ASF1A
entrez
25842
canonical
uniprot
Q9Y294
canonical
ensembl
ENSG00000111875
resolver
ensp
ENSP00000229595
resolver
enst
ENST00000229595
resolver
genesymbol
ASF1A
resolver
hgnc
HGNC:20995
resolver
uniprot
Q6IA08
resolver
uniprot
Q9P014
resolver
uniprot_entry
ASF1A_HUMAN
resolver
uniprot_sec
Q6IA08
resolver
uniprot_sec
Q9P014
resolver
amino_acid_sequence
MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM
uniprot
proteins
function
FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:10759893, PubMed:11897662, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:16151251, PubMed:21454524). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198). Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51 (PubMed:29478807). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol (PubMed:21454524, PubMed:29408485). Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit (PubMed:15621527). {ECO:0000269|PubMed:10759893, ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15664198, ECO:0000269|PubMed:16151251, ECO:0000269|PubMed:21454524, ECO:0000269|PubMed:29408485, ECO:0000269|PubMed:29478807}.
uniprot
proteins
mass_dalton
22969
uniprot
proteins
mutagenesis
MUTAGEN 36..37; /note="ED->AA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci."; /evidence="ECO:0000269|PubMed:14680630, ECO:0000269|PubMed:15621527"; MUTAGEN 37; /note="D->A: Abrogates interaction with CHAF1B and HIRA."; /evidence="ECO:0000269|PubMed:16980972"; MUTAGEN 49; /note="E->A: Loss of interaction with TLK2."; /evidence="ECO:0000269|PubMed:35136069"; MUTAGEN 54; /note="D->R: Reduces interaction with histone H3."; /evidence="ECO:0000269|PubMed:15840725"; MUTAGEN 62..64; /note="VGP->AAA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci."; /evidence="ECO:0000269|PubMed:14680630, ECO:0000269|PubMed:15621527"; MUTAGEN 88; /note="D->A: Loss of interaction with TLK2. Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:35136069"; MUTAGEN 94; /note="V->R: Abrogates interaction with histone H3 and histone H4. Loss of interaction with TLK2. Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:15840725, ECO:0000269|PubMed:29478807, ECO:0000269|PubMed:35136069"; MUTAGEN 108; /note="R->E: Reduces interaction with histone H3."; /evidence="ECO:0000269|PubMed:15840725"; MUTAGEN 166; /note="S->A: Does not affect phosphorylation in response to DNA damage."; /evidence="ECO:0000269|PubMed:29478807"; MUTAGEN 175; /note="S->A: Does not affect phosphorylation in response to DNA damage."; /evidence="ECO:0000269|PubMed:29478807"; MUTAGEN 192; /note="S->A: Abolished phosphorylation in response to DNA damage."; /evidence="ECO:0000269|PubMed:29478807"; MUTAGEN 192; /note="S->D: Mimics phosphorylation; promoting recruitment to chromatin in response to DNA damage."; /evidence="ECO:0000269|PubMed:29478807
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by TLK1 and TLK2 (PubMed:11470414, PubMed:20016786, PubMed:35136069). Highly phosphorylated in S-phase and at lower levels in M-phase (PubMed:11470414). TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation (PubMed:20016786). Phosphorylation at Ser-192 by PRKDC in response to DNA damage promotes the histone chaperone activity and ability to replace histones at double-strand breaks (DSBs) at stalled or collapsed replication forks, leading to RAD51 recruitment (PubMed:29478807). {ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:20016786, ECO:0000269|PubMed:29478807, ECO:0000269|PubMed:35136069}.
uniprot
proteins
protein_family
ASF1 family
uniprot
proteins
pubmed
10759893
uniprot
proteins
pubmed
10810093
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11470414
uniprot
proteins
pubmed
11897662
uniprot
proteins
pubmed
12093919
uniprot
proteins
pubmed
12842904
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14680630
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14718166
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15621527
uniprot
proteins
pubmed
15664198
uniprot
proteins
pubmed
15840725
uniprot
proteins
pubmed
16151251
uniprot
proteins
pubmed
16980972
uniprot
proteins
pubmed
17292837
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19029251
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20016786
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21454524
uniprot
proteins
pubmed
22195965
uniprot
proteins
pubmed
22407294
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24616510
uniprot
proteins
pubmed
29408485
uniprot
proteins
pubmed
29478807
uniprot
proteins
pubmed
33857403
uniprot
proteins
pubmed
35136069
uniprot
proteins
sequence_length
204
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12842904}. Chromosome {ECO:0000269|PubMed:29478807}.
uniprot
proteins