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Q8BTF7 (DNLI4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA nonhomologous 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 By similarity.

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 By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the ATP-dependent DNA ligase family.

Contains 2 BRCT domains.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA recombination
DNA repair
DNA replication
   Cellular componentNucleus
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA ligation

Inferred from direct assay PubMed 15194694. Source: MGI

DNA ligation involved in DNA recombination

Inferred from mutant phenotype PubMed 9823897. Source: MGI

DNA ligation involved in DNA repair

Inferred from mutant phenotype PubMed 9823897. Source: MGI

DNA repair

Inferred from mutant phenotype PubMed 11779495PubMed 21390131. Source: MGI

T cell differentiation in thymus

Inferred from mutant phenotype PubMed 10911993PubMed 9823897. Source: MGI

T cell receptor V(D)J recombination

Inferred from mutant phenotype PubMed 10911993. Source: MGI

V(D)J recombination

Inferred from direct assay PubMed 15194694. Source: MGI

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from mutant phenotype PubMed 15175260PubMed 17554302. Source: MGI

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from mutant phenotype PubMed 9875844PubMed 9889105. Source: MGI

chromosome organization

Inferred from genetic interaction PubMed 15175260. Source: MGI

double-strand break repair

Inferred from mutant phenotype PubMed 12531011PubMed 15175260PubMed 17554302. Source: MGI

double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype PubMed 10823907PubMed 16777961. Source: MGI

immunoglobulin V(D)J recombination

Inferred from mutant phenotype PubMed 9823897. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 10911993PubMed 16777961PubMed 9823897. Source: MGI

isotype switching

Inferred from mutant phenotype PubMed 17713479. Source: MGI

lagging strand elongation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 9875844. Source: MGI

neuron apoptotic process

Inferred from genetic interaction PubMed 11248063. Source: MGI

nucleotide-excision repair

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleotide-excision repair, DNA gap filling

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 10911993PubMed 9823897. Source: MGI

positive regulation of neurogenesis

Inferred from mutant phenotype PubMed 10716994PubMed 16777961PubMed 9875844. Source: MGI

pro-B cell differentiation

Inferred from mutant phenotype PubMed 10911993PubMed 9823897. Source: MGI

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from mutant phenotype PubMed 10911993PubMed 9823897. Source: MGI

response to ionizing radiation

Inferred from mutant phenotype PubMed 10823907PubMed 21390131. Source: MGI

single strand break repair

Inferred from electronic annotation. Source: Ensembl

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 17554302. Source: MGI

   Cellular_componentDNA ligase IV complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA-dependent protein kinase-DNA ligase 4 complex

Inferred from direct assay PubMed 15194694. Source: MGI

chromosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

condensed chromosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from electronic annotation. Source: Ensembl

nonhomologous end joining complex

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from direct assay PubMed 15194694. Source: MGI

DNA binding

Inferred from electronic annotation. Source: Ensembl

DNA ligase (ATP) activity

Inferred from direct assay PubMed 15194694. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 911911DNA ligase 4
PRO_0000059577

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

Experimental info

Sequence conflict2681F → L in BAC26747. Ref.1
Sequence conflict7581Y → C in BAE28333. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BTF7 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 20CDD0F6465355A2

FASTA911104,120
        10         20         30         40         50         60 
MASSQTSQTV AAHVPFADLC STLERIQKGK DRAEKIRHFK EFLDSWRKFH DALHKNRKDV 

        70         80         90        100        110        120 
TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP REGKDAQKLL NYRTPSGART 

       130        140        150        160        170        180 
DAGDFAMIAY FVLKPRCLQK GSLTIQQVNE LLDLVASNNS GKKKDLVKKS LLQLITQSSA 

       190        200        210        220        230        240 
LEQKWLIRMI IKDLKLGISQ QTIFSIFHND AVELHNVTTD LEKVCRQLHD PSVGLSDISI 

       250        260        270        280        290        300 
TLFSAFKPML AAVADVERVE KDMKQQSFYI ETKLDGERMQ MHKDGALYRY FSRNGYNYTD 

       310        320        330        340        350        360 
QFGESPQEGS LTPFIHNAFG TDVQACILDG EMMAYNPTTQ TFMQKGVKFD IKRMVEDSGL 

       370        380        390        400        410        420 
QTCYSVFDVL MVNKKKLGRE TLRKRYEILS STFTPIQGRI EIVQKTQAHT KKEVVDALND 

       430        440        450        460        470        480 
AIDKREEGIM VKHPLSIYKP DKRGEGWLKI KPEYVSGLMD ELDVLIVGGY WGKGSRGGMM 

       490        500        510        520        530        540 
SHFLCAVAET PPPGDRPSVF HTLCRVGSGY TMKELYDLGL KLAKYWKPFH KKSPPSSILC 

       550        560        570        580        590        600 
GTEKPEVYIE PQNSVIVQIK AAEIVPSDMY KTGSTLRFPR IEKIRDDKEW HECMTLGDLE 

       610        620        630        640        650        660 
QLRGKASGKL ATKHLHVGDD DEPREKRRKP ISKTKKAIRI IEHLKAPNLS NVNKVSNVFE 

       670        680        690        700        710        720 
DVEFCVMSGL DGYPKADLEN RIAEFGGYIV QNPGPDTYCV IAGSENVRVK NIISSDKNDV 

       730        740        750        760        770        780 
VKPEWLLECF KTKTCVPWQP RFMIHMCPST KQHFAREYDC YGDSYFVDTD LDQLKEVFLG 

       790        800        810        820        830        840 
IKPSEQQTPE EMAPVIADLE CRYSWDHSPL SMFRHYTIYL DLYAVINDLS SRIEATRLGI 

       850        860        870        880        890        900 
TALELRFHGA KVVSCLSEGV SHVIIGEDQR RVTDFKIFRR MLKKKFKILQ ESWVSDSVDK 

       910 
GELQEENQYL L 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK030029 mRNA. Translation: BAC26747.1.
AK148081 mRNA. Translation: BAE28333.1.
AC138397 Genomic DNA. No translation available.
CH466566 Genomic DNA. Translation: EDL22038.1.
CH466566 Genomic DNA. Translation: EDL22040.1.
RefSeqNP_795927.2. NM_176953.3.
UniGeneMm.80584.

3D structure databases

ProteinModelPortalQ8BTF7.
SMRQ8BTF7. Positions 6-605, 654-911.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BTF7.

Proteomic databases

PaxDbQ8BTF7.
PRIDEQ8BTF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000095476; ENSMUSP00000093130; ENSMUSG00000049717.
ENSMUST00000170033; ENSMUSP00000130807; ENSMUSG00000049717.
GeneID319583.
KEGGmmu:319583.
UCSCuc009kul.1. mouse.

Organism-specific databases

CTD3981.
MGIMGI:1335098. Lig4.

Phylogenomic databases

eggNOGCOG1793.
GeneTreeENSGT00750000117695.
HOGENOMHOG000007831.
HOVERGENHBG005516.
InParanoidQ8BTF7.
KOK10777.
OMAHMCPSTK.
OrthoDBEOG7BKCT2.
TreeFamTF312980.

Gene expression databases

CleanExMM_LIG4.
GenevestigatorQ8BTF7.

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

NextBio395028.
PROQ8BTF7.
SOURCESearch...

Entry information

Entry nameDNLI4_MOUSE
AccessionPrimary (citable) accession number: Q8BTF7
Secondary accession number(s): G3UWC4, Q3UG76
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot