UniProtKB - Q96EQ9 (PRDM9_MOUSE)
Histone-lysine N-methyltransferase PRDM9
Prdm9
Functioni
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:27362481, PubMed:24785241, PubMed:29478809).
Also can 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:25894966, PubMed:16292313).
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).
10 PublicationsMiscellaneous
Caution
Catalytic activityi
- L-lysyl-[protein] + S-adenosyl-L-methionine = H+ + N6-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- N6,N6-dimethyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H+ + N6,N6,N6-trimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- L-lysyl4-[histone H3] + 3 S-adenosyl-L-methionine = 3 H+ + N6,N6,N6-trimethyl-L-lysyl4-[histone H3] + 3 S-adenosyl-L-homocysteine4 PublicationsEC:2.1.1.3544 PublicationsThis reaction proceeds in the forward4 Publications direction.
- L-lysyl36-[histone H3] + 3 S-adenosyl-L-methionine = 3 H+ + N6,N6,N6-trimethyl-L-lysyl36-[histone H3] + 3 S-adenosyl-L-homocysteine2 PublicationsEC:2.1.1.3592 PublicationsThis reaction proceeds in the forward2 Publications direction.
- L-lysyl9-[histone H3] + 3 S-adenosyl-L-methionine = 3 H+ + N6,N6,N6-trimethyl-L-lysyl9-[histone H3] + 3 S-adenosyl-L-homocysteine1 PublicationEC:2.1.1.3551 PublicationThis reaction proceeds in the forward1 Publication direction.
- L-lysyl20-[histone H4] + S-adenosyl-L-methionine = H+ + N6-methyl-L-lysyl20-[histone H4] + S-adenosyl-L-homocysteine1 PublicationEC:2.1.1.3611 PublicationThis reaction proceeds in the forward1 Publication direction.
- N6-methyl-L-lysyl20-[histone H4] + S-adenosyl-L-methionine = H+ + N6,N6-dimethyl-L-lysyl20-[histone H4] + S-adenosyl-L-homocysteine1 PublicationEC:2.1.1.3621 PublicationThis reaction proceeds in the forward1 Publication direction.
Kineticsi
- KM=0.17 µM for histone octamer1 Publication
- KM=0.19 µM for H3 protein1 Publication
- KM=3.21 µM for H3 peptide 1-211 Publication
- KM=5.47 µM for H4 peptide 1-361 Publication
- KM=22.29 µM for S-adenosyl-L-methionine (with histone octamer as substrate)1 Publication
- KM=19.01 µM for S-adenosyl-L-methionine (with H3 protein as substrate)1 Publication
- KM=8.23 µM for S-adenosyl-L-methionine (with H3 peptide 1-21 as substrate)1 Publication
- KM=81.66 µM for S-adenosyl-L-methionine (with H4 peptide 1-36 as substrate)1 Publication
- KM=34.7 µM for automethylation1 Publication
- KM=8.23 µM for H3 peptide1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 205 | Zinc 1Combined sources1 Publication | 1 | |
Metal bindingi | 208 | Zinc 1Combined sources1 Publication | 1 | |
Metal bindingi | 216 | Zinc 1Combined sources1 Publication | 1 | |
Metal bindingi | 219 | Zinc 1; via pros nitrogenCombined sources1 Publication | 1 | |
Binding sitei | 291 | S-adenosyl-L-methionineCombined sources1 Publication | 1 | |
Binding sitei | 357 | SubstrateCombined sources1 Publication | 1 | |
Metal bindingi | 390 | Zinc 2By similarity | 1 | |
Metal bindingi | 393 | Zinc 2By similarity | 1 | |
Metal bindingi | 406 | Zinc 2; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 411 | Zinc 2; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 707 | Zinc 3By similarity | 1 | |
Metal bindingi | 710 | Zinc 3By similarity | 1 | |
Metal bindingi | 723 | Zinc 3; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 727 | Zinc 3; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 735 | Zinc 4By similarity | 1 | |
Metal bindingi | 738 | Zinc 4By similarity | 1 | |
Metal bindingi | 751 | Zinc 4; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 755 | Zinc 4; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 763 | Zinc 5By similarity | 1 | |
Metal bindingi | 766 | Zinc 5By similarity | 1 | |
Metal bindingi | 779 | Zinc 5; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 783 | Zinc 5; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 791 | Zinc 6By similarity | 1 | |
Metal bindingi | 794 | Zinc 6By similarity | 1 | |
Metal bindingi | 807 | Zinc 6; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 811 | Zinc 6; via tele nitrogenBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 388 – 411 | C2H2-type 1PROSITE-ProRule annotationAdd BLAST | 24 | |
Zinc fingeri | 513 – 531 | C2H2-type 2; degeneratePROSITE-ProRule annotationAdd BLAST | 19 | |
Zinc fingeri | 537 – 559 | C2H2-type 3PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 565 – 587 | C2H2-type 4PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 593 – 615 | C2H2-type 5PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 621 – 643 | C2H2-type 6PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 649 – 671 | C2H2-type 7PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 677 – 699 | C2H2-type 8PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 705 – 727 | C2H2-type 9PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 733 – 755 | C2H2-type 10PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 761 – 783 | C2H2-type 11PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 789 – 811 | C2H2-type 12PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 817 – 839 | C2H2-type 13PROSITE-ProRule annotationAdd BLAST | 23 |
GO - Molecular functioni
- histone-lysine N-methyltransferase activity Source: MGI
- histone methyltransferase activity (H3-K36 specific) Source: UniProtKB
- histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- protein homodimerization activity Source: UniProtKB
- recombination hotspot binding Source: MGI
- sequence-specific DNA binding Source: MGI
- transcription cis-regulatory region binding Source: UniProtKB
GO - Biological processi
- double-strand break repair involved in meiotic recombination Source: UniProtKB
- female gamete generation Source: UniProtKB
- histone H3-K36 dimethylation Source: UniProtKB
- histone H3-K36 trimethylation Source: UniProtKB
- histone H3-K4 dimethylation Source: UniProtKB
- histone H3-K4 methylation Source: MGI
- histone H3-K4 monomethylation Source: UniProtKB
- histone H3-K4 trimethylation Source: UniProtKB
- histone H3-K9 methylation Source: UniProtKB
- histone lysine methylation Source: UniProtKB
- histone methylation Source: MGI
- homologous chromosome pairing at meiosis Source: UniProtKB
- male gamete generation Source: UniProtKB
- meiotic gene conversion Source: MGI
- negative regulation of apoptotic process Source: UniProtKB
- nucleosome positioning Source: UniProtKB
- positive regulation of fertilization Source: UniProtKB
- positive regulation of histone H3-K36 trimethylation Source: UniProtKB
- positive regulation of histone H3-K4 trimethylation Source: UniProtKB
- positive regulation of meiosis I Source: MGI
- positive regulation of reciprocal meiotic recombination Source: MGI
- positive regulation of transcription by RNA polymerase II Source: MGI
- regulation of gene expression Source: GO_Central
- spermatogenesis Source: MGI
Keywordsi
Molecular function | Activator, Chromatin regulator, DNA-binding, Methyltransferase, Transferase |
Biological process | Meiosis, Transcription, Transcription regulation |
Ligand | Metal-binding, S-adenosyl-L-methionine, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-3214841, PKMTs methylate histone lysines |
Names & Taxonomyi
Protein namesi | Recommended name: Histone-lysine N-methyltransferase PRDM9CuratedAlternative name(s): Hybrid sterility protein 1 Meiosis-induced factor containing a PR/SET domain and zinc-finger motif PR domain zinc finger protein 9 PR domain-containing protein 9 Protein-lysine N-methyltransferase PRDM9Curated (EC:2.1.1.-1 Publication) [histone H3]-lysine36 N-trimethyltransferase PRDM9Curated (EC:2.1.1.3592 Publications) [histone H3]-lysine4 N-trimethyltransferase PRDM9Curated (EC:2.1.1.3544 Publications) [histone H3]-lysine9 N-trimethyltransferase PRDM9Curated (EC:2.1.1.3551 Publication) [histone H4]-N-methyl-L-lysine20 N-methyltransferase PRDM9Curated (EC:2.1.1.3621 Publication) [histone H4]-lysine20 N-methyltransferase PRDM9Curated (EC:2.1.1.3611 Publication) |
Gene namesi | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:2384854, Prdm9 |
VEuPathDBi | HostDB:ENSMUSG00000051977 |
Subcellular locationi
Nucleus
- Nucleus 3 Publications
Other locations
- Chromosome 1 Publication
Note: Localizes in nuclei of pre-leptotene, leptotene, and early to mid-zygotene spermatocytes.1 Publication
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
Other locations
- chromatin Source: UniProtKB
Keywords - Cellular componenti
Chromosome, NucleusPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 207 | K → A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity. 1 Publication | 1 | |
Mutagenesisi | 226 | K → A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity. 1 Publication | 1 | |
Mutagenesisi | 276 | Y → F: Abolishes histone-lysine N-methyltransferase activity. 2 Publications | 1 | |
Mutagenesisi | 278 | G → A: Abolishes histone-lysine N-methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 297 | K → A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity. 1 Publication | 1 | |
Mutagenesisi | 321 | 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. 2 Publications | 1 | |
Mutagenesisi | 338 | K → A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity. 1 Publication | 1 | |
Mutagenesisi | 341 | Y → F: Abolishes histone-lysine N-methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 357 | Y → F: Abolishes histone-lysine N-methyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 368 | K → A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity. 1 Publication | 1 | |
Mutagenesisi | 372 | K → A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity. 1 Publication | 1 | |
Mutagenesisi | 374 | K → A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferas activity. 1 Publication | 1 | |
Mutagenesisi | 375 | K → A: Does not affect histone-lysine N-methyltransferase activity. Does not affect protein-lysine N-methyltransferase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000363960 | 1 – 843 | Histone-lysine N-methyltransferase PRDM9Add BLAST | 843 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 368 | N6,N6,N6-trimethyllysine; alternate1 Publication | 1 | |
Modified residuei | 368 | N6-methyllysine; alternate1 Publication | 1 | |
Modified residuei | 372 | N6-methyllysine1 Publication | 1 | |
Modified residuei | 374 | N6-methyllysine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
MethylationProteomic databases
PaxDbi | Q96EQ9 |
PRIDEi | Q96EQ9 |
ProteomicsDBi | 289889 [Q96EQ9-1] 289890 [Q96EQ9-2] 289891 [Q96EQ9-3] 289892 [Q96EQ9-4] |
PTM databases
iPTMneti | Q96EQ9 |
PhosphoSitePlusi | Q96EQ9 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSMUSG00000051977, Expressed in retinal neural layer and 98 other tissues |
ExpressionAtlasi | Q96EQ9, baseline and differential |
Genevisiblei | Q96EQ9, MM |
Interactioni
Subunit structurei
Homodimer (PubMed:24095733).
Interacts with EHMT2 and CDYL; interaction only takes place when PRDM9 is bound to hotspot DNA (PubMed:27932493).
Interacts with CXXC1; this interaction does not link PRDM9-activated recombination hotspot sites with DSB machinery and is not required for the hotspot recognition pathway (PubMed:27932493, PubMed:30365547).
Forms a complex with EWSR1, REC8, SYCP3 and SYCP1; complex formation is dependent of phosphorylated form of REC8 and requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the chromosomal axis through REC8 (PubMed:27932493).
3 PublicationsGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000131871 |
Miscellaneous databases
RNActi | Q96EQ9, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q96EQ9 |
SMRi | Q96EQ9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 23 – 86 | KRAB-relatedPROSITE-ProRule annotationAdd BLAST | 64 | |
Domaini | 244 – 358 | SETPROSITE-ProRule annotationAdd BLAST | 115 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 85 – 104 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 110 – 170 | DisorderedSequence analysisAdd BLAST | 61 | |
Regioni | 256 – 258 | S-adenosyl-L-methionine bindingCombined sources1 Publication | 3 | |
Regioni | 288 – 294 | Substrate bindingCombined sources1 Publication | 7 | |
Regioni | 320 – 321 | S-adenosyl-L-methionine bindingCombined sources1 Publication | 2 | |
Regioni | 418 – 493 | DisorderedSequence analysisAdd BLAST | 76 | |
Regioni | 715 – 805 | DNA-bindingBy similarityAdd BLAST | 91 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 119 – 165 | Polar residuesSequence analysisAdd BLAST | 47 | |
Compositional biasi | 440 – 459 | Basic and acidic residuesSequence analysisAdd BLAST | 20 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 388 – 411 | C2H2-type 1PROSITE-ProRule annotationAdd BLAST | 24 | |
Zinc fingeri | 513 – 531 | C2H2-type 2; degeneratePROSITE-ProRule annotationAdd BLAST | 19 | |
Zinc fingeri | 537 – 559 | C2H2-type 3PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 565 – 587 | C2H2-type 4PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 593 – 615 | C2H2-type 5PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 621 – 643 | C2H2-type 6PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 649 – 671 | C2H2-type 7PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 677 – 699 | C2H2-type 8PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 705 – 727 | C2H2-type 9PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 733 – 755 | C2H2-type 10PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 761 – 783 | C2H2-type 11PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 789 – 811 | C2H2-type 12PROSITE-ProRule annotationAdd BLAST | 23 | |
Zinc fingeri | 817 – 839 | C2H2-type 13PROSITE-ProRule annotationAdd BLAST | 23 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG1721, Eukaryota KOG2461, Eukaryota |
GeneTreei | ENSGT00940000158211 |
HOGENOMi | CLU_983403_0_0_1 |
InParanoidi | Q96EQ9 |
PhylomeDBi | Q96EQ9 |
Family and domain databases
CDDi | cd07765, KRAB_A-box, 1 hit cd19193, PR-SET_PRDM7_9, 1 hit |
Gene3Di | 2.170.270.10, 1 hit |
InterProi | View protein in InterPro IPR001909, KRAB IPR036051, KRAB_dom_sf IPR003655, Krueppel-associated_box-rel IPR044417, PRDM7_9_PR-SET IPR001214, SET_dom IPR046341, SET_dom_sf IPR019041, SSXRD_motif IPR036236, Znf_C2H2_sf IPR013087, Znf_C2H2_type |
Pfami | View protein in Pfam PF01352, KRAB, 1 hit PF00856, SET, 1 hit PF09514, SSXRD, 1 hit PF00096, zf-C2H2, 11 hits |
SMARTi | View protein in SMART SM00349, KRAB, 1 hit SM00355, ZnF_C2H2, 13 hits |
SUPFAMi | SSF109640, SSF109640, 1 hit SSF57667, SSF57667, 6 hits SSF82199, SSF82199, 1 hit |
PROSITEi | View protein in PROSITE PS50806, KRAB_RELATED, 1 hit PS50280, SET, 1 hit PS00028, ZINC_FINGER_C2H2_1, 12 hits PS50157, ZINC_FINGER_C2H2_2, 12 hits |
s (4+)i Sequence
Sequence statusi: Complete.
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MNTNKLEENS PEEDTGKFEW KPKVKDEFKD ISIYFSKEEW AEMGEWEKIR
60 70 80 90 100
YRNVKRNYKM LISIGLRAPR PAFMCYQRQA MKPQINDSED SDEEWTPKQQ
110 120 130 140 150
VSPPWVPFRV KHSKQQKESS RMPFSGESNV KEGSGIENLL NTSGSEHVQK
160 170 180 190 200
PVSSLEEGNT SGQHSGKKLK LRKKNVEVKM YRLRERKGLA YEEVSEPQDD
210 220 230 240 250
DYLYCEKCQN FFIDSCPNHG PPLFVKDSMV DRGHPNHSVL SLPPGLRISP
260 270 280 290 300
SGIPEAGLGV WNEASDLPVG LHFGPYEGQI TEDEEAANSG YSWLITKGRN
310 320 330 340 350
CYEYVDGQDE SQANWMRYVN CARDDEEQNL VAFQYHRKIF YRTCRVIRPG
360 370 380 390 400
CELLVWYGDE YGQELGIKWG SKMKKGFTAG RELRTEIHPC LLCSLAFSSQ
410 420 430 440 450
KFLTQHMEWN HRTEIFPGTS ARINPKPGDP CSDQLQEQHV DSQNKNDKAS
460 470 480 490 500
NEVKRKSKPR QRISTTFPST LKEQMRSEES KRTVEELRTG QTTNTEDTVK
510 520 530 540 550
SFIASEISSI ERQCGQYFSD KSNVNEHQKT HTGEKPYVCR ECGRGFTQNS
560 570 580 590 600
HLIQHQRTHT GEKPYVCREC GRGFTQKSDL IKHQRTHTGE KPYVCRECGR
610 620 630 640 650
GFTQKSDLIK HQRTHTGEKP YVCRECGRGF TQKSVLIKHQ RTHTGEKPYV
660 670 680 690 700
CRECGRGFTQ KSVLIKHQRT HTGEKPYVCR ECGRGFTAKS VLIQHQRTHT
710 720 730 740 750
GEKPYVCREC GRGFTAKSNL IQHQRTHTGE KPYVCRECGR GFTAKSVLIQ
760 770 780 790 800
HQRTHTGEKP YVCRECGRGF TAKSVLIQHQ RTHTGEKPYV CRECGRGFTQ
810 820 830 840
KSNLIKHQRT HTGEKPYVCR ECGWGFTQKS DLIQHQRTHT REK
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketE9Q4V2 | E9Q4V2_MOUSE | Histone-lysine N-methyltransferase | Prdm9 | 847 | Annotation score: |
Sequence cautioni
Polymorphismi
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_036374 | 1 – 121 | Missing in isoform 4. 1 PublicationAdd BLAST | 121 | |
Alternative sequenceiVSP_036375 | 382 – 418 | ELRTE…EIFPG → DLFIIICKYTVAVFRHTRRG SQILLRMVVSHHVVAGI in isoform 3. CuratedAdd BLAST | 37 | |
Alternative sequenceiVSP_036376 | 382 – 404 | ELRTE…QKFLT → GGHYYDSLKKKEKREFSLRI FIF in isoform 2 and isoform 4. 1 PublicationAdd BLAST | 23 | |
Alternative sequenceiVSP_036377 | 405 – 843 | Missing in isoform 2 and isoform 4. 1 PublicationAdd BLAST | 439 | |
Alternative sequenceiVSP_036378 | 419 – 843 | Missing in isoform 3. CuratedAdd BLAST | 425 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY294423 Genomic DNA Translation: AAQ01511.1 AC154378 Genomic DNA No translation available. CT033750 Genomic DNA No translation available. BC012016 mRNA Translation: AAH12016.1 BC049903 mRNA Translation: AAH49903.1 Different initiation. |
CCDSi | CCDS49963.2 [Q96EQ9-1] CCDS88997.1 [Q96EQ9-4] |
Genome annotation databases
Ensembli | ENSMUST00000147532; ENSMUSP00000118454; ENSMUSG00000051977 [Q96EQ9-4] ENSMUST00000167994; ENSMUSP00000131871; ENSMUSG00000051977 [Q96EQ9-1] |
UCSCi | uc008aos.1, mouse [Q96EQ9-4] uc029tan.1, mouse [Q96EQ9-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY294423 Genomic DNA Translation: AAQ01511.1 AC154378 Genomic DNA No translation available. CT033750 Genomic DNA No translation available. BC012016 mRNA Translation: AAH12016.1 BC049903 mRNA Translation: AAH49903.1 Different initiation. |
CCDSi | CCDS49963.2 [Q96EQ9-1] CCDS88997.1 [Q96EQ9-4] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4C1Q | X-ray | 2.30 | A/B | 198-368 | [»] | |
AlphaFoldDBi | Q96EQ9 | |||||
SMRi | Q96EQ9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000131871 |
PTM databases
iPTMneti | Q96EQ9 |
PhosphoSitePlusi | Q96EQ9 |
Proteomic databases
PaxDbi | Q96EQ9 |
PRIDEi | Q96EQ9 |
ProteomicsDBi | 289889 [Q96EQ9-1] 289890 [Q96EQ9-2] 289891 [Q96EQ9-3] 289892 [Q96EQ9-4] |
Protocols and materials databases
Antibodypediai | 67566, 64 antibodies from 16 providers |
Genome annotation databases
Ensembli | ENSMUST00000147532; ENSMUSP00000118454; ENSMUSG00000051977 [Q96EQ9-4] ENSMUST00000167994; ENSMUSP00000131871; ENSMUSG00000051977 [Q96EQ9-1] |
UCSCi | uc008aos.1, mouse [Q96EQ9-4] uc029tan.1, mouse [Q96EQ9-1] |
Organism-specific databases
MGIi | MGI:2384854, Prdm9 |
VEuPathDBi | HostDB:ENSMUSG00000051977 |
Phylogenomic databases
eggNOGi | KOG1721, Eukaryota KOG2461, Eukaryota |
GeneTreei | ENSGT00940000158211 |
HOGENOMi | CLU_983403_0_0_1 |
InParanoidi | Q96EQ9 |
PhylomeDBi | Q96EQ9 |
Enzyme and pathway databases
Reactomei | R-MMU-3214841, PKMTs methylate histone lysines |
Miscellaneous databases
ChiTaRSi | Prdm9, mouse |
PROi | PR:Q96EQ9 |
RNActi | Q96EQ9, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000051977, Expressed in retinal neural layer and 98 other tissues |
ExpressionAtlasi | Q96EQ9, baseline and differential |
Genevisiblei | Q96EQ9, MM |
Family and domain databases
CDDi | cd07765, KRAB_A-box, 1 hit cd19193, PR-SET_PRDM7_9, 1 hit |
Gene3Di | 2.170.270.10, 1 hit |
InterProi | View protein in InterPro IPR001909, KRAB IPR036051, KRAB_dom_sf IPR003655, Krueppel-associated_box-rel IPR044417, PRDM7_9_PR-SET IPR001214, SET_dom IPR046341, SET_dom_sf IPR019041, SSXRD_motif IPR036236, Znf_C2H2_sf IPR013087, Znf_C2H2_type |
Pfami | View protein in Pfam PF01352, KRAB, 1 hit PF00856, SET, 1 hit PF09514, SSXRD, 1 hit PF00096, zf-C2H2, 11 hits |
SMARTi | View protein in SMART SM00349, KRAB, 1 hit SM00355, ZnF_C2H2, 13 hits |
SUPFAMi | SSF109640, SSF109640, 1 hit SSF57667, SSF57667, 6 hits SSF82199, SSF82199, 1 hit |
PROSITEi | View protein in PROSITE PS50806, KRAB_RELATED, 1 hit PS50280, SET, 1 hit PS00028, ZINC_FINGER_C2H2_1, 12 hits PS50157, ZINC_FINGER_C2H2_2, 12 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | PRDM9_MOUSE | |
Accessioni | Q96EQ9Primary (citable) accession number: Q96EQ9 Secondary accession number(s): B8JJZ8, Q0D2N4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 10, 2009 |
Last sequence update: | February 10, 2009 | |
Last modified: | May 25, 2022 | |
This is version 156 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families