ID   ASF1B_BOVIN             Reviewed;         202 AA.
AC   Q17QJ0;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Histone chaperone ASF1B {ECO:0000305};
DE   AltName: Full=Anti-silencing function protein 1 homolog B;
GN   Name=ASF1B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC       histone exchange and removal during nucleosome assembly and
CC       disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to
CC       promote replication-dependent chromatin assembly. Also involved in the
CC       nuclear import of the histone H3-H4 dimer together with importin-4
CC       (IPO4): specifically recognizes and binds newly synthesized histones
CC       with the monomethylation of H3 'Lys-9' (H3K9me1) and diacetylation at
CC       'Lys-5' and 'Lys-12' of H4 (H4K5ac and H4K12ac) marks in the cytosol.
CC       Does not participate in replication-independent nucleosome deposition
CC       which is mediated by ASF1A and HIRA. Required for gonad development.
CC       {ECO:0000250|UniProtKB:Q9NVP2}.
CC   -!- SUBUNIT: Interacts with histone H3 (including both histone H3.1 and
CC       H3.3) and histone H4. Interacts with the CHAF1A, CHAF1B and RBBP4
CC       subunits of the CAF-1 complex. Interacts with HAT1, NASP and TAF1.
CC       Interacts with CDAN1. Found in a cytosolic complex with CDAN1, ASF1A,
CC       IPO4 and histones H3.1 and H4. Interacts with CREBBP.
CC       {ECO:0000250|UniProtKB:Q9NVP2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NVP2}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NVP2}.
CC   -!- PTM: Phosphorylated by TLK1 and TLK2. {ECO:0000250|UniProtKB:Q9NVP2}.
CC   -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR   EMBL; BC118332; AAI18333.1; -; mRNA.
DR   RefSeq; NP_001068921.1; NM_001075453.1.
DR   AlphaFoldDB; Q17QJ0; -.
DR   SMR; Q17QJ0; -.
DR   STRING; 9913.ENSBTAP00000005338; -.
DR   PaxDb; Q17QJ0; -.
DR   PRIDE; Q17QJ0; -.
DR   Ensembl; ENSBTAT00000005338; ENSBTAP00000005338; ENSBTAG00000004085.
DR   GeneID; 510538; -.
DR   KEGG; bta:510538; -.
DR   CTD; 55723; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004085; -.
DR   VGNC; VGNC:50605; ASF1B.
DR   eggNOG; KOG3265; Eukaryota.
DR   GeneTree; ENSGT00390000004692; -.
DR   HOGENOM; CLU_060354_1_2_1; -.
DR   InParanoid; Q17QJ0; -.
DR   OMA; SCTPVKG; -.
DR   OrthoDB; 1334998at2759; -.
DR   TreeFam; TF106429; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000004085; Expressed in oocyte and 106 other tissues.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IBA:GO_Central.
DR   GO; GO:0006336; P:DNA replication-independent chromatin assembly; IBA:GO_Central.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
DR   Gene3D; 2.60.40.1490; -; 1.
DR   InterPro; IPR006818; ASF1-like.
DR   InterPro; IPR036747; ASF1-like_sf.
DR   PANTHER; PTHR12040; PTHR12040; 1.
DR   Pfam; PF04729; ASF1_hist_chap; 1.
DR   SUPFAM; SSF101546; SSF101546; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Chromatin regulator; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..202
FT                   /note="Histone chaperone ASF1B"
FT                   /id="PRO_0000284014"
FT   REGION          1..156
FT                   /note="Interaction with histone H3 and CHAF1B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y294"
FT   MOD_RES         198
FT                   /note="Phosphoserine; by TLK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVP2"
SQ   SEQUENCE   202 AA;  22421 MW;  4A97A393B1F9BFED CRC64;
     MAKVSVLNVA VLENPSPFHS PFRFEISFEC NEALADDLEW KIIYVGSAES EEFDQILDSV
     LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT YHGQEFIRVG YYVNNEYLSP
     ELRENPPLKP DFSQLQRNIL ASNPRVTRFH INWDNNMDRL EAIENQDSSL GCGLPLSCTP
     IKGLGLPSCI PGLLPENSMD CI