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Q9Y294

- ASF1A_HUMAN

UniProt

Q9Y294 - ASF1A_HUMAN

Protein

Histone chaperone ASF1A

Gene

ASF1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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
    3. protein binding Source: UniProtKB

    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

    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

    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.
    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.
    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 TLK22 Publications

    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 H4.13 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi117368. 36 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 – 119
    Beta strandi15 – 173
    Beta strandi22 – 3211
    Beta strandi38 – 469
    Helixi51 – 533
    Beta strandi54 – 629
    Beta strandi67 – 7610
    Helixi81 – 833
    Helixi86 – 894
    Beta strandi90 – 10112
    Beta strandi104 – 11916
    Helixi120 – 1245
    Helixi132 – 1343
    Beta strandi135 – 1395
    Beta strandi145 – 1484

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MAKVQVNNVV VLDNPSPFYN PFQFEITFEC IEDLSEDLEW KIIYVGSAES    50
    EEYDQVLDSV LVGPVPAGRH MFVFQADAPN PGLIPDADAV GVTVVLITCT 100
    YRGQEFIRVG YYVNNEYTET ELRENPPVKP DFSKLQRNIL ASNPRVTRFH 150
    INWEDNTEKL EDAESSNPNL QSLLSTDALP SASKGWSTSE NSLNVMLESH 200
    MDCM 204
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 36 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.
    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

    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. 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.

    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: October 1, 2014
    This is version 123 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