PHF1_HUMAN
ID PHF1_HUMAN Reviewed; 567 AA.
AC O43189; B1AZX2; B1AZX3; O60929; Q5SU07; Q5SU08; Q96KM7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=PHD finger protein 1;
DE Short=Protein PHF1;
DE Short=hPHF1;
DE AltName: Full=Polycomb-like protein 1;
DE Short=hPCl1;
GN Name=PHF1; Synonyms=PCL1;
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 [MRNA] (ISOFORM 1), AND VARIANT LYS-304.
RC TISSUE=Placenta;
RX PubMed=9545646; DOI=10.1006/geno.1997.5201;
RA Coulson M., Robert S., Eyre H.J., Saint R.;
RT "The identification and localization of a human gene with sequence
RT similarity to Polycomblike of Drosophila melanogaster.";
RL Genomics 48:381-383(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LYS-304.
RA Wang J.H., Du G.W., Zhou Y., Yuan J.G., Qiang B.Q.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-304.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-304.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LYS-304.
RC TISSUE=Uterus;
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 [6]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH JAZF1.
RX PubMed=16397222; DOI=10.1158/0008-5472.can-05-2485;
RA Micci F., Panagopoulos I., Bjerkehagen B., Heim S.;
RT "Consistent rearrangement of chromosomal band 6p21 with generation of
RT fusion genes JAZF1/PHF1 and EPC1/PHF1 in endometrial stromal sarcoma.";
RL Cancer Res. 66:107-112(2006).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH THE
RP PRC2 COMPLEX.
RX PubMed=18086877; DOI=10.1128/mcb.01589-07;
RA Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.;
RT "Role of hPHF1 in H3K27 methylation and Hox gene silencing.";
RL Mol. Cell. Biol. 28:1862-1872(2008).
RN [8]
RP FUNCTION, INTERACTION WITH THE PRC2 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=18285464; DOI=10.1128/mcb.02017-07;
RA Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.;
RT "Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in
RT vivo.";
RL Mol. Cell. Biol. 28:2718-2731(2008).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18385154; DOI=10.1093/nar/gkn146;
RA Hong Z., Jiang J., Lan L., Nakajima S., Kanno S., Koseki H., Yasui A.;
RT "A polycomb group protein, PHF1, is involved in the response to DNA double-
RT strand breaks in human cell.";
RL Nucleic Acids Res. 36:2939-2947(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 (ISOFORM 1), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=20873783; DOI=10.1021/pr100562w;
RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J.,
RA Paes Leme A.F., Kobarg J.;
RT "Characterization of hNek6 interactome reveals an important role for its
RT short N-terminal domain and colocalization with proteins at the
RT centrosome.";
RL J. Proteome Res. 9:6298-6316(2010).
RN [12]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH MEAF6.
RX PubMed=22761769; DOI=10.1371/journal.pone.0039354;
RA Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M.,
RA Bjerkehagen B., Davidson B., Heim S.;
RT "Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial
RT stromal sarcoma.";
RL PLoS ONE 7:E39354-E39354(2012).
RN [13]
RP 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 [14]
RP FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
RX PubMed=23150668; DOI=10.1074/jbc.m111.338996;
RA Yang Y., Wang C., Zhang P., Gao K., Wang D., Yu H., Zhang T., Jiang S.,
RA Hexige S., Hong Z., Yasui A., Liu J.O., Huang H., Yu L.;
RT "Polycomb group protein PHF1 regulates p53-dependent cell growth arrest and
RT apoptosis.";
RL J. Biol. Chem. 288:529-539(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420, AND IDENTIFICATION BY
RP 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP STRUCTURE BY NMR OF 29-85.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Tudor domain of PHD finger protein 1 (PHF1
RT protein).";
RL Submitted (JUN-2007) to the PDB data bank.
RN [18]
RP STRUCTURE BY NMR OF 6-83, FUNCTION, H3K36ME3-BINDING, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF TRP-41; TYR-47; PHE-65; GLU-66 AND PHE-71.
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 [19]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-85, FUNCTION,
RP H3K36ME3-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-41 AND
RP TYR-47.
RX PubMed=23142980; DOI=10.1038/nsmb.2435;
RA Musselman C.A., Avvakumov N., Watanabe R., Abraham C.G., Lalonde M.E.,
RA Hong Z., Allen C., Roy S., Nunez J.K., Nickoloff J., Kulesza C.A.,
RA Yasui A., Cote J., Kutateladze T.G.;
RT "Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1.";
RL Nat. Struct. Mol. Biol. 19:1266-1272(2012).
CC -!- FUNCTION: Polycomb group (PcG) that specifically binds histone H3
CC trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex.
CC Involved in DNA damage response and is recruited at double-strand
CC breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional
CC activation, and recruiting the PRC2 complex: it is however unclear
CC whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or
CC inhibit H3K27me3 methylation mediated by the PRC2 complex. According to
CC some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent
CC gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3
CC loci (PubMed:18285464 and PubMed:23273982). According to another
CC report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs)
CC and inhibits the activity of PRC2 (PubMed:23142980). Regulates p53/TP53
CC stability and prolonges its turnover: may act by specifically binding
CC to a methylated from of p53/TP53. {ECO:0000269|PubMed:18086877,
CC ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:18385154,
CC ECO:0000269|PubMed:23142980, ECO:0000269|PubMed:23150668,
CC ECO:0000269|PubMed:23273982}.
CC -!- SUBUNIT: Interacts with CHMP1 (By similarity). Associated component of
CC the PRC2 complex. Interacts with p53/TP53. {ECO:0000250,
CC ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464,
CC ECO:0000269|PubMed:23150668}.
CC -!- INTERACTION:
CC O43189; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-530034, EBI-11096309;
CC O43189; Q03989: ARID5A; NbExp=3; IntAct=EBI-530034, EBI-948603;
CC O43189; Q96B67: ARRDC3; NbExp=5; IntAct=EBI-530034, EBI-2875665;
CC O43189; Q9ULK2: ATXN7L1; NbExp=3; IntAct=EBI-530034, EBI-310660;
CC O43189; Q5T686: AVPI1; NbExp=3; IntAct=EBI-530034, EBI-8640233;
CC O43189; Q6PI77: BHLHB9; NbExp=5; IntAct=EBI-530034, EBI-11519926;
CC O43189; O14503: BHLHE40; NbExp=3; IntAct=EBI-530034, EBI-711810;
CC O43189; Q96CA5: BIRC7; NbExp=4; IntAct=EBI-530034, EBI-517623;
CC O43189; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-530034, EBI-11983447;
CC O43189; Q9H6J7-2: C11orf49; NbExp=3; IntAct=EBI-530034, EBI-13328871;
CC O43189; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-530034, EBI-739580;
CC O43189; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-530034, EBI-11988027;
CC O43189; Q92782-2: DPF1; NbExp=3; IntAct=EBI-530034, EBI-23669343;
CC O43189; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-530034, EBI-2349927;
CC O43189; Q15910: EZH2; NbExp=6; IntAct=EBI-530034, EBI-530054;
CC O43189; Q14192: FHL2; NbExp=3; IntAct=EBI-530034, EBI-701903;
CC O43189; P53539: FOSB; NbExp=3; IntAct=EBI-530034, EBI-2806743;
CC O43189; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-530034, EBI-5916454;
CC O43189; Q92917: GPKOW; NbExp=3; IntAct=EBI-530034, EBI-746309;
CC O43189; Q9BPX1: HSD17B14; NbExp=8; IntAct=EBI-530034, EBI-742664;
CC O43189; Q0VD86: INCA1; NbExp=3; IntAct=EBI-530034, EBI-6509505;
CC O43189; Q5VVH5: IRAK1BP1; NbExp=3; IntAct=EBI-530034, EBI-9658404;
CC O43189; Q6ZU52: KIAA0408; NbExp=4; IntAct=EBI-530034, EBI-739493;
CC O43189; Q6A162: KRT40; NbExp=3; IntAct=EBI-530034, EBI-10171697;
CC O43189; P52954: LBX1; NbExp=3; IntAct=EBI-530034, EBI-20141748;
CC O43189; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-530034, EBI-741037;
CC O43189; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-530034, EBI-716006;
CC O43189; Q99750: MDFI; NbExp=3; IntAct=EBI-530034, EBI-724076;
CC O43189; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-530034, EBI-16439278;
CC O43189; Q6PF18: MORN3; NbExp=3; IntAct=EBI-530034, EBI-9675802;
CC O43189; Q15742: NAB2; NbExp=7; IntAct=EBI-530034, EBI-8641936;
CC O43189; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-530034, EBI-11022007;
CC O43189; Q9NR12: PDLIM7; NbExp=4; IntAct=EBI-530034, EBI-350517;
CC O43189; Q99471: PFDN5; NbExp=3; IntAct=EBI-530034, EBI-357275;
CC O43189; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-530034, EBI-14066006;
CC O43189; P86480: PRR20D; NbExp=5; IntAct=EBI-530034, EBI-12754095;
CC O43189; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-530034, EBI-11322432;
CC O43189; Q93062: RBPMS; NbExp=4; IntAct=EBI-530034, EBI-740322;
CC O43189; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-530034, EBI-740343;
CC O43189; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-530034, EBI-2872322;
CC O43189; O60504: SORBS3; NbExp=3; IntAct=EBI-530034, EBI-741237;
CC O43189; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-530034, EBI-11959123;
CC O43189; Q12800: TFCP2; NbExp=4; IntAct=EBI-530034, EBI-717422;
CC O43189; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-530034, EBI-1105213;
CC O43189; Q9NVV9: THAP1; NbExp=4; IntAct=EBI-530034, EBI-741515;
CC O43189; Q08117-2: TLE5; NbExp=3; IntAct=EBI-530034, EBI-11741437;
CC O43189; Q63HR2: TNS2; NbExp=3; IntAct=EBI-530034, EBI-949753;
CC O43189; Q96NM4-3: TOX2; NbExp=3; IntAct=EBI-530034, EBI-12815137;
CC O43189; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-530034, EBI-11952721;
CC O43189; P36406: TRIM23; NbExp=4; IntAct=EBI-530034, EBI-740098;
CC O43189; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-530034, EBI-11975223;
CC O43189; Q08AM6: VAC14; NbExp=3; IntAct=EBI-530034, EBI-2107455;
CC O43189; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-530034, EBI-12017160;
CC O43189; Q05516: ZBTB16; NbExp=3; IntAct=EBI-530034, EBI-711925;
CC O43189; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-530034, EBI-11962760;
CC O43189; O60304: ZNF500; NbExp=3; IntAct=EBI-530034, EBI-18234077;
CC O43189; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-530034, EBI-11035148;
CC O43189; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-530034, EBI-4395732;
CC O43189; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-530034, EBI-7138235;
CC O43189; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-530034, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=Localizes specifically to the
CC promoters of numerous target genes. Localizes to double-strand breaks
CC (DSBs) sites following DNA damage. Co-localizes with NEK6 in the
CC centrosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=PHF2;
CC IsoId=O43189-1; Sequence=Displayed;
CC Name=1; Synonyms=PHF1;
CC IsoId=O43189-2; Sequence=VSP_004694, VSP_004695;
CC -!- TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle, and
CC pancreas, lower levels in brain, placenta, lung, liver and kidney.
CC -!- DOMAIN: The Tudor domain recognizes and binds H3K36me3
CC (PubMed:23228662, PubMed:23273982 and PubMed:23142980).
CC -!- DISEASE: Note=A chromosomal aberration involving PHF1 may be a cause of
CC endometrial stromal tumors. Translocation t(6;7)(p21;p22) with JAZF1.
CC Translocation t(1;6)(p34;p21) with MEAF6. {ECO:0000269|PubMed:16397222,
CC ECO:0000269|PubMed:22761769}.
CC -!- SIMILARITY: Belongs to the Polycomblike family. {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; AF029678; AAC52062.1; -; mRNA.
DR EMBL; AF052205; AAC13273.1; -; mRNA.
DR EMBL; AL662799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL021366; CAA16158.1; -; Genomic_DNA.
DR EMBL; AL021366; CAA16159.1; -; Genomic_DNA.
DR EMBL; AL050332; CAC38366.1; -; Genomic_DNA.
DR EMBL; AL050332; CAC38367.1; -; Genomic_DNA.
DR EMBL; BX088650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03729.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03730.1; -; Genomic_DNA.
DR EMBL; BC008834; AAH08834.1; -; mRNA.
DR CCDS; CCDS4777.1; -. [O43189-1]
DR CCDS; CCDS4778.1; -. [O43189-2]
DR RefSeq; NP_002627.1; NM_002636.4. [O43189-2]
DR RefSeq; NP_077084.1; NM_024165.2. [O43189-1]
DR RefSeq; XP_011512964.1; XM_011514662.1. [O43189-1]
DR PDB; 2E5P; NMR; -; A=29-83.
DR PDB; 2M0O; NMR; -; A=6-83.
DR PDB; 4HCZ; X-ray; 1.85 A; A/B=28-85.
DR PDB; 5XFN; X-ray; 1.90 A; A=25-340.
DR PDB; 5XFO; X-ray; 1.90 A; A=25-340.
DR PDB; 5XFP; X-ray; 2.30 A; A/B/E=25-360.
DR PDB; 6WAT; X-ray; 1.80 A; AA/AC/BA/BC/CA/CC/DA/DC/EA/EC/FA/FC/GA/GC/HA/HC/IA/IC/JA/JC/KA/KC/LA/LC/MA/MC/NA/NC/OA/OC=28-87.
DR PDB; 6WAV; X-ray; 1.70 A; A/B/C/D=28-87.
DR PDB; 7LKY; X-ray; 1.85 A; A/B/C/D/E/F/G/H=28-87.
DR PDBsum; 2E5P; -.
DR PDBsum; 2M0O; -.
DR PDBsum; 4HCZ; -.
DR PDBsum; 5XFN; -.
DR PDBsum; 5XFO; -.
DR PDBsum; 5XFP; -.
DR PDBsum; 6WAT; -.
DR PDBsum; 6WAV; -.
DR PDBsum; 7LKY; -.
DR AlphaFoldDB; O43189; -.
DR BMRB; O43189; -.
DR SMR; O43189; -.
DR BioGRID; 111271; 171.
DR DIP; DIP-34001N; -.
DR IntAct; O43189; 82.
DR MINT; O43189; -.
DR STRING; 9606.ENSP00000363640; -.
DR BindingDB; O43189; -.
DR GlyGen; O43189; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O43189; -.
DR PhosphoSitePlus; O43189; -.
DR BioMuta; PHF1; -.
DR EPD; O43189; -.
DR jPOST; O43189; -.
DR MassIVE; O43189; -.
DR MaxQB; O43189; -.
DR PaxDb; O43189; -.
DR PeptideAtlas; O43189; -.
DR PRIDE; O43189; -.
DR ProteomicsDB; 48805; -. [O43189-1]
DR ProteomicsDB; 48806; -. [O43189-2]
DR Antibodypedia; 14271; 253 antibodies from 28 providers.
DR DNASU; 5252; -.
DR Ensembl; ENST00000374512.7; ENSP00000363636.3; ENSG00000112511.18. [O43189-2]
DR Ensembl; ENST00000374516.8; ENSP00000363640.3; ENSG00000112511.18. [O43189-1]
DR Ensembl; ENST00000427869.6; ENSP00000391901.2; ENSG00000225553.7.
DR Ensembl; ENST00000454914.6; ENSP00000407295.2; ENSG00000225553.7.
DR GeneID; 5252; -.
DR KEGG; hsa:5252; -.
DR MANE-Select; ENST00000374516.8; ENSP00000363640.3; NM_024165.3; NP_077084.2.
DR UCSC; uc003oeh.4; human. [O43189-1]
DR CTD; 5252; -.
DR DisGeNET; 5252; -.
DR GeneCards; PHF1; -.
DR HGNC; HGNC:8919; PHF1.
DR HPA; ENSG00000112511; Low tissue specificity.
DR MIM; 602881; gene.
DR neXtProt; NX_O43189; -.
DR OpenTargets; ENSG00000112511; -.
DR PharmGKB; PA33259; -.
DR VEuPathDB; HostDB:ENSG00000112511; -.
DR eggNOG; KOG4323; Eukaryota.
DR GeneTree; ENSGT00950000183180; -.
DR HOGENOM; CLU_032773_2_0_1; -.
DR InParanoid; O43189; -.
DR OMA; QPWEPTP; -.
DR OrthoDB; 281828at2759; -.
DR PhylomeDB; O43189; -.
DR TreeFam; TF106420; -.
DR PathwayCommons; O43189; -.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR SignaLink; O43189; -.
DR SIGNOR; O43189; -.
DR BioGRID-ORCS; 5252; 17 hits in 1080 CRISPR screens.
DR ChiTaRS; PHF1; human.
DR EvolutionaryTrace; O43189; -.
DR GeneWiki; PHF1; -.
DR GenomeRNAi; 5252; -.
DR Pharos; O43189; Tbio.
DR PRO; PR:O43189; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O43189; protein.
DR Bgee; ENSG00000112511; Expressed in left testis and 95 other tissues.
DR ExpressionAtlas; O43189; baseline and differential.
DR Genevisible; O43189; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:1990226; F:histone methyltransferase binding; IPI:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
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 Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID00432; -.
DR InterPro; IPR040477; KDM4_Tudor_2.
DR InterPro; IPR025894; Mtf2_C_dom.
DR InterPro; IPR031202; PHF1.
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 PANTHER; PTHR12628:SF11; PTHR12628:SF11; 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; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator;
KW Chromosomal rearrangement; Cytoplasm; Cytoskeleton; DNA damage;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..567
FT /note="PHD finger protein 1"
FT /id="PRO_0000059288"
FT DOMAIN 29..86
FT /note="Tudor"
FT ZN_FING 87..142
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 186..240
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 350..457
FT /note="SFPSGQGPGGGVSRPLGKRRRPEPEPLRRRQKGKVEELGPPSAVRNQPEPQE
FT QRERAHLQRALQASVSPPSPSPNQSYQGSSGYNFRPTDARCLPSSPIRMFASFHPS ->
FT RAGPWGRGLTSPGEAPEAGARAPEEEAEGESGGAGATLSSAQSARAPGAEGAGSSAEGT
FT AAAPSGCLLPSTLLPAPQGPLGTVDPQTGHPWNFTLVSPQTSLKVPPTR (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:9545646"
FT /id="VSP_004694"
FT VAR_SEQ 458..567
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9545646"
FT /id="VSP_004695"
FT VARIANT 42
FT /note="T -> S (in dbSNP:rs6934613)"
FT /id="VAR_044500"
FT VARIANT 304
FT /note="R -> K (in dbSNP:rs3116713)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9545646,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT /id="VAR_034382"
FT MUTAGEN 41
FT /note="W->A: Abolishes histone H3K36me3-binding and
FT localization at double-strand breaks (DSBs)."
FT /evidence="ECO:0000269|PubMed:23142980,
FT ECO:0000269|PubMed:23273982"
FT MUTAGEN 47
FT /note="Y->A: Abolishes histone H3K36me3-binding."
FT /evidence="ECO:0000269|PubMed:23142980,
FT ECO:0000269|PubMed:23273982"
FT MUTAGEN 65
FT /note="F->A: Abolishes histone H3K36me3-binding."
FT /evidence="ECO:0000269|PubMed:23273982"
FT MUTAGEN 66
FT /note="E->K: Impairs histone H3K36me3-binding."
FT /evidence="ECO:0000269|PubMed:23273982"
FT MUTAGEN 71
FT /note="F->A: Abolishes histone H3K36me3-binding."
FT /evidence="ECO:0000269|PubMed:23273982"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:6WAV"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:6WAV"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:6WAV"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6WAV"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2E5P"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:6WAV"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6WAV"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6WAV"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5XFO"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:5XFN"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5XFO"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5XFO"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:5XFN"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5XFN"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 251..266
FT /evidence="ECO:0007829|PDB:5XFN"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:5XFN"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:5XFN"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:5XFN"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:5XFN"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5XFO"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:5XFN"
FT MOD_RES O43189-2:360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 567 AA; 62106 MW; E81BA9475565957C CRC64;
MAQPPRLSRS GASSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV
CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV
PRAPAPGEGE GTSWVCRQCV FAIATKRGGA LKKGPYARAM LGMKLSLPYG LKGLDWDAGH
LSNRQQSYCY CGGPGEWNLK MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG
PEKVRRLQLR WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE
RSSRLLSALN SHKDRFISGR EIKKRKCLFG LHARMPPPVE PPTGDGALTS FPSGQGPGGG
VSRPLGKRRR PEPEPLRRRQ KGKVEELGPP SAVRNQPEPQ EQRERAHLQR ALQASVSPPS
PSPNQSYQGS SGYNFRPTDA RCLPSSPIRM FASFHPSAST AGTSGDSGPP DRSPLELHIG
FPTDIPKSAP HSMTASSSSV SSPSPGLPRR SAPPSPLCRS LSPGTGGGVR GGVGYLSRGD
PVRVLARRVR PDGSVQYLVE WGGGGIF
