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Histone chaperone ASF1A (Anti-silencing function protein 1 homolog A) (hAsf1) (hAsf1a) (CCG1-interacting factor A) (CIA) (hCIA)

 ASF1A_HUMAN             Reviewed;         204 AA.
Q9Y294; Q6IA08; Q9P014;
17-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
27-SEP-2017, entry version 151.
RecName: Full=Histone chaperone ASF1A;
AltName: Full=Anti-silencing function protein 1 homolog A;
Short=hAsf1;
Short=hAsf1a;
AltName: Full=CCG1-interacting factor A;
Short=CIA;
Short=hCIA;
Name=ASF1A; ORFNames=CGI-98, HSPC146;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH HISTONE
H3.3; HISTONE H4 AND TAF1.
PubMed=10759893; DOI=10.1046/j.1365-2443.2000.00319.x;
Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M.;
"A human homologue of yeast anti-silencing factor has histone
chaperone activity.";
Genes Cells 5:221-233(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TLK1 AND TLK2, AND
PHOSPHORYLATION BY TLK1 AND TLK2.
PubMed=11470414; DOI=10.1016/S0960-9822(01)00298-6;
Sillje H.H.W., Nigg E.A.;
"Identification of human Asf1 chromatin assembly factors as substrates
of Tousled-like kinases.";
Curr. Biol. 11:1068-1073(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
FUNCTION, INTERACTION WITH CHAF1A; CHAF1B AND RBBP4, AND SUBCELLULAR
LOCATION.
PubMed=11897662; DOI=10.1093/embo-reports/kvf068;
Mello J.A., Sillje H.H.W., Roche D.M.J., Kirschner D.B., Nigg E.A.,
Almouzni G.;
"Human Asf1 and CAF-1 interact and synergize in a repair-coupled
nucleosome assembly pathway.";
EMBO Rep. 3:329-334(2002).
[11]
INTERACTION WITH TAF1.
PubMed=12093919; DOI=10.1073/pnas.142627899;
Chimura T., Kuzuhara T., Horikoshi M.;
"Identification and characterization of CIA/ASF1 as an interactor of
bromodomains associated with TFIID.";
Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002).
[12]
INTERACTION WITH HIRA, AND MUTAGENESIS OF 36-GLU-ASP-37 AND
62-VAL--PRO-64.
PubMed=14680630; DOI=10.1016/j.cub.2003.11.027;
Daganzo S.M., Erzberger J.P., Lam W.M., Skordalakes E., Zhang R.,
Franco A.A., Brill S.J., Adams P.D., Berger J.M., Kaufman P.D.;
"Structure and function of the conserved core of histone deposition
protein Asf1.";
Curr. Biol. 13:2148-2158(2003).
[13]
FUNCTION, INTERACTION WITH HISTONE H3.3; HISTONE H4 AND TAF1,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12842904; DOI=10.1074/jbc.M303549200;
Umehara T., Horikoshi M.;
"Transcription initiation factor IID-interactive histone chaperone
CIA-II implicated in mammalian spermatogenesis.";
J. Biol. Chem. 278:35660-35667(2003).
[14]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
COMPLEXES WITH CABIN1; CHAF1A; CHAF1B; HAT1; HIRA; HISTONE H3.1;
HISTONE H3.3; HISTONE H4; NASP; RBBP4 AND UBN1.
PubMed=14718166; DOI=10.1016/S0092-8674(03)01064-X;
Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.;
"Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways
dependent or independent of DNA synthesis.";
Cell 116:51-61(2004).
[15]
FUNCTION, INTERACTION WITH HIRA, AND MUTAGENESIS OF 36-GLU-ASP-37 AND
62-VAL--PRO-64.
PubMed=15621527; DOI=10.1016/j.devcel.2004.10.019;
Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W.,
Daganzo S.M., Erzberger J.P., Serebriiskii I.G., Canutescu A.A.,
Dunbrack R.L., Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.;
"Formation of MacroH2A-containing senescence-associated
heterochromatin foci and senescence driven by ASF1a and HIRA.";
Dev. Cell 8:19-30(2005).
[16]
FUNCTION.
PubMed=16151251; DOI=10.1128/EC.4.9.1583-1590.2005;
Tamburini B.A., Carson J.J., Adkins M.W., Tyler J.K.;
"Functional conservation and specialization among eukaryotic anti-
silencing function 1 histone chaperones.";
Eukaryot. Cell 4:1583-1590(2005).
[17]
FUNCTION, AND INTERACTION WITH HISTONE H3.1; HISTONE H3.3; HISTONE H4;
NASP AND RBBP4.
PubMed=15664198; DOI=10.1016/j.molcel.2004.12.018;
Groth A., Ray-Gallet D., Quivy J.-P., Lukas J., Bartek J.,
Almouzni G.;
"Human Asf1 regulates the flow of S phase histones during
replicational stress.";
Mol. Cell 17:301-311(2005).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
INTERACTION WITH UBN1.
PubMed=19029251; DOI=10.1128/MCB.01047-08;
Banumathy G., Somaiah N., Zhang R., Tang Y., Hoffmann J., Andrake M.,
Ceulemans H., Schultz D., Marmorstein R., Adams P.D.;
"Human UBN1 is an ortholog of yeast Hpc2p and has an essential role in
the HIRA/ASF1a chromatin-remodeling pathway in senescent cells.";
Mol. Cell. Biol. 29:758-770(2009).
[21]
PHOSPHORYLATION AT SER-192 BY TLK2.
PubMed=20016786; DOI=10.1371/journal.pone.0008328;
Pilyugin M., Demmers J., Verrijzer C.P., Karch F., Moshkin Y.M.;
"Phosphorylation-mediated control of histone chaperone ASF1 levels by
Tousled-like kinases.";
PLoS ONE 4:E8328-E8328(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
INTERACTION WITH CDAN1, AND IDENTIFICATION IN A COMPLEX WITH CDNA1;
ASF1B; IPO4; HISTONES H3.2 AND H4.
PubMed=22407294; DOI=10.1038/emboj.2012.55;
Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.;
"Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1
function in S-phase histone supply.";
EMBO J. 31:2013-2023(2012).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
INTERACTION WITH CREBBP.
PubMed=24616510; DOI=10.1073/pnas.1319122111;
Das C., Roy S., Namjoshi S., Malarkey C.S., Jones D.N.,
Kutateladze T.G., Churchill M.E., Tyler J.K.;
"Binding of the histone chaperone ASF1 to the CBP bromodomain promotes
histone acetylation.";
Proc. Natl. Acad. Sci. U.S.A. 111:E1072-E1081(2014).
[29]
STRUCTURE BY NMR OF 1-156, INTERACTION WITH HISTONE H3 AND HISTONE H4,
AND MUTAGENESIS OF ASP-54; VAL-94 AND ARG-108.
PubMed=15840725; DOI=10.1073/pnas.0500149102;
Mousson F., Lautrette A., Thuret J.-Y., Agez M., Courbeyrette R.,
Amigues B., Becker E., Neumann J.-M., Guerois R., Mann C.,
Ochsenbein F.;
"Structural basis for the interaction of Asf1 with histone H3 and its
functional implications.";
Proc. Natl. Acad. Sci. U.S.A. 102:5975-5980(2005).
[30]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-157 IN COMPLEX WITH HIRA,
INTERACTION WITH CHAF1B, AND MUTAGENESIS OF ASP-37.
PubMed=16980972; DOI=10.1038/nsmb1147;
Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A.,
Dunbrack R., Adams P.D., Marmorstein R.;
"Structure of a human ASF1a-HIRA complex and insights into specificity
of histone chaperone complex assembly.";
Nat. Struct. Mol. Biol. 13:921-929(2006).
-!- FUNCTION: Histone chaperone that facilitates histone deposition
and histone exchange and removal during nucleosome assembly and
disassembly. Cooperates with chromatin assembly factor 1 (CAF-1)
to promote replication-dependent chromatin assembly and with HIRA
to promote replication-independent chromatin assembly. Required
for the formation of senescence-associated heterochromatin foci
(SAHF) and efficient senescence-associated cell cycle exit.
{ECO:0000269|PubMed:10759893, ECO:0000269|PubMed:11897662,
ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14718166,
ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15664198,
ECO:0000269|PubMed:16151251}.
-!- SUBUNIT: Interacts with histone H3 (including both histone H3.1
and H3.3) and histone H4. Interacts with the CHAF1A, CHAF1B and
RBBP4 subunits of the CAF-1 complex. Interacts with CABIN1, HAT1,
HIRA, NASP, TAF1, TLK1, TLK2 and UBN1. Interacts with CDAN1. Found
in a cytosolic complex with CDAN1, ASF1B, IPO4 and histones H3.1
and H4. Interacts with CREBBP. {ECO:0000269|PubMed:10759893,
ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:11897662,
ECO:0000269|PubMed:12093919, ECO:0000269|PubMed:12842904,
ECO:0000269|PubMed:14680630, ECO:0000269|PubMed:14718166,
ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15664198,
ECO:0000269|PubMed:15840725, ECO:0000269|PubMed:16980972,
ECO:0000269|PubMed:19029251, ECO:0000269|PubMed:22407294,
ECO:0000269|PubMed:24616510}.
-!- INTERACTION:
P03372:ESR1; NbExp=2; IntAct=EBI-749553, EBI-78473;
P02309:HHF2 (xeno); NbExp=3; IntAct=EBI-749553, EBI-8113;
P54198:HIRA; NbExp=7; IntAct=EBI-749553, EBI-372342;
P68431:HIST1H3D; NbExp=4; IntAct=EBI-749553, EBI-79722;
P62805:HIST2H4B; NbExp=14; IntAct=EBI-749553, EBI-302023;
P79522:PRR3; NbExp=5; IntAct=EBI-749553, EBI-2803328;
Q12161:PSH1 (xeno); NbExp=3; IntAct=EBI-749553, EBI-34372;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11897662,
ECO:0000269|PubMed:12842904}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:12842904}.
-!- PTM: Phosphorylated by TLK1 and TLK2. Highly phosphorylated in S-
phase and at lower levels in M-phase. TLK2-mediated
phosphorylation at Ser-192 prevents proteasome-dependent
degradation. {ECO:0000269|PubMed:11470414,
ECO:0000269|PubMed:20016786}.
-!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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EMBL; AB028628; BAA96542.1; -; mRNA.
EMBL; AF279306; AAK82972.1; -; mRNA.
EMBL; AF151856; AAD34093.1; -; mRNA.
EMBL; AF161495; AAF29110.1; -; mRNA.
EMBL; AL050261; CAB43363.1; -; mRNA.
EMBL; AK025738; BAB15228.1; -; mRNA.
EMBL; CR457347; CAG33628.1; -; mRNA.
EMBL; AC022098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010878; AAH10878.1; -; mRNA.
CCDS; CCDS47469.1; -.
PIR; T08661; T08661.
RefSeq; NP_054753.1; NM_014034.2.
UniGene; Hs.292316; -.
PDB; 1TEY; NMR; -; A=1-156.
PDB; 2I32; X-ray; 2.70 A; A/B=1-157.
PDB; 2IIJ; NMR; -; A=1-156.
PDB; 2IO5; X-ray; 2.70 A; A=1-172.
PDB; 3AAD; X-ray; 3.30 A; B/D=1-155.
PDB; 5C3I; X-ray; 3.50 A; A/E/I/M/Q/U=1-175.
PDBsum; 1TEY; -.
PDBsum; 2I32; -.
PDBsum; 2IIJ; -.
PDBsum; 2IO5; -.
PDBsum; 3AAD; -.
PDBsum; 5C3I; -.
ProteinModelPortal; Q9Y294; -.
SMR; Q9Y294; -.
BioGrid; 117368; 56.
CORUM; Q9Y294; -.
DIP; DIP-29241N; -.
IntAct; Q9Y294; 38.
MINT; MINT-1385638; -.
STRING; 9606.ENSP00000229595; -.
BindingDB; Q9Y294; -.
ChEMBL; CHEMBL3392950; -.
iPTMnet; Q9Y294; -.
PhosphoSitePlus; Q9Y294; -.
BioMuta; ASF1A; -.
DMDM; 74735206; -.
EPD; Q9Y294; -.
MaxQB; Q9Y294; -.
PaxDb; Q9Y294; -.
PeptideAtlas; Q9Y294; -.
PRIDE; Q9Y294; -.
DNASU; 25842; -.
Ensembl; ENST00000229595; ENSP00000229595; ENSG00000111875.
GeneID; 25842; -.
KEGG; hsa:25842; -.
UCSC; uc011ebn.3; human.
CTD; 25842; -.
DisGeNET; 25842; -.
EuPathDB; HostDB:ENSG00000111875.7; -.
GeneCards; ASF1A; -.
HGNC; HGNC:20995; ASF1A.
HPA; HPA030502; -.
HPA; HPA071495; -.
MIM; 609189; gene.
neXtProt; NX_Q9Y294; -.
OpenTargets; ENSG00000111875; -.
PharmGKB; PA128394636; -.
eggNOG; KOG3265; Eukaryota.
eggNOG; COG5137; LUCA.
GeneTree; ENSGT00390000004692; -.
HOGENOM; HOG000197425; -.
HOVERGEN; HBG105617; -.
InParanoid; Q9Y294; -.
KO; K10753; -.
OMA; FNPFQFE; -.
OrthoDB; EOG091G0K07; -.
PhylomeDB; Q9Y294; -.
TreeFam; TF106429; -.
Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
EvolutionaryTrace; Q9Y294; -.
GeneWiki; ASF1A; -.
GenomeRNAi; 25842; -.
PRO; PR:Q9Y294; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000111875; -.
CleanEx; HS_ASF1A; -.
Genevisible; Q9Y294; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:LIFEdb.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:MGI.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IDA:MGI.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:UniProtKB.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IDA:UniProtKB.
GO; GO:0042692; P:muscle cell differentiation; IEA:Ensembl.
GO; GO:0031936; P:negative regulation of chromatin silencing; NAS:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:MGI.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.60.40.1490; -; 1.
InterPro; IPR006818; ASF1-like.
PANTHER; PTHR12040; PTHR12040; 1.
Pfam; PF04729; ASF1_hist_chap; 1.
SUPFAM; SSF101546; SSF101546; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Chromatin regulator; Complete proteome;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 204 Histone chaperone ASF1A.
/FTId=PRO_0000284012.
REGION 1 156 Interaction with histone H3, CHAF1B, and
HIRA.
REGION 155 204 Required for interaction with HIRA.
MOTIF 31 37 Required for interaction with HIRA.
MOD_RES 192 192 Phosphoserine; by TLK2.
{ECO:0000269|PubMed:20016786}.
MUTAGEN 36 37 ED->AA: Abrogates interaction with HIRA
and induction of senescence-associated
heterochromatin foci.
{ECO:0000269|PubMed:14680630,
ECO:0000269|PubMed:15621527}.
MUTAGEN 37 37 D->A: Abrogates interaction with CHAF1B
and HIRA. {ECO:0000269|PubMed:16980972}.
MUTAGEN 54 54 D->R: Reduces interaction with histone
H3. {ECO:0000269|PubMed:15840725}.
MUTAGEN 62 64 VGP->AAA: Abrogates interaction with HIRA
and induction of senescence-associated
heterochromatin foci.
{ECO:0000269|PubMed:14680630,
ECO:0000269|PubMed:15621527}.
MUTAGEN 94 94 V->R: Abrogates interaction with histone
H3 and histone H4.
{ECO:0000269|PubMed:15840725}.
MUTAGEN 108 108 R->E: Reduces interaction with histone
H3. {ECO:0000269|PubMed:15840725}.
CONFLICT 74 74 F -> I (in Ref. 4; AAF29110).
{ECO:0000305}.
CONFLICT 204 204 M -> I (in Ref. 7; CAG33628).
{ECO:0000305}.
STRAND 3 11 {ECO:0000244|PDB:2I32}.
STRAND 15 17 {ECO:0000244|PDB:2I32}.
STRAND 22 32 {ECO:0000244|PDB:2I32}.
STRAND 34 36 {ECO:0000244|PDB:5C3I}.
STRAND 38 46 {ECO:0000244|PDB:2I32}.
HELIX 51 53 {ECO:0000244|PDB:2I32}.
STRAND 54 62 {ECO:0000244|PDB:2I32}.
STRAND 67 76 {ECO:0000244|PDB:2I32}.
HELIX 81 83 {ECO:0000244|PDB:2I32}.
HELIX 86 89 {ECO:0000244|PDB:2I32}.
STRAND 90 101 {ECO:0000244|PDB:2I32}.
STRAND 104 119 {ECO:0000244|PDB:2I32}.
HELIX 120 124 {ECO:0000244|PDB:2I32}.
HELIX 132 134 {ECO:0000244|PDB:2I32}.
STRAND 135 139 {ECO:0000244|PDB:2I32}.
STRAND 145 148 {ECO:0000244|PDB:2I32}.
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


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