Q9Y294 (ASF1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	204 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 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.19 Ref.24 Ref.25 Ref.26
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.20
Sequence similarities	Belongs to the ASF1 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chaperone Chromatin regulator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from direct assay Ref.10. Source: MGI chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW muscle cell differentiation Inferred from electronic annotation. Source: Compara 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: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	chromatin binding Non-traceable author statement Ref.1. Source: UniProtKB histone binding Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESR1	P03372	2	EBI-749553,EBI-78473

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 204

204

Histone chaperone ASF1A

PRO_0000284012

Regions

Region

1 – 156

156

Interaction with histone H3, CHAF1B, and HIRA

Region

155 – 204

50

Required for interaction with HIRA

Motif

31 – 37

7

Required for interaction with HIRA

Amino acid modifications

Modified residue

192

1

Phosphoserine; by TLK2 Ref.20

Experimental info

Mutagenesis

36 – 37

2

ED → AA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci. Ref.26

Mutagenesis

37

1

D → A: Abrogates interaction with CHAF1B and HIRA. Ref.26

Mutagenesis

54

1

D → R: Reduces interaction with histone H3. Ref.25

Mutagenesis

62 – 64

3

VGP → AAA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci. Ref.12 Ref.15

Mutagenesis

94

1

V → R: Abrogates interaction with histone H3 and histone H4. Ref.25

Mutagenesis

108

1

R → E: Reduces interaction with histone H3. Ref.25

Sequence conflict

74

1

F → I in AAF29110. Ref.4

Sequence conflict

204

1

M → I in CAG33628. Ref.7

Secondary structure

1

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204

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Beta strand

15 – 17

3

Beta strand

22 – 32

11

Beta strand

38 – 46

9

Helix

51 – 53

3

Beta strand

54 – 62

9

Beta strand

67 – 76

10

Helix

81 – 83

3

Helix

86 – 89

4

Beta strand

90 – 101

12

Beta strand

104 – 119

16

Helix

120 – 124

5

Helix

132 – 134

3

Beta strand

135 – 139

5

Beta strand

145 – 148

4

Sequences

	Sequence		Length	Mass (Da)
	Q9Y294 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 9819D531D3A9FC68	FASTA	204	22,969
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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]	"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.
[20]	"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.
[21]	"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.
[22]	"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].
[23]	"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].
[24]	"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.
[25]	"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.
[26]	"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.

IPI

IPI00292168.

PIR

T08661.

RefSeq

NP_054753.1. NM_014034.2.

UniGene

Hs.292316.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TEY	NMR	-	A	1-156	[»]
2I32	X-ray	2.70	A/B	1-157	[»]
2IIJ	NMR	-	A	1-156	[»]
2IO5	X-ray	2.70	A	1-172	[»]
3AAD	X-ray	3.30	B/D	1-155	[»]

ProteinModelPortal

Q9Y294.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29241N.

IntAct

Q9Y294. 8 interactions.

MINT

MINT-1385638.

STRING

9606.ENSP00000229595.

PTM databases

PhosphoSite

Q9Y294.

Polymorphism databases

DMDM

74735206.

Proteomic databases

PaxDb

Q9Y294.

PRIDE

Q9Y294.

Protocols and materials databases

DNASU

25842.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000229595; ENSP00000229595; ENSG00000111875.

GeneID

25842.

KEGG

hsa:25842.

UCSC

uc011ebn.2. human.

Organism-specific databases

CTD

25842.

GeneCards

GC06P119215.

HGNC

HGNC:20995. ASF1A.

MIM

609189. gene.

neXtProt

NX_Q9Y294.

PharmGKB

PA128394636.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5137.

HOGENOM

HOG000197425.

HOVERGEN

HBG105617.

InParanoid

Q9Y294.

KO

K10753.

OMA

ADPPDVS.

OrthoDB

EOG4R7VBQ.

Gene expression databases

ArrayExpress

Q9Y294.

Bgee

Q9Y294.

CleanEx

HS_ASF1A.

Genevestigator

Q9Y294.

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

EvolutionaryTrace

Q9Y294.

GenomeRNAi

25842.

NextBio

47163.

SOURCE

Search...

Entry information

Entry name

ASF1A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 111 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.