ASF1B_HUMAN
ID ASF1B_HUMAN Reviewed; 202 AA.
AC Q9NVP2; Q53G51; Q9NVZ0;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Histone chaperone ASF1B {ECO:0000305};
DE AltName: Full=Anti-silencing function protein 1 homolog B {ECO:0000303|PubMed:11470414};
DE Short=hAsf1 {ECO:0000303|PubMed:11470414};
DE Short=hAsf1b {ECO:0000303|PubMed:11470414};
DE AltName: Full=CCG1-interacting factor A-II {ECO:0000303|PubMed:12842904};
DE Short=CIA-II {ECO:0000303|PubMed:12842904};
DE Short=hCIA-II {ECO:0000303|PubMed:12842904};
GN Name=ASF1B {ECO:0000303|PubMed:11470414, ECO:0000312|HGNC:HGNC:20996};
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HISTONE H3.3;
RP HISTONE H4 AND TAF1, SUBCELLULAR 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis, and Uterus;
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 [8]
RP FUNCTION, AND INTERACTION WITH CHAF1A; CHAF1B AND RBBP4.
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 [9]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN
RP COMPLEXES WITH CHAF1A; CHAF1B; HAT1; HISTONE H3.1; HISTONE H3.3; HISTONE
RP H4; NASP AND RBBP4.
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 [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH HISTONE H3.1; HISTONE H3.3 AND HISTONE H4.
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 [12]
RP INTERACTION WITH CHAF1B; HISTONE H3 AND HISTONE H4.
RX PubMed=16537536; DOI=10.1074/jbc.m511590200;
RA Sanematsu F., Takami Y., Barman H.K., Fukagawa T., Ono T., Shibahara K.,
RA Nakayama T.;
RT "Asf1 is required for viability and chromatin assembly during DNA
RT replication in vertebrate cells.";
RL J. Biol. Chem. 281:13817-13827(2006).
RN [13]
RP INTERACTION WITH CHAF1B.
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).
RN [14]
RP PHOSPHORYLATION AT SER-198 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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH IPO4;
RP HISTONES H3 AND H4.
RX PubMed=20953179; DOI=10.1038/nsmb.1911;
RA Campos E.I., Fillingham J., Li G., Zheng H., Voigt P., Kuo W.H.,
RA Seepany H., Gao Z., Day L.A., Greenblatt J.F., Reinberg D.;
RT "The program for processing newly synthesized histones H3.1 and H4.";
RL Nat. Struct. Mol. Biol. 17:1343-1351(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [18]
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 [19]
RP INTERACTION WITH CDAN1, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX
RP WITH CDNA1; ASF1A; IPO4; HISTONES H3.2 AND H4, AND MUTAGENESIS OF ASP-36
RP AND ASP-37.
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 [20]
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 [21]
RP FUNCTION.
RX PubMed=26527279; DOI=10.1016/j.molcel.2015.08.005;
RA Campos E.I., Smits A.H., Kang Y.H., Landry S., Escobar T.M., Nayak S.,
RA Ueberheide B.M., Durocher D., Vermeulen M., Hurwitz J., Reinberg D.;
RT "Analysis of the histone H3.1 interactome: a suitable chaperone for the
RT right event.";
RL Mol. Cell 60:697-709(2015).
CC -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC histone exchange and removal during nucleosome assembly and disassembly
CC (PubMed:11897662, PubMed:14718166, PubMed:15664198, PubMed:16151251,
CC PubMed:21454524, PubMed:26527279). Cooperates with chromatin assembly
CC factor 1 (CAF-1) to promote replication-dependent chromatin assembly
CC (PubMed:11897662, PubMed:14718166, PubMed:15664198, PubMed:16151251).
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' (H3K9me1)
CC and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in
CC the cytosol (PubMed:20953179, PubMed:21454524, PubMed:26527279). Does
CC not participate in replication-independent nucleosome deposition which
CC is mediated by ASF1A and HIRA (PubMed:11897662, PubMed:14718166,
CC PubMed:15664198, PubMed:16151251). Required for gonad development
CC (PubMed:12842904). {ECO:0000269|PubMed:11897662,
CC ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14718166,
CC ECO:0000269|PubMed:15664198, ECO:0000269|PubMed:16151251,
CC ECO:0000269|PubMed:20953179, ECO:0000269|PubMed:21454524,
CC ECO:0000269|PubMed:26527279}.
CC -!- SUBUNIT: Interacts with histone H3 (including both histone H3.1 and
CC H3.3) and histone H4 (PubMed:12842904, PubMed:14718166,
CC PubMed:15664198, PubMed:16537536). Interacts with the CHAF1A, CHAF1B
CC and RBBP4 subunits of the CAF-1 complex (PubMed:11897662,
CC PubMed:14718166, PubMed:16537536, PubMed:16980972). Interacts with
CC HAT1, NASP and TAF1 (PubMed:12842904). Interacts with CDAN1
CC (PubMed:22407294). Found in a cytosolic complex with IPO4 and histones
CC H3 and H4 (PubMed:20953179. PubMed:21454524, PubMed:22407294).
CC Interacts with CREBBP (PubMed:24616510). {ECO:0000269|PubMed:11897662,
CC ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:14718166,
CC ECO:0000269|PubMed:15664198, ECO:0000269|PubMed:16537536,
CC ECO:0000269|PubMed:16980972, ECO:0000269|PubMed:20953179,
CC ECO:0000269|PubMed:22407294, ECO:0000269|PubMed:24616510}.
CC -!- INTERACTION:
CC Q9NVP2; Q13112: CHAF1B; NbExp=3; IntAct=EBI-1055650, EBI-1052944;
CC Q9NVP2; P84243: H3-3B; NbExp=4; IntAct=EBI-1055650, EBI-120658;
CC Q9NVP2; P54198: HIRA; NbExp=4; IntAct=EBI-1055650, EBI-372342;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12842904}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:22407294}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and at lower levels in
CC colon, small intestine and thymus. {ECO:0000269|PubMed:12842904}.
CC -!- PTM: Phosphorylated by TLK1 and TLK2. {ECO:0000269|PubMed:11470414,
CC ECO:0000269|PubMed:20016786}.
CC -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR EMBL; AF279307; AAK82973.1; -; mRNA.
DR EMBL; AB104486; BAC87709.1; -; mRNA.
DR EMBL; CR457235; CAG33516.1; -; mRNA.
DR EMBL; AK001288; BAA91602.1; -; mRNA.
DR EMBL; AK001466; BAA91708.1; -; mRNA.
DR EMBL; AK223080; BAD96800.1; -; mRNA.
DR EMBL; AC022098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007726; AAH07726.1; -; mRNA.
DR EMBL; BC010014; AAH10014.1; -; mRNA.
DR EMBL; BC036521; AAH36521.1; -; mRNA.
DR CCDS; CCDS12306.1; -.
DR RefSeq; NP_060624.1; NM_018154.2.
DR PDB; 5BNX; X-ray; 2.31 A; D=1-158.
DR PDB; 5BO0; X-ray; 2.91 A; D=1-158.
DR PDBsum; 5BNX; -.
DR PDBsum; 5BO0; -.
DR AlphaFoldDB; Q9NVP2; -.
DR SMR; Q9NVP2; -.
DR BioGRID; 120845; 84.
DR CORUM; Q9NVP2; -.
DR DIP; DIP-29242N; -.
DR IntAct; Q9NVP2; 43.
DR MINT; Q9NVP2; -.
DR STRING; 9606.ENSP00000263382; -.
DR GlyGen; Q9NVP2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVP2; -.
DR MetOSite; Q9NVP2; -.
DR PhosphoSitePlus; Q9NVP2; -.
DR SwissPalm; Q9NVP2; -.
DR BioMuta; ASF1B; -.
DR CPTAC; CPTAC-953; -.
DR EPD; Q9NVP2; -.
DR jPOST; Q9NVP2; -.
DR MassIVE; Q9NVP2; -.
DR MaxQB; Q9NVP2; -.
DR PaxDb; Q9NVP2; -.
DR PeptideAtlas; Q9NVP2; -.
DR PRIDE; Q9NVP2; -.
DR ProteomicsDB; 82838; -.
DR ABCD; Q9NVP2; 1 sequenced antibody.
DR Antibodypedia; 26631; 320 antibodies from 30 providers.
DR DNASU; 55723; -.
DR Ensembl; ENST00000263382.8; ENSP00000263382.3; ENSG00000105011.9.
DR Ensembl; ENST00000672225.1; ENSP00000499863.1; ENSG00000288210.1.
DR GeneID; 55723; -.
DR KEGG; hsa:55723; -.
DR MANE-Select; ENST00000263382.8; ENSP00000263382.3; NM_018154.3; NP_060624.1.
DR UCSC; uc002mye.4; human.
DR CTD; 55723; -.
DR DisGeNET; 55723; -.
DR GeneCards; ASF1B; -.
DR HGNC; HGNC:20996; ASF1B.
DR HPA; ENSG00000105011; Tissue enhanced (lymphoid tissue, testis).
DR MIM; 609190; gene.
DR neXtProt; NX_Q9NVP2; -.
DR OpenTargets; ENSG00000105011; -.
DR PharmGKB; PA134931112; -.
DR VEuPathDB; HostDB:ENSG00000105011; -.
DR eggNOG; KOG3265; Eukaryota.
DR GeneTree; ENSGT00390000004692; -.
DR HOGENOM; CLU_060354_1_2_1; -.
DR InParanoid; Q9NVP2; -.
DR OMA; SCTPVKG; -.
DR OrthoDB; 1334998at2759; -.
DR PhylomeDB; Q9NVP2; -.
DR TreeFam; TF106429; -.
DR PathwayCommons; Q9NVP2; -.
DR SignaLink; Q9NVP2; -.
DR SIGNOR; Q9NVP2; -.
DR BioGRID-ORCS; 55723; 186 hits in 1087 CRISPR screens.
DR ChiTaRS; ASF1B; human.
DR GeneWiki; ASF1B; -.
DR GenomeRNAi; 55723; -.
DR Pharos; Q9NVP2; Tbio.
DR PRO; PR:Q9NVP2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NVP2; protein.
DR Bgee; ENSG00000105011; Expressed in right testis and 95 other tissues.
DR ExpressionAtlas; Q9NVP2; baseline and differential.
DR Genevisible; Q9NVP2; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0006334; P:nucleosome assembly; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 3D-structure; Chaperone; Chromatin regulator; Cytoplasm;
KW Developmental protein; Differentiation; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..202
FT /note="Histone chaperone ASF1B"
FT /id="PRO_0000284015"
FT REGION 1..156
FT /note="Interaction with histone H3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y294"
FT REGION 1..155
FT /note="Interaction with CHAF1B"
FT MOD_RES 198
FT /note="Phosphoserine; by TLK2"
FT /evidence="ECO:0000269|PubMed:20016786"
FT MUTAGEN 36
FT /note="D->A: Abolishes CDAN1 interaction."
FT /evidence="ECO:0000269|PubMed:22407294"
FT MUTAGEN 37
FT /note="D->A: Abolishes CDAN1 interaction."
FT /evidence="ECO:0000269|PubMed:22407294"
FT CONFLICT 11
FT /note="V -> A (in Ref. 4; BAA91602)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="R -> Q (in Ref. 5; BAD96800)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 22..32
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:5BNX"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:5BNX"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5BNX"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 104..117
FT /evidence="ECO:0007829|PDB:5BNX"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:5BNX"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:5BNX"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5BNX"
SQ SEQUENCE 202 AA; 22434 MW; BD62F726610E3A70 CRC64;
MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALADDLEW KIIYVGSAES EEFDQILDSV
LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT YHGQEFIRVG YYVNNEYLNP
ELRENPPMKP DFSQLQRNIL ASNPRVTRFH INWDNNMDRL EAIETQDPSL GCGLPLNCTP
IKGLGLPGCI PGLLPENSMD CI
