PHF19_HUMAN
ID PHF19_HUMAN Reviewed; 580 AA.
AC Q5T6S3; Q32NF2; Q5T6S4; Q6N038; Q8TBL6; Q9UFS9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=PHD finger protein 19;
DE AltName: Full=Polycomb-like protein 3;
DE Short=hPCL3;
GN Name=PHF19; Synonyms=PCL3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Esophageal carcinoma, and Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Prostate, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15563832; DOI=10.1016/j.gene.2004.09.006;
RA Wang S., Robertson G.P., Zhu J.;
RT "A novel human homologue of Drosophila polycomblike gene is up-regulated in
RT multiple cancers.";
RL Gene 343:69-78(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP FUNCTION, ALTERNATIVE SPLICING, AND INTERACTION WITH EZH2.
RX PubMed=21143197; DOI=10.1042/bj20100944;
RA Boulay G., Rosnoblet C., Guerardel C., Angrand P.O., Leprince D.;
RT "Functional characterization of human Polycomb-like 3 isoforms identifies
RT them as components of distinct EZH2 protein complexes.";
RL Biochem. J. 434:333-342(2011).
RN [7]
RP DOWN-REGULATION IN SPHEROID MELANOMA CELLS.
RX PubMed=22487681; DOI=10.4161/cc.20095;
RA Ghislin S., Deshayes F., Middendorp S., Boggetto N., Alcaide-Loridan C.;
RT "PHF19 and Akt control the switch between proliferative and invasive states
RT in melanoma.";
RL Cell Cycle 11:1634-1645(2012).
RN [8]
RP FUNCTION, H3K36ME3-BINDING, DOMAIN, INTERACTION WITH RIOX1, AND MUTAGENESIS
RP OF TRP-50 AND TYR-56.
RX PubMed=23160351; DOI=10.1038/nsmb.2449;
RA Brien G.L., Gambero G., O'Connell D.J., Jerman E., Turner S.A., Egan C.M.,
RA Dunne E.J., Jurgens M.C., Wynne K., Piao L., Lohan A.J., Ferguson N.,
RA Shi X., Sinha K.M., Loftus B.J., Cagney G., Bracken A.P.;
RT "Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to
RT embryonic stem cell genes during differentiation.";
RL Nat. Struct. Mol. Biol. 19:1273-1281(2012).
RN [9]
RP FUNCTION, AND H3K36ME3-BINDING.
RX PubMed=23228662; DOI=10.1016/j.bbrc.2012.11.116;
RA Qin S., Guo Y., Xu C., Bian C., Fu M., Gong S., Min J.;
RT "Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to
RT histone H3K36me3.";
RL Biochem. Biophys. Res. Commun. 430:547-553(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-187; SER-365 AND
RP SER-366, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP FUNCTION, H3K36ME3-BINDING, AND MUTAGENESIS OF TYR-56.
RX PubMed=23273982; DOI=10.1016/j.molcel.2012.11.026;
RA Cai L., Rothbart S.B., Lu R., Xu B., Chen W.Y., Tripathy A., Rockowitz S.,
RA Zheng D., Patel D.J., Allis C.D., Strahl B.D., Song J., Wang G.G.;
RT "An H3K36 methylation-engaging Tudor motif of Polycomb-like proteins
RT mediates PRC2 complex targeting.";
RL Mol. Cell 49:571-582(2013).
RN [12] {ECO:0000305}
RP FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, AND INTERACTION WITH SUZ12.
RX PubMed=29499137; DOI=10.1016/j.molcel.2018.01.039;
RA Chen S., Jiao L., Shubbar M., Yang X., Liu X.;
RT "Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for
RT Chromatin Binding.";
RL Mol. Cell 69:840-852.e5(2018).
RN [13]
RP STRUCTURE BY NMR OF 40-95.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the tudor domain of PHD finger protein 19, isoform B
RT [Homo sapiens].";
RL Submitted (FEB-2009) to the PDB data bank.
RN [14]
RP STRUCTURE BY NMR OF 38-95, FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX,
RP H3K36ME3-BINDING, DOMAIN, INTERACTION WITH SUZ12, AND MUTAGENESIS OF
RP TRP-50.
RX PubMed=23104054; DOI=10.1038/nsmb.2434;
RA Ballare C., Lange M., Lapinaite A., Martin G.M., Morey L., Pascual G.,
RA Liefke R., Simon B., Shi Y., Gozani O., Carlomagno T., Benitah S.A.,
RA Di Croce L.;
RT "Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb
RT activity.";
RL Nat. Struct. Mol. Biol. 19:1257-1265(2012).
RN [15] {ECO:0007744|PDB:6NQ3}
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 500-580 IN COMPLEX WITH SUZ12;
RP RBBP4 AND JARID2, FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 331-LYS-LYS-332.
RX PubMed=31959557; DOI=10.1016/j.molcel.2019.12.019;
RA Chen S., Jiao L., Liu X., Yang X., Liu X.;
RT "A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island
RT Chromatin.";
RL Mol. Cell 77:1265-1278.e7(2020).
CC -!- FUNCTION: Polycomb group (PcG) protein that specifically binds histone
CC H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex,
CC thus enhancing PRC2 H3K27me3 methylation activity (PubMed:15563832,
CC PubMed:18691976, PubMed:23160351, PubMed:23228662, PubMed:23273982,
CC PubMed:29499137, PubMed:23104054, PubMed:31959557). Probably involved
CC in the transition from an active state to a repressed state in
CC embryonic stem cells: acts by binding to H3K36me3, a mark for
CC transcriptional activation, and recruiting H3K36me3 histone
CC demethylases RIOX1 or KDM2B, leading to demethylation of H3K36 and
CC recruitment of the PRC2 complex that mediates H3K27me3 methylation,
CC followed by de novo silencing (PubMed:23160351). Recruits the PRC2
CC complex to CpG islands and contributes to embryonic stem cell self-
CC renewal. Also binds histone H3 dimethylated at 'Lys-36' (H3K36me2)
CC (PubMed:23104054). Isoform 1 and isoform 2 inhibit transcription from
CC an HSV-tk promoter (PubMed:15563832). {ECO:0000269|PubMed:15563832,
CC ECO:0000269|PubMed:18691976, ECO:0000269|PubMed:23104054,
CC ECO:0000269|PubMed:23160351, ECO:0000269|PubMed:23228662,
CC ECO:0000269|PubMed:23273982, ECO:0000269|PubMed:29499137,
CC ECO:0000269|PubMed:31959557}.
CC -!- SUBUNIT: Associates with the PRC2 complex, which consists of the core
CC components EED, EZH1 or EZH2, SUZ12, and RBBP4, and various
CC combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2
CC and EPOP (PubMed:23104054, PubMed:29499137, PubMed:31959557). Forms a
CC dimeric PRC2.1 (class 1, PRC-PCL) complex consisting of at least SUZ12,
CC RBBP4, and PHF19 or MTF2; PHF19 and MTF2 stabilize the dimeric
CC structure which enhances PRC2 interaction with chromatin
CC (PubMed:31959557). Interacts with SUZ12; competes with AEBP2 for SUZ12
CC binding (PubMed:29499137, PubMed:31959557). Interacts with EZH2 (via
CC its Tudor domain) (PubMed:21143197). Isoform 1 interacts with SUZ12;
CC isoform 2 does not interact with SUZ12 (PubMed:23104054). Interacts
CC with RIOX1 (PubMed:23160351). {ECO:0000269|PubMed:21143197,
CC ECO:0000269|PubMed:23104054, ECO:0000269|PubMed:23160351,
CC ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}.
CC -!- INTERACTION:
CC Q5T6S3; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-2339674, EBI-702390;
CC Q5T6S3; O95429: BAG4; NbExp=3; IntAct=EBI-2339674, EBI-2949658;
CC Q5T6S3; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-2339674, EBI-2837444;
CC Q5T6S3; P68400: CSNK2A1; NbExp=3; IntAct=EBI-2339674, EBI-347804;
CC Q5T6S3; Q01658: DR1; NbExp=3; IntAct=EBI-2339674, EBI-750300;
CC Q5T6S3; Q92997: DVL3; NbExp=3; IntAct=EBI-2339674, EBI-739789;
CC Q5T6S3; P29692-2: EEF1D; NbExp=3; IntAct=EBI-2339674, EBI-5280572;
CC Q5T6S3; P14136: GFAP; NbExp=3; IntAct=EBI-2339674, EBI-744302;
CC Q5T6S3; Q00403: GTF2B; NbExp=3; IntAct=EBI-2339674, EBI-389564;
CC Q5T6S3; P09067: HOXB5; NbExp=3; IntAct=EBI-2339674, EBI-3893317;
CC Q5T6S3; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-2339674, EBI-769401;
CC Q5T6S3; O60341: KDM1A; NbExp=2; IntAct=EBI-2339674, EBI-710124;
CC Q5T6S3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2339674, EBI-741037;
CC Q5T6S3; P19404: NDUFV2; NbExp=3; IntAct=EBI-2339674, EBI-713665;
CC Q5T6S3; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2339674, EBI-79165;
CC Q5T6S3; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2339674, EBI-25882629;
CC Q5T6S3; A0JP26: POTEB3; NbExp=3; IntAct=EBI-2339674, EBI-18165900;
CC Q5T6S3; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-2339674, EBI-1504830;
CC Q5T6S3; Q8TAD8: SNIP1; NbExp=3; IntAct=EBI-2339674, EBI-749336;
CC Q5T6S3; O43463: SUV39H1; NbExp=2; IntAct=EBI-2339674, EBI-349968;
CC Q5T6S3; Q9H5I1: SUV39H2; NbExp=2; IntAct=EBI-2339674, EBI-723127;
CC Q5T6S3; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-2339674, EBI-741515;
CC Q5T6S3; Q9BT49: THAP7; NbExp=3; IntAct=EBI-2339674, EBI-741350;
CC Q5T6S3; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-2339674, EBI-947459;
CC Q5T6S3; Q96MU7: YTHDC1; NbExp=3; IntAct=EBI-2339674, EBI-2849854;
CC Q5T6S3; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-2339674, EBI-11962574;
CC Q5T6S3; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2339674, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15563832,
CC ECO:0000269|PubMed:31959557}. Note=Localizes to chromatin as part of
CC the PRC2 complex. {ECO:0000269|PubMed:31959557}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=PCL3L, hPCL3L;
CC IsoId=Q5T6S3-1; Sequence=Displayed;
CC Name=2; Synonyms=PCL3S, hPCL3S;
CC IsoId=Q5T6S3-2; Sequence=VSP_031224, VSP_031225;
CC Name=3;
CC IsoId=Q5T6S3-3; Sequence=VSP_031222, VSP_031223;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in thymus, heart, lung and
CC kidney. Isoform 2 is predominantly expressed in placenta, skeletal
CC muscle and kidney, whereas isoform 1 is predominantly expressed in
CC liver and peripheral blood leukocytes. Overexpressed in many types of
CC cancers, including colon, skin, lung, rectal, cervical, uterus, liver
CC cancers, in cell lines derived from different stages of melanoma and in
CC glioma cell lines. {ECO:0000269|PubMed:15563832}.
CC -!- DOMAIN: The Tudor domain recognizes and binds H3K36me3
CC (PubMed:23273982, PubMed:23160351, PubMed:23104054 and
CC PubMed:23228662). May also bind H3K27me3, with a lower affinity
CC (PubMed:23160351). {ECO:0000269|PubMed:23104054,
CC ECO:0000269|PubMed:23160351}.
CC -!- MISCELLANEOUS: Down-regulated in spheroid melanoma cells that display
CC an invasive phenotype, characterized by a higher motility, a poor
CC proliferation rate and a gain of pluripotency gene expression. PHF19
CC favors the proliferation and reduces the transmigration capacity of
CC melanoma cell lines, 2 properties of invasive cells, suggesting that
CC down-regulation may participate in the switch from proliferative to
CC invasive states in melanoma cells (PubMed:22487681).
CC {ECO:0000305|PubMed:22487681}.
CC -!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE45832.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL117477; CAB55950.1; -; mRNA.
DR EMBL; BX640713; CAE45832.1; ALT_INIT; mRNA.
DR EMBL; AL161911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022374; AAH22374.1; -; mRNA.
DR EMBL; BC108663; AAI08664.1; -; mRNA.
DR EMBL; BC125076; AAI25077.1; -; mRNA.
DR EMBL; BC125077; AAI25078.1; -; mRNA.
DR CCDS; CCDS35116.1; -. [Q5T6S3-1]
DR CCDS; CCDS35117.1; -. [Q5T6S3-2]
DR PIR; T17260; T17260.
DR RefSeq; NP_001009936.1; NM_001009936.2. [Q5T6S3-2]
DR RefSeq; NP_001273769.1; NM_001286840.1.
DR RefSeq; NP_001273772.1; NM_001286843.1. [Q5T6S3-3]
DR RefSeq; NP_056466.1; NM_015651.2. [Q5T6S3-1]
DR RefSeq; XP_005251963.1; XM_005251906.2. [Q5T6S3-1]
DR RefSeq; XP_011516811.1; XM_011518509.2. [Q5T6S3-1]
DR RefSeq; XP_016870101.1; XM_017014612.1. [Q5T6S3-1]
DR PDB; 2E5Q; NMR; -; A=40-95.
DR PDB; 4BD3; NMR; -; A=38-95.
DR PDB; 6NQ3; X-ray; 2.89 A; C/G=500-580.
DR PDB; 6WAU; X-ray; 1.75 A; A/B/C/D/E/F=38-96.
DR PDBsum; 2E5Q; -.
DR PDBsum; 4BD3; -.
DR PDBsum; 6NQ3; -.
DR PDBsum; 6WAU; -.
DR AlphaFoldDB; Q5T6S3; -.
DR BMRB; Q5T6S3; -.
DR SMR; Q5T6S3; -.
DR BioGRID; 117578; 69.
DR CORUM; Q5T6S3; -.
DR IntAct; Q5T6S3; 56.
DR MINT; Q5T6S3; -.
DR STRING; 9606.ENSP00000483946; -.
DR BindingDB; Q5T6S3; -.
DR iPTMnet; Q5T6S3; -.
DR PhosphoSitePlus; Q5T6S3; -.
DR BioMuta; PHF19; -.
DR DMDM; 74745265; -.
DR EPD; Q5T6S3; -.
DR jPOST; Q5T6S3; -.
DR MassIVE; Q5T6S3; -.
DR MaxQB; Q5T6S3; -.
DR PaxDb; Q5T6S3; -.
DR PeptideAtlas; Q5T6S3; -.
DR PRIDE; Q5T6S3; -.
DR ProteomicsDB; 64610; -. [Q5T6S3-1]
DR ProteomicsDB; 64611; -. [Q5T6S3-2]
DR ProteomicsDB; 64612; -. [Q5T6S3-3]
DR Antibodypedia; 30114; 158 antibodies from 26 providers.
DR DNASU; 26147; -.
DR Ensembl; ENST00000312189.10; ENSP00000310372.6; ENSG00000119403.15. [Q5T6S3-2]
DR Ensembl; ENST00000373896.8; ENSP00000363003.3; ENSG00000119403.15. [Q5T6S3-1]
DR GeneID; 26147; -.
DR KEGG; hsa:26147; -.
DR MANE-Select; ENST00000373896.8; ENSP00000363003.3; NM_015651.3; NP_056466.1.
DR UCSC; uc004bks.3; human. [Q5T6S3-1]
DR CTD; 26147; -.
DR DisGeNET; 26147; -.
DR GeneCards; PHF19; -.
DR HGNC; HGNC:24566; PHF19.
DR HPA; ENSG00000119403; Low tissue specificity.
DR MIM; 609740; gene.
DR neXtProt; NX_Q5T6S3; -.
DR OpenTargets; ENSG00000119403; -.
DR PharmGKB; PA134911501; -.
DR VEuPathDB; HostDB:ENSG00000119403; -.
DR eggNOG; KOG4323; Eukaryota.
DR GeneTree; ENSGT00950000183180; -.
DR HOGENOM; CLU_032773_1_0_1; -.
DR InParanoid; Q5T6S3; -.
DR OrthoDB; 281828at2759; -.
DR PhylomeDB; Q5T6S3; -.
DR TreeFam; TF106420; -.
DR PathwayCommons; Q5T6S3; -.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR SignaLink; Q5T6S3; -.
DR BioGRID-ORCS; 26147; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; PHF19; human.
DR EvolutionaryTrace; Q5T6S3; -.
DR GenomeRNAi; 26147; -.
DR Pharos; Q5T6S3; Tbio.
DR PRO; PR:Q5T6S3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5T6S3; protein.
DR Bgee; ENSG00000119403; Expressed in ventricular zone and 169 other tissues.
DR ExpressionAtlas; Q5T6S3; baseline and differential.
DR Genevisible; Q5T6S3; HS.
DR GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR CDD; cd15581; PHD2_PHF19; 1.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID00480; -.
DR InterPro; IPR040477; KDM4_Tudor_2.
DR InterPro; IPR025894; Mtf2_C_dom.
DR InterPro; IPR042017; PHF19_PHD2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14061; Mtf2_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..580
FT /note="PHD finger protein 19"
FT /id="PRO_0000318570"
FT DOMAIN 40..93
FT /note="Tudor"
FT ZN_FING 96..151
FT /note="PHD-type 1"
FT ZN_FING 195..249
FT /note="PHD-type 2"
FT REGION 74..80
FT /note="Histone H3K36me3 binding"
FT REGION 347..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..580
FT /note="Interaction with SUZ12"
FT /evidence="ECO:0000269|PubMed:29499137"
FT REGION 531..544
FT /note="Important for PRC2 dimer stability"
FT /evidence="ECO:0000269|PubMed:31959557"
FT SITE 47
FT /note="Histone H3K36me3 binding"
FT SITE 55
FT /note="Histone H3K36me3 binding"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 122..130
FT /note="GYHQQCHIP -> VPHPHSGQC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031222"
FT VAR_SEQ 131..580
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031223"
FT VAR_SEQ 155..207
FT /note="RKGGALKKGAIARTLQAVKMVLSYQPEELEWDSPHRTNQQQCYCYCGGPGEW
FT Y -> RVSLPSSPVPASPASSSGADQRLPSQSLSSKQKGHTWALETDSASATVLGQDL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031224"
FT VAR_SEQ 208..580
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031225"
FT MUTAGEN 50
FT /note="W->A: In muthPhf19; abolishes histone H3K36me3-
FT binding and impaired activity of the PRC2 complex and
FT subsequent H3K27me3 methylation."
FT /evidence="ECO:0000269|PubMed:23104054,
FT ECO:0000269|PubMed:23160351"
FT MUTAGEN 50
FT /note="W->C: Abolishes histone H3K36me3-binding and
FT recruitment of the PRC2 complex and RIOX1; when associated
FT with A-56."
FT /evidence="ECO:0000269|PubMed:23104054,
FT ECO:0000269|PubMed:23160351"
FT MUTAGEN 56
FT /note="Y->A: Abolishes histone H3K36me3-binding. Abolishes
FT histone H3K36me3-binding and recruitment of the PRC2
FT complex and RIOX1; when associated with C-50."
FT /evidence="ECO:0000269|PubMed:23160351,
FT ECO:0000269|PubMed:23273982"
FT MUTAGEN 331..332
FT /note="KK->AA: Impairs chromatin binding as part of the
FT PRC2 complex."
FT /evidence="ECO:0000269|PubMed:31959557"
FT CONFLICT 181
FT /note="E -> G (in Ref. 1; CAE45832)"
FT /evidence="ECO:0000305"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6WAU"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:6WAU"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:6WAU"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6WAU"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6WAU"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6WAU"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6WAU"
FT HELIX 531..543
FT /evidence="ECO:0007829|PDB:6NQ3"
FT HELIX 545..551
FT /evidence="ECO:0007829|PDB:6NQ3"
FT STRAND 555..563
FT /evidence="ECO:0007829|PDB:6NQ3"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:6NQ3"
FT STRAND 567..574
FT /evidence="ECO:0007829|PDB:6NQ3"
FT MOD_RES Q5T6S3-2:166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
SQ SEQUENCE 580 AA; 65591 MW; 17CCF21BA2827826 CRC64;
MENRALDPGT RDSYGATSHL PNKGALAKVK NNFKDLMSKL TEGQYVLCRW TDGLYYLGKI
KRVSSSKQSC LVTFEDNSKY WVLWKDIQHA GVPGEEPKCN ICLGKTSGPL NEILICGKCG
LGYHQQCHIP IAGSADQPLL TPWFCRRCIF ALAVRKGGAL KKGAIARTLQ AVKMVLSYQP
EELEWDSPHR TNQQQCYCYC GGPGEWYLRM LQCYRCRQWF HEACTQCLNE PMMFGDRFYL
FFCSVCNQGP EYIERLPLRW VDVVHLALYN LGVQSKKKYF DFEEILAFVN HHWELLQLGK
LTSTPVTDRG PHLLNALNSY KSRFLCGKEI KKKKCIFRLR IRVPPNPPGK LLPDKGLLPN
ENSASSELRK RGKSKPGLLP HEFQQQKRRV YRRKRSKFLL EDAIPSSDFT SAWSTNHHLA
SIFDFTLDEI QSLKSASSGQ TFFSDVDSTD AASTSGSAST SLSYDSRWTV GSRKRKLAAK
AYMPLRAKRW AAELDGRCPS DSSAEGASVP ERPDEGIDSH TFESISEDDS SLSHLKSSIT
NYFGAAGRLA CGEKYQVLAR RVTPEGKVQY LVEWEGTTPY
