PRDM9
entrez
56979
canonical
uniprot
Q9NQV7
canonical
ensembl
ENSG00000164256
resolver
ensembl
ENSG00000292167
resolver
ensp
ENSP00000296682
resolver
ensp
ENSP00000425471
resolver
ensp
ENSP00000517945
resolver
ensp
ENSP00000517946
resolver
enst
ENST00000296682
resolver
enst
ENST00000502755
resolver
enst
ENST00000709930
resolver
enst
ENST00000709931
resolver
genesymbol
PRDM9
resolver
genesymbol_syn
PFM6
resolver
hgnc
HGNC:13994
resolver
uniprot
A0AAG2UW24
resolver
uniprot
B4DX22
resolver
uniprot
Q27Q50
resolver
uniprot_entry
A0AAG2UW24_HUMAN
resolver
uniprot_entry
PRDM9_HUMAN
resolver
uniprot_sec
B4DX22
resolver
uniprot_sec
Q27Q50
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by suramin with an IC(50) of 4.1 uM. {ECO:0000269|PubMed:24634223}.
uniprot
proteins
amino_acid_sequence
MSPEKSQEESPEEDTERTERKPMVKDAFKDISIYFTKEEWAEMGDWEKTRYRNVKRNYNALITIGLRATRPAFMCHRRQAIKLQVDDTEDSDEEWTPRQQVKPPWMALRVEQRKHQKGMPKASFSNESSLKELSRTANLLNASGSEQAQKPVSPSGEASTSGQHSRLKLELRKKETERKMYSLRERKGHAYKEVSEPQDDDYLYCEMCQNFFIDSCAAHGPPTFVKDSAVDKGHPNRSALSLPPGLRIGPSGIPQAGLGVWNEASDLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYEYVDGKDKSWANWMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELGIKWGSKWKKELMAGREPKPEIHPCPSCCLAFSSQKFLSQHVERNHSSQNFPGPSARKLLQPENPCPGDQNQEQQYPDPHSRNDKTKGQEIKERSKLLNKRTWQREISRAFSSPPKGQMGSCRVGKRIMEEESRTGQKVNPGNTGKLFVGVGISRIAKVKYGECGQGFSVKSDVITHQRTHTGEKLYVCRECGRGFSWKSHLLIHQRIHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEKPYVCRECGRGFSRQSVLLTHQRRHTGEKPYVCRECGRGFSRQSVLLTHQRRHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEKPYVCRECGRGFSWQSVLLTHQRTHTGEKPYVCRECGRGFSNKSHLLRHQRTHTGEKPYVCRECGRGFRDKSHLLRHQRTHTGEKPYVCRECGRGFRDKSNLLSHQRTHTGEKPYVCRECGRGFSNKSHLLRHQRTHTGEKPYVCRECGRGFRNKSHLLRHQRTHTGEKPYVCRECGRGFSDRSSLCYHQRTHTGEKPYVCREDE
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:18941885, PubMed:24095733, PubMed:24634223, PubMed:26833727, PubMed:27129774). Can also methylate all four core histones with H3 being the best substrate and the most highly modified (PubMed:24095733, PubMed:24634223, PubMed:26833727). 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 (By similarity). 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:26833727). Thereby promotes double-stranded breaks (DSB) formation, at this subset of PRDM9-binding sites, that initiates meiotic recombination for the proper meiotic progression (By similarity). 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. EWSR1 joins PRDM9 with the chromosomal axis through REC8 (By similarity). In this way, controls the DSB repair pathway, pairing of homologous chromosomes and sex body formation (By similarity). 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 (By similarity). In addition performs automethylation (By similarity). Acetylation and phosphorylation of histone H3 attenuate or prevent histone H3 methylation (By similarity). {ECO:0000250|UniProtKB:Q96EQ9, ECO:0000269|PubMed:18941885, ECO:0000269|PubMed:24095733, ECO:0000269|PubMed:24634223, ECO:0000269|PubMed:26833727}.
uniprot
proteins
mass_dalton
103376
uniprot
proteins
mutagenesis
MUTAGEN 199; /note="D->Y: Increases histone-lysine N-methyltransferase activity; when associated with D-374."; /evidence="ECO:0000269|PubMed:24095733"; MUTAGEN 357; /note="Y->S: Loss of histone-lysine N-methyltransferase activity."; /evidence="ECO:0000269|PubMed:27129774"; MUTAGEN 374; /note="K->D: Increases histone-lysine N-methyltransferase activity; when associated with Y-199."; /evidence="ECO:0000269|PubMed:24095733
uniprot
proteins
post_translational_modification
PTM: Mono-methylated; automethylated. Tri-methylated; automethylated. Mono-methylation is predominant; automethylation is lower and slower than H3 peptide methylation and is in a highest S-adenosyl-L-methionine concentration-dependent. There are two major sites for automethylation at Lys-368 and Lys-374. 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). Automethylation is an intramolecular (cis) process. {ECO:0000250|UniProtKB:Q96EQ9}.
uniprot
proteins
protein_family
Class V-like SAM-binding methyltransferase superfamily
uniprot
proteins
pubmed
10668202
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
18941885
uniprot
proteins
pubmed
24095733
uniprot
proteins
pubmed
24634223
uniprot
proteins
pubmed
26833727
uniprot
proteins
pubmed
27129774
uniprot
proteins
pubmed
32001511
uniprot
proteins
sequence_length
894
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96EQ9}. Chromosome {ECO:0000250|UniProtKB:Q96EQ9}. Note=Localizes in nuclei of pre-leptotene, leptotene, and early to mid-zygotene spermatocytes. {ECO:0000250|UniProtKB:Q96EQ9}.
uniprot
proteins