PHF1_MOUSE
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 03-AUG-2022, entry version 167.
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}.
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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; Q9Z1B8; -.
DR PeptideAtlas; Q9Z1B8; -.
DR PRIDE; Q9Z1B8; -.
DR ProteomicsDB; 288196; -.
DR Antibodypedia; 14271; 253 antibodies from 28 providers.
DR DNASU; 21652; -.
DR Ensembl; ENSMUST00000073724; ENSMUSP00000073402; ENSMUSG00000024193.
DR GeneID; 21652; -.
DR KEGG; mmu:21652; -.
DR UCSC; uc008bes.2; mouse.
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; QPWEPTP; -.
DR OrthoDB; 281828at2759; -.
DR PhylomeDB; Q9Z1B8; -.
DR TreeFam; TF106420; -.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR BioGRID-ORCS; 21652; 5 hits in 74 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 206 other tissues.
DR ExpressionAtlas; Q9Z1B8; baseline and differential.
DR Genevisible; Q9Z1B8; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
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; 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
