ASF1A_HUMAN
ID ASF1A_HUMAN Reviewed; 204 AA.
AC Q9Y294; Q6IA08; Q9P014;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Histone chaperone ASF1A;
DE AltName: Full=Anti-silencing function protein 1 homolog A {ECO:0000303|PubMed:10759893};
DE Short=hAsf1 {ECO:0000303|PubMed:10759893};
DE Short=hAsf1a {ECO:0000303|PubMed:10759893};
DE AltName: Full=CCG1-interacting factor A {ECO:0000303|PubMed:12093919};
DE Short=CIA {ECO:0000303|PubMed:12093919};
DE Short=hCIA {ECO:0000303|PubMed:12093919};
GN Name=ASF1A {ECO:0000303|PubMed:10759893, ECO:0000312|HGNC:HGNC:20995};
GN ORFNames=CGI-98 {ECO:0000303|PubMed:10810093},
GN HSPC146 {ECO:0000303|PubMed:11042152};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH HISTONE H3.3;
RP HISTONE H4 AND TAF1.
RX PubMed=10759893; DOI=10.1046/j.1365-2443.2000.00319.x;
RA Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M.;
RT "A human homologue of yeast anti-silencing factor has histone chaperone
RT activity.";
RL Genes Cells 5:221-233(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION BY TLK1 AND TLK2.
RX PubMed=11470414; DOI=10.1016/s0960-9822(01)00298-6;
RA Sillje H.H.W., Nigg E.A.;
RT "Identification of human Asf1 chromatin assembly factors as substrates of
RT Tousled-like kinases.";
RL Curr. Biol. 11:1068-1073(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [10]
RP FUNCTION, INTERACTION WITH CHAF1A; CHAF1B AND RBBP4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11897662; DOI=10.1093/embo-reports/kvf068;
RA Mello J.A., Sillje H.H.W., Roche D.M.J., Kirschner D.B., Nigg E.A.,
RA Almouzni G.;
RT "Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome
RT assembly pathway.";
RL EMBO Rep. 3:329-334(2002).
RN [11]
RP INTERACTION WITH TAF1.
RX PubMed=12093919; DOI=10.1073/pnas.142627899;
RA Chimura T., Kuzuhara T., Horikoshi M.;
RT "Identification and characterization of CIA/ASF1 as an interactor of
RT bromodomains associated with TFIID.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002).
RN [12]
RP INTERACTION WITH HIRA, AND MUTAGENESIS OF 36-GLU-ASP-37 AND 62-VAL--PRO-64.
RX PubMed=14680630; DOI=10.1016/j.cub.2003.11.027;
RA Daganzo S.M., Erzberger J.P., Lam W.M., Skordalakes E., Zhang R.,
RA Franco A.A., Brill S.J., Adams P.D., Berger J.M., Kaufman P.D.;
RT "Structure and function of the conserved core of histone deposition protein
RT Asf1.";
RL Curr. Biol. 13:2148-2158(2003).
RN [13]
RP FUNCTION, INTERACTION WITH HISTONE H3.3; HISTONE H4 AND TAF1, SUBCELLULAR
RP LOCATION, 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 [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
RP COMPLEXES WITH CABIN1; CHAF1A; CHAF1B; HAT1; HIRA; HISTONE H3.1; HISTONE
RP H3.3; HISTONE H4; NASP; RBBP4 AND UBN1.
RX PubMed=14718166; DOI=10.1016/s0092-8674(03)01064-x;
RA Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.;
RT "Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways
RT dependent or independent of DNA synthesis.";
RL Cell 116:51-61(2004).
RN [15]
RP FUNCTION, INTERACTION WITH HIRA, AND MUTAGENESIS OF 36-GLU-ASP-37 AND
RP 62-VAL--PRO-64.
RX PubMed=15621527; DOI=10.1016/j.devcel.2004.10.019;
RA Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., Daganzo S.M.,
RA Erzberger J.P., Serebriiskii I.G., Canutescu A.A., Dunbrack R.L.,
RA Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.;
RT "Formation of MacroH2A-containing senescence-associated heterochromatin
RT foci and senescence driven by ASF1a and HIRA.";
RL Dev. Cell 8:19-30(2005).
RN [16]
RP FUNCTION.
RX PubMed=16151251; DOI=10.1128/ec.4.9.1583-1590.2005;
RA Tamburini B.A., Carson J.J., Adkins M.W., Tyler J.K.;
RT "Functional conservation and specialization among eukaryotic anti-silencing
RT function 1 histone chaperones.";
RL Eukaryot. Cell 4:1583-1590(2005).
RN [17]
RP FUNCTION, AND INTERACTION WITH HISTONE H3.1; HISTONE H3.3; HISTONE H4; NASP
RP AND RBBP4.
RX PubMed=15664198; DOI=10.1016/j.molcel.2004.12.018;
RA Groth A., Ray-Gallet D., Quivy J.-P., Lukas J., Bartek J., Almouzni G.;
RT "Human Asf1 regulates the flow of S phase histones during replicational
RT stress.";
RL Mol. Cell 17:301-311(2005).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP INTERACTION WITH UBN1.
RX PubMed=19029251; DOI=10.1128/mcb.01047-08;
RA Banumathy G., Somaiah N., Zhang R., Tang Y., Hoffmann J., Andrake M.,
RA Ceulemans H., Schultz D., Marmorstein R., Adams P.D.;
RT "Human UBN1 is an ortholog of yeast Hpc2p and has an essential role in the
RT HIRA/ASF1a chromatin-remodeling pathway in senescent cells.";
RL Mol. Cell. Biol. 29:758-770(2009).
RN [21]
RP PHOSPHORYLATION AT SER-192 BY TLK2.
RX PubMed=20016786; DOI=10.1371/journal.pone.0008328;
RA Pilyugin M., Demmers J., Verrijzer C.P., Karch F., Moshkin Y.M.;
RT "Phosphorylation-mediated control of histone chaperone ASF1 levels by
RT Tousled-like kinases.";
RL PLoS ONE 4:E8328-E8328(2009).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [24]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH IPO4; HISTONES H3 AND H4.
RX PubMed=21454524; DOI=10.1074/jbc.m111.223453;
RA Alvarez F., Munoz F., Schilcher P., Imhof A., Almouzni G., Loyola A.;
RT "Sequential establishment of marks on soluble histones H3 and H4.";
RL J. Biol. Chem. 286:17714-17721(2011).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP INTERACTION WITH CDAN1, AND IDENTIFICATION IN A COMPLEX WITH CDNA1; ASF1B;
RP IPO4; HISTONES H3.2 AND H4.
RX PubMed=22407294; DOI=10.1038/emboj.2012.55;
RA Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.;
RT "Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1 function in
RT S-phase histone supply.";
RL EMBO J. 31:2013-2023(2012).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP INTERACTION WITH CREBBP.
RX PubMed=24616510; DOI=10.1073/pnas.1319122111;
RA Das C., Roy S., Namjoshi S., Malarkey C.S., Jones D.N., Kutateladze T.G.,
RA Churchill M.E., Tyler J.K.;
RT "Binding of the histone chaperone ASF1 to the CBP bromodomain promotes
RT histone acetylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E1072-E1081(2014).
RN [30]
RP FUNCTION.
RX PubMed=29408485; DOI=10.1016/j.jmb.2018.01.015;
RA Yoon J., Kim S.J., An S., Cho S., Leitner A., Jung T., Aebersold R.,
RA Hebert H., Cho U.S., Song J.J.;
RT "Integrative structural investigation on the architecture of human
RT Importin4_Histone H3/H4_Asf1a complex and its histone H3 tail binding.";
RL J. Mol. Biol. 430:822-841(2018).
RN [31]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-192, AND MUTAGENESIS
RP OF VAL-94; SER-166; SER-175 AND SER-192.
RX PubMed=29478807; DOI=10.1016/j.molcel.2018.01.031;
RA Huang T.H., Fowler F., Chen C.C., Shen Z.J., Sleckman B., Tyler J.K.;
RT "The histone chaperones ASF1 and CAF-1 promote MMS22L-TONSL-mediated Rad51
RT loading onto ssDNA during homologous recombination in human cells.";
RL Mol. Cell 69:879-892(2018).
RN [32]
RP INTERACTION WITH HISTONE H3.3.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
RN [33]
RP STRUCTURE BY NMR OF 1-156, INTERACTION WITH HISTONE H3 AND HISTONE H4, AND
RP MUTAGENESIS OF ASP-54; VAL-94 AND ARG-108.
RX PubMed=15840725; DOI=10.1073/pnas.0500149102;
RA Mousson F., Lautrette A., Thuret J.-Y., Agez M., Courbeyrette R.,
RA Amigues B., Becker E., Neumann J.-M., Guerois R., Mann C., Ochsenbein F.;
RT "Structural basis for the interaction of Asf1 with histone H3 and its
RT functional implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5975-5980(2005).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-157 IN COMPLEX WITH HIRA,
RP INTERACTION WITH CHAF1B, AND MUTAGENESIS OF ASP-37.
RX PubMed=16980972; DOI=10.1038/nsmb1147;
RA Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A.,
RA Dunbrack R., Adams P.D., Marmorstein R.;
RT "Structure of a human ASF1a-HIRA complex and insights into specificity of
RT histone chaperone complex assembly.";
RL Nat. Struct. Mol. Biol. 13:921-929(2006).
CC -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC histone exchange and removal during nucleosome assembly and disassembly
CC (PubMed:10759893, PubMed:11897662, PubMed:12842904, PubMed:14718166,
CC PubMed:15664198, PubMed:16151251, PubMed:21454524). Cooperates with
CC chromatin assembly factor 1 (CAF-1) to promote replication-dependent
CC chromatin assembly and with HIRA to promote replication-independent
CC chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198).
CC Promotes homologous recombination-mediated repair of double-strand
CC breaks (DSBs) at stalled or collapsed replication forks: acts by
CC mediating histone replacement at DSBs, leading to recruitment of the
CC MMS22L-TONSL complex and subsequent loading of RAD51 (PubMed:29478807).
CC Also involved in the nuclear import of the histone H3-H4 dimer together
CC with importin-4 (IPO4): specifically recognizes and binds newly
CC synthesized histones with the monomethylation of H3 'Lys-9' and
CC acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at
CC 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol
CC (PubMed:21454524, PubMed:29408485). Required for the formation of
CC senescence-associated heterochromatin foci (SAHF) and efficient
CC senescence-associated cell cycle exit (PubMed:15621527).
CC {ECO:0000269|PubMed:10759893, ECO:0000269|PubMed:11897662,
CC ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14718166,
CC ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15664198,
CC ECO:0000269|PubMed:16151251, ECO:0000269|PubMed:21454524,
CC ECO:0000269|PubMed:29408485, ECO:0000269|PubMed:29478807}.
CC -!- SUBUNIT: Interacts with histone H3 (including both histone H3.1 and
CC H3.3) and histone H4 (PubMed:10759893, PubMed:12842904,
CC PubMed:14718166, PubMed:15664198, PubMed:33857403, PubMed:15840725).
CC Interacts with the CHAF1A, CHAF1B and RBBP4 subunits of the CAF-1
CC complex (PubMed:11897662, PubMed:16980972). Interacts with CABIN1,
CC HAT1, HIRA, NASP, TAF1 and UBN1 (PubMed:12093919, PubMed:14680630,
CC PubMed:14718166, PubMed:15621527, PubMed:16980972, PubMed:19029251).
CC Interacts with CDAN1 (PubMed:22407294). Found in a cytosolic complex
CC with IPO4 and histones H3 and H4 (PubMed:21454524, PubMed:22407294).
CC Interacts with CREBBP (PubMed:24616510). {ECO:0000269|PubMed:10759893,
CC ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12093919,
CC ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14680630,
CC ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:15621527,
CC ECO:0000269|PubMed:15664198, ECO:0000269|PubMed:15840725,
CC ECO:0000269|PubMed:16980972, ECO:0000269|PubMed:19029251,
CC ECO:0000269|PubMed:21454524, ECO:0000269|PubMed:22407294,
CC ECO:0000269|PubMed:24616510, ECO:0000269|PubMed:33857403}.
CC -!- INTERACTION:
CC Q9Y294; Q13112: CHAF1B; NbExp=3; IntAct=EBI-749553, EBI-1052944;
CC Q9Y294; P03372: ESR1; NbExp=4; IntAct=EBI-749553, EBI-78473;
CC Q9Y294; P62805: H4C9; NbExp=15; IntAct=EBI-749553, EBI-302023;
CC Q9Y294; P54198: HIRA; NbExp=14; IntAct=EBI-749553, EBI-372342;
CC Q9Y294; P49736: MCM2; NbExp=10; IntAct=EBI-749553, EBI-374819;
CC Q9Y294; P49321-2: NASP; NbExp=3; IntAct=EBI-749553, EBI-7038920;
CC Q9Y294; P79522: PRR3; NbExp=6; IntAct=EBI-749553, EBI-2803328;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11897662,
CC ECO:0000269|PubMed:12842904}. Chromosome {ECO:0000269|PubMed:29478807}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12842904}.
CC -!- PTM: Phosphorylated by TLK1 and TLK2 (PubMed:11470414,
CC PubMed:20016786). Highly phosphorylated in S-phase and at lower levels
CC in M-phase (PubMed:11470414). TLK2-mediated phosphorylation at Ser-192
CC prevents proteasome-dependent degradation (PubMed:20016786).
CC Phosphorylation at Ser-192 by PRKDC in response to DNA damage promotes
CC the histone chaperone activity and ability to replace histones at
CC double-strand breaks (DSBs) at stalled or collapsed replication forks,
CC leading to RAD51 recruitment (PubMed:29478807).
CC {ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:20016786,
CC ECO:0000269|PubMed:29478807}.
CC -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR EMBL; AB028628; BAA96542.1; -; mRNA.
DR EMBL; AF279306; AAK82972.1; -; mRNA.
DR EMBL; AF151856; AAD34093.1; -; mRNA.
DR EMBL; AF161495; AAF29110.1; -; mRNA.
DR EMBL; AL050261; CAB43363.1; -; mRNA.
DR EMBL; AK025738; BAB15228.1; -; mRNA.
DR EMBL; CR457347; CAG33628.1; -; mRNA.
DR EMBL; AC022098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010878; AAH10878.1; -; mRNA.
DR CCDS; CCDS47469.1; -.
DR PIR; T08661; T08661.
DR RefSeq; NP_054753.1; NM_014034.2.
DR PDB; 1TEY; NMR; -; A=1-156.
DR PDB; 2I32; X-ray; 2.70 A; A/B=1-157.
DR PDB; 2IIJ; NMR; -; A=1-156.
DR PDB; 2IO5; X-ray; 2.70 A; A=1-172.
DR PDB; 3AAD; X-ray; 3.30 A; B/D=1-155.
DR PDB; 5C3I; X-ray; 3.50 A; A/E/I/M/Q/U=1-175.
DR PDB; 6F0F; X-ray; 2.00 A; A=1-156.
DR PDB; 6F0G; X-ray; 2.30 A; A/B=1-156.
DR PDB; 6F0H; X-ray; 1.98 A; A/C=1-156.
DR PDB; 6ZUF; X-ray; 1.80 A; A/B=1-156.
DR PDB; 7LNY; X-ray; 2.10 A; A/B/C/D/E/F/G=1-155.
DR PDB; 7LO0; X-ray; 2.71 A; A/B/C/D/E/F/G/H=1-155.
DR PDB; 7V6Q; X-ray; 3.00 A; A/E=1-156.
DR PDBsum; 1TEY; -.
DR PDBsum; 2I32; -.
DR PDBsum; 2IIJ; -.
DR PDBsum; 2IO5; -.
DR PDBsum; 3AAD; -.
DR PDBsum; 5C3I; -.
DR PDBsum; 6F0F; -.
DR PDBsum; 6F0G; -.
DR PDBsum; 6F0H; -.
DR PDBsum; 6ZUF; -.
DR PDBsum; 7LNY; -.
DR PDBsum; 7LO0; -.
DR PDBsum; 7V6Q; -.
DR AlphaFoldDB; Q9Y294; -.
DR BMRB; Q9Y294; -.
DR SMR; Q9Y294; -.
DR BioGRID; 117368; 241.
DR CORUM; Q9Y294; -.
DR DIP; DIP-29241N; -.
DR IntAct; Q9Y294; 53.
DR MINT; Q9Y294; -.
DR STRING; 9606.ENSP00000229595; -.
DR BindingDB; Q9Y294; -.
DR ChEMBL; CHEMBL3392950; -.
DR GlyGen; Q9Y294; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y294; -.
DR PhosphoSitePlus; Q9Y294; -.
DR BioMuta; ASF1A; -.
DR DMDM; 74735206; -.
DR EPD; Q9Y294; -.
DR jPOST; Q9Y294; -.
DR MassIVE; Q9Y294; -.
DR MaxQB; Q9Y294; -.
DR PaxDb; Q9Y294; -.
DR PeptideAtlas; Q9Y294; -.
DR PRIDE; Q9Y294; -.
DR ProteomicsDB; 85702; -.
DR Antibodypedia; 32585; 438 antibodies from 36 providers.
DR DNASU; 25842; -.
DR Ensembl; ENST00000229595.6; ENSP00000229595.5; ENSG00000111875.8.
DR GeneID; 25842; -.
DR KEGG; hsa:25842; -.
DR MANE-Select; ENST00000229595.6; ENSP00000229595.5; NM_014034.3; NP_054753.1.
DR UCSC; uc011ebn.3; human.
DR CTD; 25842; -.
DR DisGeNET; 25842; -.
DR GeneCards; ASF1A; -.
DR HGNC; HGNC:20995; ASF1A.
DR HPA; ENSG00000111875; Low tissue specificity.
DR MIM; 609189; gene.
DR neXtProt; NX_Q9Y294; -.
DR OpenTargets; ENSG00000111875; -.
DR PharmGKB; PA128394636; -.
DR VEuPathDB; HostDB:ENSG00000111875; -.
DR eggNOG; KOG3265; Eukaryota.
DR GeneTree; ENSGT00390000004692; -.
DR HOGENOM; CLU_060354_1_2_1; -.
DR InParanoid; Q9Y294; -.
DR OMA; KINWDYG; -.
DR PhylomeDB; Q9Y294; -.
DR TreeFam; TF106429; -.
DR PathwayCommons; Q9Y294; -.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; Q9Y294; -.
DR SIGNOR; Q9Y294; -.
DR BioGRID-ORCS; 25842; 74 hits in 1087 CRISPR screens.
DR EvolutionaryTrace; Q9Y294; -.
DR GeneWiki; ASF1A; -.
DR GenomeRNAi; 25842; -.
DR Pharos; Q9Y294; Tchem.
DR PRO; PR:Q9Y294; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y294; protein.
DR Bgee; ENSG00000111875; Expressed in oocyte and 209 other tissues.
DR Genevisible; Q9Y294; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
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:0006281; P:DNA repair; IDA:MGI.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0042692; P:muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IDA:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR Gene3D; 2.60.40.1490; -; 1.
DR IDEAL; IID00182; -.
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 3D-structure; Chaperone; Chromatin regulator; Chromosome; DNA damage;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..204
FT /note="Histone chaperone ASF1A"
FT /id="PRO_0000284012"
FT REGION 1..156
FT /note="Interaction with histone H3, CHAF1B, and HIRA"
FT /evidence="ECO:0000269|PubMed:15840725"
FT REGION 155..204
FT /note="Required for interaction with HIRA"
FT /evidence="ECO:0000269|PubMed:15621527,
FT ECO:0000269|PubMed:16980972"
FT MOTIF 31..37
FT /note="Required for interaction with HIRA"
FT /evidence="ECO:0000269|PubMed:15621527,
FT ECO:0000269|PubMed:16980972"
FT MOD_RES 192
FT /note="Phosphoserine; by PRKDC and TLK2"
FT /evidence="ECO:0000269|PubMed:20016786,
FT ECO:0000269|PubMed:29478807"
FT MUTAGEN 36..37
FT /note="ED->AA: Abrogates interaction with HIRA and
FT induction of senescence-associated heterochromatin foci."
FT /evidence="ECO:0000269|PubMed:14680630,
FT ECO:0000269|PubMed:15621527"
FT MUTAGEN 37
FT /note="D->A: Abrogates interaction with CHAF1B and HIRA."
FT /evidence="ECO:0000269|PubMed:16980972"
FT MUTAGEN 54
FT /note="D->R: Reduces interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:15840725"
FT MUTAGEN 62..64
FT /note="VGP->AAA: Abrogates interaction with HIRA and
FT induction of senescence-associated heterochromatin foci."
FT /evidence="ECO:0000269|PubMed:14680630,
FT ECO:0000269|PubMed:15621527"
FT MUTAGEN 94
FT /note="V->R: Abrogates interaction with histone H3 and
FT histone H4."
FT /evidence="ECO:0000269|PubMed:15840725,
FT ECO:0000269|PubMed:29478807"
FT MUTAGEN 108
FT /note="R->E: Reduces interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:15840725"
FT MUTAGEN 166
FT /note="S->A: Does not affect phosphorylation in response to
FT DNA damage."
FT /evidence="ECO:0000269|PubMed:29478807"
FT MUTAGEN 175
FT /note="S->A: Does not affect phosphorylation in response to
FT DNA damage."
FT /evidence="ECO:0000269|PubMed:29478807"
FT MUTAGEN 192
FT /note="S->A: Abolished phosphorylation in response to DNA
FT damage."
FT /evidence="ECO:0000269|PubMed:29478807"
FT MUTAGEN 192
FT /note="S->D: Mimics phosphorylation; promoting recruitment
FT to chromatin in response to DNA damage."
FT /evidence="ECO:0000269|PubMed:29478807"
FT CONFLICT 74
FT /note="F -> I (in Ref. 4; AAF29110)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="M -> I (in Ref. 7; CAG33628)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 22..32
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:6ZUF"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:6ZUF"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6ZUF"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 104..117
FT /evidence="ECO:0007829|PDB:6ZUF"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:6ZUF"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:6ZUF"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6ZUF"
SQ SEQUENCE 204 AA; 22969 MW; 9819D531D3A9FC68 CRC64;
MAKVQVNNVV VLDNPSPFYN PFQFEITFEC IEDLSEDLEW KIIYVGSAES EEYDQVLDSV
LVGPVPAGRH MFVFQADAPN PGLIPDADAV GVTVVLITCT YRGQEFIRVG YYVNNEYTET
ELRENPPVKP DFSKLQRNIL ASNPRVTRFH INWEDNTEKL EDAESSNPNL QSLLSTDALP
SASKGWSTSE NSLNVMLESH MDCM
