Q9NVP2 (ASF1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone chaperone ASF1B

Alternative name(s):
Anti-silencing function protein 1 homolog B
Short name=hAsf1
Short name=hAsf1b
CCG1-interacting factor A-II
Short name=CIA-II
Short name=hCIA-II

Gene names

Name:

ASF1B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	202 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA. Required for spermatogenesis. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11
Subunit structure	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 HAT1, NASP, TAF1, TLK1 and TLK2. Interacts with CDAN1. Found in a cytosolic complex with CDAN1, ASF1A, IPO4 and histones H3.1 and H4. Ref.1 Ref.2 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.17
Subcellular location	Nucleus Ref.2.
Tissue specificity	Highly expressed in testis and at lower levels in colon, small intestine and thymus. Ref.2
Post-translational modification	Phosphorylated by TLK1 and TLK2. Ref.1 Ref.14
Sequence similarities	Belongs to the ASF1 family.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chaperone Chromatin regulator Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW nucleosome assembly Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromatin Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 202	202	Histone chaperone ASF1B		PRO_0000284015
Regions
	Region	1 – 156	156	Interaction with histone H3 By similarity
	Region	1 – 155	155	Interaction with CHAF1B
Amino acid modifications
	Modified residue	198	1	Phosphoserine; by TLK2 Ref.14
Experimental info
	Mutagenesis	36	1	D → A: Abolishes CDAN1 interaction. Ref.17
	Mutagenesis	37	1	D → A: Abolishes CDAN1 interaction. Ref.17
	Sequence conflict	11	1	V → A in BAA91602. Ref.4
	Sequence conflict	23	1	R → Q in BAD96800. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9NVP2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: BD62F726610E3A70	FASTA	202	22,434
	10 20 30 40 50 60 MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALADDLEW KIIYVGSAES EEFDQILDSV 70 80 90 100 110 120 LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT YHGQEFIRVG YYVNNEYLNP 130 140 150 160 170 180 ELRENPPMKP DFSQLQRNIL ASNPRVTRFH INWDNNMDRL EAIETQDPSL GCGLPLNCTP 190 200 IKGLGLPGCI PGLLPENSMD CI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of human Asf1 chromatin assembly factors as substrates of Tousled-like kinases." Sillje H.H.W., Nigg E.A. Curr. Biol. 11:1068-1073(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TLK1 AND TLK2, PHOSPHORYLATION BY TLK1 AND TLK2.
[2]	"Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis." Umehara T., Horikoshi M. J. Biol. Chem. 278:35660-35667(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HISTONE H3.3; HISTONE H4 AND TAF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Teratocarcinoma.
[5]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis and Uterus.
[8]	"Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway." Mello J.A., Sillje H.H.W., Roche D.M.J., Kirschner D.B., Nigg E.A., Almouzni G. EMBO Rep. 3:329-334(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CHAF1A; CHAF1B AND RBBP4.
[9]	"Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis." Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y. Cell 116:51-61(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN COMPLEXES WITH CHAF1A; CHAF1B; HAT1; HISTONE H3.1; HISTONE H3.3; HISTONE H4; NASP AND RBBP4.
[10]	"Functional conservation and specialization among eukaryotic anti-silencing function 1 histone chaperones." Tamburini B.A., Carson J.J., Adkins M.W., Tyler J.K. Eukaryot. Cell 4:1583-1590(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Human Asf1 regulates the flow of S phase histones during replicational stress." Groth A., Ray-Gallet D., Quivy J.-P., Lukas J., Bartek J., Almouzni G. Mol. Cell 17:301-311(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HISTONE H3.1; HISTONE H3.3 AND HISTONE H4.
[12]	"Asf1 is required for viability and chromatin assembly during DNA replication in vertebrate cells." Sanematsu F., Takami Y., Barman H.K., Fukagawa T., Ono T., Shibahara K., Nakayama T. J. Biol. Chem. 281:13817-13827(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHAF1B; HISTONE H3 AND HISTONE H4.
[13]	"Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly." Tang Y., Poustovoitov M.V., Zhao K., Garfinkel M., Canutescu A., Dunbrack R., Adams P.D., Marmorstein R. Nat. Struct. Mol. Biol. 13:921-929(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHAF1B.
[14]	"Phosphorylation-mediated control of histone chaperone ASF1 levels by Tousled-like kinases." Pilyugin M., Demmers J., Verrijzer C.P., Karch F., Moshkin Y.M. PLoS ONE 4:E8328-E8328(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-198 BY TLK2.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1 function in S-phase histone supply." Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A. EMBO J. 31:2013-2023(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDAN1, IDENTIFICATION IN A COMPLEX WITH CDNA1; ASF1A; IPO4; HISTONES H3.2 AND H4, MUTAGENESIS OF ASP-36 AND ASP-37.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF279307 mRNA. Translation: AAK82973.1. AB104486 mRNA. Translation: BAC87709.1. CR457235 mRNA. Translation: CAG33516.1. AK001288 mRNA. Translation: BAA91602.1. AK001466 mRNA. Translation: BAA91708.1. AK223080 mRNA. Translation: BAD96800.1. AC022098 Genomic DNA. No translation available. BC007726 mRNA. Translation: AAH07726.1. BC010014 mRNA. Translation: AAH10014.1. BC036521 mRNA. Translation: AAH36521.1.
IPI	IPI00041127.
RefSeq	NP_060624.1. NM_018154.2.
UniGene	Hs.26516.
3D structure databases
HSSP	HSSP built from PDB template 1TEY based on UniProtKB Q9Y294.
ProteinModelPortal	Q9NVP2.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29242N.
IntAct	Q9NVP2. 3 interactions.
STRING	9606.ENSP00000263382.
PTM databases
PhosphoSite	Q9NVP2.
Polymorphism databases
DMDM	74734533.
Proteomic databases
PaxDb	Q9NVP2.
PeptideAtlas	Q9NVP2.
PRIDE	Q9NVP2.
Protocols and materials databases
DNASU	55723.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263382; ENSP00000263382; ENSG00000105011.
GeneID	55723.
KEGG	hsa:55723.
UCSC	uc002mye.3. human.
Organism-specific databases
CTD	55723.
GeneCards	GC19M014230.
HGNC	HGNC:20996. ASF1B.
MIM	609190. gene.
neXtProt	NX_Q9NVP2.
PharmGKB	PA134931112.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5137.
HOGENOM	HOG000197425.
HOVERGEN	HBG105617.
InParanoid	Q9NVP2.
KO	K10753.
OMA	FIFQADA.
OrthoDB	EOG4R7VBQ.
PhylomeDB	Q9NVP2.
Gene expression databases
ArrayExpress	Q9NVP2.
Bgee	Q9NVP2.
CleanEx	HS_ASF1B.
Genevestigator	Q9NVP2.
Family and domain databases
Gene3D	2.60.40.1490. 1 hit.
InterPro	IPR006818. Histone_chaperone_ASF1-like. [Graphical view]
PANTHER	PTHR12040. PTHR12040. 1 hit.
Pfam	PF04729. ASF1_hist_chap. 1 hit. [Graphical view]
SUPFAM	SSF101546. Anti-silence. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	ASF1B. human.
GenomeRNAi	55723.
NextBio	60631.
SOURCE	Search...

Entry information

Entry name

ASF1B_HUMAN

Accession

Primary (citable) accession number: Q9NVP2
Secondary accession number(s): Q53G51, Q9NVZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.