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Q13111

- CAF1A_HUMAN

UniProt

Q13111 - CAF1A_HUMAN

Protein

Chromatin assembly factor 1 subunit A

Gene

CHAF1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Core component of the CAF-1 complex, a complex thought to mediate chromatin assembly in DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. CHAF1A binds to histones H3 and H4. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci By similarity. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene.By similarity2 Publications

    GO - Molecular functioni

    1. chromatin binding Source: ProtInc
    2. chromo shadow domain binding Source: BHF-UCL
    3. identical protein binding Source: IntAct
    4. protein binding Source: IntAct
    5. unfolded protein binding Source: ProtInc

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. chromatin assembly Source: UniProtKB
    3. DNA repair Source: UniProtKB-KW
    4. DNA replication Source: UniProtKB-KW
    5. DNA replication-dependent nucleosome assembly Source: UniProt
    6. protein complex assembly Source: ProtInc
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair, DNA replication, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromatin assembly factor 1 subunit A
    Short name:
    CAF-1 subunit A
    Alternative name(s):
    Chromatin assembly factor I p150 subunit
    Short name:
    CAF-I 150 kDa subunit
    Short name:
    CAF-I p150
    Short name:
    hp150
    Gene namesi
    Name:CHAF1A
    Synonyms:CAF, CAF1P150
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:1910. CHAF1A.

    Subcellular locationi

    Nucleus 1 Publication
    Note: DNA replication foci.

    GO - Cellular componenti

    1. CAF-1 complex Source: UniProtKB
    2. nuclear chromatin Source: UniProt
    3. protein complex Source: UniProt

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi240 – 2401V → E: Abolishes interaction with CBX5; when associated with E-242. 1 Publication
    Mutagenesisi242 – 2421L → E: Abolishes interaction with CBX5; when associated with E-240. 1 Publication

    Organism-specific databases

    PharmGKBiPA26446.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 956956Chromatin assembly factor 1 subunit APRO_0000089276Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei65 – 651Phosphoserine2 Publications
    Modified residuei123 – 1231Phosphoserine1 Publication
    Modified residuei138 – 1381Phosphoserine1 Publication
    Modified residuei141 – 1411Phosphoserine2 Publications
    Modified residuei143 – 1431Phosphoserine2 Publications
    Modified residuei206 – 2061Phosphoserine1 Publication
    Modified residuei224 – 2241Phosphoserine2 Publications
    Modified residuei310 – 3101Phosphoserine1 Publication
    Modified residuei722 – 7221Phosphothreonine3 Publications
    Modified residuei772 – 7721Phosphoserine3 Publications
    Modified residuei775 – 7751Phosphoserine2 Publications
    Modified residuei865 – 8651Phosphothreonine1 Publication
    Modified residuei873 – 8731Phosphoserine2 Publications
    Modified residuei951 – 9511Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13111.
    PaxDbiQ13111.
    PRIDEiQ13111.

    PTM databases

    PhosphoSiteiQ13111.

    Miscellaneous databases

    PMAP-CutDBQ13111.

    Expressioni

    Developmental stagei

    Active complex is found in G1, S and G2 phases.

    Gene expression databases

    ArrayExpressiQ13111.
    BgeeiQ13111.
    CleanExiHS_CHAF1A.
    GenevestigatoriQ13111.

    Organism-specific databases

    HPAiCAB015186.

    Interactioni

    Subunit structurei

    Homodimer. Part of the CAF-1 complex that contains RBBP4, CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor amounts of RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase. CHAF1A binds directly to PCNA and to CBX1. Binds MBD1. Interacts directly with CBX5 via the PxVxL motif. During DNA replication, it forms a S phase-specific complex that facilitates DNA methylation and histone H3 'Lys-9' methylation during replication-coupled chromatin assembly and is at least composed of the CHAF1A, MBD1 and SETDB1. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with CBX5.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-1020839,EBI-1020839
    CBX5P459737EBI-1020839,EBI-78219
    GFI1Q996844EBI-1020839,EBI-949368
    MBD1Q9UIS93EBI-1020839,EBI-867196
    NCK1P163332EBI-1020839,EBI-389883
    PCNAP120043EBI-1020839,EBI-358311

    Protein-protein interaction databases

    BioGridi115349. 66 interactions.
    DIPiDIP-31135N.
    IntActiQ13111. 32 interactions.
    MINTiMINT-2806241.
    STRINGi9606.ENSP00000301280.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13111.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 314314Binds to CBX1 chromo shadow domainAdd
    BLAST
    Regioni1 – 4949Binds to PCNAAdd
    BLAST
    Regioni642 – 67837Necessary for homodimerization and competence for chromatin assemblyAdd
    BLAST
    Regioni660 – 956297Binds to p60Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi233 – 24614PxVxL motifAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi323 – 453131Arg/Glu/Lys-richAdd
    BLAST
    Compositional biasi602 – 6087Poly-Glu
    Compositional biasi619 – 6235Poly-Asp
    Compositional biasi905 – 9117Poly-Glu

    Domaini

    Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain.

    Sequence similaritiesi

    Belongs to the CHAF1A family.Curated

    Phylogenomic databases

    eggNOGiNOG259938.
    HOGENOMiHOG000111290.
    HOVERGENiHBG050779.
    InParanoidiQ13111.
    KOiK10750.
    OMAiHMVLAPR.
    OrthoDBiEOG76X60P.
    PhylomeDBiQ13111.
    TreeFamiTF350377.

    Family and domain databases

    InterProiIPR029105. CAF1-p150_C2.
    IPR029091. CAF1-p150_N.
    IPR022043. CAF1A.
    [Graphical view]
    PfamiPF15539. CAF1-p150_C2. 1 hit.
    PF15557. CAF1-p150_N. 1 hit.
    PF12253. CAF1A. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q13111-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLEELECGAP GARGAATAMD CKDRPAFPVK KLIQARLPFK RLNLVPKGKA    50
    DDMSDDQGTS VQSKSPDLEA SLDTLENNCH VGSDIDFRPK LVNGKGPLDN 100
    FLRNRIETSI GQSTVIIDLT EDSNEQPDSL VDHNKLNSEA SPSREAINGQ 150
    REDTGDQQGL LKAIQNDKLA FPGETLSDIP CKTEEEGVGC GGAGRRGDSQ 200
    ECSPRSCPEL TSGPRMCPRK EQDSWSEAGG ILFKGKVPMV VLQDILAVRP 250
    PQIKSLPATP QGKNMTPESE VLESFPEEDS VLSHSSLSSP SSTSSPEGPP 300
    APPKQHSSTS PFPTSTPLRR ITKKFVKGST EKNKLRLQRD QERLGKQLKL 350
    RAEREEKEKL KEEAKRAKEE AKKKKEEEKE LKEKERREKR EKDEKEKAEK 400
    QRLKEERRKE RQEALEAKLE EKRKKEEEKR LREEEKRIKA EKAEITRFFQ 450
    KPKTPQAPKT LAGSCGKFAP FEIKEHMVLA PRRRTAFHPD LCSQLDQLLQ 500
    QQSGEFSFLK DLKGRQPLRS GPTHVSTRNA DIFNSDVVIV ERGKGDGVPE 550
    RRKFGRMKLL QFCENHRPAY WGTWNKKTAL IRARDPWAQD TKLLDYEVDS 600
    DEEWEEEEPG ESLSHSEGDD DDDMGEDEDE DDGFFVPHGY LSEDEGVTEE 650
    CADPENHKVR QKLKAKEWDE FLAKGKRFRV LQPVKIGCVW AADRDCAGDD 700
    LKVLQQFAAC FLETLPAQEE QTPKASKRER RDEQILAQLL PLLHGNVNGS 750
    KVIIREFQEH CRRGLLSNHT GSPRSPSTTY LHTPTPSEDA AIPSKSRLKR 800
    LISENSVYEK RPDFRMCWYV HPQVLQSFQQ EHLPVPCQWS YVTSVPSAPK 850
    EDSGSVPSTG PSQGTPISLK RKSAGSMCIT QFMKKRRHDG QIGAEDMDGF 900
    QADTEEEEEE EGDCMIVDVP DAAEVQAPCG AASGAGGGVG VDTGKATLTS 950
    SPLGAS 956
    Length:956
    Mass (Da):106,926
    Last modified:May 5, 2009 - v2
    Checksum:i90617F8FE8DB67B0
    GO
    Isoform 2 (identifier: Q13111-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         710-749: CFLETLPAQE...LPLLHGNVNG → HWVHPESRGD...CVKSTLSCFT
         750-956: Missing.

    Show »
    Length:749
    Mass (Da):84,685
    Checksum:iA7176E2D8D18CA0F
    GO
    Isoform 3 (identifier: Q13111-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         772-944: Missing.

    Show »
    Length:783
    Mass (Da):88,285
    Checksum:i44E39E1CCE192850
    GO

    Sequence cautioni

    The sequence AAH52620.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 426.
    The sequence AAA76736.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAF04291.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH52620.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti775 – 7751S → T in AAA76736. (PubMed:7600578)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671D → V.
    Corresponds to variant rs35651457 [ dbSNP | Ensembl ].
    VAR_055329
    Natural varianti239 – 2391M → V.
    Corresponds to variant rs2230635 [ dbSNP | Ensembl ].
    VAR_055330
    Natural varianti850 – 8501K → R.
    Corresponds to variant rs8100525 [ dbSNP | Ensembl ].
    VAR_055331
    Natural varianti923 – 9231A → V.2 Publications
    Corresponds to variant rs9352 [ dbSNP | Ensembl ].
    VAR_055332
    Natural varianti950 – 9501S → A.7 Publications
    Corresponds to variant rs243383 [ dbSNP | Ensembl ].
    VAR_055333

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei710 – 74940CFLET…GNVNG → HWVHPESRGDVCRTLRVSSP QSRYLNRLNSCVKSTLSCFT in isoform 2. CuratedVSP_004149Add
    BLAST
    Alternative sequencei750 – 956207Missing in isoform 2. CuratedVSP_004150Add
    BLAST
    Alternative sequencei772 – 944173Missing in isoform 3. CuratedVSP_004151Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190465 Genomic DNA. Translation: AAF04291.1. Different initiation.
    AC011498 Genomic DNA. No translation available.
    BC052620 mRNA. Translation: AAH52620.1. Sequence problems.
    BC067093 mRNA. Translation: AAH67093.1.
    U20979 mRNA. Translation: AAA76736.1. Different initiation.
    CCDSiCCDS32875.1. [Q13111-1]
    PIRiA56731.
    RefSeqiNP_005474.2. NM_005483.2.
    UniGeneiHs.79018.

    Genome annotation databases

    EnsembliENST00000301280; ENSP00000301280; ENSG00000167670. [Q13111-1]
    GeneIDi10036.
    KEGGihsa:10036.
    UCSCiuc002mal.3. human. [Q13111-1]

    Polymorphism databases

    DMDMi229462842.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190465 Genomic DNA. Translation: AAF04291.1 . Different initiation.
    AC011498 Genomic DNA. No translation available.
    BC052620 mRNA. Translation: AAH52620.1 . Sequence problems.
    BC067093 mRNA. Translation: AAH67093.1 .
    U20979 mRNA. Translation: AAA76736.1 . Different initiation.
    CCDSi CCDS32875.1. [Q13111-1 ]
    PIRi A56731.
    RefSeqi NP_005474.2. NM_005483.2.
    UniGenei Hs.79018.

    3D structure databases

    ProteinModelPortali Q13111.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115349. 66 interactions.
    DIPi DIP-31135N.
    IntActi Q13111. 32 interactions.
    MINTi MINT-2806241.
    STRINGi 9606.ENSP00000301280.

    PTM databases

    PhosphoSitei Q13111.

    Polymorphism databases

    DMDMi 229462842.

    Proteomic databases

    MaxQBi Q13111.
    PaxDbi Q13111.
    PRIDEi Q13111.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301280 ; ENSP00000301280 ; ENSG00000167670 . [Q13111-1 ]
    GeneIDi 10036.
    KEGGi hsa:10036.
    UCSCi uc002mal.3. human. [Q13111-1 ]

    Organism-specific databases

    CTDi 10036.
    GeneCardsi GC19P004402.
    HGNCi HGNC:1910. CHAF1A.
    HPAi CAB015186.
    MIMi 601246. gene.
    neXtProti NX_Q13111.
    PharmGKBi PA26446.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259938.
    HOGENOMi HOG000111290.
    HOVERGENi HBG050779.
    InParanoidi Q13111.
    KOi K10750.
    OMAi HMVLAPR.
    OrthoDBi EOG76X60P.
    PhylomeDBi Q13111.
    TreeFami TF350377.

    Miscellaneous databases

    GeneWikii CHAF1A.
    GenomeRNAii 10036.
    NextBioi 37903.
    PMAP-CutDB Q13111.
    PROi Q13111.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13111.
    Bgeei Q13111.
    CleanExi HS_CHAF1A.
    Genevestigatori Q13111.

    Family and domain databases

    InterProi IPR029105. CAF1-p150_C2.
    IPR029091. CAF1-p150_N.
    IPR022043. CAF1A.
    [Graphical view ]
    Pfami PF15539. CAF1-p150_C2. 1 hit.
    PF15557. CAF1-p150_N. 1 hit.
    PF12253. CAF1A. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic sequence and expression analyses of human chromatin assembly factor 1 p150 gene."
      Dong H., Lin W., Zhang C.-K., Xiong H., Fu G., Jin W.-R., Chen R., Chen Z., Qi Z.-T., Huang G.M.
      Gene 264:187-196(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), VARIANTS VAL-923 AND ALA-950.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORM 1), VARIANT ALA-950.
      Tissue: Brain and Ovary.
    4. "The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication."
      Kaufman P.D., Kobayashi R., Kessler N., Stillman B.
      Cell 81:1105-1114(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-956 (ISOFORM 1), VARIANTS VAL-923 AND ALA-950.
      Tissue: Cervix adenocarcinoma.
    5. "Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin."
      Shibahara K., Stillman B.
      Cell 96:575-585(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCNA, SUBCELLULAR LOCATION.
    6. "A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing DNA damage."
      Moggs J.G., Grandi P., Quivy J.P., Jonsson Z.O., Hubscher U., Becker P.B., Almouzni G.
      Mol. Cell. Biol. 20:1206-1218(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCNA.
    7. "CAF-1 and the inheritance of chromatin states: at the crossroads of DNA replication and repair."
      Ridgway P., Almouzni G.
      J. Cell Sci. 113:2647-2658(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    8. "Dimerization of the largest subunit of chromatin assembly factor 1: importance in vitro and during Xenopus early development."
      Quivy J.-P., Grandi P., Almouzni G.
      EMBO J. 20:2015-2027(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION.
    9. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
      Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
      Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
    10. "The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1."
      Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.
      Mol. Cell. Biol. 23:3226-3236(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBD1.
    11. "Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly."
      Sarraf S.A., Stancheva I.
      Mol. Cell 15:595-605(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MBD1 AND SETDB1.
    12. "The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
      Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
      Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX5.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; THR-722; SER-772; SER-775; SER-873 AND SER-951, VARIANT [LARGE SCALE ANALYSIS] ALA-950, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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.
    17. "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
      Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
      Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBX5, MUTAGENESIS OF VAL-240 AND LEU-242.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-138; SER-141; SER-143; SER-224; THR-722; SER-772; THR-865; SER-873 AND SER-951, VARIANT [LARGE SCALE ANALYSIS] ALA-950, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-141; SER-143; SER-206; SER-310; THR-722; SER-772; SER-775 AND SER-951, VARIANT [LARGE SCALE ANALYSIS] ALA-950, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: VARIANT [LARGE SCALE ANALYSIS] ALA-950, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCAF1A_HUMAN
    AccessioniPrimary (citable) accession number: Q13111
    Secondary accession number(s): Q6NXG5, Q7Z7K3, Q9UJY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3