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   24-JAN-2024, entry version 161.
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   -!- PTM: Ubiquitinated by TRIM26; leading to proteasomal degradation.
CC       {ECO:0000250|UniProtKB:Q9BVI0}.
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; 10090-ENSMUSP00000043138; -.
DR   ProteomicsDB; 288197; -. [Q8BLG0-1]
DR   ProteomicsDB; 288198; -. [Q8BLG0-2]
DR   Antibodypedia; 26384; 143 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000037401.10; ENSMUSP00000043138.9; ENSMUSG00000038116.17. [Q8BLG0-1]
DR   GeneID; 228829; -.
DR   KEGG; mmu:228829; -.
DR   UCSC; uc008nmy.1; mouse. [Q8BLG0-1]
DR   AGR; MGI:2444148; -.
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; IRAIWIK; -.
DR   OrthoDB; 5491784at2759; -.
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   Reactome; R-MMU-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   BioGRID-ORCS; 228829; 5 hits in 82 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 255 other cell types or tissues.
DR   ExpressionAtlas; Q8BLG0; baseline and differential.
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:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd20104; MBT_PHF20L1-like; 1.
DR   CDD; cd20453; Tudor_PHF20; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR041297; Crb2_Tudor.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR043449; PHF20-like.
DR   InterPro; IPR022255; PHF20_AT-hook.
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:SF27; PHD FINGER PROTEIN 20; 1.
DR   PANTHER; PTHR15856; PHD FINGER PROTEIN 20-RELATED; 1.
DR   Pfam; PF02820; MBT; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   Pfam; PF12618; PHF20_AT-hook; 1.
DR   Pfam; PF18115; Tudor_3; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
DR   Genevisible; Q8BLG0; MM.
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; Ubl conjugation; Zinc;
KW   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
//