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Q9Y294 (ASF1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone chaperone ASF1A
Alternative name(s):
Anti-silencing function protein 1 homolog A
Short name=hAsf1
Short name=hAsf1a
CCG1-interacting factor A
Short name=CIA
Short name=hCIA
Gene names
Name:ASF1A
ORF Names:CGI-98, HSPC146
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. Ref.1 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

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 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. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.20 Ref.25 Ref.26 Ref.27

Subcellular location

Nucleus Ref.10 Ref.13.

Tissue specificity

Ubiquitously expressed. Ref.13

Post-translational modification

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. Ref.2 Ref.21

Sequence similarities

Belongs to the ASF1 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionChaperone
Chromatin regulator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from direct assay Ref.10. Source: MGI

DNA replication-dependent nucleosome assembly

Inferred from direct assay Ref.14. Source: UniProt

DNA replication-independent nucleosome assembly

Inferred from direct assay Ref.14. Source: UniProt

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of chromatin silencing

Non-traceable author statement Ref.1. Source: UniProtKB

nucleosome assembly

Inferred from direct assay Ref.10. Source: MGI

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear chromatin

Inferred from direct assay Ref.14. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

protein complex

Inferred from direct assay Ref.14. Source: UniProt

   Molecular_functionchromatin binding

Non-traceable author statement Ref.1. Source: UniProtKB

histone binding

Inferred from direct assay Ref.1. Source: MGI

protein binding

Inferred from physical interaction Ref.25. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ESR1P033722EBI-749553,EBI-78473

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 204204Histone chaperone ASF1A
PRO_0000284012

Regions

Region1 – 156156Interaction with histone H3, CHAF1B, and HIRA
Region155 – 20450Required for interaction with HIRA
Motif31 – 377Required for interaction with HIRA

Amino acid modifications

Modified residue1921Phosphoserine; by TLK2 Ref.21

Experimental info

Mutagenesis36 – 372ED → AA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci. Ref.27
Mutagenesis371D → A: Abrogates interaction with CHAF1B and HIRA. Ref.27
Mutagenesis541D → R: Reduces interaction with histone H3. Ref.26
Mutagenesis62 – 643VGP → AAA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci. Ref.12 Ref.15
Mutagenesis941V → R: Abrogates interaction with histone H3 and histone H4. Ref.26
Mutagenesis1081R → E: Reduces interaction with histone H3. Ref.26
Sequence conflict741F → I in AAF29110. Ref.4
Sequence conflict2041M → I in CAG33628. Ref.7

Secondary structure

........................... 204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y294 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 9819D531D3A9FC68

FASTA20422,969
        10         20         30         40         50         60 
MAKVQVNNVV VLDNPSPFYN PFQFEITFEC IEDLSEDLEW KIIYVGSAES EEYDQVLDSV 

        70         80         90        100        110        120 
LVGPVPAGRH MFVFQADAPN PGLIPDADAV GVTVVLITCT YRGQEFIRVG YYVNNEYTET 

       130        140        150        160        170        180 
ELRENPPVKP DFSKLQRNIL ASNPRVTRFH INWEDNTEKL EDAESSNPNL QSLLSTDALP 

       190        200 
SASKGWSTSE NSLNVMLESH MDCM 

« Hide

References

« Hide 'large scale' references
[1]"A human homologue of yeast anti-silencing factor has histone chaperone activity."
Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M.
Genes Cells 5:221-233(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HISTONE H3.3; HISTONE H4 AND TAF1.
[2]"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.
[3]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
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. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[5]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"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. expand/collapse author list , 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].
[7]"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].
[8]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Placenta.
[10]"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, SUBCELLULAR LOCATION.
[11]"Identification and characterization of CIA/ASF1 as an interactor of bromodomains associated with TFIID."
Chimura T., Kuzuhara T., Horikoshi M.
Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAF1.
[12]"Structure and function of the conserved core of histone deposition protein Asf1."
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.
Curr. Biol. 13:2148-2158(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIRA, MUTAGENESIS OF 36-GLU-ASP-37 AND 62-VAL--PRO-64.
[13]"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: FUNCTION, INTERACTION WITH HISTONE H3.3; HISTONE H4 AND TAF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[14]"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 CABIN1; CHAF1A; CHAF1B; HAT1; HIRA; HISTONE H3.1; HISTONE H3.3; HISTONE H4; NASP; RBBP4 AND UBN1.
[15]"Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA."
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.
Dev. Cell 8:19-30(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HIRA, MUTAGENESIS OF 36-GLU-ASP-37 AND 62-VAL--PRO-64.
[16]"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.
[17]"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; HISTONE H4; NASP AND RBBP4.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Human UBN1 is an ortholog of yeast Hpc2p and has an essential role in the HIRA/ASF1a chromatin-remodeling pathway in senescent cells."
Banumathy G., Somaiah N., Zhang R., Tang Y., Hoffmann J., Andrake M., Ceulemans H., Schultz D., Marmorstein R., Adams P.D.
Mol. Cell. Biol. 29:758-770(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBN1.
[21]"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-192 BY TLK2.
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"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].
[24]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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; ASF1B; IPO4; HISTONES H3.2 AND H4.
[26]"Structural basis for the interaction of Asf1 with histone H3 and its functional implications."
Mousson F., Lautrette A., Thuret J.-Y., Agez M., Courbeyrette R., Amigues B., Becker E., Neumann J.-M., Guerois R., Mann C., Ochsenbein F.
Proc. Natl. Acad. Sci. U.S.A. 102:5975-5980(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-156, INTERACTION WITH HISTONE H3 AND HISTONE H4, MUTAGENESIS OF ASP-54; VAL-94 AND ARG-108.
[27]"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: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-157 IN COMPLEX WITH HIRA, INTERACTION WITH CHAF1B, MUTAGENESIS OF ASP-37.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028628 mRNA. Translation: BAA96542.1.
AF279306 mRNA. Translation: AAK82972.1.
AF151856 mRNA. Translation: AAD34093.1.
AF161495 mRNA. Translation: AAF29110.1.
AL050261 mRNA. Translation: CAB43363.1.
AK025738 mRNA. Translation: BAB15228.1.
CR457347 mRNA. Translation: CAG33628.1.
AC022098 Genomic DNA. No translation available.
BC010878 mRNA. Translation: AAH10878.1.
CCDSCCDS47469.1.
PIRT08661.
RefSeqNP_054753.1. NM_014034.2.
UniGeneHs.292316.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TEYNMR-A1-156[»]
2I32X-ray2.70A/B1-157[»]
2IIJNMR-A1-156[»]
2IO5X-ray2.70A1-172[»]
3AADX-ray3.30B/D1-155[»]
ProteinModelPortalQ9Y294.
SMRQ9Y294. Positions 1-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117368. 33 interactions.
DIPDIP-29241N.
IntActQ9Y294. 13 interactions.
MINTMINT-1385638.
STRING9606.ENSP00000229595.

PTM databases

PhosphoSiteQ9Y294.

Polymorphism databases

DMDM74735206.

Proteomic databases

MaxQBQ9Y294.
PaxDbQ9Y294.
PRIDEQ9Y294.

Protocols and materials databases

DNASU25842.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229595; ENSP00000229595; ENSG00000111875.
GeneID25842.
KEGGhsa:25842.
UCSCuc011ebn.2. human.

Organism-specific databases

CTD25842.
GeneCardsGC06P119215.
HGNCHGNC:20995. ASF1A.
MIM609189. gene.
neXtProtNX_Q9Y294.
PharmGKBPA128394636.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5137.
HOGENOMHOG000197425.
HOVERGENHBG105617.
InParanoidQ9Y294.
KOK10753.
OMAWRLIYVS.
OrthoDBEOG7B5WWX.
PhylomeDBQ9Y294.
TreeFamTF106429.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

BgeeQ9Y294.
CleanExHS_ASF1A.
GenevestigatorQ9Y294.

Family and domain databases

Gene3D2.60.40.1490. 1 hit.
InterProIPR006818. Histone_chaperone_ASF1-like.
[Graphical view]
PANTHERPTHR12040. PTHR12040. 1 hit.
PfamPF04729. ASF1_hist_chap. 1 hit.
[Graphical view]
SUPFAMSSF101546. SSF101546. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y294.
GeneWikiASF1A.
GenomeRNAi25842.
NextBio47163.
PROQ9Y294.
SOURCESearch...

Entry information

Entry nameASF1A_HUMAN
AccessionPrimary (citable) accession number: Q9Y294
Secondary accession number(s): Q6IA08, Q9P014
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM