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Entry version 134 (07 Apr 2021)
Sequence version 1 (05 Jul 2004)
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Protein

Histone-lysine N-methyltransferase PRDM9

Gene

prdm9

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Also can methylate all four core histones with H3 being the best substrate and the most highly modified. 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. 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. Thereby promotes double-stranded breaks (DSB) formation, at this subset of PRDM9-binding sites, that initiates meiotic recombination for the proper meiotic progression. 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. In this way, controls the DSB repair pathway, pairing of homologous chromosomes and sex body formation. 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. In addition performs automethylation. Acetylation and phosphorylation of histone H3 attenuate or prevent histone H3 methylation.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei196SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi235Zinc 1By similarity1
Metal bindingi407Zinc 2By similarity1
Metal bindingi410Zinc 2By similarity1
Metal bindingi423Zinc 2; via tele nitrogenBy similarity1
Metal bindingi428Zinc 2; via tele nitrogenBy similarity1
Metal bindingi747Zinc 3By similarity1
Metal bindingi750Zinc 3By similarity1
Metal bindingi763Zinc 3; via tele nitrogenBy similarity1
Metal bindingi767Zinc 3; via tele nitrogenBy similarity1
Metal bindingi775Zinc 4By similarity1
Metal bindingi778Zinc 4By similarity1
Metal bindingi791Zinc 4; via tele nitrogenBy similarity1
Metal bindingi795Zinc 4; via tele nitrogenBy similarity1
Metal bindingi803Zinc 5By similarity1
Metal bindingi806Zinc 5By similarity1
Metal bindingi819Zinc 5; via tele nitrogenBy similarity1
Metal bindingi823Zinc 5; via tele nitrogenBy similarity1
Metal bindingi831Zinc 6By similarity1
Metal bindingi834Zinc 6By similarity1
Metal bindingi847Zinc 6; via tele nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri230 – 253C2H2-type 1PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri337 – 360C2H2-type 2PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri366 – 388C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri405 – 428C2H2-type 4PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri508 – 528C2H2-type 5; degeneratePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri547 – 569C2H2-type 6; degeneratePROSITE-ProRule annotationAdd BLAST23
Zinc fingeri575 – 598C2H2-type 7PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri604 – 626C2H2-type 8PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri644 – 666C2H2-type 9PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri689 – 711C2H2-type 10; degeneratePROSITE-ProRule annotationAdd BLAST23
Zinc fingeri717 – 739C2H2-type 11PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri745 – 767C2H2-type 12PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri773 – 795C2H2-type 13PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri801 – 823C2H2-type 14PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri829 – 852C2H2-type 15PROSITE-ProRule annotationAdd BLAST24

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Chromatin regulator, DNA-binding, Methyltransferase, Transferase
Biological processMeiosis, Transcription, Transcription regulation
LigandMetal-binding, S-adenosyl-L-methionine, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone-lysine N-methyltransferase PRDM9By similarity
Alternative name(s):
PR domain zinc finger protein 9
PR domain-containing protein 9
Protein-lysine N-methyltransferase PRDM9By similarity (EC:2.1.1.-By similarity)
[histone H3]-lysine36 N-trimethyltransferase PRDM9By similarity (EC:2.1.1.359By similarity)
[histone H3]-lysine4 N-trimethyltransferase PRDM9By similarity (EC:2.1.1.354By similarity)
[histone H3]-lysine9 N-trimethyltransferase PRDM9By similarity (EC:2.1.1.355By similarity)
[histone H4]-N-methyl-L-lysine20 N-methyltransferase PRDM9By similarity (EC:2.1.1.362By similarity)
[histone H4]-lysine20 N-methyltransferase PRDM9By similarity (EC:2.1.1.361By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:prdm9
ORF Names:zgc:63970
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7955 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesDanionidaeDanioninaeDanio
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000437 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Zebrafish Information Network genome database

More...
ZFINi
ZDB-GENE-040426-1319, prdm9

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chromosome, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003639621 – 853Histone-lysine N-methyltransferase PRDM9Add BLAST853

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Mono-methylated; automethylated. Tri-methylated; automethylated.By similarity

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q6P2A1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSDARG00000005382, Expressed in blastula and 33 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q6P2A1, baseline

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
7955.ENSDARP00000026323

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q6P2A1

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini83 – 197SETPROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni127 – 133Substrate bindingBy similarity7
Regioni275 – 277S-adenosyl-L-methionine bindingBy similarity3
Regioni341 – 342S-adenosyl-L-methionine bindingBy similarity2
Regioni755 – 845DNA-bindingBy similarityAdd BLAST91

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C2H2-type zinc fingers determines the hotspot localization through its binding to specific DNA sequences. Variations in their sequence affects affinity towards DNA-binding motif.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri230 – 253C2H2-type 1PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri337 – 360C2H2-type 2PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri366 – 388C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri405 – 428C2H2-type 4PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri508 – 528C2H2-type 5; degeneratePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri547 – 569C2H2-type 6; degeneratePROSITE-ProRule annotationAdd BLAST23
Zinc fingeri575 – 598C2H2-type 7PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri604 – 626C2H2-type 8PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri644 – 666C2H2-type 9PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri689 – 711C2H2-type 10; degeneratePROSITE-ProRule annotationAdd BLAST23
Zinc fingeri717 – 739C2H2-type 11PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri745 – 767C2H2-type 12PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri773 – 795C2H2-type 13PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri801 – 823C2H2-type 14PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri829 – 852C2H2-type 15PROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1721, Eukaryota
KOG2461, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000167583

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_002678_32_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6P2A1

Identification of Orthologs from Complete Genome Data

More...
OMAi
FYCEECL

Database of Orthologous Groups

More...
OrthoDBi
1318335at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6P2A1

TreeFam database of animal gene trees

More...
TreeFami
TF315885

Family and domain databases

Conserved Domains Database

More...
CDDi
cd19193, PR-SET_PRDM7_9, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR044417, PRDM7_9_PR-SET
IPR001214, SET_dom
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00096, zf-C2H2, 7 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00355, ZnF_C2H2, 13 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57667, SSF57667, 6 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50280, SET, 1 hit
PS00028, ZINC_FINGER_C2H2_1, 12 hits
PS50157, ZINC_FINGER_C2H2_2, 12 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q6P2A1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLSPDLPPS EEQNLEIQGS ATNCYSVVII EEQDDTFNDQ PFYCEMCQQH
60 70 80 90 100
FIDQCETHGP PSFTCDSPAA LGTPQRALLT LPQGLVIGRS SISHAGLGVF
110 120 130 140 150
NQGQTVPLGM HFGPFDGEEI SEEKALDSAN SWVICRGNNQ YSYIDAEKDT
160 170 180 190 200
HSNWMKFVVC SRSETEQNLV AFQQNGRILF RCCRPISPGQ EFRVWYAEEY
210 220 230 240 250
AQGLGAIWDK IWDNKCISQG STEEQATQNC PCPFCHYSFP TLVYLHAHVK
260 270 280 290 300
RTHPNEYAQF TQTHPLESEA HTPITEVEQC LVASDEALST QTQPVTESPQ
310 320 330 340 350
EQISTQNGQP IHQTENSDEP DASDIYTAAG EISDEIHACV DCGRSFLRSC
360 370 380 390 400
HLKRHQRTIH SKEKPYCCSQ CKKCFSQATG LKRHQHTHQE QEKNIESPDR
410 420 430 440 450
PSDIYPCTKC TLSFVAKINL HQHLKRHHHG EYLRLVESGS LTAETEEDHT
460 470 480 490 500
EVCFDKQDPN YEPPSRGRKS TKNSLKGRGC PKKVAVGRPR GRPPKNKNLE
510 520 530 540 550
VEVQKISPIC TNCEQSFSDL ETLKTHQCPR RDDEGDNVEH PQEASQYICG
560 570 580 590 600
ECIRAFSNLD LLKAHECIQQ GEGSYCCPHC DLYFNRMCNL RRHERTIHSK
610 620 630 640 650
EKPYCCTVCL KSFTQSSGLK RHQQSHLRRK SHRQSSALFT AAIFPCAYCP
660 670 680 690 700
FSFTDERYLY KHIRRHHPEM SLKYLSFQEG GVLSVEKPHS CSQCCKSFST
710 720 730 740 750
IKGFKNHSCF KQGEKVYLCP DCGKAFSWFN SLKQHQRIHT GEKPYTCSQC
760 770 780 790 800
GKSFVHSGQL NVHLRTHTGE KPFLCSQCGE SFRQSGDLRR HEQKHSGVRP
810 820 830 840 850
CQCPDCGKSF SRPQSLKAHQ QLHVGTKLFP CTQCGKSFTR RYHLTRHHQK

MHS
Length:853
Mass (Da):97,136
Last modified:July 5, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i44A40327A3F0BAC4
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8W4Z5F8W4Z5_DANRE
Histone-lysine N-methyltransferase ...
prdm9
84Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BC064665 mRNA Translation: AAH64665.1
DQ851831 mRNA Translation: ABI34500.1

NCBI Reference Sequences

More...
RefSeqi
NP_957196.1, NM_200902.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSDART00000027321; ENSDARP00000026323; ENSDARG00000005382
ENSDART00000180739; ENSDARP00000148547; ENSDARG00000110150

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
393876

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dre:393876

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC064665 mRNA Translation: AAH64665.1
DQ851831 mRNA Translation: ABI34500.1
RefSeqiNP_957196.1, NM_200902.1

3D structure databases

SMRiQ6P2A1
ModBaseiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000026323

Proteomic databases

PaxDbiQ6P2A1

Genome annotation databases

EnsembliENSDART00000027321; ENSDARP00000026323; ENSDARG00000005382
ENSDART00000180739; ENSDARP00000148547; ENSDARG00000110150
GeneIDi393876
KEGGidre:393876

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
56979
ZFINiZDB-GENE-040426-1319, prdm9

Phylogenomic databases

eggNOGiKOG1721, Eukaryota
KOG2461, Eukaryota
GeneTreeiENSGT00940000167583
HOGENOMiCLU_002678_32_1_1
InParanoidiQ6P2A1
OMAiFYCEECL
OrthoDBi1318335at2759
PhylomeDBiQ6P2A1
TreeFamiTF315885

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q6P2A1

Gene expression databases

BgeeiENSDARG00000005382, Expressed in blastula and 33 other tissues
ExpressionAtlasiQ6P2A1, baseline

Family and domain databases

CDDicd19193, PR-SET_PRDM7_9, 1 hit
InterProiView protein in InterPro
IPR044417, PRDM7_9_PR-SET
IPR001214, SET_dom
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type
PfamiView protein in Pfam
PF00096, zf-C2H2, 7 hits
SMARTiView protein in SMART
SM00355, ZnF_C2H2, 13 hits
SUPFAMiSSF57667, SSF57667, 6 hits
PROSITEiView protein in PROSITE
PS50280, SET, 1 hit
PS00028, ZINC_FINGER_C2H2_1, 12 hits
PS50157, ZINC_FINGER_C2H2_2, 12 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPRDM9_DANRE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q6P2A1
Secondary accession number(s): A5XCD9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 5, 2004
Last modified: April 7, 2021
This is version 134 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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