Reviewed, UniProtKB/Swiss-Prot Q8BTF7 (DNLI4_MOUSE)

Names and origin

Protein names

Recommended name:
    DNA ligase 4
    EC=6.5.1.1
Alternative name(s):
    DNA ligase IV
    Polydeoxyribonucleotide synthase [ATP] 4

Gene names

Name:

Lig4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	911 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 By similarity.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the ATP-dependent DNA ligase family. Contains 2 BRCT domains.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA recombination DNA repair DNA replication
Cellular component	Nucleus
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	DNA ligation during DNA recombination Inferred from mutant phenotype. Source: MGI DNA ligation during DNA repair Inferred from mutant phenotype. Source: MGI DNA replication Inferred from electronic annotation. Source: UniProtKB-KW T cell differentiation in the thymus Inferred from mutant phenotype. Source: MGI T cell receptor V(D)J recombination Inferred from mutant phenotype. 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. Source: MGI central nervous system development Inferred from mutant phenotype. Source: MGI chromosome organization Inferred from genetic interaction. Source: MGI double-strand break repair via nonhomologous end joining Inferred from mutant phenotype. Source: MGI immunoglobulin V(D)J recombination Inferred from mutant phenotype. Source: MGI in utero embryonic development Inferred from mutant phenotype. Source: MGI isotype switching Inferred from mutant phenotype. Source: MGI negative regulation of neuron apoptosis Inferred from mutant phenotype. Source: MGI neuron apoptosis Inferred from genetic interaction. Source: MGI positive regulation of fibroblast proliferation Inferred from mutant phenotype. Source: MGI positive regulation of neurogenesis Inferred from mutant phenotype. Source: MGI pro-B cell differentiation Inferred from mutant phenotype. Source: MGI response to gamma radiation Inferred from mutant phenotype. Source: MGI somatic stem cell maintenance Inferred from mutant phenotype. Source: MGI
Cellular component	DNA-dependent protein kinase-DNA ligase 4 complex Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from direct assay. Source: MGI DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (ATP) activity Inferred from direct assay. Source: MGI magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 911	911	DNA ligase 4		PRO_0000059577
Regions
	Domain	654 – 743	90	BRCT 1
	Domain	808 – 911	104	BRCT 2
Sites
	Active site	273	1	N6-AMP-lysine intermediate By similarity
	Metal binding	331	1	Magnesium 1 Potential
	Metal binding	427	1	Magnesium 2 Potential
	Binding site	271	1	ATP By similarity
	Binding site	278	1	ATP By similarity
	Binding site	293	1	ATP By similarity
	Binding site	432	1	ATP By similarity
	Binding site	443	1	ATP By similarity
	Binding site	449	1	ATP By similarity
Experimental info
	Sequence conflict	268	1	L → F in BAE28333. Ref.1
	Sequence conflict	758	1	Y → C in BAE28333. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BTF7-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: A2CE39D521393BE8	FASTA	911	104,086
	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 KDMKQQSLYI 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

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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK030029 mRNA. Translation: BAC26747.1. AK148081 mRNA. Translation: BAE28333.1.
IPI	IPI00225019.
UniGene	Mm.80584
3D structure databases
HSSP	HSSP built from PDB template 1IK9 based on UniProtKB P49917.
SMR	Q8BTF7. Positions 654-759.
ModBase	Search...
PTM databases
PhosphoSite	Q8BTF7.
Proteomic databases
PRIDE	Q8BTF7.
Genome annotation databases
Ensembl	ENSMUSG00000049717. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:1335098. Lig4.
Phylogenomic databases
HOGENOM	Q8BTF7.
HOVERGEN	Q8BTF7.
Enzyme and pathway databases
BRENDA	6.5.1.1. 244.
Gene expression databases
ArrayExpress	Q8BTF7.
Bgee	Q8BTF7.
CleanEx	MM_LIG4.
GermOnline	ENSMUSG00000049717. Mus musculus.
Family and domain databases
InterPro	IPR001357. BRCT. IPR000977. DNA_ligase. IPR012309. DNA_ligase_A_C. IPR012310. DNA_ligase_A_M. IPR012308. DNA_ligase_A_N. IPR016059. DNA_ligase_CS. IPR012340. NA-bd_OB-fold. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	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. [Graphical view]
SMART	SM00292. BRCT. 2 hits. [Graphical view]
TIGRFAMs	TIGR00574. dnl1. 1 hit.
PROSITE	PS50172. BRCT. 2 hits. PS00697. DNA_LIGASE_A1. 1 hit. PS00333. DNA_LIGASE_A2. 1 hit. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

DNLI4_MOUSE

Accession

Primary (citable) accession number: Q8BTF7
Secondary accession number(s): Q3UG76

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)