APLF
entrez
200558
canonical
uniprot
Q8IW19
canonical
ensembl
ENSG00000169621
resolver
ensp
ENSP00000307004
resolver
enst
ENST00000303795
resolver
genesymbol
APLF
resolver
genesymbol_syn
C2orf13
resolver
genesymbol_syn
PALF
resolver
genesymbol_syn
XIP1
resolver
hgnc
HGNC:28724
resolver
uniprot
A8K476
resolver
uniprot
Q53P47
resolver
uniprot
Q53PB9
resolver
uniprot
Q53QU0
resolver
uniprot_entry
APLF_HUMAN
resolver
uniprot_sec
A8K476
resolver
uniprot_sec
Q53P47
resolver
uniprot_sec
Q53PB9
resolver
uniprot_sec
Q53QU0
resolver
amino_acid_sequence
MSGGFELQPRDGGPRVALAPGETVIGRGPLLGITDKRVSRRHAILEVAGGQLRIKPIHTNPCFYQSSEKSQLLPLKPNLWCYLNPGDSFSLLVDKYIFRILSIPSEVEMQCTLRNSQVLDEDNILNETPKSPVINLPHETTGASQLEGSTEIAKTQMTPTNSVSFLGENRDCNKQQPILAERKRILPTWMLAEHLSDQNLSVPAISGGNVIQGSGKEEICKDKSQLNTTQQGRRQLISSGSSENTSAEQDTGEECKNTDQEESTISSKEMPQSFSAITLSNTEMNNIKTNAQRNKLPIEELGKVSKHKIATKRTPHKEDEAMSCSENCSSAQGDSLQDESQGSHSESSSNPSNPETLHAKATDSVLQGSEGNKVKRTSCMYGANCYRKNPVHFQHFSHPGDSDYGGVQIVGQDETDDRPECPYGPSCYRKNPQHKIEYRHNTLPVRNVLDEDNDNVGQPNEYDLNDSFLDDEEEDYEPTDEDSDWEPGKEDEEKEDVEELLKEAKRFMKRK
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
FUNCTION: Histone chaperone involved in single-strand and double-strand DNA break repair (PubMed:17353262, PubMed:17396150, PubMed:21211721, PubMed:21211722, PubMed:29905837, PubMed:30104678). 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 (PubMed:17353262, PubMed:17396150, PubMed:21211721, PubMed:30104678). 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:21211722, PubMed:29905837, PubMed:30104678). Also has a nuclease activity: displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro (PubMed:17353262, PubMed:17396150). Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage (PubMed:17353262, PubMed:17396150). 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, PubMed:23689425). Also acts as a negative regulator of cell pluripotency by promoting histone exchange (By similarity). Required for the embryo implantation during the epithelial to mesenchymal transition in females (By similarity). {ECO:0000250|UniProtKB:Q9D842, ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:21211721, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:23689425, ECO:0000269|PubMed:29905837, ECO:0000269|PubMed:30104678}.
uniprot
proteins
mass_dalton
56956
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="R->A: Does not affect interaction with XRCC5 and XRCC6; decreased ability to promote non-homologous end-joining (NHEJ)."; /evidence="ECO:0000269|PubMed:23689425"; MUTAGEN 116; /note="S->A: Decreases phosphorylation by ATM."; /evidence="ECO:0000269|PubMed:17507382"; MUTAGEN 182..184; /note="RKR->AKA: Abolished interaction with XRCC5 and XRCC6."; /evidence="ECO:0000269|PubMed:23689425"; MUTAGEN 182; /note="R->A: Reduced interaction with XRCC5 and XRCC6; impaired localization to the nucleus."; /evidence="ECO:0000269|PubMed:23689425"; MUTAGEN 184; /note="R->A: Abolished interaction with XRCC5 and XRCC6; impaired localization to the nucleus."; /evidence="ECO:0000269|PubMed:23689425"; MUTAGEN 189..191; /note="WML->AAA: Abolished interaction with XRCC5 and XRCC6."; /evidence="ECO:0000269|PubMed:23689425"; MUTAGEN 189; /note="W->A: Abolished interaction with XRCC5 and XRCC6; impaired localization to the nucleus; decreased ability to promote non-homologous end-joining (NHEJ)."; /evidence="ECO:0000269|PubMed:23689425"; MUTAGEN 190; /note="M->A: Reduced interaction with XRCC5 and XRCC6."; /evidence="ECO:0000269|PubMed:23689425"; MUTAGEN 191; /note="L->A: Does not affect interaction with XRCC5 and XRCC6."; /evidence="ECO:0000269|PubMed:23689425"; MUTAGEN 376; /note="R->A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-421 and A-427. Does not affect histone chaperone activity; when associated with A-421 and A-427."; /evidence="ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:21211722"; MUTAGEN 379; /note="C->A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-385; A-421 and A-427. Does not affect histone chaperone activity; when associated with A-385; A-421 and A-427."; /evidence="ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:21211722"; MUTAGEN 385; /note="C->A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-421 and A-427. Does not affect histone chaperone activity; when associated with A-379; A-421 and A-427."; /evidence="ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:21211722"; MUTAGEN 421; /note="C->A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-385 and A-427. Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-376 and A-427. Does not affect histone chaperone activity; when associated with A-376 and A-427."; /evidence="ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:21211722"; MUTAGEN 427; /note="C->A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-385 and A-421. Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-376 and A-421. Does not affect histone chaperone activity; when associated with A-376 and A-421."; /evidence="ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:21211722"; MUTAGEN 477; /note="E->A: Impaired binding to histones and ability to mediate histone chaperone activity."; /evidence="ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837"; MUTAGEN 485; /note="W->A: Impaired binding to histones and ability to mediate histone chaperone activity."; /evidence="ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837
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:0000269|PubMed:17396150, ECO:0000269|PubMed:18172500}.; PTM: Phosphorylated in an ATM-dependent manner upon double-strand DNA break. {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17507382, ECO:0000269|PubMed:18077224}.
uniprot
proteins
protein_family
APLF family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17353262
uniprot
proteins
pubmed
17396150
uniprot
proteins
pubmed
17507382
uniprot
proteins
pubmed
18077224
uniprot
proteins
pubmed
18172500
uniprot
proteins
pubmed
18474613
uniprot
proteins
pubmed
20098424
uniprot
proteins
pubmed
20439749
uniprot
proteins
pubmed
21211721
uniprot
proteins
pubmed
21211722
uniprot
proteins
pubmed
23689425
uniprot
proteins
pubmed
27063109
uniprot
proteins
pubmed
29905837
uniprot
proteins
pubmed
30104678
uniprot
proteins
pubmed
31733588
uniprot
proteins
sequence_length
511
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:17507382, ECO:0000269|PubMed:23689425}. Chromosome {ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:18474613, ECO:0000269|PubMed:21211721, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:23689425, ECO:0000269|PubMed:27063109}. Cytoplasm, cytosol {ECO:0000269|PubMed:17353262}. Note=Localizes to DNA damage sites (PubMed:18172500, PubMed:18474613, PubMed:21211721, PubMed:21211722, PubMed:23689425). Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers (PubMed:18172500). {ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:18474613, ECO:0000269|PubMed:21211721, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:23689425}.
uniprot
proteins