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ASF1A_BOVIN
ID   ASF1A_BOVIN             Reviewed;         204 AA.
AC   Q2KIG1;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Histone chaperone ASF1A;
DE   AltName: Full=Anti-silencing function protein 1 homolog A;
GN   Name=ASF1A;
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=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-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 and with HIRA to
CC       promote replication-independent chromatin assembly. Required for the
CC       formation of senescence-associated heterochromatin foci (SAHF) and
CC       efficient senescence-associated cell cycle exit.
CC       {ECO:0000250|UniProtKB:Q9Y294}.
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 CABIN1, HAT1, HIRA, NASP,
CC       TAF1, TLK1, TLK2 and UBN1 (By similarity). Interacts with CDAN1 (By
CC       similarity). Found in a cytosolic complex with CDAN1, ASF1B, IPO4 and
CC       histones H3.1 and H4. Interacts with CREBBP (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y294}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y294}.
CC   -!- PTM: Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-phase
CC       and at lower levels in M-phase. TLK2-mediated phosphorylation at Ser-
CC       192 prevents proteasome-dependent degradation.
CC       {ECO:0000250|UniProtKB:Q9Y294}.
CC   -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR   EMBL; BC112651; AAI12652.1; -; mRNA.
DR   RefSeq; NP_001069961.1; NM_001076493.2.
DR   AlphaFoldDB; Q2KIG1; -.
DR   BMRB; Q2KIG1; -.
DR   SMR; Q2KIG1; -.
DR   STRING; 9913.ENSBTAP00000002664; -.
DR   PaxDb; Q2KIG1; -.
DR   PRIDE; Q2KIG1; -.
DR   Ensembl; ENSBTAT00000002664; ENSBTAP00000002664; ENSBTAG00000002058.
DR   GeneID; 618099; -.
DR   KEGG; bta:618099; -.
DR   CTD; 25842; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002058; -.
DR   VGNC; VGNC:50604; ASF1A.
DR   eggNOG; KOG3265; Eukaryota.
DR   GeneTree; ENSGT00390000004692; -.
DR   HOGENOM; CLU_060354_1_2_1; -.
DR   InParanoid; Q2KIG1; -.
DR   OMA; KINWDYG; -.
DR   OrthoDB; 1334998at2759; -.
DR   TreeFam; TF106429; -.
DR   Reactome; R-BTA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000002058; Expressed in oocyte and 107 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:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0140713; F:histone chaperone activity; IEA:Ensembl.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; 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:0042692; P:muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
DR   GO; GO:0001649; P:osteoblast differentiation; 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; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..204
FT                   /note="Histone chaperone ASF1A"
FT                   /id="PRO_0000284011"
FT   REGION          1..156
FT                   /note="Interaction with histone H3, CHAF1B, and HIRA"
FT                   /evidence="ECO:0000250"
FT   REGION          155..204
FT                   /note="Required for interaction with HIRA"
FT                   /evidence="ECO:0000250"
FT   MOTIF           31..37
FT                   /note="Required for interaction with HIRA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         192
FT                   /note="Phosphoserine; by TLK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y294"
SQ   SEQUENCE   204 AA;  22938 MW;  98187E2B63A9FC68 CRC64;
     MAKVQVNNVV VLDNPSPFYN PFQFEITFEC IEDLSEDLEW KIIYVGSAES EEYDQVLDSV
     LVGPVPAGRH MFVFQADAPN PGLIPDADAV GVTVVLITCT YRGQEFIRVG YYVNNEYTET
     ELRENPPVKP DFSKLQRNIL ASNPRVTRFH INWEDNTEKL EDAESSNPNL PSLLSTDALP
     SASKGWSTSE NSLNVMLESH MDCM
 
 
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