about
P688
Phosphorylation and regulation of DNA ligase IV stability by DNA-dependent protein kinaseThe transposase domain protein Metnase/SETMAR suppresses chromosomal translocationsDNA ligase III is critical for mtDNA integrity but not Xrcc1-mediated nuclear DNA repairThe nonhomologous end-joining pathway of DNA repair is required for genomic stability and the suppression of translocationsIgH class switching and translocations use a robust non-classical end-joining pathwayA critical role for DNA end-joining proteins in both lymphogenesis and neurogenesisLate embryonic lethality and impaired V(D)J recombination in mice lacking DNA ligase IVDefective embryonic neurogenesis in Ku-deficient but not DNA-dependent protein kinase catalytic subunit-deficient miceImpaired nonhomologous end-joining provokes soft tissue sarcomas harboring chromosomal translocations, amplifications, and deletionsThe embryonic lethality in DNA ligase IV-deficient mice is rescued by deletion of Ku: implications for unifying the heterogeneous phenotypes of NHEJ mutantsDNA ligase IV deficiency in mice leads to defective neurogenesis and embryonic lethality via the p53 pathwayRad54 and DNA Ligase IV cooperate to maintain mammalian chromatid stabilityDNA processing is not required for ATM-mediated telomere damage response after TRF2 deletionDNA repair is limiting for haematopoietic stem cells during ageingDNA ligase IV-dependent NHEJ of deprotected mammalian telomeres in G1 and G2Targeted disruption of the gene encoding DNA ligase IV leads to lethality in embryonic miceGenetic interactions between ATM and the nonhomologous end-joining factors in genomic stability and developmentSelective utilization of nonhomologous end-joining and homologous recombination DNA repair pathways during nervous system development
P921
Q24296672-02E061DC-1C2E-4107-9151-D3465D1CEF5AQ24338398-2482485F-45F2-4A1F-920E-23D309AA1C9FQ24612486-3C12BDD1-1C5D-48D1-B185-C651F4019CD0Q24685574-849528CE-A811-4C0E-A2F4-E9653D9FD1E8Q28241679-509E1A6F-0048-4EB4-A7F9-C130388AC18FQ28292871-DB3D9B72-D624-4AAD-8587-A2AAFC71EEF8Q28504490-FC27E60A-7BD4-4E12-AA65-00E43F0DADADQ28504593-7ACAF90D-7018-41DE-853A-7A6FB44A74E3Q28505083-3476F982-A76D-42C0-A948-9B762DBEF6F3Q28506030-782B9355-471D-4D87-A1CC-DFC3874E47A1Q28506076-06E1FA14-341A-4AE3-B525-D38B505B03FCQ28506612-A8ED4226-751B-4D4E-A189-CCB8F4661E84Q28507823-DC25BA6C-89F7-420C-82D5-4520968D0BA4Q28509105-698437A7-DB1C-4F91-96AE-F9AAAED606F0Q28509254-6AFAF02A-0C8B-412C-9C01-8F5D3AD64F3DQ28510493-047DCCFA-C872-4795-8A2A-172790643DD7Q28512255-B61B6F55-1D35-485E-B431-B00EF119EAB5Q28585656-1441CECB-214C-4A68-B3B1-815F12568498
P921
description
mammalian protein found in Mus musculus
@en
protein
@id
proteinë
@sq
proteïne in Ligase IV, DNA, ATP-dependent
@nl
protèin
@ace
بروتين في فأر المنازل
@ar
name
Ligase IV, DNA, ATP-dependent
@en
Ligase IV, DNA, ATP-dependent
@nl
type
label
Ligase IV, DNA, ATP-dependent
@en
Ligase IV, DNA, ATP-dependent
@nl
altLabel
DNA ligase 4
@en
DNA ligase IV
@en
Lig4
@en
polydeoxyribonucleotide synthase [ATP] 4
@en
prefLabel
Ligase IV, DNA, ATP-dependent
@en
Ligase IV, DNA, ATP-dependent
@nl
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ENSMUSP00000093130
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