PHF20_MOUSE
ID PHF20_MOUSE Reviewed; 1010 AA.
AC Q8BLG0; Q8BMA2; Q8BYR4; Q921N1;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=PHD finger protein 20;
DE AltName: Full=Hepatocellular carcinoma-associated antigen 58 homolog;
GN Name=Phf20; Synonyms=Hca58;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 621-1010.
RC TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TUDOR DOMAINS, MUTAGENESIS OF TRP-97 AND
RP TYR-103, AND DISRUPTION PHENOTYPE.
RX PubMed=22072714; DOI=10.1074/jbc.m111.271163;
RA Badeaux A.I., Yang Y., Cardenas K., Vemulapalli V., Chen K., Kusewitt D.,
RA Richie E., Li W., Bedford M.T.;
RT "Loss of the methyl-lysine effector molecule PHF20 impacts the expression
RT of genes regulated by the lysine acetyltransferase MOF.";
RL J. Biol. Chem. 287:429-437(2012).
CC -!- FUNCTION: Contributes to methyllysine-dependent p53/TP53 stabilization
CC and up-regulation after DNA damage (By similarity). Methyllysine-
CC binding protein, component of the MOF histone acetyltransferase protein
CC complex. Not required for maintaining the global histone H4 'Lys-16'
CC acetylation (H4K16ac) levels or locus specific histone acetylation, but
CC instead works downstream in transcriptional regulation of MOF target
CC genes. As part of the NSL complex it may be involved in acetylation of
CC nucleosomal histone H4 on several lysine residues. {ECO:0000250,
CC ECO:0000269|PubMed:22072714}.
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, MYST1/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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22072714}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BLG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLG0-2; Sequence=VSP_007762;
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. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice die shortly after birth and display a wide
CC variety of phenotypes within the skeletal and hematopoietic systems.
CC {ECO:0000269|PubMed:22072714}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
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DR EMBL; AK033017; BAC28129.1; -; mRNA.
DR EMBL; AK038573; BAC30050.2; -; mRNA.
DR EMBL; AK045309; BAC32304.1; -; mRNA.
DR EMBL; BC011337; AAH11337.1; -; mRNA.
DR CCDS; CCDS38297.1; -. [Q8BLG0-1]
DR RefSeq; NP_766262.2; NM_172674.2. [Q8BLG0-1]
DR AlphaFoldDB; Q8BLG0; -.
DR SMR; Q8BLG0; -.
DR BioGRID; 230779; 15.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR IntAct; Q8BLG0; 4.
DR STRING; 10090.ENSMUSP00000043138; -.
DR iPTMnet; Q8BLG0; -.
DR PhosphoSitePlus; Q8BLG0; -.
DR jPOST; Q8BLG0; -.
DR MaxQB; Q8BLG0; -.
DR PaxDb; Q8BLG0; -.
DR PRIDE; Q8BLG0; -.
DR ProteomicsDB; 288197; -. [Q8BLG0-1]
DR ProteomicsDB; 288198; -. [Q8BLG0-2]
DR Antibodypedia; 26384; 128 antibodies from 26 providers.
DR Ensembl; ENSMUST00000037401; ENSMUSP00000043138; ENSMUSG00000038116. [Q8BLG0-1]
DR GeneID; 228829; -.
DR KEGG; mmu:228829; -.
DR UCSC; uc008nmy.1; mouse. [Q8BLG0-1]
DR CTD; 51230; -.
DR MGI; MGI:2444148; Phf20.
DR VEuPathDB; HostDB:ENSMUSG00000038116; -.
DR eggNOG; KOG1844; Eukaryota.
DR GeneTree; ENSGT00940000156477; -.
DR HOGENOM; CLU_012707_0_0_1; -.
DR InParanoid; Q8BLG0; -.
DR OMA; CSRHFRR; -.
DR OrthoDB; 147824at2759; -.
DR PhylomeDB; Q8BLG0; -.
DR TreeFam; TF106475; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR Reactome; R-MMU-69541; Stabilization of p53.
DR BioGRID-ORCS; 228829; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Phf20; mouse.
DR PRO; PR:Q8BLG0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BLG0; protein.
DR Bgee; ENSMUSG00000038116; Expressed in animal zygote and 253 other tissues.
DR ExpressionAtlas; Q8BLG0; baseline and differential.
DR Genevisible; Q8BLG0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
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; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041297; Crb2_Tudor.
DR InterPro; IPR022255; DUF3776.
DR InterPro; IPR004092; Mbt.
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; PF02820; MBT; 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 Acetylation; Alternative splicing; Chromatin regulator; Disulfide bond;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1010
FT /note="PHD finger protein 20"
FT /id="PRO_0000059311"
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 455..485
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 657..703
FT /note="PHD-type"
FT REGION 142..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..902
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 267..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 501..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVI0"
FT MOD_RES 841
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVI0"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVI0"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVI0"
FT DISULFID 96
FT /note="Interchain (with C-100)"
FT /evidence="ECO:0000250"
FT DISULFID 100
FT /note="Interchain (with C-96)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..28
FT /note="MTKHPPNRRGISFEVGAQLEARDRLKNW -> GAARTVLLSVGLERRSRSGA
FT VR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_007762"
FT MUTAGEN 97
FT /note="W->A: Abolishes Methyllysine-binding."
FT /evidence="ECO:0000269|PubMed:22072714"
FT MUTAGEN 103
FT /note="Y->A: Abolishes Methyllysine-binding."
FT /evidence="ECO:0000269|PubMed:22072714"
FT CONFLICT 817
FT /note="A -> T (in Ref. 2; AAH11337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1010 AA; 115280 MW; 2BC32811A520342D CRC64;
MTKHPPNRRG ISFEVGAQLE ARDRLKNWYP AHIEDIDYEE GRVLIHFKRW NHRYDEWFCW
DSPYLRPLEK IQLRKEGLHD EDGSSEFQIN QQVLACWSDC RFYPARVTAV NKDGTYTVKF
YDGVVQTVKH IHVKAFSKDQ NIVGNARPKE TDHKSLSSSP EKREKFKEQR KVTVNVKKDK
VEKALKTEKR PKQPDKEGKL ICSEKGKVSE KSLPKNEKED KENISENERE YSGDAQVEKK
PEKDLVKNPQ ENLKEPKRKR GRPPSITPTA VDSNSQTLQP ITLELRRRKI SKRSDTPLKR
PRLDKNSPQE QSKKRSENSD KDLSRRRSSR LSTNGTREIL DPDSIVPDLV HTVDTNPLPD
KSPSAKDSAE GQLKSPLEAG QVSSALTCHP IGDGLGAADL ELNCKSMGEN TMKTEPVSPL
AEVQEVSTVE VPNTLKKVDD SVTLNVPAVD LDHKFRCKVL DCLKFFRKAK LLHYHMKYFH
GMEKSPEPEE GPGKTHVQTR GSAVPDKTSQ ESLTRKRVSA SSPTAKEKEK TKEKKFKELV
RVKPKKKKKK KKKTKPECPC SEDISDTSQE PSPPKTFAVT RCGSSHKPGV HMSPQLHGSD
NGNHKGKLKT CEEDNLSESS SESFLWSDEE YGQDVDVTTN PDEELEGDDR YDFEVVRCIC
EVQEENDFMI QCEECQCWQH GVCMGLLEEN VPEKYTCYVC QDPPGQRPGF KYWYDKEWLS
RGHMHGLAFL DQNYSHQNAR KIVATHQLLG DVQRVIQVLH GLQLKMSILQ SREHPDLQLW
CQPWKQHSGE GRAHPRHIHI TDARSEESPS YRTLNGAVEK PSPLPRSVEE SYITSEHCYQ
KPRAYYPAVE QRLVVETRGS ALDAAVSPLC ENGDDSLSPR LGWPIDQDRS RGDIDPKPSS
PKVREYISKN VLPEETPARK LLDRGGEGLV SSQHQWQFNL LTHVESLQDE VTHRMDSIEK
ELDVLESWLD YTGELEPPEP LARLPQLKHC IKQLLTDLGK VQQIALCCST
