PRDM9_MOUSE
ID PRDM9_MOUSE Reviewed; 843 AA.
AC Q96EQ9; B8JJZ8; Q0D2N4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Histone-lysine N-methyltransferase PRDM9 {ECO:0000305};
DE AltName: Full=Hybrid sterility protein 1;
DE AltName: Full=Meiosis-induced factor containing a PR/SET domain and zinc-finger motif;
DE AltName: Full=PR domain zinc finger protein 9;
DE AltName: Full=PR domain-containing protein 9;
DE AltName: Full=Protein-lysine N-methyltransferase PRDM9 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:28126738};
DE AltName: Full=[histone H3]-lysine36 N-trimethyltransferase PRDM9 {ECO:0000305};
DE EC=2.1.1.359 {ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:27362481};
DE AltName: Full=[histone H3]-lysine4 N-trimethyltransferase PRDM9 {ECO:0000305};
DE EC=2.1.1.354 {ECO:0000269|PubMed:16292313, ECO:0000269|PubMed:24095733, ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:27362481};
DE AltName: Full=[histone H3]-lysine9 N-trimethyltransferase PRDM9 {ECO:0000305};
DE EC=2.1.1.355 {ECO:0000269|PubMed:27362481};
DE AltName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase PRDM9 {ECO:0000305};
DE EC=2.1.1.362 {ECO:0000269|PubMed:24785241};
DE AltName: Full=[histone H4]-lysine20 N-methyltransferase PRDM9 {ECO:0000305};
DE EC=2.1.1.361 {ECO:0000269|PubMed:24785241};
GN Name=Prdm9 {ECO:0000312|MGI:MGI:2384854}; Synonyms=Hst1, Meisetz;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RA Brathwaite M., Waeltz P., Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Eye;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3),
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF TYR-276 AND GLY-278.
RX PubMed=16292313; DOI=10.1038/nature04112;
RA Hayashi K., Yoshida K., Matsui Y.;
RT "A histone H3 methyltransferase controls epigenetic events required for
RT meiotic prophase.";
RL Nature 438:374-378(2005).
RN [5]
RP IDENTIFICATION AS A SPECIATION GENE.
RX PubMed=19074312; DOI=10.1126/science.1163601;
RA Mihola O., Trachtulec Z., Vlcek C., Schimenti J.C., Forejt J.;
RT "A mouse speciation gene encodes a meiotic histone H3 methyltransferase.";
RL Science 323:373-375(2009).
RN [6]
RP FUNCTION, DOMAIN, AND POLYMORPHISM.
RX PubMed=22028627; DOI=10.1371/journal.pbio.1001176;
RA Grey C., Barthes P., Chauveau-Le Friec G., Langa F., Baudat F.,
RA de Massy B.;
RT "Mouse PRDM9 DNA-binding specificity determines sites of histone H3 lysine
RT 4 trimethylation for initiation of meiotic recombination.";
RL PLoS Biol. 9:E1001176-E1001176(2011).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-321.
RX PubMed=24785241; DOI=10.1042/bj20140374;
RA Koh-Stenta X., Joy J., Poulsen A., Li R., Tan Y., Shim Y., Min J.H., Wu L.,
RA Ngo A., Peng J., Seetoh W.G., Cao J., Wee J.L., Kwek P.Z., Hung A.,
RA Lakshmanan U., Flotow H., Guccione E., Hill J.;
RT "Characterization of the histone methyltransferase PRDM9 using biochemical,
RT biophysical and chemical biology techniques.";
RL Biochem. J. 461:323-334(2014).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25894966; DOI=10.1007/s00412-015-0511-3;
RA Sun F., Fujiwara Y., Reinholdt L.G., Hu J., Saxl R.L., Baker C.L.,
RA Petkov P.M., Paigen K., Handel M.A.;
RT "Nuclear localization of PRDM9 and its role in meiotic chromatin
RT modifications and homologous synapsis.";
RL Chromosoma 124:397-415(2015).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27362481; DOI=10.1371/journal.pgen.1006146;
RA Powers N.R., Parvanov E.D., Baker C.L., Walker M., Petkov P.M., Paigen K.;
RT "The Meiotic Recombination Activator PRDM9 Trimethylates Both H3K36 and
RT H3K4 at Recombination Hotspots In Vivo.";
RL PLoS Genet. 12:E1006146-E1006146(2016).
RN [10]
RP METHYLATION AT LYS-368; LYS-374 AND LYS-372, BIOPHYSICOCHEMICAL PROPERTIES,
RP IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-207; LYS-226;
RP LYS-297; CYS-321; LYS-338; LYS-368; LYS-372; LYS-374 AND LYS-375, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=28126738; DOI=10.1042/bcj20161067;
RA Koh-Stenta X., Poulsen A., Li R., Wee J.L., Kwek P.Z., Chew S.Y., Peng J.,
RA Wu L., Guccione E., Joy J., Hill J.;
RT "Discovery and characterisation of the automethylation properties of
RT PRDM9.";
RL Biochem. J. 474:971-982(2017).
RN [11]
RP INTERACTION WITH CXXC1; EWSR1; EHMT2; REC8; SYCP3; SYCP1 AND CDYL,
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=27932493; DOI=10.1091/mbc.e16-09-0686;
RA Parvanov E.D., Tian H., Billings T., Saxl R.L., Spruce C., Aithal R.,
RA Krejci L., Paigen K., Petkov P.M.;
RT "PRDM9 interactions with other proteins provide a link between
RT recombination hotspots and the chromosomal axis in meiosis.";
RL Mol. Biol. Cell 28:488-499(2017).
RN [12]
RP SUBCELLULAR LOCATION, POLYMORPHISM, FUNCTION, AND DOMAIN.
RX PubMed=29478809; DOI=10.1016/j.molcel.2018.01.033;
RA Diagouraga B., Clement J.A.J., Duret L., Kadlec J., de Massy B., Baudat F.;
RT "PRDM9 Methyltransferase Activity Is Essential for Meiotic DNA Double-
RT Strand Break Formation at Its Binding Sites.";
RL Mol. Cell 69:853-865(2018).
RN [13]
RP INTERACTION WITH CXXC1.
RX PubMed=30365547; DOI=10.1371/journal.pgen.1007657;
RA Tian H., Billings T., Petkov P.M.;
RT "CXXC1 is not essential for normal DNA double-strand break formation and
RT meiotic recombination in mouse.";
RL PLoS Genet. 14:E1007657-E1007657(2018).
RN [14]
RP FUNCTION.
RX PubMed=32374261; DOI=10.7554/elife.53459;
RA Huang T., Yuan S., Gao L., Li M., Yu X., Zhang J., Yin Y., Liu C.,
RA Zhang C., Lu G., Li W., Liu J., Chen Z.J., Liu H.;
RT "The histone modification reader ZCWPW1 links histone methylation to PRDM9-
RT induced double-strand break repair.";
RL Elife 9:0-0(2020).
RN [15] {ECO:0007744|PDB:4C1Q}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 198-368 IN COMPLEX WITH
RP DIMETHYLATED H3K4 PEPTIDE; ZINC AND S-ADENOSYL-L-METHIONINE, CATALYTIC
RP ACTIVITY, REGION, SUBUNIT, MUTAGENESIS OF TYR-276; TYR-341 AND TYR-357, AND
RP FUNCTION.
RX PubMed=24095733; DOI=10.1016/j.celrep.2013.08.035;
RA Wu H., Mathioudakis N., Diagouraga B., Dong A., Dombrovski L., Baudat F.,
RA Cusack S., de Massy B., Kadlec J.;
RT "Molecular basis for the regulation of the H3K4 methyltransferase activity
RT of PRDM9.";
RL Cell Rep. 5:13-20(2013).
CC -!- FUNCTION: Histone methyltransferase that sequentially mono-, di-, and
CC tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3
CC to produce respectively trimethylated 'Lys-4' (H3K4me3) and
CC trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in
CC meiotic prophase by determining hotspot localization thereby promoting
CC meiotic recombination (PubMed:16292313, PubMed:24095733,
CC PubMed:27362481, PubMed:24785241, PubMed:29478809). Can also methylate
CC all four core histones with H3 being the best substrate and the most
CC highly modified (PubMed:24785241, PubMed:27362481). Is also able, on
CC one hand, to mono and di-methylate H4K20 and on other hand to
CC trimethylate H3K9 with the di-methylated H3K9 as the best substrate
CC (PubMed:24785241, PubMed:27362481). During meiotic prophase, binds
CC specific DNA sequences through its zinc finger domains thereby
CC determining hotspot localization where it promotes local H3K4me3 and
CC H3K36me3 enrichment on the same nucleosomes through its histone
CC methyltransferase activity (PubMed:22028627, PubMed:27362481,
CC PubMed:29478809). Thereby promotes double-stranded breaks (DSB)
CC formation, at this subset of PRDM9-binding sites, that initiates
CC meiotic recombination for the proper meiotic progression
CC (PubMed:16292313, PubMed:29478809). During meiotic progression hotspot-
CC bound PRDM9 interacts with several complexes; in early leptonema binds
CC CDYL and EHMT2 followed by EWSR1 and CXXC1 by the end of leptonema
CC (PubMed:27932493). EWSR1 joins PRDM9 with the chromosomal axis through
CC REC8 (PubMed:27932493). In this way, controls the DSB repair pathway,
CC pairing of homologous chromosomes and sex body formation
CC (PubMed:25894966, PubMed:16292313). Moreover plays a central role in
CC the transcriptional activation of genes during early meiotic prophase
CC thanks to H3K4me3 and H3K36me3 enrichment that represents a specific
CC tag for epigenetic transcriptional activation (PubMed:16292313). In
CC addition performs automethylation (PubMed:28126738). Acetylation and
CC phosphorylation of histone H3 attenuate or prevent histone H3
CC methylation (PubMed:27362481). {ECO:0000269|PubMed:16292313,
CC ECO:0000269|PubMed:22028627, ECO:0000269|PubMed:24095733,
CC ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:25894966,
CC ECO:0000269|PubMed:27362481, ECO:0000269|PubMed:27932493,
CC ECO:0000269|PubMed:28126738, ECO:0000269|PubMed:29478809,
CC ECO:0000269|PubMed:32374261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000269|PubMed:28126738};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000269|PubMed:28126738};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54200, Rhea:RHEA-COMP:13826, Rhea:RHEA-
CC COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61961, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000269|PubMed:28126738};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54201;
CC Evidence={ECO:0000269|PubMed:28126738};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000269|PubMed:16292313, ECO:0000269|PubMed:24095733,
CC ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:27362481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60261;
CC Evidence={ECO:0000269|PubMed:16292313, ECO:0000269|PubMed:24095733,
CC ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:27362481};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:27362481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60325;
CC Evidence={ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:27362481};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000269|PubMed:27362481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60277;
CC Evidence={ECO:0000269|PubMed:27362481};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000269|PubMed:24785241};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60345;
CC Evidence={ECO:0000269|PubMed:24785241};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC Evidence={ECO:0000269|PubMed:24785241};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000269|PubMed:24785241};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 uM for histone octamer {ECO:0000269|PubMed:24785241};
CC KM=0.19 uM for H3 protein {ECO:0000269|PubMed:24785241};
CC KM=3.21 uM for H3 peptide 1-21 {ECO:0000269|PubMed:24785241};
CC KM=5.47 uM for H4 peptide 1-36 {ECO:0000269|PubMed:24785241};
CC KM=22.29 uM for S-adenosyl-L-methionine (with histone octamer as
CC substrate) {ECO:0000269|PubMed:24785241};
CC KM=19.01 uM for S-adenosyl-L-methionine (with H3 protein as
CC substrate) {ECO:0000269|PubMed:24785241};
CC KM=8.23 uM for S-adenosyl-L-methionine (with H3 peptide 1-21 as
CC substrate) {ECO:0000269|PubMed:24785241};
CC KM=81.66 uM for S-adenosyl-L-methionine (with H4 peptide 1-36 as
CC substrate) {ECO:0000269|PubMed:24785241};
CC KM=34.7 uM for automethylation {ECO:0000269|PubMed:28126738};
CC KM=8.23 uM for H3 peptide {ECO:0000269|PubMed:28126738};
CC -!- SUBUNIT: Homodimer (PubMed:24095733). Interacts with EHMT2 and CDYL;
CC interaction only takes place when PRDM9 is bound to hotspot DNA
CC (PubMed:27932493). Interacts with CXXC1; this interaction does not link
CC PRDM9-activated recombination hotspot sites with DSB machinery and is
CC not required for the hotspot recognition pathway (PubMed:27932493,
CC PubMed:30365547). Forms a complex with EWSR1, REC8, SYCP3 and SYCP1;
CC complex formation is dependent of phosphorylated form of REC8 and
CC requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the
CC chromosomal axis through REC8 (PubMed:27932493).
CC {ECO:0000269|PubMed:24095733, ECO:0000269|PubMed:27932493,
CC ECO:0000269|PubMed:30365547}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25894966,
CC ECO:0000269|PubMed:27932493, ECO:0000269|PubMed:29478809}. Chromosome
CC {ECO:0000269|PubMed:29478809}. Note=Localizes in nuclei of pre-
CC leptotene, leptotene, and early to mid-zygotene spermatocytes.
CC {ECO:0000269|PubMed:25894966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Meisetz;
CC IsoId=Q96EQ9-1; Sequence=Displayed;
CC Name=2; Synonyms=Meisetz-S1;
CC IsoId=Q96EQ9-2; Sequence=VSP_036376, VSP_036377;
CC Name=3; Synonyms=Meisetz-S2;
CC IsoId=Q96EQ9-3; Sequence=VSP_036375, VSP_036378;
CC Name=4;
CC IsoId=Q96EQ9-4; Sequence=VSP_036374, VSP_036376, VSP_036377;
CC -!- TISSUE SPECIFICITY: Specifically expressed in germ cells entering
CC meiotic prophase in female fetal gonads and in postnatal testis
CC (PubMed:16292313). Expressed in early meiotic prophase
CC (PubMed:27932493). {ECO:0000269|PubMed:16292313,
CC ECO:0000269|PubMed:27932493}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed during meiotic prophase.
CC Transiently increases in female gonads from 13.5 dpc to 16.5 dpc, the
CC time during which meiosis proceeds from pre-meiotic replication to
CC pachytene stages. Its expression is barely detectable in fetal male
CC gonads. In adults, it is expressed in testis, but not in any other
CC tissue tested. Abundance increases from 10 d post partum (dpp) to 18
CC dpp, during which time the first wave of spermatogenesis proceeds
CC synchronously from pre-leptotene to pachytene stages.
CC {ECO:0000269|PubMed:16292313}.
CC -!- DOMAIN: The C2H2-type zinc fingers determine the hotspot localization
CC through its binding to specific DNA sequences (PubMed:22028627,
CC PubMed:29478809). Variations in their sequence affect affinity towards
CC DNA-binding motif (PubMed:22028627, PubMed:29478809).
CC {ECO:0000269|PubMed:22028627, ECO:0000269|PubMed:29478809}.
CC -!- PTM: Mono-methylated; automethylated (PubMed:28126738). Tri-methylated;
CC automethylated (PubMed:28126738). Mono-methylation is predominant;
CC automethylation is lower and slower than H3 peptide methylation and is
CC in a highest S-adenosyl-L-methionine concentration-dependent
CC (PubMed:28126738). There are two major sites for automethylation at
CC Lys-368 and Lys-374 (PubMed:28126738). Lysines can be simultaneously
CC methylated, such as Lys-368(me3)/Lys-372(me1), Lys-368(me1)/Lys-
CC 374(me1) and Lys-368(me1)/Lys-372(me1)/Lys-374(me1) (PubMed:28126738).
CC Automethylation is an intramolecular (cis) process (PubMed:28126738).
CC {ECO:0000269|PubMed:28126738}.
CC -!- POLYMORPHISM: Several alleles exist depending on both the number of
CC zinc finger C2H2 type domains and their identity (PubMed:22028627).
CC Each allele binds to a specific hotspot set (PubMed:29478809). Both
CC polymorphisms in the zinc finger C2H2 type domains and in DNA target
CC sequence control recombination at hotspot (PubMed:22028627). The
CC affinity of each allele for its DNA-binding site can vary histone
CC methyltransferase activity (PubMed:29478809).
CC {ECO:0000269|PubMed:22028627, ECO:0000269|PubMed:29478809}.
CC -!- DISRUPTION PHENOTYPE: Knockout homozygous mice are sterile in both
CC sexes. {ECO:0000269|PubMed:16292313, ECO:0000269|PubMed:27932493}.
CC -!- MISCELLANEOUS: Represents a speciation gene in mus genus. Prdm9 is one
CC of several genes responsible for hybrid sterility between M.musculus
CC and house mouse (PubMed:19074312). Hybrid sterility is defined as a
CC situation where parental forms, each fertile inter se, produce
CC infertile offspring (PubMed:19074312). Intersubspecific hybrids of
CC house mouse display spermatogenic failures that are due to variations
CC in the Prdm9 gene (PubMed:19074312). {ECO:0000269|PubMed:19074312}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- CAUTION: Firstly described as not catalyzing the monomethylation of
CC unmethylated H3 peptide (PubMed:16292313). However other in vitro
CC experiments described that can also methylate unmodified 'Lys-4' of
CC histone H3 (PubMed:24095733, PubMed:24785241, PubMed:27362481).
CC {ECO:0000269|PubMed:16292313, ECO:0000269|PubMed:24095733,
CC ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:27362481}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49903.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY294423; AAQ01511.1; -; Genomic_DNA.
DR EMBL; AC154378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT033750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012016; AAH12016.1; -; mRNA.
DR EMBL; BC049903; AAH49903.1; ALT_INIT; mRNA.
DR CCDS; CCDS49963.2; -. [Q96EQ9-1]
DR CCDS; CCDS88997.1; -. [Q96EQ9-4]
DR PDB; 4C1Q; X-ray; 2.30 A; A/B=198-368.
DR PDBsum; 4C1Q; -.
DR AlphaFoldDB; Q96EQ9; -.
DR SMR; Q96EQ9; -.
DR STRING; 10090.ENSMUSP00000131871; -.
DR iPTMnet; Q96EQ9; -.
DR PhosphoSitePlus; Q96EQ9; -.
DR PaxDb; Q96EQ9; -.
DR PRIDE; Q96EQ9; -.
DR ProteomicsDB; 289889; -. [Q96EQ9-1]
DR ProteomicsDB; 289890; -. [Q96EQ9-2]
DR ProteomicsDB; 289891; -. [Q96EQ9-3]
DR ProteomicsDB; 289892; -. [Q96EQ9-4]
DR Antibodypedia; 67566; 66 antibodies from 16 providers.
DR Ensembl; ENSMUST00000147532; ENSMUSP00000118454; ENSMUSG00000051977. [Q96EQ9-4]
DR Ensembl; ENSMUST00000167994; ENSMUSP00000131871; ENSMUSG00000051977. [Q96EQ9-1]
DR UCSC; uc008aos.1; mouse. [Q96EQ9-4]
DR UCSC; uc029tan.1; mouse. [Q96EQ9-1]
DR MGI; MGI:2384854; Prdm9.
DR VEuPathDB; HostDB:ENSMUSG00000051977; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000158211; -.
DR HOGENOM; CLU_983403_0_0_1; -.
DR InParanoid; Q96EQ9; -.
DR PhylomeDB; Q96EQ9; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR ChiTaRS; Prdm9; mouse.
DR PRO; PR:Q96EQ9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q96EQ9; protein.
DR Bgee; ENSMUSG00000051977; Expressed in retinal neural layer and 70 other tissues.
DR ExpressionAtlas; Q96EQ9; baseline and differential.
DR Genevisible; Q96EQ9; MM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IMP:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0010844; F:recombination hotspot binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:UniProtKB.
DR GO; GO:0007292; P:female gamete generation; IMP:UniProtKB.
DR GO; GO:0097676; P:histone H3-K36 dimethylation; IDA:UniProtKB.
DR GO; GO:0097198; P:histone H3-K36 trimethylation; IDA:UniProtKB.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; IDA:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; IDA:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IDA:UniProtKB.
DR GO; GO:0051567; P:histone H3-K9 methylation; IDA:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; IDA:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0048232; P:male gamete generation; IMP:UniProtKB.
DR GO; GO:0007127; P:meiosis I; IMP:MGI.
DR GO; GO:0006311; P:meiotic gene conversion; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1905516; P:positive regulation of fertilization; IMP:UniProtKB.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; ISS:UniProtKB.
DR GO; GO:1905437; P:positive regulation of histone H3-K4 trimethylation; IDA:UniProtKB.
DR GO; GO:0060903; P:positive regulation of meiosis I; IMP:MGI.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd19193; PR-SET_PRDM7_9; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR003655; aKRAB.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR044417; PRDM7_9_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019041; SSXRD_motif.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF09514; SSXRD; 1.
DR Pfam; PF00096; zf-C2H2; 11.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50806; KRAB_RELATED; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Chromatin regulator;
KW Chromosome; DNA-binding; Meiosis; Metal-binding; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..843
FT /note="Histone-lysine N-methyltransferase PRDM9"
FT /id="PRO_0000363960"
FT DOMAIN 23..86
FT /note="KRAB-related"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00120"
FT DOMAIN 244..358
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 388..411
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..531
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 537..559
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 565..587
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 593..615
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 621..643
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 649..671
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 677..699
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 705..727
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 733..755
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 761..783
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 789..811
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 817..839
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..805
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT COMPBIAS 119..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 256..258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 288..294
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 320..321
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24095733,
FT ECO:0007744|PDB:4C1Q"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 707
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 735
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 738
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 751
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 755
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 763
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 766
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 779
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 783
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 794
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 807
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT MOD_RES 368
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:28126738"
FT MOD_RES 368
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:28126738"
FT MOD_RES 372
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:28126738"
FT MOD_RES 374
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:28126738"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036374"
FT VAR_SEQ 382..418
FT /note="ELRTEIHPCLLCSLAFSSQKFLTQHMEWNHRTEIFPG -> DLFIIICKYTV
FT AVFRHTRRGSQILLRMVVSHHVVAGI (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_036375"
FT VAR_SEQ 382..404
FT /note="ELRTEIHPCLLCSLAFSSQKFLT -> GGHYYDSLKKKEKREFSLRIFIF
FT (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036376"
FT VAR_SEQ 405..843
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036377"
FT VAR_SEQ 419..843
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_036378"
FT MUTAGEN 207
FT /note="K->A: Does not affect histone-lysine N-
FT methyltransferase activity. Does not affect protein-lysine
FT N-methyltransferas activity."
FT /evidence="ECO:0000269|PubMed:28126738"
FT MUTAGEN 226
FT /note="K->A: Does not affect histone-lysine N-
FT methyltransferase activity. Does not affect protein-lysine
FT N-methyltransferas activity."
FT /evidence="ECO:0000269|PubMed:28126738"
FT MUTAGEN 276
FT /note="Y->F: Abolishes histone-lysine N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:16292313,
FT ECO:0000269|PubMed:24095733"
FT MUTAGEN 278
FT /note="G->A: Abolishes histone-lysine N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:16292313"
FT MUTAGEN 297
FT /note="K->A: Does not affect histone-lysine N-
FT methyltransferase activity. Does not affect protein-lysine
FT N-methyltransferas activity."
FT /evidence="ECO:0000269|PubMed:28126738"
FT MUTAGEN 321
FT /note="C->P: Abolishes histone-lysine N-methyltransferase
FT activity over enzyme concentration of 0-80 nM. Weakened
FT histone-lysine N-methyltransferase activity over enzyme
FT concentration > 5 uM. Abolishes binding with S-adenosyl-L-
FT methionine. Abolishes protein-lysine N-methyltransferas."
FT /evidence="ECO:0000269|PubMed:24785241,
FT ECO:0000269|PubMed:28126738"
FT MUTAGEN 338
FT /note="K->A: Does not affect histone-lysine N-
FT methyltransferase activity. Does not affect protein-lysine
FT N-methyltransferas activity."
FT /evidence="ECO:0000269|PubMed:28126738"
FT MUTAGEN 341
FT /note="Y->F: Abolishes histone-lysine N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:24095733"
FT MUTAGEN 357
FT /note="Y->F: Abolishes histone-lysine N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:24095733"
FT MUTAGEN 368
FT /note="K->A: Does not affect histone-lysine N-
FT methyltransferase activity. Does not affect protein-lysine
FT N-methyltransferas activity."
FT /evidence="ECO:0000269|PubMed:28126738"
FT MUTAGEN 372
FT /note="K->A: Does not affect histone-lysine N-
FT methyltransferase activity. Does not affect protein-lysine
FT N-methyltransferas activity."
FT /evidence="ECO:0000269|PubMed:28126738"
FT MUTAGEN 374
FT /note="K->A: Does not affect histone-lysine N-
FT methyltransferase activity. Does not affect protein-lysine
FT N-methyltransferas activity."
FT /evidence="ECO:0000269|PubMed:28126738"
FT MUTAGEN 375
FT /note="K->A: Does not affect histone-lysine N-
FT methyltransferase activity. Does not affect protein-lysine
FT N-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28126738"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4C1Q"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:4C1Q"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4C1Q"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:4C1Q"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:4C1Q"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:4C1Q"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:4C1Q"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:4C1Q"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:4C1Q"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:4C1Q"
SQ SEQUENCE 843 AA; 97365 MW; 323DD4F00447D598 CRC64;
MNTNKLEENS PEEDTGKFEW KPKVKDEFKD ISIYFSKEEW AEMGEWEKIR YRNVKRNYKM
LISIGLRAPR PAFMCYQRQA MKPQINDSED SDEEWTPKQQ VSPPWVPFRV KHSKQQKESS
RMPFSGESNV KEGSGIENLL NTSGSEHVQK PVSSLEEGNT SGQHSGKKLK LRKKNVEVKM
YRLRERKGLA YEEVSEPQDD DYLYCEKCQN FFIDSCPNHG PPLFVKDSMV DRGHPNHSVL
SLPPGLRISP SGIPEAGLGV WNEASDLPVG LHFGPYEGQI TEDEEAANSG YSWLITKGRN
CYEYVDGQDE SQANWMRYVN CARDDEEQNL VAFQYHRKIF YRTCRVIRPG CELLVWYGDE
YGQELGIKWG SKMKKGFTAG RELRTEIHPC LLCSLAFSSQ KFLTQHMEWN HRTEIFPGTS
ARINPKPGDP CSDQLQEQHV DSQNKNDKAS NEVKRKSKPR QRISTTFPST LKEQMRSEES
KRTVEELRTG QTTNTEDTVK SFIASEISSI ERQCGQYFSD KSNVNEHQKT HTGEKPYVCR
ECGRGFTQNS HLIQHQRTHT GEKPYVCREC GRGFTQKSDL IKHQRTHTGE KPYVCRECGR
GFTQKSDLIK HQRTHTGEKP YVCRECGRGF TQKSVLIKHQ RTHTGEKPYV CRECGRGFTQ
KSVLIKHQRT HTGEKPYVCR ECGRGFTAKS VLIQHQRTHT GEKPYVCREC GRGFTAKSNL
IQHQRTHTGE KPYVCRECGR GFTAKSVLIQ HQRTHTGEKP YVCRECGRGF TAKSVLIQHQ
RTHTGEKPYV CRECGRGFTQ KSNLIKHQRT HTGEKPYVCR ECGWGFTQKS DLIQHQRTHT
REK
