PHF20_HUMAN
ID PHF20_HUMAN Reviewed; 1012 AA.
AC Q9BVI0; A7E235; B2RB56; E1P5S3; Q566Q2; Q5JWY9; Q66K49; Q9BWV4; Q9BXA3;
AC Q9BZW3; Q9H421; Q9H4J6; Q9NZ22;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=PHD finger protein 20;
DE AltName: Full=Glioma-expressed antigen 2;
DE AltName: Full=Hepatocellular carcinoma-associated antigen 58;
DE AltName: Full=Novel zinc finger protein;
DE AltName: Full=Transcription factor TZP;
GN Name=PHF20; Synonyms=C20orf104, GLEA2, HCA58, NZF, TZP;
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 2), TISSUE SPECIFICITY, AND
RP IDENTIFICATION AS ANTIGEN IN HEPATOCELLULAR CARCINOMA.
RC TISSUE=Hepatoma;
RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA Chen W.-F.;
RT "Large scale identification of human hepatocellular carcinoma-associated
RT antigens by autoantibodies.";
RL J. Immunol. 169:1102-1109(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Cheng J.Q., Kaneko S., Dan H.C., Testa J.R.;
RT "Cloning and characterization of a novel transcription factor (TZP).";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-605.
RC TISSUE=Brain, Eye, and Lymph;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-543 (ISOFORM 1), AND IDENTIFICATION AS
RP ANTIGEN IN GLIOBLASTOMA.
RC TISSUE=Glioblastoma;
RX PubMed=11703362; DOI=10.1046/j.1365-2249.2001.01635.x;
RA Fischer U., Struss A.-K., Hemmer D., Pallasch C.P., Steudel W.-I.,
RA Meese E.;
RT "Glioma-expressed antigen 2 (GLEA2): a novel protein that can elicit immune
RT responses in glioblastoma patients and some controls.";
RL Clin. Exp. Immunol. 126:206-213(2001).
RN [8]
RP IDENTIFICATION AS ANTIGEN IN CHILDHOOD MEDULLOBLASTOMA.
RX PubMed=12800201; DOI=10.1002/ijc.11208;
RA Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A.,
RA Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S.,
RA Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F.,
RA Asmuss H.-P., Bise K., Mautner J.;
RT "Novel tumor antigens identified by autologous antibody screening of
RT childhood medulloblastoma cDNA libraries.";
RL Int. J. Cancer 106:244-251(2003).
RN [9]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-880, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-880, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-843, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20018852; DOI=10.1074/jbc.c109.087981;
RA Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
RA Washburn M.P., Conaway J.W., Conaway R.C.;
RT "Subunit composition and substrate specificity of a MOF-containing histone
RT acetyltransferase distinct from the male-specific lethal (MSL) complex.";
RL J. Biol. Chem. 285:4268-4272(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 4-69 AND 84-147 AND TUDOR DOMAINS.
RX PubMed=22449972; DOI=10.1016/j.febslet.2012.02.012;
RA Adams-Cioaba M.A., Li Z., Tempel W., Guo Y., Bian C., Li Y., Lam R.,
RA Min J.;
RT "Crystal structures of the Tudor domains of human PHF20 reveal novel
RT structural variations on the Royal Family of proteins.";
RL FEBS Lett. 586:859-865(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-69 AND 84-147, STRUCTURE BY NMR
RP OF 84-147 IN COMPLEX WITH DIMETHYLATED P53 PEPTIDE, FUNCTION, SUBUNIT,
RP DISULFIDE BONDS, AND MUTAGENESIS OF CYS-96; TRP-97; CYS-100 AND TYR-103.
RX PubMed=22864287; DOI=10.1038/nsmb.2353;
RA Cui G., Park S., Badeaux A.I., Kim D., Lee J., Thompson J.R., Yan F.,
RA Kaneko S., Yuan Z., Botuyan M.V., Bedford M.T., Cheng J.Q., Mer G.;
RT "PHF20 is an effector protein of p53 double lysine methylation that
RT stabilizes and activates p53.";
RL Nat. Struct. Mol. Biol. 19:916-924(2012).
CC -!- FUNCTION: Methyllysine-binding protein, component of the MOF histone
CC acetyltransferase protein complex. Not required for maintaining the
CC global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus
CC specific histone acetylation, but instead works downstream in
CC transcriptional regulation of MOF target genes (By similarity). As part
CC of the NSL complex it may be involved in acetylation of nucleosomal
CC histone H4 on several lysine residues. Contributes to methyllysine-
CC dependent p53/TP53 stabilization and up-regulation after DNA damage.
CC {ECO:0000250, ECO:0000269|PubMed:20018852,
CC ECO:0000269|PubMed:22864287}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Component of some MLL1/MLL
CC complex, at least composed of the core components KMT2A/MLL1, ASH2L,
CC HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18,
CC CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF,
CC PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1,
CC TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the NSL complex at least
CC composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT,
CC WDR5 and HCFC1. {ECO:0000269|PubMed:15960975,
CC ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:22864287}.
CC -!- INTERACTION:
CC Q9BVI0; P68431: H3C12; NbExp=6; IntAct=EBI-2560802, EBI-79722;
CC Q9BVI0; P62805: H4C9; NbExp=3; IntAct=EBI-2560802, EBI-302023;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20018852}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BVI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVI0-2; Sequence=VSP_007760, VSP_007761;
CC -!- TISSUE SPECIFICITY: Expressed in heart, kidney, liver, lung, pancreas,
CC placenta, spleen and testis. Not expressed in brain, skeletal muscle,
CC colon, ovary, prostate, small intestine and thymus. Expressed in colon
CC and ovary cancer cell lines while it is not expressed in the respective
CC normal tissues. {ECO:0000269|PubMed:12097419}.
CC -!- DOMAIN: The Tudor domain 2 mediates reading of dimethyl-lysine
CC residues.
CC -!- DOMAIN: The Tudor domain 1 doesn't bind dimethyl-lysine residues, due
CC to an atypical and occluded aromatic cage.
CC -!- MISCELLANEOUS: Antibodies against PHF20 are present in sera from
CC patients with hepatocellular carcinoma, glioblastoma and childhood
CC medulloblastula.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF34184.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAK19748.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF220416; AAF34184.1; ALT_FRAME; mRNA.
DR EMBL; AF348207; AAK19748.1; ALT_FRAME; mRNA.
DR EMBL; AY027523; AAK13046.1; -; mRNA.
DR EMBL; AK314503; BAG37103.1; -; mRNA.
DR EMBL; AL078461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76153.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76155.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76156.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76157.1; -; Genomic_DNA.
DR EMBL; BC048210; AAH48210.1; -; mRNA.
DR EMBL; BC080598; AAH80598.1; -; mRNA.
DR EMBL; BC093405; AAH93405.1; -; mRNA.
DR EMBL; BC150178; AAI50179.1; -; mRNA.
DR EMBL; AF258787; AAG49888.1; -; mRNA.
DR CCDS; CCDS13268.1; -. [Q9BVI0-1]
DR RefSeq; NP_057520.2; NM_016436.4. [Q9BVI0-1]
DR RefSeq; XP_016883353.1; XM_017027864.1.
DR RefSeq; XP_016883354.1; XM_017027865.1.
DR RefSeq; XP_016883355.1; XM_017027866.1.
DR RefSeq; XP_016883356.1; XM_017027867.1.
DR PDB; 2LDM; NMR; -; A=84-147.
DR PDB; 3P8D; X-ray; 2.00 A; A/B=84-147.
DR PDB; 3Q1J; X-ray; 2.35 A; A=4-69.
DR PDB; 3QII; X-ray; 2.30 A; A=83-150.
DR PDB; 3SD4; X-ray; 1.93 A; A/B=4-69.
DR PDB; 5TAB; X-ray; 1.25 A; A=651-698.
DR PDB; 5TBN; NMR; -; A=646-699.
DR PDBsum; 2LDM; -.
DR PDBsum; 3P8D; -.
DR PDBsum; 3Q1J; -.
DR PDBsum; 3QII; -.
DR PDBsum; 3SD4; -.
DR PDBsum; 5TAB; -.
DR PDBsum; 5TBN; -.
DR AlphaFoldDB; Q9BVI0; -.
DR SMR; Q9BVI0; -.
DR BioGRID; 119393; 45.
DR ComplexPortal; CPX-809; NSL histone acetyltransferase complex.
DR CORUM; Q9BVI0; -.
DR IntAct; Q9BVI0; 16.
DR MINT; Q9BVI0; -.
DR STRING; 9606.ENSP00000363124; -.
DR iPTMnet; Q9BVI0; -.
DR PhosphoSitePlus; Q9BVI0; -.
DR BioMuta; PHF20; -.
DR DMDM; 32699605; -.
DR EPD; Q9BVI0; -.
DR jPOST; Q9BVI0; -.
DR MassIVE; Q9BVI0; -.
DR MaxQB; Q9BVI0; -.
DR PaxDb; Q9BVI0; -.
DR PeptideAtlas; Q9BVI0; -.
DR PRIDE; Q9BVI0; -.
DR ProteomicsDB; 79207; -. [Q9BVI0-1]
DR ProteomicsDB; 79208; -. [Q9BVI0-2]
DR Antibodypedia; 26384; 128 antibodies from 26 providers.
DR DNASU; 51230; -.
DR Ensembl; ENST00000374012.8; ENSP00000363124.3; ENSG00000025293.17. [Q9BVI0-1]
DR GeneID; 51230; -.
DR KEGG; hsa:51230; -.
DR MANE-Select; ENST00000374012.8; ENSP00000363124.3; NM_016436.5; NP_057520.2.
DR UCSC; uc002xek.2; human. [Q9BVI0-1]
DR CTD; 51230; -.
DR DisGeNET; 51230; -.
DR GeneCards; PHF20; -.
DR HGNC; HGNC:16098; PHF20.
DR HPA; ENSG00000025293; Low tissue specificity.
DR MIM; 610335; gene.
DR neXtProt; NX_Q9BVI0; -.
DR OpenTargets; ENSG00000025293; -.
DR PharmGKB; PA25644; -.
DR VEuPathDB; HostDB:ENSG00000025293; -.
DR eggNOG; KOG1844; Eukaryota.
DR GeneTree; ENSGT00940000156477; -.
DR HOGENOM; CLU_012707_0_0_1; -.
DR InParanoid; Q9BVI0; -.
DR OMA; CSRHFRR; -.
DR OrthoDB; 147824at2759; -.
DR PhylomeDB; Q9BVI0; -.
DR TreeFam; TF106475; -.
DR PathwayCommons; Q9BVI0; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR Reactome; R-HSA-69541; Stabilization of p53.
DR SignaLink; Q9BVI0; -.
DR SIGNOR; Q9BVI0; -.
DR BioGRID-ORCS; 51230; 38 hits in 1082 CRISPR screens.
DR ChiTaRS; PHF20; human.
DR EvolutionaryTrace; Q9BVI0; -.
DR GeneWiki; PHF20; -.
DR GenomeRNAi; 51230; -.
DR Pharos; Q9BVI0; Tbio.
DR PRO; PR:Q9BVI0; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BVI0; protein.
DR Bgee; ENSG00000025293; Expressed in endothelial cell and 210 other tissues.
DR ExpressionAtlas; Q9BVI0; baseline and differential.
DR Genevisible; Q9BVI0; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0044545; C:NSL complex; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd04508; TUDOR; 1.
DR DisProt; DP02427; -.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041297; Crb2_Tudor.
DR InterPro; IPR022255; DUF3776.
DR InterPro; IPR037915; PHF20.
DR InterPro; IPR043449; PHF20-like.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15856; PTHR15856; 1.
DR PANTHER; PTHR15856:SF27; PTHR15856:SF27; 1.
DR Pfam; PF12618; DUF3776; 1.
DR Pfam; PF18115; Tudor_3; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Disulfide bond; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1012
FT /note="PHD finger protein 20"
FT /id="PRO_0000059310"
FT DOMAIN 4..69
FT /note="Tudor 1"
FT DOMAIN 83..147
FT /note="Tudor 2"
FT DNA_BIND 257..269
FT /note="A.T hook"
FT ZN_FING 452..477
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 654..700
FT /note="PHD-type"
FT REGION 142..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..551
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 843
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT DISULFID 96
FT /note="Interchain (with C-100)"
FT /evidence="ECO:0000305|PubMed:22864287"
FT DISULFID 100
FT /note="Interchain (with C-96)"
FT /evidence="ECO:0000305|PubMed:22864287"
FT VAR_SEQ 237..273
FT /note="VDKKPENDIVKSPQENLREPKRKRGRPPSIAPTAVDS -> KTRQTPFHSSY
FT CCGFKLSNFATNNIGTEKKENIKRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12097419"
FT /id="VSP_007760"
FT VAR_SEQ 274..1012
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12097419"
FT /id="VSP_007761"
FT VARIANT 605
FT /note="V -> M (in dbSNP:rs17431878)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051600"
FT MUTAGEN 96
FT /note="C->S: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:22864287"
FT MUTAGEN 97
FT /note="W->A: Abolishes interaction with methylated p53."
FT /evidence="ECO:0000269|PubMed:22864287"
FT MUTAGEN 100
FT /note="C->S: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:22864287"
FT MUTAGEN 103
FT /note="Y->A: Abolishes interaction with methylated p53."
FT /evidence="ECO:0000269|PubMed:22864287"
FT CONFLICT 221..222
FT /note="KE -> QG (in Ref. 7; AAG49888)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="E -> G (in Ref. 7; AAG49888)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="S -> F (in Ref. 6; AAH80598)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="S -> F (in Ref. 7; AAG49888)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="K -> E (in Ref. 3; BAG37103)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="E -> G (in Ref. 3; BAG37103)"
FT /evidence="ECO:0000305"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:3SD4"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:3SD4"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:3SD4"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3SD4"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3SD4"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3SD4"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3P8D"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:3P8D"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3P8D"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3P8D"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3P8D"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3P8D"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:5TAB"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:5TAB"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:5TAB"
FT TURN 678..682
FT /evidence="ECO:0007829|PDB:5TAB"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:5TAB"
FT TURN 695..697
FT /evidence="ECO:0007829|PDB:5TAB"
FT CONFLICT Q9BVI0-2:237..239
FT /note="KTR -> KKTS (in Ref. 1; AAF34184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 115386 MW; 1CDBADC23D007503 CRC64;
MTKHPPNRRG ISFEVGAQLE ARDRLKNWYP AHIEDIDYEE GKVLIHFKRW NHRYDEWFCW
DSPYLRPLEK IQLRKEGLHE EDGSSEFQIN EQVLACWSDC RFYPAKVTAV NKDGTYTVKF
YDGVVQTVKH IHVKAFSKDQ NIVGNARPKE TDHKSLSSSP DKREKFKEQR KATVNVKKDK
EDKPLKTEKR PKQPDKEGKL ICSEKGKVSE KSLPKNEKED KENISENDRE YSGDAQVDKK
PENDIVKSPQ ENLREPKRKR GRPPSIAPTA VDSNSQTLQP ITLELRRRKI SKGCEVPLKR
PRLDKNSSQE KSKNYSENTD KDLSRRRSSR LSTNGTHEIL DPDLVVSDLV DTDPLQDTLS
STKESEEGQL KSALEAGQVS SALTCHSFGD GSGAAGLELN CPSMGENTMK TEPTSPLVEL
QEISTVEVTN TFKKTDDFGS SNAPAVDLDH KFRCKVVDCL KFFRKAKLLH YHMKYFHGME
KSLEPEESPG KRHVQTRGPS ASDKPSQETL TRKRVSASSP TTKDKEKNKE KKFKEFVRVK
PKKKKKKKKK TKPECPCSEE ISDTSQEPSP PKAFAVTRCG SSHKPGVHMS PQLHGPESGH
HKGKVKALEE DNLSESSSES FLWSDDEYGQ DVDVTTNPDE ELDGDDRYDF EVVRCICEVQ
EENDFMIQCE ECQCWQHGVC MGLLEENVPE KYTCYVCQDP PGQRPGFKYW YDKEWLSRGH
MHGLAFLEEN YSHQNAKKIV ATHQLLGDVQ RVIEVLHGLQ LKMSILQSRE HPDLPLWCQP
WKQHSGEGRS HFRNIPVTDT RSKEEAPSYR TLNGAVEKPR PLALPLPRSV EESYITSEHC
YQKPRAYYPA VEQKLVVETR GSALDDAVNP LHENGDDSLS PRLGWPLDQD RSKGDSDPKP
GSPKVKEYVS KKALPEEAPA RKLLDRGGEG LLSSQHQWQF NLLTHVESLQ DEVTHRMDSI
EKELDVLESW LDYTGELEPP EPLARLPQLK HCIKQLLMDL GKVQQIALCC ST
