ID PHF1_MOUSE Reviewed; 559 AA. AC Q9Z1B8; O54808; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 24-JAN-2024, entry version 175. DE RecName: Full=PHD finger protein 1; DE Short=Protein PHF1; DE AltName: Full=Polycomb-like protein 1; DE Short=mPCl1; DE AltName: Full=T-complex testis-expressed 3; GN Name=Phf1; Synonyms=Plc1, Tctex-3, Tctex3; 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 [MRNA]. RC TISSUE=Testis; RX PubMed=9799836; DOI=10.1007/s003359900886; RA Kawakami S., Mitsunaga K., Kikuti Y.Y., Ando A., Inoko H., Yamamura K., RA Abe K.; RT "Tctex3, related to Drosophila polycomblike, is expressed in male germ RT cells and mapped to the mouse T-complex."; RL Mamm. Genome 9:874-880(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NIH Swiss; RX PubMed=10545244; DOI=10.1006/dbio.1999.9473; RA Yoshitake Y., Howard T.L., Christian J.L., Hollenberg S.M.; RT "Misexpression of Polycomb-group proteins in Xenopus alters anterior neural RT development and represses neural target genes."; RL Dev. Biol. 215:375-387(1999). RN [3] RP INTERACTION WITH CHMP1. RX PubMed=11559747; DOI=10.1242/jcs.114.13.2383; RA Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.; RT "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and RT cell-cycle progression."; RL J. Cell Sci. 114:2383-2393(2001). RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [6] RP H3K36ME3-BINDING. 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). 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:18086877). According to other reports, PHF1 recruits the CC PRC2 complex at double-strand breaks (DSBs) and inhibits the activity CC of PRC2. Regulates p53/TP53 stability and prolonges its turnover: may CC act by specifically binding to a methylated from of p53/TP53. CC {ECO:0000269|PubMed:18086877}. CC -!- SUBUNIT: Associated component of the PRC2 complex. Interacts with CC p53/TP53 (By similarity). Interacts with CHMP1. {ECO:0000250, CC ECO:0000269|PubMed:11559747}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18086877}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. CC Note=Localizes specifically to the promoters of numerous target genes. CC Localizes to double-strand breaks (DSBs) sites following DNA damage. CC Colocalizes with NEK6 in the centrosome (By similarity). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Testis-specific. CC -!- DOMAIN: The Tudor domain recognizes and binds H3K36me3. CC {ECO:0000269|PubMed:23104054}. 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; AB011550; BAA25074.1; -; mRNA. DR EMBL; U81490; AAD00518.1; -; mRNA. DR CCDS; CCDS37518.1; -. DR RefSeq; NP_033369.2; NM_009343.3. DR PDB; 5XFQ; X-ray; 2.40 A; A/B=25-360. DR PDBsum; 5XFQ; -. DR AlphaFoldDB; Q9Z1B8; -. DR BMRB; Q9Z1B8; -. DR SMR; Q9Z1B8; -. DR BioGRID; 204083; 3. DR IntAct; Q9Z1B8; 2. DR STRING; 10090.ENSMUSP00000073402; -. DR iPTMnet; Q9Z1B8; -. DR PhosphoSitePlus; Q9Z1B8; -. DR EPD; Q9Z1B8; -. DR MaxQB; Q9Z1B8; -. DR PaxDb; 10090-ENSMUSP00000073402; -. DR PeptideAtlas; Q9Z1B8; -. DR ProteomicsDB; 288196; -. DR Pumba; Q9Z1B8; -. DR Antibodypedia; 14271; 273 antibodies from 28 providers. DR DNASU; 21652; -. DR Ensembl; ENSMUST00000073724.7; ENSMUSP00000073402.6; ENSMUSG00000024193.9. DR GeneID; 21652; -. DR KEGG; mmu:21652; -. DR UCSC; uc008bes.2; mouse. DR AGR; MGI:98647; -. DR CTD; 5252; -. DR MGI; MGI:98647; Phf1. DR VEuPathDB; HostDB:ENSMUSG00000024193; -. DR eggNOG; KOG4323; Eukaryota. DR GeneTree; ENSGT00950000183180; -. DR HOGENOM; CLU_032773_2_0_1; -. DR InParanoid; Q9Z1B8; -. DR OMA; CAGPGWN; -. DR OrthoDB; 5483634at2759; -. DR PhylomeDB; Q9Z1B8; -. DR TreeFam; TF106420; -. DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA. DR BioGRID-ORCS; 21652; 5 hits in 80 CRISPR screens. DR ChiTaRS; Phf1; mouse. DR PRO; PR:Q9Z1B8; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q9Z1B8; Protein. DR Bgee; ENSMUSG00000024193; Expressed in granulocyte and 209 other cell types or tissues. DR ExpressionAtlas; Q9Z1B8; baseline and differential. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:1990226; F:histone methyltransferase binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. 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; ISO:MGI. DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central. DR GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd15500; PHD1_PHF1; 1. DR CDD; cd15582; PHD2_PHF1; 1. DR CDD; cd20449; Tudor_PHF1; 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 InterPro; IPR040477; KDM4-like_Tudor. DR InterPro; IPR025894; Mtf2_C_dom. DR InterPro; IPR031202; PHF1_PDH-finger1. DR InterPro; IPR047010; PHF1_PHD-finger2. DR InterPro; IPR002999; Tudor. DR InterPro; IPR047399; Tudor_PHF1. 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; PHD FINGER PROTEIN 1; 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 PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q9Z1B8; MM. PE 1: Evidence at protein level; KW 3D-structure; Chromatin regulator; Cytoplasm; Cytoskeleton; DNA damage; KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..559 FT /note="PHD finger protein 1" FT /id="PRO_0000059289" 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 338..434 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 448..526 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 367..385 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 478..498 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 249 FT /note="L -> F (in Ref. 2; AAD00518)" FT /evidence="ECO:0000305" FT CONFLICT 344 FT /note="G -> E (in Ref. 1; BAA25074)" FT /evidence="ECO:0000305" FT CONFLICT 377 FT /note="R -> S (in Ref. 1; BAA25074)" FT /evidence="ECO:0000305" FT CONFLICT 555 FT /note="G -> R (in Ref. 1; BAA25074)" FT /evidence="ECO:0000305" FT CONFLICT 558..559 FT /note="IF -> HLPDSLLLLPSPFTHWHFHALDL (in Ref. 1; BAA25074)" FT /evidence="ECO:0000305" FT STRAND 36..40 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 46..55 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 56..59 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 126..130 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 137..144 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 155..164 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 197..200 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 230..233 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 235..238 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 243..246 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 251..265 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 273..276 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 277..283 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 285..288 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 298..311 FT /evidence="ECO:0007829|PDB:5XFQ" FT TURN 313..315 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:5XFQ" FT HELIX 319..322 FT /evidence="ECO:0007829|PDB:5XFQ" FT STRAND 328..334 FT /evidence="ECO:0007829|PDB:5XFQ" SQ SEQUENCE 559 AA; 61140 MW; 6D2EE5F53D6164C2 CRC64; MAQLPRLSRL GAPSLWDPAS PAPTSGPRPR LWEGQDVLAR WTDGLLYLGT IKKVDSAREV CLVQFEDDSQ FLVLWKDISP AALPGEELLC CVCRSETVVP GNRLVSCEKC RHAYHQDCHV PRAPAPGEGE GASWVCRQCV FAIATKRGGA LKKGPYARAM LGMKLSLPYG LKGLDWDAGH LSNRQQSYCY CGGPGEWNLK MLQCRSCLQW FHEACTQCLS KPLLYGDRFY EFECCVCRGG PEKVRRLQLR WVDVAHLVLY HLSVCCKKKY FDFDREILPF TSENWDSLLL GELSDTPKGE RSSQLLSALN SHKDRFISGR EIKKRKCLFG LHARTPPPVE LLTGDGAPTS FPSGQGPGGG VSRPLGKRWR SEPEPLRRRQ KGKVEELGPP TAAHSRHGSR EQRALQASVS PPPPSPNQSY EGSSGYNFRP TDARCLPSSP IRMFASFHPS ASTAGTSGDS EPPDRSPLGL HIGFPTDTPK SSPHSVTASS SSVPALTPGF SRHSPPSPLC RSLSPGTGGG VRGGVSYLSR GDPVRVLARR VRPDGSVQYL VEWGGGGIF //