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Q9Y294

- ASF1A_HUMAN

UniProt

Q9Y294 - ASF1A_HUMAN

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Protein

Histone chaperone ASF1A

Gene

ASF1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. histone binding Source: MGI

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. DNA repair Source: MGI
  3. DNA replication-dependent nucleosome assembly Source: UniProt
  4. DNA replication-independent nucleosome assembly Source: UniProt
  5. muscle cell differentiation Source: Ensembl
  6. negative regulation of chromatin silencing Source: UniProtKB
  7. nucleosome assembly Source: MGI
  8. osteoblast differentiation Source: Ensembl
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Names & Taxonomyi

Protein namesi
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 namesi
Name:ASF1A
ORF Names:CGI-98, HSPC146
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:20995. ASF1A.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nuclear chromatin Source: UniProt
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. protein complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 372ED → AA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci. 2 Publications
Mutagenesisi37 – 371D → A: Abrogates interaction with CHAF1B and HIRA. 1 Publication
Mutagenesisi54 – 541D → R: Reduces interaction with histone H3. 1 Publication
Mutagenesisi62 – 643VGP → AAA: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci. 2 Publications
Mutagenesisi94 – 941V → R: Abrogates interaction with histone H3 and histone H4. 1 Publication
Mutagenesisi108 – 1081R → E: Reduces interaction with histone H3. 1 Publication

Organism-specific databases

PharmGKBiPA128394636.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Histone chaperone ASF1APRO_0000284012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921Phosphoserine; by TLK21 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y294.
PaxDbiQ9Y294.
PRIDEiQ9Y294.

PTM databases

PhosphoSiteiQ9Y294.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ9Y294.
CleanExiHS_ASF1A.
GenevestigatoriQ9Y294.

Interactioni

Subunit structurei

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. Interacts with CREBBP.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033722EBI-749553,EBI-78473

Protein-protein interaction databases

BioGridi117368. 37 interactions.
DIPiDIP-29241N.
IntActiQ9Y294. 13 interactions.
MINTiMINT-1385638.
STRINGi9606.ENSP00000229595.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Beta strandi15 – 173Combined sources
Beta strandi22 – 3211Combined sources
Beta strandi38 – 469Combined sources
Helixi51 – 533Combined sources
Beta strandi54 – 629Combined sources
Beta strandi67 – 7610Combined sources
Helixi81 – 833Combined sources
Helixi86 – 894Combined sources
Beta strandi90 – 10112Combined sources
Beta strandi104 – 11916Combined sources
Helixi120 – 1245Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi145 – 1484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TEYNMR-A1-156[»]
2I32X-ray2.70A/B1-157[»]
2IIJNMR-A1-156[»]
2IO5X-ray2.70A1-172[»]
3AADX-ray3.30B/D1-155[»]
ProteinModelPortaliQ9Y294.
SMRiQ9Y294. Positions 1-154.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y294.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 156156Interaction with histone H3, CHAF1B, and HIRAAdd
BLAST
Regioni155 – 20450Required for interaction with HIRAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi31 – 377Required for interaction with HIRA

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Phylogenomic databases

eggNOGiCOG5137.
GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
HOVERGENiHBG105617.
InParanoidiQ9Y294.
KOiK10753.
OMAiWRLIYVS.
OrthoDBiEOG7B5WWX.
PhylomeDBiQ9Y294.
TreeFamiTF106429.

Family and domain databases

Gene3Di2.60.40.1490. 1 hit.
InterProiIPR006818. Histone_chaperone_ASF1-like.
[Graphical view]
PANTHERiPTHR12040. PTHR12040. 1 hit.
PfamiPF04729. ASF1_hist_chap. 1 hit.
[Graphical view]
SUPFAMiSSF101546. SSF101546. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y294-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKVQVNNVV VLDNPSPFYN PFQFEITFEC IEDLSEDLEW KIIYVGSAES
60 70 80 90 100
EEYDQVLDSV LVGPVPAGRH MFVFQADAPN PGLIPDADAV GVTVVLITCT
110 120 130 140 150
YRGQEFIRVG YYVNNEYTET ELRENPPVKP DFSKLQRNIL ASNPRVTRFH
160 170 180 190 200
INWEDNTEKL EDAESSNPNL QSLLSTDALP SASKGWSTSE NSLNVMLESH

MDCM
Length:204
Mass (Da):22,969
Last modified:November 1, 1999 - v1
Checksum:i9819D531D3A9FC68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741F → I in AAF29110. (PubMed:11042152)Curated
Sequence conflicti204 – 2041M → I in CAG33628. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47469.1.
PIRiT08661.
RefSeqiNP_054753.1. NM_014034.2.
UniGeneiHs.292316.

Genome annotation databases

EnsembliENST00000229595; ENSP00000229595; ENSG00000111875.
GeneIDi25842.
KEGGihsa:25842.
UCSCiuc011ebn.2. human.

Polymorphism databases

DMDMi74735206.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS47469.1.
PIRi T08661.
RefSeqi NP_054753.1. NM_014034.2.
UniGenei Hs.292316.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q9Y294.
SMRi Q9Y294. Positions 1-154.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117368. 37 interactions.
DIPi DIP-29241N.
IntActi Q9Y294. 13 interactions.
MINTi MINT-1385638.
STRINGi 9606.ENSP00000229595.

PTM databases

PhosphoSitei Q9Y294.

Polymorphism databases

DMDMi 74735206.

Proteomic databases

MaxQBi Q9Y294.
PaxDbi Q9Y294.
PRIDEi Q9Y294.

Protocols and materials databases

DNASUi 25842.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229595 ; ENSP00000229595 ; ENSG00000111875 .
GeneIDi 25842.
KEGGi hsa:25842.
UCSCi uc011ebn.2. human.

Organism-specific databases

CTDi 25842.
GeneCardsi GC06P119215.
HGNCi HGNC:20995. ASF1A.
MIMi 609189. gene.
neXtProti NX_Q9Y294.
PharmGKBi PA128394636.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5137.
GeneTreei ENSGT00390000004692.
HOGENOMi HOG000197425.
HOVERGENi HBG105617.
InParanoidi Q9Y294.
KOi K10753.
OMAi WRLIYVS.
OrthoDBi EOG7B5WWX.
PhylomeDBi Q9Y294.
TreeFami TF106429.

Enzyme and pathway databases

Reactomei REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

EvolutionaryTracei Q9Y294.
GeneWikii ASF1A.
GenomeRNAii 25842.
NextBioi 47163.
PROi Q9Y294.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y294.
CleanExi HS_ASF1A.
Genevestigatori Q9Y294.

Family and domain databases

Gene3Di 2.60.40.1490. 1 hit.
InterProi IPR006818. Histone_chaperone_ASF1-like.
[Graphical view ]
PANTHERi PTHR12040. PTHR12040. 1 hit.
Pfami PF04729. ASF1_hist_chap. 1 hit.
[Graphical view ]
SUPFAMi SSF101546. SSF101546. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. "Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation."
    Das C., Roy S., Namjoshi S., Malarkey C.S., Jones D.N., Kutateladze T.G., Churchill M.E., Tyler J.K.
    Proc. Natl. Acad. Sci. U.S.A. 111:E1072-E1081(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CREBBP.
  27. Cited for: STRUCTURE BY NMR OF 1-156, INTERACTION WITH HISTONE H3 AND HISTONE H4, MUTAGENESIS OF ASP-54; VAL-94 AND ARG-108.
  28. "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.

Entry informationi

Entry nameiASF1A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y294
Secondary accession number(s): Q6IA08, Q9P014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3