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 24-JAN-2024, entry version 162. 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, PubMed:23228662). CC May also bind H3K27me3, with a lower affinity (PubMed:23160351). CC {ECO:0000269|PubMed:23104054, 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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; 70. DR ComplexPortal; CPX-2196; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL3-PALI1 variant. DR ComplexPortal; CPX-2198; Polycomb repressive complex 2.1,EZH2-RBBP4-PCL3-PALI1 variant. DR ComplexPortal; CPX-2316; Polycomb repressive complex 2.1,EZH2-RBBP7-PCL3-PALI1 variant. DR ComplexPortal; CPX-2322; Polycomb repressive complex 2.1, EZH1-RBBP4-PCL3-EPOP variant. DR ComplexPortal; CPX-2323; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL3-EPOP variant. DR ComplexPortal; CPX-2328; Polycomb repressive complex 2.1, EZH2-RBBP4-PCL3-EPOP variant. DR ComplexPortal; CPX-2329; Polycomb repressive complex 2.1, EZH2-RBBP7-PCL3-EPOP variant. DR ComplexPortal; CPX-2570; Polycomb repressive complex 2.1, EZH1-RBBP7-PCL3-PALI1 variant. DR CORUM; Q5T6S3; -. DR IntAct; Q5T6S3; 56. DR MINT; Q5T6S3; -. DR STRING; 9606.ENSP00000483946; -. DR BindingDB; Q5T6S3; -. DR GlyGen; Q5T6S3; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000483946; -. DR PeptideAtlas; Q5T6S3; -. DR ProteomicsDB; 64610; -. [Q5T6S3-1] DR ProteomicsDB; 64611; -. [Q5T6S3-2] DR ProteomicsDB; 64612; -. [Q5T6S3-3] DR Pumba; Q5T6S3; -. DR Antibodypedia; 30114; 171 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 AGR; HGNC:24566; -. 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; 5483634at2759; -. 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 1155 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 171 other cell types or tissues. DR ExpressionAtlas; Q5T6S3; baseline and differential. 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:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; cd15579; PHD1_PHF19; 1. DR CDD; cd15581; PHD2_PHF19; 1. DR CDD; cd20451; Tudor_PHF19; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.90.980.20; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR IDEAL; IID00480; -. DR InterPro; IPR040477; KDM4-like_Tudor. DR InterPro; IPR025894; Mtf2_C_dom. DR InterPro; IPR042017; PHF19_PHD2. DR InterPro; IPR002999; Tudor. DR InterPro; IPR047400; Tudor_PHF19. 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 PANTHER; PTHR12628:SF6; PHD FINGER PROTEIN 19; 1. DR PANTHER; PTHR12628; POLYCOMB-LIKE TRANSCRIPTION FACTOR; 1. 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; FYVE/PHD zinc finger; 2. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR PROSITE; PS01359; ZF_PHD_1; 2. DR Genevisible; Q5T6S3; HS. 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 FT H3K36me3-binding and impaired activity of the PRC2 complex FT and 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 //