ASF1B_MOUSE
ID ASF1B_MOUSE Reviewed; 202 AA.
AC Q9DAP7; Q8BP41; Q9CTX3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Histone chaperone ASF1B {ECO:0000305};
DE AltName: Full=Anti-silencing function protein 1 homolog B;
DE AltName: Full=CCG1-interacting factor A-II {ECO:0000303|PubMed:12842904};
DE Short=CIA-II {ECO:0000303|PubMed:12842904};
DE Short=mCIA-II {ECO:0000303|PubMed:12842904};
GN Name=Asf1b {ECO:0000303|PubMed:12842904, ECO:0000312|MGI:MGI:1914179};
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;
RC TISSUE=Bone marrow, Embryo, Olfactory bulb, Spleen, and Testis;
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=Czech II; TISSUE=Mammary tumor;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12842904; DOI=10.1074/jbc.m303549200;
RA Umehara T., Horikoshi M.;
RT "Transcription initiation factor IID-interactive histone chaperone CIA-II
RT implicated in mammalian spermatogenesis.";
RL J. Biol. Chem. 278:35660-35667(2003).
RN [4]
RP FUNCTION, AND PHOSPHORYLATION BY TLK1.
RX PubMed=17054786; DOI=10.1186/1471-2199-7-37;
RA Sen S.P., De Benedetti A.;
RT "TLK1B promotes repair of UV-damaged DNA through chromatin remodeling by
RT Asf1.";
RL BMC Mol. Biol. 7:37-37(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, 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 [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26850882; DOI=10.1530/rep-15-0327;
RA Messiaen S., Guiard J., Aigueperse C., Fliniaux I., Tourpin S., Barroca V.,
RA Allemand I., Fouchet P., Livera G., Vernet M.;
RT "Loss of the histone chaperone ASF1B reduces female reproductive capacity
RT in mice.";
RL Reproduction 151:477-489(2016).
CC -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC histone exchange and removal during nucleosome assembly and disassembly
CC (PubMed:12842904, PubMed:17054786). Cooperates with chromatin assembly
CC factor 1 (CAF-1) to promote replication-dependent chromatin assembly
CC (By similarity). Also involved in the nuclear import of the histone H3-
CC H4 dimer together with importin-4 (IPO4): specifically recognizes and
CC binds newly synthesized histones with the monomethylation of H3 'Lys-9'
CC (H3K9me1) and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5ac and
CC H4K12ac) marks in the cytosol (By similarity). Does not participate in
CC replication-independent nucleosome deposition which is mediated by
CC ASF1A and HIRA (By similarity). Required for gonad development
CC (PubMed:26850882). {ECO:0000250|UniProtKB:Q9NVP2,
CC ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:17054786,
CC ECO:0000269|PubMed:26850882}.
CC -!- SUBUNIT: Interacts with histone H3 (including both histone H3.1 and
CC H3.3) and histone H4 (By similarity). Interacts with the CHAF1A, CHAF1B
CC and RBBP4 subunits of the CAF-1 complex (By similarity). Interacts with
CC HAT1, NASP and TAF1 (By similarity). Interacts with CDAN1. Found in a
CC cytosolic complex with CDAN1, ASF1A, IPO4 and histones H3.1 and H4 (By
CC similarity). Interacts with CREBBP (By similarity).
CC {ECO:0000250|UniProtKB:Q9NVP2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NVP2}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NVP2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in germ cells (PubMed:26850882).
CC Restricted to premeiotic to meiotic stages during spermatogenesis
CC (PubMed:12842904). {ECO:0000269|PubMed:12842904,
CC ECO:0000269|PubMed:26850882}.
CC -!- DEVELOPMENTAL STAGE: Expressed in early embryos and germ cells.
CC {ECO:0000269|PubMed:26850882}.
CC -!- PTM: Phosphorylated by TLK2 (By similarity). Phosphorylated by TLK1
CC (PubMed:17054786). {ECO:0000250|UniProtKB:Q9NVP2,
CC ECO:0000269|PubMed:17054786}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but display subfertility caused
CC by altered gamete formation (PubMed:26850882). The timing of meiotic
CC entry and the subsequent gonad development is more severely impaired in
CC female than in male mice (PubMed:26850882). Increased perinatal
CC lethality is also increased in the offspring of knockout females
CC (PubMed:26850882). {ECO:0000269|PubMed:26850882}.
CC -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR EMBL; AK005646; BAB24166.1; -; mRNA.
DR EMBL; AK019594; BAB31809.1; -; mRNA.
DR EMBL; AK077005; BAC36561.1; -; mRNA.
DR EMBL; AK077718; BAC36978.1; -; mRNA.
DR EMBL; AK134906; BAE22334.1; -; mRNA.
DR EMBL; AK150818; BAE29881.1; -; mRNA.
DR EMBL; AK151951; BAE30824.1; -; mRNA.
DR EMBL; AK165322; BAE38137.1; -; mRNA.
DR EMBL; BC003428; AAH03428.1; -; mRNA.
DR CCDS; CCDS22462.1; -.
DR RefSeq; NP_077146.1; NM_024184.2.
DR AlphaFoldDB; Q9DAP7; -.
DR SMR; Q9DAP7; -.
DR BioGRID; 211816; 1.
DR IntAct; Q9DAP7; 5.
DR MINT; Q9DAP7; -.
DR STRING; 10090.ENSMUSP00000005607; -.
DR iPTMnet; Q9DAP7; -.
DR PhosphoSitePlus; Q9DAP7; -.
DR EPD; Q9DAP7; -.
DR jPOST; Q9DAP7; -.
DR MaxQB; Q9DAP7; -.
DR PaxDb; Q9DAP7; -.
DR PeptideAtlas; Q9DAP7; -.
DR PRIDE; Q9DAP7; -.
DR ProteomicsDB; 281918; -.
DR Antibodypedia; 26631; 320 antibodies from 30 providers.
DR DNASU; 66929; -.
DR Ensembl; ENSMUST00000005607; ENSMUSP00000005607; ENSMUSG00000005470.
DR GeneID; 66929; -.
DR KEGG; mmu:66929; -.
DR UCSC; uc009mlk.1; mouse.
DR CTD; 55723; -.
DR MGI; MGI:1914179; Asf1b.
DR VEuPathDB; HostDB:ENSMUSG00000005470; -.
DR eggNOG; KOG3265; Eukaryota.
DR GeneTree; ENSGT00390000004692; -.
DR HOGENOM; CLU_060354_1_2_1; -.
DR InParanoid; Q9DAP7; -.
DR OMA; SCTPVKG; -.
DR OrthoDB; 1334998at2759; -.
DR PhylomeDB; Q9DAP7; -.
DR TreeFam; TF106429; -.
DR BioGRID-ORCS; 66929; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Asf1b; mouse.
DR PRO; PR:Q9DAP7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9DAP7; protein.
DR Bgee; ENSMUSG00000005470; Expressed in fetal liver hematopoietic progenitor cell and 202 other tissues.
DR Genevisible; Q9DAP7; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IDA:MGI.
DR GO; GO:0140713; F:histone chaperone activity; IDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0001835; P:blastocyst hatching; IMP: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:0006334; P:nucleosome assembly; IDA: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; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..202
FT /note="Histone chaperone ASF1B"
FT /id="PRO_0000284016"
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"
FT CONFLICT 93
FT /note="T -> N (in Ref. 1; BAC36978)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="N -> K (in Ref. 1; BAC36978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22464 MW; A02546180DA18A48 CRC64;
MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALSDDLEW KIIYVGSAES EEFDQILDSV
LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT YHGQEFIRVG YYVNNEYPDP
ELRENPPPKP DFSQLQRNIL ASNPRVTRFH INWDNNPDSL EAIENQDPNV DFSLSLSCTP
VKSLGLPSCI PGLLPENSMD CI
