Aplf
entrez
72103
canonical
uniprot
Q9D842
canonical
ensembl
ENSMUSG00000030051
resolver
ensp
ENSMUSP00000032130
resolver
ensp
ENSMUSP00000066232
resolver
genesymbol
Aplf
resolver
uniprot
Q8BZL5
resolver
uniprot
Q99LX6
resolver
uniprot_entry
APLF_MOUSE
resolver
uniprot_sec
Q8BZL5
resolver
uniprot_sec
Q99LX6
resolver
amino_acid_sequence
MPSDFFLQPLDGGPRVPVGPGQTVIGRGPLLGITDKRVSRRHAILEVVDSQLRIKPIHRNPCFYQSSEKSQHSPMETQVWSQLHPGDSFSLLLDKYAFRVFSAESEVEMECTLRNSQMLDEDDILSEMQKSPVVNLPDKTTGASQLQGSPEITKTKCPTIDPMSSSGECRAFSEHQPRPTQRKRILPAWMLAESLSDQSLSTPAEGGDKDVIQRSGKAGTCEDRTPGNTSWHGKKRLSPSGNSKSVSAEQDPGKKCRKADQEGPGVSSENVPESSSSNIVKDPDVDIVKTNKQKDGILIEELGEVSKHKAATKPTTNEEGESCARVQSKSPPEKSQGCHPESSSAPSSPDALHTDTADPVLGCSEESKVRRTACMYGANCYRRNPLHFQHFSHPGDSDYGEVHGTDEGVIGDRPECPYGASCYRKNPQHKMEYRHSALPARVALDEDDDDVGQPSDDEDEEDYEPTDEDSDWHPGKDDEEQEDVDELLKEAKSSLHLKH
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
FUNCTION: Histone chaperone involved in single-strand and double-strand DNA break repair (By similarity). Recruited to sites of DNA damage through interaction with branched poly-ADP-ribose chains, a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions (By similarity). Following recruitment to DNA damage sites, acts as a histone chaperone that mediates histone eviction during DNA repair and promotes recruitment of histone variant MACROH2A1 (PubMed:27875275). Also has a nuclease activity: displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro (By similarity). Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage (By similarity). Together with PARP3, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (PubMed:21211721). Also acts as a negative regulator of cell pluripotency by promoting histone exchange (PubMed:27875275). Required for the embryo implantation during the epithelial to mesenchymal transition in females (PubMed:33277378). {ECO:0000250|UniProtKB:Q8IW19, ECO:0000269|PubMed:21211721, ECO:0000269|PubMed:27875275, ECO:0000269|PubMed:33277378}.
uniprot
proteins
mass_dalton
54968
uniprot
proteins
post_translational_modification
PTM: Poly-ADP-ribosylated. In addition to binding non covalently poly-ADP-ribose via its PBZ-type zinc fingers, the protein is also covalently poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:Q8IW19}.; PTM: Phosphorylated in an ATM-dependent manner upon double-strand DNA break. {ECO:0000250|UniProtKB:Q8IW19}.
uniprot
proteins
protein_family
APLF family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21211721
uniprot
proteins
pubmed
27875275
uniprot
proteins
pubmed
33277378
uniprot
proteins
sequence_length
499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33277378}. Chromosome {ECO:0000250|UniProtKB:Q8IW19}. Cytoplasm, cytosol {ECO:0000269|PubMed:33277378}. Note=Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers. {ECO:0000250|UniProtKB:Q8IW19}.
uniprot
proteins