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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.
08-MAY-2019, entry version 164.
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:
Q13112:CHAF1B; NbExp=2; IntAct=EBI-749553, EBI-1052944;
P03372:ESR1; NbExp=2; IntAct=EBI-749553, EBI-78473;
P54198:HIRA; NbExp=13; IntAct=EBI-749553, EBI-372342;
P68431:HIST1H3D; NbExp=9; IntAct=EBI-749553, EBI-79722;
P62805:HIST2H4B; NbExp=19; IntAct=EBI-749553, EBI-302023;
P49736:MCM2; NbExp=7; IntAct=EBI-749553, EBI-374819;
P79522:PRR3; NbExp=5; IntAct=EBI-749553, EBI-2803328;
-!- 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.
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; -.
SMR; Q9Y294; -.
BioGrid; 117368; 85.
CORUM; Q9Y294; -.
DIP; DIP-29241N; -.
IntAct; Q9Y294; 40.
MINT; Q9Y294; -.
STRING; 9606.ENSP00000229595; -.
BindingDB; Q9Y294; -.
ChEMBL; CHEMBL3392950; -.
iPTMnet; Q9Y294; -.
PhosphoSitePlus; Q9Y294; -.
BioMuta; ASF1A; -.
DMDM; 74735206; -.
EPD; Q9Y294; -.
jPOST; Q9Y294; -.
MaxQB; Q9Y294; -.
PaxDb; Q9Y294; -.
PeptideAtlas; Q9Y294; -.
PRIDE; Q9Y294; -.
ProteomicsDB; 85702; -.
DNASU; 25842; -.
Ensembl; ENST00000229595; ENSP00000229595; ENSG00000111875.
GeneID; 25842; -.
KEGG; hsa:25842; -.
UCSC; uc011ebn.3; human.
CTD; 25842; -.
DisGeNET; 25842; -.
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; -.
InParanoid; Q9Y294; -.
KO; K10753; -.
OMA; YADPEMR; -.
OrthoDB; 266497at2759; -.
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; Expressed in 230 organ(s), highest expression level in oocyte.
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:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:MGI.
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.
Gene3D; 2.60.40.1490; -; 1.
InterPro; IPR006818; ASF1-like.
InterPro; IPR036747; ASF1-like_sf.
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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Pathways :
WP1624: Bacterial secretion system
WP1983: Splicing factor NOVA regulated synpatic proteins
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1689: Porphyrin and chlorophyll metabolism
WP2369: Histone modifications
WP1693: Purine metabolism
WP300: Histone modifications
WP1650: Fluorobenzoate degradation
WP211: BMP signaling pathway
WP1049: G Protein Signaling Pathways
WP1659: Glycine, serine and threonine metabolism
WP2203: TSLP Signaling Pathway
WP1206: Signaling of Hepatocyte Growth Factor Receptor
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WP346: Protein Modifications
WP1888: Post-translational protein modification
WP525: Mitochondrial Unfolded-Protein Response
WP1665: Limonene and pinene degradation
WP2292: Chemokine signaling pathway
WP1438: Influenza A virus infection
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1531: Vitamin D synthesis
WP1909: Signal regulatory protein (SIRP) family interactions
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1675: Nitrogen metabolism

Related Genes :
[ASF1A CGI-98 HSPC146] Histone chaperone ASF1A (Anti-silencing function protein 1 homolog A) (hAsf1) (hAsf1a) (CCG1-interacting factor A) (CIA) (hCIA)
[ASF1B] Histone chaperone ASF1B (Anti-silencing function protein 1 homolog B) (hAsf1) (hAsf1b) (CCG1-interacting factor A-II) (CIA-II) (hCIA-II)
[TAF1 BA2R CCG1 CCGS TAF2A] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[ASF1A SGA2 SP7 At1g66740 F4N21.13] Probable histone chaperone ASF1A (Anti-silencing function protein 1-like protein a) (Anti-silencing function 1a protein) (S-locus protein 7) (AtSP7) (Silencing group A protein 2)
[ASF1 CIA1 YJL115W J0755] Histone chaperone ASF1 (Anti-silencing function protein 1) (yASF1)
[TAF1 CCG1] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[Taf1 Ccg1] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[ASF1B SGA01 SGA1 At5g38110 F16F17.110] Histone chaperone ASF1B (Anti-silencing function protein 1-like protein b) (Anti-silencing function 1b protein) (Silencing group A protein 1)
[asf1aa asf1 asf1a] Histone chaperone asf1a-A (Anti-silencing function protein 1 homolog) (XAsf1) (Anti-silencing function protein 1 homolog A-A)
[HIST1H3A H3FA; HIST1H3B H3FL; HIST1H3C H3FC; HIST1H3D H3FB; HIST1H3E H3FD; HIST1H3F H3FI; HIST1H3G H3FH; HIST1H3H H3FK; HIST1H3I H3FF; HIST1H3J H3FJ] Histone H3.1 (Histone H3/a) (Histone H3/b) (Histone H3/c) (Histone H3/d) (Histone H3/f) (Histone H3/h) (Histone H3/i) (Histone H3/j) (Histone H3/k) (Histone H3/l)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[HIST2H3A; HIST2H3C H3F2 H3FM; HIST2H3D] Histone H3.2 (Histone H3/m) (Histone H3/o)
[HIST1H4A H4/A H4FA; HIST1H4B H4/I H4FI; HIST1H4C H4/G H4FG; HIST1H4D H4/B H4FB; HIST1H4E H4/J H4FJ; HIST1H4F H4/C H4FC; HIST1H4H H4/H H4FH; HIST1H4I H4/M H4FM; HIST1H4J H4/E H4FE; HIST1H4K H4/D H4FD; HIST1H4L H4/K H4FK; HIST2H4A H4/N H4F2 H4FN HIST2H4; HIST2H4B H4/O H4FO; HIST4H4] Histone H4
[SETD2 HIF1 HYPB KIAA1732 KMT3A SET2 HSPC069] Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43) (HIF-1) (Huntingtin yeast partner B) (Huntingtin-interacting protein 1) (HIP-1) (Huntingtin-interacting protein B) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) (hSET2) (p231HBP)
[asf-1 NCU09436] Histone chaperone asf-1 (Anti-silencing function protein 1)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[KMT2B HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7] Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.43) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)
[H2AFY MACROH2A1] Core histone macro-H2A.1 (Histone macroH2A1) (mH2A1) (Histone H2A.y) (H2A/y) (Medulloblastoma antigen MU-MB-50.205)
[Atrx Hp1bp2 Xnp] Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (HP1 alpha-interacting protein) (HP1-BP38 protein) (Heterochromatin protein 2) (X-linked nuclear protein)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[HIRA DGCR1 HIR TUPLE1] Protein HIRA (TUP1-like enhancer of split protein 1)
[DNAJB11 EDJ ERJ3 HDJ9 PSEC0121 UNQ537/PRO1080] DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (DnaJ protein homolog 9) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (HEDJ) (Human DnaJ protein 9) (hDj-9) (PWP1-interacting protein 4)
[Hist1h3b H3-53 H3.2 H3b; Hist1h3c H3-143; Hist1h3d H3-B; Hist1h3e H3-F; Hist1h3f H3.2-221 H3f; Hist2h3b H3.2-616; Hist2h3c1 H3.2-615 Hist2h3ca1; Hist2h3c2 H3.2-614 Hist2h3ca2] Histone H3.2
[MCM2 BM28 CCNL1 CDCL1 KIAA0030] DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2 homolog) (Nuclear protein BM28)
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[PRMT5 HRMT1L5 IBP72 JBP1 SKB1] Protein arginine N-methyltransferase 5 (EC 2.1.1.320) (72 kDa ICln-binding protein) (Histone-arginine N-methyltransferase PRMT5) (Jak-binding protein 1) (Shk1 kinase-binding protein 1 homolog) (SKB1 homolog) (SKB1Hs) [Cleaved into: Protein arginine N-methyltransferase 5, N-terminally processed]
[ARID1A BAF250 BAF250A C1orf4 OSA1 SMARCF1] AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (B120) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (hOSA1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1) (hELD)
[Trim28 Kap1 Krip1 Tif1b] Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-A-interacting protein) (KRIP-1) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)
[CUL4A] Cullin-4A (CUL-4A)

Bibliography :