Prdm9
entrez
213389
canonical
uniprot
Q96EQ9
canonical
ensembl
ENSMUSG00000051977
resolver
ensp
ENSMUSP00000118454
resolver
ensp
ENSMUSP00000131871
resolver
ensp
ENSMUSP00000156841
resolver
enst
ENSMUST00000233295
resolver
genesymbol
Prdm9
resolver
genesymbol_syn
Hst1
resolver
genesymbol_syn
Meisetz
resolver
uniprot
A0A3B2WD41
resolver
uniprot
B8JJZ8
resolver
uniprot
E9Q4V2
resolver
uniprot
Q0D2N4
resolver
uniprot_entry
A0A3B2WD41_MOUSE
resolver
uniprot_entry
E9Q4V2_MOUSE
resolver
uniprot_entry
PRDM9_MOUSE
resolver
uniprot_sec
B8JJZ8
resolver
uniprot_sec
Q0D2N4
resolver
amino_acid_sequence
MNTNKLEENSPEEDTGKFEWKPKVKDEFKDISIYFSKEEWAEMGEWEKIRYRNVKRNYKMLISIGLRAPRPAFMCYQRQAMKPQINDSEDSDEEWTPKQQVSPPWVPFRVKHSKQQKESSRMPFSGESNVKEGSGIENLLNTSGSEHVQKPVSSLEEGNTSGQHSGKKLKLRKKNVEVKMYRLRERKGLAYEEVSEPQDDDYLYCEKCQNFFIDSCPNHGPPLFVKDSMVDRGHPNHSVLSLPPGLRISPSGIPEAGLGVWNEASDLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYVNCARDDEEQNLVAFQYHRKIFYRTCRVIRPGCELLVWYGDEYGQELGIKWGSKMKKGFTAGRELRTEIHPCLLCSLAFSSQKFLTQHMEWNHRTEIFPGTSARINPKPGDPCSDQLQEQHVDSQNKNDKASNEVKRKSKPRQRISTTFPSTLKEQMRSEESKRTVEELRTGQTTNTEDTVKSFIASEISSIERQCGQYFSDKSNVNEHQKTHTGEKPYVCRECGRGFTQNSHLIQHQRTHTGEKPYVCRECGRGFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKSDLIKHQRTHTGEKPYVCRECGRGFTQKSVLIKHQRTHTGEKPYVCRECGRGFTQKSVLIKHQRTHTGEKPYVCRECGRGFTAKSVLIQHQRTHTGEKPYVCRECGRGFTAKSNLIQHQRTHTGEKPYVCRECGRGFTAKSVLIQHQRTHTGEKPYVCRECGRGFTAKSVLIQHQRTHTGEKPYVCRECGRGFTQKSNLIKHQRTHTGEKPYVCRECGWGFTQKSDLIQHQRTHTREK
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
ec_number
2.1.1.354
uniprot
proteins
ec_number
2.1.1.355
uniprot
proteins
ec_number
2.1.1.359
uniprot
proteins
ec_number
2.1.1.361
uniprot
proteins
ec_number
2.1.1.362
uniprot
proteins
function
FUNCTION: Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localization thereby promoting meiotic recombination (PubMed:16292313, PubMed:24095733, PubMed:24785241, PubMed:27362481, PubMed:29478809, PubMed:32001511). Can also methylate all four core histones with H3 being the best substrate and the most highly modified (PubMed:24785241, PubMed:27362481). Is also able, on one hand, to mono and di-methylate H4K20 and on other hand to trimethylate H3K9 with the di-methylated H3K9 as the best substrate (PubMed:24785241, PubMed:27362481). During meiotic prophase, binds specific DNA sequences through its zinc finger domains thereby determining hotspot localization where it promotes local H3K4me3 and H3K36me3 enrichment on the same nucleosomes through its histone methyltransferase activity (PubMed:22028627, PubMed:27362481, PubMed:29478809). Thereby promotes double-stranded breaks (DSB) formation, at this subset of PRDM9-binding sites, that initiates meiotic recombination for the proper meiotic progression (PubMed:16292313, PubMed:29478809). During meiotic progression hotspot-bound PRDM9 interacts with several complexes; in early leptonema binds CDYL and EHMT2 followed by EWSR1 and CXXC1 by the end of leptonema (PubMed:27932493). EWSR1 joins PRDM9 with the chromosomal axis through REC8 (PubMed:27932493). In this way, controls the DSB repair pathway, pairing of homologous chromosomes and sex body formation (PubMed:16292313, PubMed:25894966). Moreover plays a central role in the transcriptional activation of genes during early meiotic prophase thanks to H3K4me3 and H3K36me3 enrichment that represents a specific tag for epigenetic transcriptional activation (PubMed:16292313). In addition performs automethylation (PubMed:28126738). Acetylation and phosphorylation of histone H3 attenuate or prevent histone H3 methylation (PubMed:27362481). {ECO:0000269|PubMed:16292313, ECO:0000269|PubMed:22028627, ECO:0000269|PubMed:24095733, ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:25894966, ECO:0000269|PubMed:27362481, ECO:0000269|PubMed:27932493, ECO:0000269|PubMed:28126738, ECO:0000269|PubMed:29478809, ECO:0000269|PubMed:32001511, ECO:0000269|PubMed:32374261}.
uniprot
proteins
mass_dalton
97365
uniprot
proteins
mutagenesis
MUTAGEN 207; /note="K->A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity."; /evidence="ECO:0000269|PubMed:28126738"; MUTAGEN 226; /note="K->A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity."; /evidence="ECO:0000269|PubMed:28126738"; MUTAGEN 276; /note="Y->F: Abolishes histone-lysine N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:16292313, ECO:0000269|PubMed:24095733"; MUTAGEN 278; /note="G->A: Abolishes histone-lysine N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:16292313"; MUTAGEN 297; /note="K->A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity."; /evidence="ECO:0000269|PubMed:28126738"; MUTAGEN 321; /note="C->P: Abolishes histone-lysine N-methyltransferase activity over enzyme concentration of 0-80 nM. Weakened histone-lysine N-methyltransferase activity over enzyme concentration > 5 uM. Abolishes binding with S-adenosyl-L-methionine. Abolishes protein-lysine N-methyltransferas."; /evidence="ECO:0000269|PubMed:24785241, ECO:0000269|PubMed:28126738"; MUTAGEN 338; /note="K->A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity."; /evidence="ECO:0000269|PubMed:28126738"; MUTAGEN 341; /note="Y->F: Abolishes histone-lysine N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:24095733"; MUTAGEN 357; /note="Y->F: Abolishes histone-lysine N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:24095733"; MUTAGEN 368; /note="K->A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity."; /evidence="ECO:0000269|PubMed:28126738"; MUTAGEN 372; /note="K->A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity."; /evidence="ECO:0000269|PubMed:28126738"; MUTAGEN 374; /note="K->A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity."; /evidence="ECO:0000269|PubMed:28126738"; MUTAGEN 375; /note="K->A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:28126738
uniprot
proteins
post_translational_modification
PTM: Mono-methylated; automethylated (PubMed:28126738). Tri-methylated; automethylated (PubMed:28126738). Mono-methylation is predominant; automethylation is lower and slower than H3 peptide methylation and is in a highest S-adenosyl-L-methionine concentration-dependent (PubMed:28126738). There are two major sites for automethylation at Lys-368 and Lys-374 (PubMed:28126738). Lysines can be simultaneously methylated, such as Lys-368(me3)/Lys-372(me1), Lys-368(me1)/Lys-374(me1) and Lys-368(me1)/Lys-372(me1)/Lys-374(me1) (PubMed:28126738). Automethylation is an intramolecular (cis) process (PubMed:28126738). {ECO:0000269|PubMed:28126738}.
uniprot
proteins
protein_family
Class V-like SAM-binding methyltransferase superfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16292313
uniprot
proteins
pubmed
19074312
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
22028627
uniprot
proteins
pubmed
24095733
uniprot
proteins
pubmed
24785241
uniprot
proteins
pubmed
25894966
uniprot
proteins
pubmed
27362481
uniprot
proteins
pubmed
27932493
uniprot
proteins
pubmed
28126738
uniprot
proteins
pubmed
29478809
uniprot
proteins
pubmed
30365547
uniprot
proteins
pubmed
32001511
uniprot
proteins
pubmed
32374261
uniprot
proteins
sequence_length
843
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25894966, ECO:0000269|PubMed:27932493, ECO:0000269|PubMed:29478809}. Chromosome {ECO:0000269|PubMed:29478809}. Note=Localizes in nuclei of pre-leptotene, leptotene, and early to mid-zygotene spermatocytes. {ECO:0000269|PubMed:25894966}.
uniprot
proteins