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Q5T6S3

- PHF19_HUMAN

UniProt

Q5T6S3 - PHF19_HUMAN

Protein

PHD finger protein 19

Gene

PHF19

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases NO66 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys-36' (H3K36me2). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei47 – 471Histone H3K36me3
    Binding sitei55 – 551Histone H3K36me3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri96 – 15156PHD-type 1Add
    BLAST
    Zinc fingeri195 – 24955PHD-type 2Add
    BLAST

    GO - Molecular functioni

    1. methylated histone binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    3. positive regulation of histone H3-K27 methylation Source: UniProtKB
    4. stem cell maintenance Source: Ensembl
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    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 19
    Alternative name(s):
    Polycomb-like protein 3
    Short name:
    hPCL3
    Gene namesi
    Name:PHF19
    Synonyms:PCL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:24566. PHF19.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. ESC/E(Z) complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501W → A in muthPhf19; abolishes histone H3K36me3-binding and impaired activity of the PRC2 complex and subsequent H3K27me3 methylation. 2 Publications
    Mutagenesisi50 – 501W → C: Abolishes histone H3K36me3-binding and recruitment of the PRC2 complex and NO66; when associated with A-56. 2 Publications
    Mutagenesisi56 – 561Y → A: Abolishes histone H3K36me3-binding. Abolishes histone H3K36me3-binding and recruitment of the PRC2 complex and NO66; when associated with C-50. 2 Publications

    Organism-specific databases

    PharmGKBiPA134911501.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 580580PHD finger protein 19PRO_0000318570Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5T6S3.
    PaxDbiQ5T6S3.
    PRIDEiQ5T6S3.

    PTM databases

    PhosphoSiteiQ5T6S3.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed in thymus, heart, lung and kidney. Isoform 2 is predominantly expressed in placenta, skeletal muscle and kidney, whereas isoform 1 is predominantly expressed in liver and peripheral blood leukocytes. Overexpressed in many types of cancers, including colon, skin, lung, rectal, cervical, uterus, liver cancers, in cell lines derived from different stages of melanoma and in glioma cell lines.1 Publication

    Gene expression databases

    ArrayExpressiQ5T6S3.
    BgeeiQ5T6S3.
    CleanExiHS_PHF19.
    GenevestigatoriQ5T6S3.

    Organism-specific databases

    HPAiHPA051458.

    Interactioni

    Subunit structurei

    Associated component of the PRC2 complex. Interacts with EZH2 (via its Tudor domain). Isoform 1 interacts with SUZ12; isoform 2 does not interact with SUZ12. Interacts with NO66.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KDM1AO603412EBI-2339674,EBI-710124
    SUV39H1O434632EBI-2339674,EBI-349968
    SUV39H2Q9H5I12EBI-2339674,EBI-723127

    Protein-protein interaction databases

    BioGridi117578. 8 interactions.
    IntActiQ5T6S3. 4 interactions.
    MINTiMINT-8417713.
    STRINGi9606.ENSP00000363003.

    Structurei

    Secondary structure

    1
    580
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 495
    Beta strandi55 – 606
    Beta strandi68 – 747
    Beta strandi79 – 835
    Helixi84 – 863
    Beta strandi87 – 893

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E5QNMR-A40-95[»]
    4BD3NMR-A38-95[»]
    ProteinModelPortaliQ5T6S3.
    SMRiQ5T6S3. Positions 38-156, 195-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5T6S3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 9354TudorAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni74 – 807Histone H3K36me3 binding

    Domaini

    The Tudor domain recognizes and binds H3K36me3 (PubMed:23273982, PubMed:23160351, PubMed:23104054 and PubMed:23228662). May also bind H3K27me3, with a lower affinity (PubMed:23160351).2 Publications

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri96 – 15156PHD-type 1Add
    BLAST
    Zinc fingeri195 – 24955PHD-type 2Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG244542.
    HOGENOMiHOG000010307.
    HOVERGENiHBG004755.
    InParanoidiQ5T6S3.
    KOiK11486.
    OMAiDWDSPHR.
    OrthoDBiEOG73V6JJ.
    PhylomeDBiQ5T6S3.
    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.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5T6S3-1) [UniParc]FASTAAdd to Basket

    Also known as: PCL3L, hPCL3L

    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

    MENRALDPGT RDSYGATSHL PNKGALAKVK NNFKDLMSKL TEGQYVLCRW    50
    TDGLYYLGKI KRVSSSKQSC LVTFEDNSKY WVLWKDIQHA GVPGEEPKCN 100
    ICLGKTSGPL NEILICGKCG LGYHQQCHIP IAGSADQPLL TPWFCRRCIF 150
    ALAVRKGGAL KKGAIARTLQ AVKMVLSYQP EELEWDSPHR TNQQQCYCYC 200
    GGPGEWYLRM LQCYRCRQWF HEACTQCLNE PMMFGDRFYL FFCSVCNQGP 250
    EYIERLPLRW VDVVHLALYN LGVQSKKKYF DFEEILAFVN HHWELLQLGK 300
    LTSTPVTDRG PHLLNALNSY KSRFLCGKEI KKKKCIFRLR IRVPPNPPGK 350
    LLPDKGLLPN ENSASSELRK RGKSKPGLLP HEFQQQKRRV YRRKRSKFLL 400
    EDAIPSSDFT SAWSTNHHLA SIFDFTLDEI QSLKSASSGQ TFFSDVDSTD 450
    AASTSGSAST SLSYDSRWTV GSRKRKLAAK AYMPLRAKRW AAELDGRCPS 500
    DSSAEGASVP ERPDEGIDSH TFESISEDDS SLSHLKSSIT NYFGAAGRLA 550
    CGEKYQVLAR RVTPEGKVQY LVEWEGTTPY 580
    Length:580
    Mass (Da):65,591
    Last modified:December 21, 2004 - v1
    Checksum:i17CCF21BA2827826
    GO
    Isoform 2 (identifier: Q5T6S3-2) [UniParc]FASTAAdd to Basket

    Also known as: PCL3S, hPCL3S

    The sequence of this isoform differs from the canonical sequence as follows:
         155-207: RKGGALKKGA...CYCGGPGEWY → RVSLPSSPVP...ASATVLGQDL
         208-580: Missing.

    Note: Contains a phosphoserine at position 166.

    Show »
    Length:207
    Mass (Da):22,512
    Checksum:i34F3EF834B17FAF0
    GO
    Isoform 3 (identifier: Q5T6S3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         122-130: GYHQQCHIP → VPHPHSGQC
         131-580: Missing.

    Show »
    Length:130
    Mass (Da):14,386
    Checksum:iE10645A3F782774C
    GO

    Sequence cautioni

    The sequence CAE45832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811E → G in CAE45832. (PubMed:17974005)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei122 – 1309GYHQQCHIP → VPHPHSGQC in isoform 3. 1 PublicationVSP_031222
    Alternative sequencei131 – 580450Missing in isoform 3. 1 PublicationVSP_031223Add
    BLAST
    Alternative sequencei155 – 20753RKGGA…PGEWY → RVSLPSSPVPASPASSSGAD QRLPSQSLSSKQKGHTWALE TDSASATVLGQDL in isoform 2. 1 PublicationVSP_031224Add
    BLAST
    Alternative sequencei208 – 580373Missing in isoform 2. 1 PublicationVSP_031225Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL117477 mRNA. Translation: CAB55950.1.
    BX640713 mRNA. Translation: CAE45832.1. Different initiation.
    AL354792 Genomic DNA. Translation: CAI15690.1.
    AL354792 Genomic DNA. Translation: CAI15691.1.
    AL354792, AL161911 Genomic DNA. Translation: CAI15692.1.
    AL161911, AL354792 Genomic DNA. Translation: CAI95112.1.
    BC022374 mRNA. Translation: AAH22374.1.
    BC108663 mRNA. Translation: AAI08664.1.
    BC125076 mRNA. Translation: AAI25077.1.
    BC125077 mRNA. Translation: AAI25078.1.
    CCDSiCCDS35116.1. [Q5T6S3-1]
    CCDS35117.1. [Q5T6S3-2]
    PIRiT17260.
    RefSeqiNP_001009936.1. NM_001009936.2. [Q5T6S3-2]
    NP_001273769.1. NM_001286840.1.
    NP_001273772.1. NM_001286843.1. [Q5T6S3-3]
    NP_056466.1. NM_015651.2. [Q5T6S3-1]
    XP_005251963.1. XM_005251906.1. [Q5T6S3-1]
    XP_006717108.1. XM_006717045.1. [Q5T6S3-1]
    UniGeneiHs.460124.

    Genome annotation databases

    EnsembliENST00000312189; ENSP00000310372; ENSG00000119403. [Q5T6S3-2]
    ENST00000373896; ENSP00000363003; ENSG00000119403. [Q5T6S3-1]
    GeneIDi26147.
    KEGGihsa:26147.
    UCSCiuc004bks.1. human. [Q5T6S3-1]
    uc004bkt.3. human. [Q5T6S3-2]

    Polymorphism databases

    DMDMi74745265.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL117477 mRNA. Translation: CAB55950.1 .
    BX640713 mRNA. Translation: CAE45832.1 . Different initiation.
    AL354792 Genomic DNA. Translation: CAI15690.1 .
    AL354792 Genomic DNA. Translation: CAI15691.1 .
    AL354792 , AL161911 Genomic DNA. Translation: CAI15692.1 .
    AL161911 , AL354792 Genomic DNA. Translation: CAI95112.1 .
    BC022374 mRNA. Translation: AAH22374.1 .
    BC108663 mRNA. Translation: AAI08664.1 .
    BC125076 mRNA. Translation: AAI25077.1 .
    BC125077 mRNA. Translation: AAI25078.1 .
    CCDSi CCDS35116.1. [Q5T6S3-1 ]
    CCDS35117.1. [Q5T6S3-2 ]
    PIRi T17260.
    RefSeqi NP_001009936.1. NM_001009936.2. [Q5T6S3-2 ]
    NP_001273769.1. NM_001286840.1.
    NP_001273772.1. NM_001286843.1. [Q5T6S3-3 ]
    NP_056466.1. NM_015651.2. [Q5T6S3-1 ]
    XP_005251963.1. XM_005251906.1. [Q5T6S3-1 ]
    XP_006717108.1. XM_006717045.1. [Q5T6S3-1 ]
    UniGenei Hs.460124.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E5Q NMR - A 40-95 [» ]
    4BD3 NMR - A 38-95 [» ]
    ProteinModelPortali Q5T6S3.
    SMRi Q5T6S3. Positions 38-156, 195-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117578. 8 interactions.
    IntActi Q5T6S3. 4 interactions.
    MINTi MINT-8417713.
    STRINGi 9606.ENSP00000363003.

    PTM databases

    PhosphoSitei Q5T6S3.

    Polymorphism databases

    DMDMi 74745265.

    Proteomic databases

    MaxQBi Q5T6S3.
    PaxDbi Q5T6S3.
    PRIDEi Q5T6S3.

    Protocols and materials databases

    DNASUi 26147.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312189 ; ENSP00000310372 ; ENSG00000119403 . [Q5T6S3-2 ]
    ENST00000373896 ; ENSP00000363003 ; ENSG00000119403 . [Q5T6S3-1 ]
    GeneIDi 26147.
    KEGGi hsa:26147.
    UCSCi uc004bks.1. human. [Q5T6S3-1 ]
    uc004bkt.3. human. [Q5T6S3-2 ]

    Organism-specific databases

    CTDi 26147.
    GeneCardsi GC09M123617.
    HGNCi HGNC:24566. PHF19.
    HPAi HPA051458.
    MIMi 609740. gene.
    neXtProti NX_Q5T6S3.
    PharmGKBi PA134911501.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244542.
    HOGENOMi HOG000010307.
    HOVERGENi HBG004755.
    InParanoidi Q5T6S3.
    KOi K11486.
    OMAi DWDSPHR.
    OrthoDBi EOG73V6JJ.
    PhylomeDBi Q5T6S3.
    TreeFami TF106420.

    Enzyme and pathway databases

    Reactomei REACT_200808. PRC2 methylates histones and DNA.

    Miscellaneous databases

    ChiTaRSi PHF19. human.
    EvolutionaryTracei Q5T6S3.
    GenomeRNAii 26147.
    NextBioi 48205.
    PROi Q5T6S3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5T6S3.
    Bgeei Q5T6S3.
    CleanExi HS_PHF19.
    Genevestigatori Q5T6S3.

    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Esophageal carcinoma and Mammary cancer.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(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] (ISOFORMS 1; 2 AND 3).
      Tissue: Prostate and Skin.
    4. "A novel human homologue of Drosophila polycomblike gene is up-regulated in multiple cancers."
      Wang S., Robertson G.P., Zhu J.
      Gene 343:69-78(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Functional characterization of human Polycomb-like 3 isoforms identifies them as components of distinct EZH2 protein complexes."
      Boulay G., Rosnoblet C., Guerardel C., Angrand P.O., Leprince D.
      Biochem. J. 434:333-342(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING, INTERACTION WITH EZH2.
    7. "PHF19 and Akt control the switch between proliferative and invasive states in melanoma."
      Ghislin S., Deshayes F., Middendorp S., Boggetto N., Alcaide-Loridan C.
      Cell Cycle 11:1634-1645(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOWN-REGULATION IN SPHEROID MELANOMA CELLS.
    8. "Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to embryonic stem cell genes during differentiation."
      Brien G.L., Gambero G., O'Connell D.J., Jerman E., Turner S.A., Egan C.M., Dunne E.J., Jurgens M.C., Wynne K., Piao L., Lohan A.J., Ferguson N., Shi X., Sinha K.M., Loftus B.J., Cagney G., Bracken A.P.
      Nat. Struct. Mol. Biol. 19:1273-1281(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, H3K36ME3-BINDING, DOMAIN, INTERACTION WITH NO66, MUTAGENESIS OF TRP-50 AND TYR-56.
    9. "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.
    10. "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: H3K36ME3-BINDING, MUTAGENESIS OF TYR-56.
    11. "Solution structure of the tudor domain of PHD finger protein 19, isoform B [Homo sapiens]."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 40-95.
    12. Cited for: STRUCTURE BY NMR OF 38-95, FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, H3K36ME3-BINDING, DOMAIN, INTERACTION WITH SUZ12, MUTAGENESIS OF TRP-50.

    Entry informationi

    Entry nameiPHF19_HUMAN
    AccessioniPrimary (citable) accession number: Q5T6S3
    Secondary accession number(s): Q32NF2
    , Q5T6S4, Q6N038, Q8TBL6, Q9UFS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 98 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

    Miscellaneous

    Down-regulated in spheroid melanoma cells that display an invasive phenotype, characterized by a higher motility, a poor proliferation rate and a gain of pluripotency gene expression. PHF19 favors the proliferation and reduces the transmigration capacity of melanoma cell lines, 2 properties of invasive cells, suggesting that down-regulation may participate in the switch from proliferative to invasive states in melanoma cells (PubMed:22487681).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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