ASF1A_MOUSE
ID ASF1A_MOUSE Reviewed; 204 AA.
AC Q9CQE6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Histone chaperone ASF1A;
DE AltName: Full=Anti-silencing function protein 1 homolog A;
GN Name=Asf1a {ECO:0000303|PubMed:21987787, ECO:0000312|MGI:MGI:1913653};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Pancreas, Thymus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=21987787; DOI=10.1073/pnas.1113524108;
RA Hartford S.A., Luo Y., Southard T.L., Min I.M., Lis J.T., Schimenti J.C.;
RT "Minichromosome maintenance helicase paralog MCM9 is dispensible for DNA
RT replication but functions in germ-line stem cells and tumor suppression.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17702-17707(2011).
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. Promotes homologous
CC recombination-mediated repair of double-strand breaks (DSBs) at stalled
CC or collapsed replication forks: acts by mediating histone replacement
CC at DSBs, leading to recruitment of the MMS22L-TONSL complex and
CC subsequent loading of RAD51. Also involved in the nuclear import of the
CC histone H3-H4 dimer together with importin-4 (IPO4): specifically
CC recognizes and binds newly synthesized histones with the
CC monomethylation of H3 'Lys-9' and acetylation at 'Lys-14'
CC (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4
CC (H4K5K12ac) marks in the cytosol. Required for the formation of
CC senescence-associated heterochromatin foci (SAHF) and efficient
CC senescence-associated cell cycle exit. {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 and UBN1. Interacts with CDAN1. Found in a cytosolic complex with
CC IPO4 and histones H3 and H4. Interacts with CREBBP.
CC {ECO:0000250|UniProtKB:Q9Y294}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y294}.
CC Chromosome {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. Phosphorylation at Ser-
CC 192 by PRKDC in response to DNA damage promotes the histone chaperone
CC activity and ability to replace histones at double-strand breaks (DSBs)
CC at stalled or collapsed replication forks, leading to RAD51
CC recruitment. {ECO:0000250|UniProtKB:Q9Y294}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality at mid-gestation (9.5 dpc).
CC {ECO:0000269|PubMed:21987787}.
CC -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR EMBL; AK007804; BAB25269.1; -; mRNA.
DR EMBL; AK010210; BAB26770.1; -; mRNA.
DR EMBL; AK012376; BAB28198.1; -; mRNA.
DR EMBL; AK088618; BAC40457.1; -; mRNA.
DR EMBL; BC027628; AAH27628.1; -; mRNA.
DR CCDS; CCDS23847.1; -.
DR RefSeq; NP_079817.1; NM_025541.3.
DR AlphaFoldDB; Q9CQE6; -.
DR BMRB; Q9CQE6; -.
DR SMR; Q9CQE6; -.
DR BioGRID; 211447; 6.
DR IntAct; Q9CQE6; 61.
DR MINT; Q9CQE6; -.
DR STRING; 10090.ENSMUSP00000020004; -.
DR iPTMnet; Q9CQE6; -.
DR PhosphoSitePlus; Q9CQE6; -.
DR EPD; Q9CQE6; -.
DR jPOST; Q9CQE6; -.
DR MaxQB; Q9CQE6; -.
DR PaxDb; Q9CQE6; -.
DR PeptideAtlas; Q9CQE6; -.
DR PRIDE; Q9CQE6; -.
DR ProteomicsDB; 265117; -.
DR Antibodypedia; 32585; 438 antibodies from 36 providers.
DR DNASU; 66403; -.
DR Ensembl; ENSMUST00000020004; ENSMUSP00000020004; ENSMUSG00000019857.
DR GeneID; 66403; -.
DR KEGG; mmu:66403; -.
DR UCSC; uc007fbr.1; mouse.
DR CTD; 25842; -.
DR MGI; MGI:1913653; Asf1a.
DR VEuPathDB; HostDB:ENSMUSG00000019857; -.
DR eggNOG; KOG3265; Eukaryota.
DR GeneTree; ENSGT00390000004692; -.
DR HOGENOM; CLU_060354_1_2_1; -.
DR InParanoid; Q9CQE6; -.
DR OMA; KINWDYG; -.
DR OrthoDB; 1334998at2759; -.
DR PhylomeDB; Q9CQE6; -.
DR TreeFam; TF106429; -.
DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR BioGRID-ORCS; 66403; 9 hits in 109 CRISPR screens.
DR ChiTaRS; Asf1a; mouse.
DR PRO; PR:Q9CQE6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CQE6; protein.
DR Bgee; ENSMUSG00000019857; Expressed in animal zygote and 274 other tissues.
DR ExpressionAtlas; Q9CQE6; baseline and differential.
DR Genevisible; Q9CQE6; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; ISO:MGI.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR GO; GO:0042692; P:muscle cell differentiation; IGI:MGI.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
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 1: Evidence at protein level;
KW Chaperone; Chromatin regulator; Chromosome; DNA damage; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..204
FT /note="Histone chaperone ASF1A"
FT /id="PRO_0000284013"
FT REGION 1..156
FT /note="Interaction with histone H3, CHAF1B, and HIRA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y294"
FT REGION 155..204
FT /note="Required for interaction with HIRA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y294"
FT MOTIF 31..37
FT /note="Required for interaction with HIRA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y294"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y294"
SQ SEQUENCE 204 AA; 22943 MW; 9803653A63B8FC68 CRC64;
MAKVQVNNVV VLDNPSPFYN PFQFEITFEC IEDLSEDLEW KIIYVGSAES EEYDQVLDSV
LVGPVPAGRH MFVFQADAPN AGLIPDADAV GVTVVLITCT YRGQEFIRVG YYVNNEYTET
ELRENPPVKP DFSKLQRNIL ASNPRVTRFH INWEDNTEKL EDAESSNPNL QSLLSTDALP
SASKGWSTSE NSLNVMLESH MDCM
