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Database: UniProt/SWISS-PROT
Entry: DNLI4_MOUSE
LinkDB: DNLI4_MOUSE
Original site: DNLI4_MOUSE 
ID   DNLI4_MOUSE             Reviewed;         911 AA.
AC   Q8BTF7; G3UWC4; Q3UG76;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   28-FEB-2018, entry version 130.
DE   RecName: Full=DNA ligase 4;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase IV;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=Lig4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Efficiently joins single-strand breaks in a double-
CC       stranded polydeoxynucleotide in an ATP-dependent reaction.
CC       Involved in DNA nonhomologous end joining (NHEJ) required for
CC       double-strand break repair and V(D)J recombination. The LIG4-XRCC4
CC       complex is responsible for the NHEJ ligation step, and XRCC4
CC       enhances the joining activity of LIG4. Binding of the LIG4-XRCC4
CC       complex to DNA ends is dependent on the assembly of the DNA-
CC       dependent protein kinase complex DNA-PK to these DNA ends.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with XRCC4. The LIG4-XRCC4 complex has probably
CC       a 1:2 stoichiometry. The LIG4-XRCC4 complex associates in a DNA-
CC       dependent manner with the DNA-PK complex composed of PRKDC,
CC       XRCC6/Ku70 and XRCC5/Ku86 to form the core non-homologous end
CC       joining (NHEJ) complex. Additional components of the NHEJ complex
CC       include NHEJ1/XLF and PAXX. Interacts with APLF.
CC       {ECO:0000250|UniProtKB:P49917}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; AK030029; BAC26747.1; -; mRNA.
DR   EMBL; AK148081; BAE28333.1; -; mRNA.
DR   EMBL; AC138397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466566; EDL22038.1; -; Genomic_DNA.
DR   EMBL; CH466566; EDL22040.1; -; Genomic_DNA.
DR   CCDS; CCDS22092.1; -.
DR   RefSeq; NP_795927.2; NM_176953.3.
DR   RefSeq; XP_017168343.1; XM_017312854.1.
DR   UniGene; Mm.80584; -.
DR   ProteinModelPortal; Q8BTF7; -.
DR   SMR; Q8BTF7; -.
DR   BioGrid; 235376; 2.
DR   CORUM; Q8BTF7; -.
DR   STRING; 10090.ENSMUSP00000093130; -.
DR   iPTMnet; Q8BTF7; -.
DR   PhosphoSitePlus; Q8BTF7; -.
DR   MaxQB; Q8BTF7; -.
DR   PaxDb; Q8BTF7; -.
DR   PRIDE; Q8BTF7; -.
DR   Ensembl; ENSMUST00000095476; ENSMUSP00000093130; ENSMUSG00000049717.
DR   Ensembl; ENSMUST00000170033; ENSMUSP00000130807; ENSMUSG00000049717.
DR   GeneID; 319583; -.
DR   KEGG; mmu:319583; -.
DR   UCSC; uc009kul.1; mouse.
DR   CTD; 3981; -.
DR   MGI; MGI:1335098; Lig4.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   GeneTree; ENSGT00860000133881; -.
DR   HOGENOM; HOG000007831; -.
DR   HOVERGEN; HBG005516; -.
DR   InParanoid; Q8BTF7; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG091G03K0; -.
DR   TreeFam; TF312980; -.
DR   Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR   PRO; PR:Q8BTF7; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000049717; -.
DR   CleanEx; MM_LIG4; -.
DR   Genevisible; Q8BTF7; MM.
DR   GO; GO:0000793; C:condensed chromosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR   GO; GO:0032807; C:DNA ligase IV complex; ISO:MGI.
DR   GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IDA:MGI.
DR   GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; ISO:MGI.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IDA:MGI.
DR   GO; GO:0003909; F:DNA ligase activity; ISO:MGI.
DR   GO; GO:0016874; F:ligase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0051276; P:chromosome organization; IGI:MGI.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006266; P:DNA ligation; IDA:MGI.
DR   GO; GO:0051102; P:DNA ligation involved in DNA recombination; IMP:MGI.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; IMP:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR   GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; ISO:MGI.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:BHF-UCL.
DR   GO; GO:0033152; P:immunoglobulin V(D)J recombination; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045190; P:isotype switching; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; ISO:MGI.
DR   GO; GO:2001252; P:positive regulation of chromosome organization; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IMP:MGI.
DR   GO; GO:0002328; P:pro-B cell differentiation; IMP:MGI.
DR   GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR   GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR   GO; GO:0010165; P:response to X-ray; ISO:MGI.
DR   GO; GO:0000012; P:single strand break repair; ISO:MGI.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0033153; P:T cell receptor V(D)J recombination; IMP:MGI.
DR   GO; GO:0033151; P:V(D)J recombination; IDA:MGI.
DR   CDD; cd00027; BRCT; 2.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR021536; DNA_ligase_IV_dom.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF7; PTHR10459:SF7; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   Pfam; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN         1    911       DNA ligase 4.
FT                                /FTId=PRO_0000059577.
FT   DOMAIN      654    743       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      808    911       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    273    273       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       331    331       Magnesium 1. {ECO:0000255}.
FT   METAL       427    427       Magnesium 2. {ECO:0000255}.
FT   BINDING     271    271       ATP. {ECO:0000250}.
FT   BINDING     278    278       ATP. {ECO:0000250}.
FT   BINDING     293    293       ATP. {ECO:0000250}.
FT   BINDING     432    432       ATP. {ECO:0000250}.
FT   BINDING     443    443       ATP. {ECO:0000250}.
FT   BINDING     449    449       ATP. {ECO:0000250}.
FT   CONFLICT    268    268       F -> L (in Ref. 1; BAC26747).
FT                                {ECO:0000305}.
FT   CONFLICT    758    758       Y -> C (in Ref. 1; BAE28333).
FT                                {ECO:0000305}.
SQ   SEQUENCE   911 AA;  104120 MW;  20CDD0F6465355A2 CRC64;
     MASSQTSQTV AAHVPFADLC STLERIQKGK DRAEKIRHFK EFLDSWRKFH DALHKNRKDV
     TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP REGKDAQKLL NYRTPSGART
     DAGDFAMIAY FVLKPRCLQK GSLTIQQVNE LLDLVASNNS GKKKDLVKKS LLQLITQSSA
     LEQKWLIRMI IKDLKLGISQ QTIFSIFHND AVELHNVTTD LEKVCRQLHD PSVGLSDISI
     TLFSAFKPML AAVADVERVE KDMKQQSFYI ETKLDGERMQ MHKDGALYRY FSRNGYNYTD
     QFGESPQEGS LTPFIHNAFG TDVQACILDG EMMAYNPTTQ TFMQKGVKFD IKRMVEDSGL
     QTCYSVFDVL MVNKKKLGRE TLRKRYEILS STFTPIQGRI EIVQKTQAHT KKEVVDALND
     AIDKREEGIM VKHPLSIYKP DKRGEGWLKI KPEYVSGLMD ELDVLIVGGY WGKGSRGGMM
     SHFLCAVAET PPPGDRPSVF HTLCRVGSGY TMKELYDLGL KLAKYWKPFH KKSPPSSILC
     GTEKPEVYIE PQNSVIVQIK AAEIVPSDMY KTGSTLRFPR IEKIRDDKEW HECMTLGDLE
     QLRGKASGKL ATKHLHVGDD DEPREKRRKP ISKTKKAIRI IEHLKAPNLS NVNKVSNVFE
     DVEFCVMSGL DGYPKADLEN RIAEFGGYIV QNPGPDTYCV IAGSENVRVK NIISSDKNDV
     VKPEWLLECF KTKTCVPWQP RFMIHMCPST KQHFAREYDC YGDSYFVDTD LDQLKEVFLG
     IKPSEQQTPE EMAPVIADLE CRYSWDHSPL SMFRHYTIYL DLYAVINDLS SRIEATRLGI
     TALELRFHGA KVVSCLSEGV SHVIIGEDQR RVTDFKIFRR MLKKKFKILQ ESWVSDSVDK
     GELQEENQYL L
//
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