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UniProtKB/Swiss-Prot entry Q9NVP2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ASF1B_HUMAN
Primary accession number Q9NVP2
Secondary accession numbers Q53G51 Q9NVZ0
Integrated into Swiss-Prot on April 17, 2007
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 52)
Name and origin of the protein
Protein name Histone chaperone ASF1B
Synonyms Anti-silencing function protein 1 homolog B
hAsf1
hAsf1b
CCG1-interacting factor A-II
CIA-II
hCIA-II
Gene name
Name: ASF1B
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TLK1 AND TLK2, AND PHOSPHORYLATION BY TLK1 AND TLK2.
DOI=10.1016/S0960-9822(01)00298-6; PubMed=11470414 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HISTONE H3.3; HISTONE H4 AND TAF1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M303549200; PubMed=12842904 [NCBI, ExPASy, EBI, Israel, Japan]
Umehara T., Horikoshi M.;
"Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis.";
J. Biol. Chem. 278:35660-35667(2003).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
FUNCTION, AND INTERACTION WITH CHAF1A; CHAF1B AND RBBP4.
DOI=10.1093/embo-reports/kvf068; PubMed=11897662 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN COMPLEXES WITH CHAF1A; CHAF1B; HAT1; HISTONE H3.1; HISTONE H3.3; HISTONE H4; NASP AND RBBP4.
DOI=10.1016/S0092-8674(03)01064-X; PubMed=14718166 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
FUNCTION.
DOI=10.1128/EC.4.9.1583-1590.2005; PubMed=16151251 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
FUNCTION, AND INTERACTION WITH HISTONE H3.1; HISTONE H3.3 AND HISTONE H4.
DOI=10.1016/j.molcel.2004.12.018; PubMed=15664198 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
INTERACTION WITH CHAF1B; HISTONE H3 AND HISTONE H4.
DOI=10.1074/jbc.M511590200; PubMed=16537536 [NCBI, ExPASy, EBI, Israel, Japan]
Sanematsu F., Takami Y., Barman H.K., Fukagawa T., Ono T., Shibahara K., Nakayama T.;
"Asf1 is required for viability and chromatin assembly during DNA replication in vertebrate cells.";
J. Biol. Chem. 281:13817-13827(2006).
[12]
INTERACTION WITH CHAF1B.
DOI=10.1038/nsmb1147; PubMed=16980972 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF279307; AAK82973.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB104486; BAC87709.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457235; CAG33516.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001288; BAA91602.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001466; BAA91708.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223080; BAD96800.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007726; AAH07726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010014; AAH10014.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036521; AAH36521.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060624.1; -.
UniGene Hs.26516
3D structure databases
HSSP P32447; 1ROC. [HSSP ENTRY / PDB]
SMR Q9NVP2; 1-154.
ModBase Q9NVP2.
Protein-protein interaction databases
IntAct Q9NVP2; -.
Organism-specific databases
HGNC HGNC:20996; ASF1B.
GenAtlas ASF1B.
MIM 609190; gene. [NCBI / EBI]
PharmGKB PA134931112; -.
GeneCards Q9NVP2.
Gene expression databases
ArrayExpress Q9NVP2; -.
CleanEx HS_ASF1B; -.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR006818; Anti-silence.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.1490; Anti-silence; 1.
PANTHER PTHR12040; Anti-silence; 1.
Pfam PF04729; Anti-silence; 1.
Pfam graphical view of domain structure.
BLOCKS Q9NVP2.
Proteomic databases
PeptideAtlas Q9NVP2; -.
Genome annotation databases
Ensembl ENSG00000105011; Homo sapiens. [Contig view]
GeneID 55723; -.
KEGG hsa:55723; -.
Phylogenomic databases
HOVERGEN Q9NVP2; -.
Other
SOURCE ASF1B; Homo sapiens.
ProtoNet Q9NVP2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chaperone; Chromatin regulator; Developmental protein; Differentiation; Nucleus; Phosphoprotein; Spermatogenesis; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   202  202     Histone chaperone ASF1B. PRO_0000284015
REGION   1   156  156     Interaction with histone H3 (By similarity). 
REGION   1   155  155     Interaction with CHAF1B. 
CONFLICT   11    11        V -> A (in Ref. 4; BAA91602). 
CONFLICT   23    23        R -> Q (in Ref. 5; BAD96800). 
Sequence information
Length: 202 AA [This is the length of the unprocessed precursor] Molecular weight: 22434 Da [This is the MW of the unprocessed precursor] CRC64: BD62F726610E3A70 [This is a checksum on the sequence]
        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 

Q9NVP2 in FASTA format

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