UniProt functional annotation for Q9Y294



	UniProt functional annotation for Q9Y294

UniProt code: Q9Y294.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {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}.

Subunit: Interacts with histone H3 (including both histone H3.1 and H3.3) and histone H4. Interacts with the CHAF1A, CHAF1B and RBBP4 subunits of the CAF-1 complex. Interacts with CABIN1, HAT1, HIRA, NASP, TAF1, TLK1, TLK2 and UBN1. Interacts with CDAN1. Found in a cytosolic complex with CDAN1, ASF1B, IPO4 and histones H3.1 and H4. Interacts with CREBBP. {ECO:0000269|PubMed:10759893, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12093919, ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14680630, ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15664198, ECO:0000269|PubMed:15840725, ECO:0000269|PubMed:16980972, ECO:0000269|PubMed:19029251, ECO:0000269|PubMed:22407294, ECO:0000269|PubMed:24616510}.

Subcellular location: Nucleus {ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12842904}.

Tissue specificity: Ubiquitously expressed. {ECO:0000269|PubMed:12842904}.

Ptm: Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser- 192 prevents proteasome-dependent degradation. {ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:20016786}.

Similarity: Belongs to the ASF1 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit. {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}.


Subunit:		Interacts with histone H3 (including both histone H3.1 and H3.3) and histone H4. Interacts with the CHAF1A, CHAF1B and RBBP4 subunits of the CAF-1 complex. Interacts with CABIN1, HAT1, HIRA, NASP, TAF1, TLK1, TLK2 and UBN1. Interacts with CDAN1. Found in a cytosolic complex with CDAN1, ASF1B, IPO4 and histones H3.1 and H4. Interacts with CREBBP. {ECO:0000269\|PubMed:10759893, ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:11897662, ECO:0000269\|PubMed:12093919, ECO:0000269\|PubMed:12842904, ECO:0000269\|PubMed:14680630, ECO:0000269\|PubMed:14718166, ECO:0000269\|PubMed:15621527, ECO:0000269\|PubMed:15664198, ECO:0000269\|PubMed:15840725, ECO:0000269\|PubMed:16980972, ECO:0000269\|PubMed:19029251, ECO:0000269\|PubMed:22407294, ECO:0000269\|PubMed:24616510}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:11897662, ECO:0000269\|PubMed:12842904}.
Tissue specificity:		Ubiquitously expressed. {ECO:0000269\|PubMed:12842904}.
Ptm:		Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser- 192 prevents proteasome-dependent degradation. {ECO:0000269\|PubMed:11470414, ECO:0000269\|PubMed:20016786}.
Similarity:		Belongs to the ASF1 family. {ECO:0000305}.