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O43189

- PHF1_HUMAN

UniProt

O43189 - PHF1_HUMAN

Protein

PHD finger protein 1

Gene

PHF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci (PubMed:18285464 and PubMed:23273982). According to another report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2 (PubMed:23142980). Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53.6 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri87 – 14256PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri186 – 24055PHD-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. methylated histone binding Source: UniProtKB
    2. sequence-specific DNA binding transcription factor activity Source: ProtInc
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. chromatin modification Source: UniProtKB-KW
    3. negative regulation of histone H3-K27 methylation Source: UniProtKB
    4. positive regulation of histone H3-K27 methylation Source: UniProtKB
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    DNA damage, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200808. PRC2 methylates histones and DNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PHD finger protein 1
    Short name:
    Protein PHF1
    Short name:
    hPHF1
    Alternative name(s):
    Polycomb-like protein 1
    Short name:
    hPCl1
    Gene namesi
    Name:PHF1
    Synonyms:PCL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8919. PHF1.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Co-localizes with NEK6 in the centrosome.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. site of double-strand break Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving PHF1 may be a cause of endometrial stromal tumors. Translocation t(6;7)(p21;p22) with JAZF1. Translocation t(1;6)(p34;p21) with MEAF6.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi41 – 411W → A: Abolishes histone H3K36me3-binding and localization at double-strand breaks (DSBs). 2 Publications
    Mutagenesisi47 – 471Y → A: Abolishes histone H3K36me3-binding. 2 Publications
    Mutagenesisi65 – 651F → A: Abolishes histone H3K36me3-binding. 1 Publication
    Mutagenesisi66 – 661E → K: Impairs histone H3K36me3-binding. 1 Publication
    Mutagenesisi71 – 711F → A: Abolishes histone H3K36me3-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA33259.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 567567PHD finger protein 1PRO_0000059288Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43189.
    PaxDbiO43189.
    PRIDEiO43189.

    PTM databases

    PhosphoSiteiO43189.

    Expressioni

    Tissue specificityi

    Highest levels in heart, skeletal muscle, and pancreas, lower levels in brain, placenta, lung, liver and kidney.

    Gene expression databases

    ArrayExpressiO43189.
    BgeeiO43189.
    CleanExiHS_PHF1.
    GenevestigatoriO43189.

    Organism-specific databases

    HPAiHPA031038.

    Interactioni

    Subunit structurei

    Interacts with CHMP1 By similarity. Associated component of the PRC2 complex. Interacts with p53/TP53.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi111271. 27 interactions.
    DIPiDIP-34001N.
    IntActiO43189. 10 interactions.
    MINTiMINT-1437706.

    Structurei

    Secondary structure

    1
    567
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 405
    Beta strandi46 – 5510
    Turni56 – 594
    Beta strandi60 – 656
    Turni66 – 683
    Beta strandi70 – 745
    Helixi75 – 773
    Beta strandi78 – 803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E5PNMR-A29-83[»]
    2M0ONMR-A6-83[»]
    4HCZX-ray1.85A/B28-85[»]
    ProteinModelPortaliO43189.
    SMRiO43189. Positions 6-82, 85-147, 187-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43189.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 8658TudorAdd
    BLAST

    Domaini

    The Tudor domain recognizes and binds H3K36me3 (PubMed:23228662, PubMed:23273982 and PubMed:23142980).

    Sequence similaritiesi

    Belongs to the Polycomblike family.Curated
    Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 Tudor domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri87 – 14256PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri186 – 24055PHD-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG244542.
    HOVERGENiHBG004755.
    InParanoidiO43189.
    KOiK11467.
    PhylomeDBiO43189.
    TreeFamiTF106420.

    Family and domain databases

    Gene3Di3.30.40.10. 2 hits.
    InterProiIPR025894. Mtf2_C_dom.
    IPR002999. Tudor.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF14061. Mtf2_C. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 2 hits.
    SM00333. TUDOR. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 2 hits.
    PROSITEiPS01359. ZF_PHD_1. 2 hits.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: O43189-1) [UniParc]FASTAAdd to Basket

    Also known as: PHF2

    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

    MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT    50
    IKKVDSAREV CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP 100
    GNRLVSCEKC RHAYHQDCHV PRAPAPGEGE GTSWVCRQCV FAIATKRGGA 150
    LKKGPYARAM LGMKLSLPYG LKGLDWDAGH LSNRQQSYCY CGGPGEWNLK 200
    MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG PEKVRRLQLR 250
    WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE 300
    RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTS 350
    FPSGQGPGGG VSRPLGKRRR PEPEPLRRRQ KGKVEELGPP SAVRNQPEPQ 400
    EQRERAHLQR ALQASVSPPS PSPNQSYQGS SGYNFRPTDA RCLPSSPIRM 450
    FASFHPSAST AGTSGDSGPP DRSPLELHIG FPTDIPKSAP HSMTASSSSV 500
    SSPSPGLPRR SAPPSPLCRS LSPGTGGGVR GGVGYLSRGD PVRVLARRVR 550
    PDGSVQYLVE WGGGGIF 567
    Length:567
    Mass (Da):62,106
    Last modified:January 11, 2011 - v3
    Checksum:iE81BA9475565957C
    GO
    Isoform 1 (identifier: O43189-2) [UniParc]FASTAAdd to Basket

    Also known as: PHF1

    The sequence of this isoform differs from the canonical sequence as follows:
         350-457: SFPSGQGPGG...IRMFASFHPS → RAGPWGRGLT...QTSLKVPPTR
         458-567: Missing.

    Note: Contains a phosphoserine at position 360.

    Show »
    Length:457
    Mass (Da):49,643
    Checksum:i611EF2B5A416841C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421T → S.
    Corresponds to variant rs6934613 [ dbSNP | Ensembl ].
    VAR_044500
    Natural varianti304 – 3041R → K.5 Publications
    Corresponds to variant rs3116713 [ dbSNP | Ensembl ].
    VAR_034382

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei350 – 457108SFPSG…SFHPS → RAGPWGRGLTSPGEAPEAGA RAPEEEAEGESGGAGATLSS AQSARAPGAEGAGSSAEGTA AAPSGCLLPSTLLPAPQGPL GTVDPQTGHPWNFTLVSPQT SLKVPPTR in isoform 1. 1 PublicationVSP_004694Add
    BLAST
    Alternative sequencei458 – 567110Missing in isoform 1. 1 PublicationVSP_004695Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF029678 mRNA. Translation: AAC52062.1.
    AF052205 mRNA. Translation: AAC13273.1.
    AL662799 Genomic DNA. Translation: CAI18271.1.
    AL662799 Genomic DNA. Translation: CAI18272.1.
    AL021366 Genomic DNA. Translation: CAA16158.1.
    AL021366 Genomic DNA. Translation: CAA16159.1.
    AL050332 Genomic DNA. Translation: CAC38366.1.
    AL050332 Genomic DNA. Translation: CAC38367.1.
    BX088650 Genomic DNA. Translation: CAM26298.1.
    BX088650 Genomic DNA. Translation: CAM26299.1.
    CH471081 Genomic DNA. Translation: EAX03729.1.
    CH471081 Genomic DNA. Translation: EAX03730.1.
    BC008834 mRNA. Translation: AAH08834.1.
    CCDSiCCDS4777.1. [O43189-1]
    CCDS4778.1. [O43189-2]
    RefSeqiNP_002627.1. NM_002636.4.
    NP_077084.1. NM_024165.2.
    UniGeneiHs.166204.

    Genome annotation databases

    EnsembliENST00000374512; ENSP00000363636; ENSG00000112511. [O43189-2]
    ENST00000374516; ENSP00000363640; ENSG00000112511. [O43189-1]
    ENST00000427869; ENSP00000391901; ENSG00000225553.
    ENST00000454914; ENSP00000407295; ENSG00000225553.
    GeneIDi5252.
    KEGGihsa:5252.
    UCSCiuc003oeh.3. human. [O43189-1]
    uc003oei.3. human. [O43189-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF029678 mRNA. Translation: AAC52062.1 .
    AF052205 mRNA. Translation: AAC13273.1 .
    AL662799 Genomic DNA. Translation: CAI18271.1 .
    AL662799 Genomic DNA. Translation: CAI18272.1 .
    AL021366 Genomic DNA. Translation: CAA16158.1 .
    AL021366 Genomic DNA. Translation: CAA16159.1 .
    AL050332 Genomic DNA. Translation: CAC38366.1 .
    AL050332 Genomic DNA. Translation: CAC38367.1 .
    BX088650 Genomic DNA. Translation: CAM26298.1 .
    BX088650 Genomic DNA. Translation: CAM26299.1 .
    CH471081 Genomic DNA. Translation: EAX03729.1 .
    CH471081 Genomic DNA. Translation: EAX03730.1 .
    BC008834 mRNA. Translation: AAH08834.1 .
    CCDSi CCDS4777.1. [O43189-1 ]
    CCDS4778.1. [O43189-2 ]
    RefSeqi NP_002627.1. NM_002636.4.
    NP_077084.1. NM_024165.2.
    UniGenei Hs.166204.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E5P NMR - A 29-83 [» ]
    2M0O NMR - A 6-83 [» ]
    4HCZ X-ray 1.85 A/B 28-85 [» ]
    ProteinModelPortali O43189.
    SMRi O43189. Positions 6-82, 85-147, 187-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111271. 27 interactions.
    DIPi DIP-34001N.
    IntActi O43189. 10 interactions.
    MINTi MINT-1437706.

    PTM databases

    PhosphoSitei O43189.

    Proteomic databases

    MaxQBi O43189.
    PaxDbi O43189.
    PRIDEi O43189.

    Protocols and materials databases

    DNASUi 5252.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374512 ; ENSP00000363636 ; ENSG00000112511 . [O43189-2 ]
    ENST00000374516 ; ENSP00000363640 ; ENSG00000112511 . [O43189-1 ]
    ENST00000427869 ; ENSP00000391901 ; ENSG00000225553 .
    ENST00000454914 ; ENSP00000407295 ; ENSG00000225553 .
    GeneIDi 5252.
    KEGGi hsa:5252.
    UCSCi uc003oeh.3. human. [O43189-1 ]
    uc003oei.3. human. [O43189-2 ]

    Organism-specific databases

    CTDi 5252.
    GeneCardsi GC06P033379.
    GC06Po33517.
    HGNCi HGNC:8919. PHF1.
    HPAi HPA031038.
    MIMi 602881. gene.
    neXtProti NX_O43189.
    PharmGKBi PA33259.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244542.
    HOVERGENi HBG004755.
    InParanoidi O43189.
    KOi K11467.
    PhylomeDBi O43189.
    TreeFami TF106420.

    Enzyme and pathway databases

    Reactomei REACT_200808. PRC2 methylates histones and DNA.

    Miscellaneous databases

    EvolutionaryTracei O43189.
    GeneWikii PHF1.
    GenomeRNAii 5252.
    NextBioi 20290.
    PROi O43189.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43189.
    Bgeei O43189.
    CleanExi HS_PHF1.
    Genevestigatori O43189.

    Family and domain databases

    Gene3Di 3.30.40.10. 2 hits.
    InterProi IPR025894. Mtf2_C_dom.
    IPR002999. Tudor.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF14061. Mtf2_C. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 2 hits.
    SM00333. TUDOR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 2 hits.
    PROSITEi PS01359. ZF_PHD_1. 2 hits.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The identification and localization of a human gene with sequence similarity to Polycomblike of Drosophila melanogaster."
      Coulson M., Robert S., Eyre H.J., Saint R.
      Genomics 48:381-383(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-304.
      Tissue: Placenta.
    2. Wang J.H., Du G.W., Zhou Y., Yuan J.G., Qiang B.Q.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LYS-304.
    3. "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], VARIANT LYS-304.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LYS-304.
    5. "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 2), VARIANT LYS-304.
      Tissue: Uterus.
    6. "Consistent rearrangement of chromosomal band 6p21 with generation of fusion genes JAZF1/PHF1 and EPC1/PHF1 in endometrial stromal sarcoma."
      Micci F., Panagopoulos I., Bjerkehagen B., Heim S.
      Cancer Res. 66:107-112(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH JAZF1.
    7. "Role of hPHF1 in H3K27 methylation and Hox gene silencing."
      Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.
      Mol. Cell. Biol. 28:1862-1872(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE PRC2 COMPLEX.
    8. "Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo."
      Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.
      Mol. Cell. Biol. 28:2718-2731(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THE PRC2 COMPLEX, SUBCELLULAR LOCATION.
    9. "A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell."
      Hong Z., Jiang J., Lan L., Nakajima S., Kanno S., Koseki H., Yasui A.
      Nucleic Acids Res. 36:2939-2947(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
      Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
      J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial stromal sarcoma."
      Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M., Bjerkehagen B., Davidson B., Heim S.
      PLoS ONE 7:E39354-E39354(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH MEAF6.
    13. "Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3."
      Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J.
      Biochem. Biophys. Res. Commun. 430:547-553(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: H3K36ME3-BINDING.
    14. "Polycomb group protein PHF1 regulates p53-dependent cell growth arrest and apoptosis."
      Yang Y., Wang C., Zhang P., Gao K., Wang D., Yu H., Zhang T., Jiang S., Hexige S., Hong Z., Yasui A., Liu J.O., Huang H., Yu L.
      J. Biol. Chem. 288:529-539(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
    15. "Solution structure of the Tudor domain of PHD finger protein 1 (PHF1 protein)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 29-85.
    16. "An H3K36 methylation-engaging Tudor motif of Polycomb-like proteins mediates PRC2 complex targeting."
      Cai L., Rothbart S.B., Lu R., Xu B., Chen W.Y., Tripathy A., Rockowitz S., Zheng D., Patel D.J., Allis C.D., Strahl B.D., Song J., Wang G.G.
      Mol. Cell 49:571-582(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 6-83, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-41; TYR-47; PHE-65; GLU-66 AND PHE-71.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-85, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-41 AND TYR-47.

    Entry informationi

    Entry nameiPHF1_HUMAN
    AccessioniPrimary (citable) accession number: O43189
    Secondary accession number(s): B1AZX2
    , B1AZX3, O60929, Q5SU07, Q5SU08, Q96KM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 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. 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3