequence or structural similarity. Source: UniProtKB

condensed chromosome

Inferred from direct assay PubMed 12589063. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

focal adhesion

Inferred from direct assay. Source: HPA

nonhomologous end joining complex

Inferred from direct assay PubMed 20383123. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12589063Ref.5. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from direct assay Ref.5. Source: UniProtKB

DNA ligase (ATP) activity

Inferred from direct assay Ref.5. Source: UniProtKB

DNA ligase activity

Inferred from direct assay PubMed 12517771. Source: UniProtKB

ligase activity

Inferred from direct assay PubMed 9242410. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction PubMed 12589063. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16439205Ref.10PubMed 9242410PubMed 9259651Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 911911DNA ligase 4
PRO_0000059576

Regions

Domain654 – 74390BRCT 1
Domain808 – 911104BRCT 2

Sites

Active site2731N6-AMP-lysine intermediate By similarity
Metal binding3311Magnesium 1 Potential
Metal binding4271Magnesium 2 Potential
Binding site2711ATP By similarity
Binding site2781ATP By similarity
Binding site2931ATP By similarity
Binding site4321ATP By similarity
Binding site4431ATP By similarity
Binding site4491ATP By similarity

Natural variations

Natural variant31A → V Associated with resistance to multiple myeloma. Ref.17
Corresponds to variant rs1805389 [ dbSNP | Ensembl ].
VAR_029352
Natural variant91T → I Associated with resistance to multiple myeloma. Ref.17
Corresponds to variant rs1805388 [ dbSNP | Ensembl ].
VAR_033884
Natural variant621D → H.
Corresponds to variant rs3093763 [ dbSNP | Ensembl ].
VAR_029353
Natural variant2311P → S. Ref.2
Corresponds to variant rs3093765 [ dbSNP | Ensembl ].
VAR_018808
Natural variant2781R → H in LIG4S and leukemia; impairs activity. Ref.14 Ref.15 Ref.16
VAR_012774
Natural variant4331Missing in RS-SCID. Ref.18
VAR_044123
Natural variant4611E → G.
Corresponds to variant rs2232640 [ dbSNP | Ensembl ].
VAR_044124
Natural variant4691G → E in LIG4S. Ref.16
VAR_012775
Natural variant5391L → F.
Corresponds to variant rs3742212 [ dbSNP | Ensembl ].
VAR_016771
Natural variant6581I → V.
Corresponds to variant rs2232641 [ dbSNP | Ensembl ].
VAR_016772
Natural variant8571A → T. Ref.2
Corresponds to variant rs2232642 [ dbSNP | Ensembl ].
VAR_016773

Experimental info

Sequence conflict2461F → S in CAA58467. Ref.1

Secondary structure

........................................................................................................................................................... 911
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49917 [UniParc].

Last modified February 7, 2006. Version 2.
Checksum: 2122813E1EFA63B9

FASTA911103,971
        10         20         30         40         50         60 
MAASQTSQTV ASHVPFADLC STLERIQKSK GRAEKIRHFR EFLDSWRKFH DALHKNHKDV 

        70         80         90        100        110        120 
TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP RDGKDALKLL NYRTPTGTHG 

       130        140        150        160        170        180 
DAGDFAMIAY FVLKPRCLQK GSLTIQQVND LLDSIASNNS AKRKDLIKKS LLQLITQSSA 

       190        200        210        220        230        240 
LEQKWLIRMI IKDLKLGVSQ QTIFSVFHND AAELHNVTTD LEKVCRQLHD PSVGLSDISI 

       250        260        270        280        290        300 
TLFSAFKPML AAIADIEHIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYKY FSRNGYNYTD 

       310        320        330        340        350        360 
QFGASPTEGS LTPFIHNAFK ADIQICILDG EMMAYNPNTQ TFMQKGTKFD IKRMVEDSDL 

       370        380        390        400        410        420 
QTCYCVFDVL MVNNKKLGHE TLRKRYEILS SIFTPIPGRI EIVQKTQAHT KNEVIDALNE 

       430        440        450        460        470        480 
AIDKREEGIM VKQPLSIYKP DKRGEGWLKI KPEYVSGLMD ELDILIVGGY WGKGSRGGMM 

       490        500        510        520        530        540 
SHFLCAVAEK PPPGEKPSVF HTLSRVGSGC TMKELYDLGL KLAKYWKPFH RKAPPSSILC 

       550        560        570        580        590        600 
GTEKPEVYIE PCNSVIVQIK AAEIVPSDMY KTGCTLRFPR IEKIRDDKEW HECMTLDDLE 

       610        620        630        640        650        660 
QLRGKASGKL ASKHLYIGGD DEPQEKKRKA APKMKKVIGI IEHLKAPNLT NVNKISNIFE 

       670        680        690        700        710        720 
DVEFCVMSGT DSQPKPDLEN RIAEFGGYIV QNPGPDTYCV IAGSENIRVK NIILSNKHDV 

       730        740        750        760        770        780 
VKPAWLLECF KTKSFVPWQP RFMIHMCPST KEHFAREYDC YGDSYFIDTD LNQLKEVFSG 

       790        800        810        820        830        840 
IKNSNEQTPE EMASLIADLE YRYSWDCSPL SMFRRHTVYL DSYAVINDLS TKNEGTRLAI 

       850        860        870        880        890        900 
KALELRFHGA KVVSCLAEGV SHVIIGEDHS RVADFKAFRR TFKRKFKILK ESWVTDSIDK 

       910 
CELQEENQYL I 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"DNA ligase IV from HeLa cell nuclei."
Robins P., Lindahl T.
J. Biol. Chem. 271:24257-24261(1996) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Crystal structure of an Xrcc4-DNA ligase IV complex."
Sibanda B.L., Critchlow S.E., Begun J., Pei X.Y., Jackson S.P., Blundell T.L., Pellegrini L.
Nat. Struct. Biol. 8:1015-1019(2001) [PubMed] [Europe PMC] [Abstract]
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]"Identification of a defect in DNA ligase IV in a radiosensitive leukaemia patient."
Riballo E., Critchlow S.E., Teo S.-H., Doherty A.J., Priestley A., Broughton B.C., Kysela B., Beamish H., Plowman N., Arlett C.F., Lehmann A.R., Jackson S.P., Jeggo P.A.
Curr. Biol. 9:699-702(1999) [PubMed] [Europe PMC] [Abstract]
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]"DNA ligase IV mutations identified in patients exhibiting developmental delay and immunodeficiency."
O'Driscoll M., Cerosaletti K.M., Girard P.-M., Dai Y., Stumm M., Kysela B., Hirsch B., Gennery A., Palmer S.E., Seidel J., Gatti R.A., Varon R., Oettinger M.A., Neitzel H., Jeggo P.A., Concannon P.
Mol. Cell 8:1175-1185(2001) [PubMed] [Europe PMC] [Abstract]
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]"A new type of radiosensitive T-B-NK(+) severe combined immunodeficiency caused by a LIG4 mutation."
van der Burg M., van Veelen L.R., Verkaik N.S., Wiegant W.W., Hartwig N.G., Barendregt B.H., Brugmans L., Raams A., Jaspers N.G.J., Zdzienicka M.Z., van Dongen J.J.M., van Gent D.C.
J. Clin. Invest. 116:137-145(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RS-SCID GLN-433 DEL.
+Additional computationally mapped references.

Web resources

LIG4base

LIG4 mutation db

NIEHS-SNPs
Wikipedia

DNA ligase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9508.1.
PIRI37079.
RefSeqNP_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.
UniGeneHs.166091.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP49917.
SMRP49917. Positions 6-605, 654-911.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110169. 128 interactions.
DIPDIP-37958N.
IntActP49917. 7 interactions.
MINTMINT-3018022.
STRING9606.ENSP00000349393.

PTM databases

PhosphoSiteP49917.

Polymorphism databases

DMDM88911290.

Proteomic databases

MaxQBP49917.
PaxDbP49917.
PRIDEP49917.

Protocols and materials databases

DNASU3981.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356922; ENSP00000349393; ENSG00000174405.
ENST00000405925; ENSP00000385955; ENSG00000174405.
ENST00000442234; ENSP00000402030; ENSG00000174405.
GeneID3981.
KEGGhsa:3981.
UCSCuc001vqn.3. human.

Organism-specific databases

CTD3981.
GeneCardsGC13M108859.
HGNCHGNC:6601. LIG4.
HPAHPA001334.
MIM601837. gene.
602450. phenotype.
606593. phenotype.
neXtProtNX_P49917.
Orphanet99812. LIG4 syndrome.
39041. Omenn syndrome.
PharmGKBPA30375.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1793.
HOGENOMHOG000007831.
HOVERGENHBG005516.
InParanoidP49917.
KOK10777.
OMAHMCPSTK.
OrthoDBEOG7BKCT2.
PhylomeDBP49917.
TreeFamTF312980.

Enzyme and pathway databases

BRENDA6.5.1.1. 2681.
ReactomeREACT_116125. Disease.
REACT_216. DNA Repair.
SignaLinkP49917.

Gene expression databases

BgeeP49917.
CleanExHS_LIG4.
GenevestigatorP49917.

Family and domain databases

Gene3D1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
3.40.50.10190. 2 hits.
InterProIPR001357. 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.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF00533. 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]
SMARTSM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF52113. SSF52113. 2 hits.
TIGRFAMsTIGR00574. dnl1. 1 hit.
PROSITEPS50172. BRCT. 2 hits.
PS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLIG4. human.
EvolutionaryTraceP49917.
GeneWikiLIG4.
GenomeRNAi3981.
NextBio15604.
PROP49917.
SOURCESearch...

Entry information

Entry nameDNLI4_HUMAN
AccessionPrimary (citable) accession number: P49917
Secondary accession number(s): Q8IY66, Q8TEU5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

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Human chromosome 13

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