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Entry version 94 (12 Aug 2020)
Sequence version 1 (10 Feb 2009)
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Protein

Histone-lysine N-methyltransferase PRDM9

Gene

Prdm9

Organism
Rattus norvegicus (Rat)
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>
-Protein inferred from homologyi <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 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 bindingi209Zinc 1By similarity1
Metal bindingi212Zinc 1By similarity1
Metal bindingi220Zinc 1By similarity1
Metal bindingi223Zinc 1; via pros nitrogenBy similarity1
<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 sitei295S-adenosyl-L-methionineBy similarity1
Binding sitei361SubstrateBy similarity1
Metal bindingi394Zinc 2By similarity1
Metal bindingi397Zinc 2By similarity1
Metal bindingi410Zinc 2; via tele nitrogenBy similarity1
Metal bindingi415Zinc 2; via tele nitrogenBy similarity1
Metal bindingi716Zinc 3By similarity1
Metal bindingi719Zinc 3By similarity1
Metal bindingi732Zinc 3; via tele nitrogenBy similarity1
Metal bindingi736Zinc 3; via tele nitrogenBy similarity1
Metal bindingi744Zinc 4By similarity1
Metal bindingi747Zinc 4By similarity1
Metal bindingi760Zinc 4; via tele nitrogenBy similarity1
Metal bindingi764Zinc 4; via tele nitrogenBy similarity1
Metal bindingi772Zinc 5By similarity1
Metal bindingi775Zinc 5By similarity1
Metal bindingi788Zinc 5; via tele nitrogenBy similarity1
Metal bindingi792Zinc 5; 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 fingeri392 – 415C2H2-type 1PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri522 – 540C2H2-type 2; degeneratePROSITE-ProRule annotationAdd BLAST19
Zinc fingeri546 – 568C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri574 – 596C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri602 – 624C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri630 – 652C2H2-type 6PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri658 – 680C2H2-type 7PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri686 – 708C2H2-type 8PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri714 – 736C2H2-type 9PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri742 – 764C2H2-type 10PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri770 – 792C2H2-type 11PROSITE-ProRule annotationAdd BLAST23

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-212436, Generic Transcription Pathway
R-RNO-3214841, PKMTs methylate histone lysines

<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 PRDM9Curated
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:Prdm9Imported
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 1
  • UP000234681 Componentsi: Chromosome 1, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...
RGDi
1305247, 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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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_00003639611 – 796Histone-lysine N-methyltransferase PRDM9Add BLAST796

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei372N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei372N6-methyllysine; alternateBy similarity1
Modified residuei376N6-methyllysineBy similarity1
Modified residuei378N6-methyllysineBy similarity1

<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. 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-372 and Lys-378. Lysines can be simultaneously methylated, such as Lys-372(me3)/Lys-376(me1), Lys-372(me1)/Lys-378(me1) and Lys-372(me1)/Lys-376(me1)/Lys-378(me1). Automethylation is an intramolecular (cis) process.By similarity

Keywords - PTMi

Methylation

Proteomic databases

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

More...
PaxDbi
P0C6Y7

PRoteomics IDEntifications database

More...
PRIDEi
P0C6Y7

<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
ENSRNOG00000021493, Expressed in testis and 21 other tissues

<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.

Interacts with EHMT2 and CDYL; interaction only takes place when PRDM9 is bound to hotspot DNA.

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.

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.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000060531

<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
P0C6Y7

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>Domaini27 – 90KRAB-relatedPROSITE-ProRule annotationAdd BLAST64
Domaini248 – 362SETPROSITE-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>Regioni260 – 262S-adenosyl-L-methionine bindingBy similarity3
Regioni292 – 298Substrate bindingBy similarity7
Regioni324 – 325S-adenosyl-L-methionine bindingBy similarity2

<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 determine the hotspot localization through its binding to specific DNA sequences. Variations in their sequence affect 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 fingeri392 – 415C2H2-type 1PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri522 – 540C2H2-type 2; degeneratePROSITE-ProRule annotationAdd BLAST19
Zinc fingeri546 – 568C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri574 – 596C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri602 – 624C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri630 – 652C2H2-type 6PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri658 – 680C2H2-type 7PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri686 – 708C2H2-type 8PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri714 – 736C2H2-type 9PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri742 – 764C2H2-type 10PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri770 – 792C2H2-type 11PROSITE-ProRule annotationAdd BLAST23

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
ENSGT00940000158211

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_002678_32_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0C6Y7

KEGG Orthology (KO)

More...
KOi
K20796

Identification of Orthologs from Complete Genome Data

More...
OMAi
RSCNDKT

Database of Orthologous Groups

More...
OrthoDBi
1318335at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0C6Y7

TreeFam database of animal gene trees

More...
TreeFami
TF338096

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07765, KRAB_A-box, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001909, KRAB
IPR036051, KRAB_dom_sf
IPR003655, Krueppel-associated_box-rel
IPR001214, SET_dom
IPR019041, SSXRD_motif
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01352, KRAB, 1 hit
PF00856, SET, 1 hit
PF09514, SSXRD, 1 hit
PF00096, zf-C2H2, 8 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00349, KRAB, 1 hit
SM00317, SET, 1 hit
SM00355, ZnF_C2H2, 11 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF109640, SSF109640, 1 hit
SSF57667, SSF57667, 5 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50806, KRAB_RELATED, 1 hit
PS50280, SET, 1 hit
PS00028, ZINC_FINGER_C2H2_1, 10 hits
PS50157, ZINC_FINGER_C2H2_2, 10 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>Sequences (2)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 describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P0C6Y7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSRTMNTNKP EENSTEGDAG KLEWKPKVKD EFKDISIYFS KEEWAEMGEW
60 70 80 90 100
EKIRYRNVKR NYKMLISIGL RAPRPAFMCY QRQAIKPQIN DNEDSDEEWT
110 120 130 140 150
PKQQVSSPWV PFRVKHSKQQ KETPRMPLSD KSSVKEVFGI ENLLNTSGSE
160 170 180 190 200
HAQKPVCSPE EGNTSGQHFG KKLKLRRKNV EVNRYRLRER KDLAYEEVSE
210 220 230 240 250
PQDDDYLYCE KCQNFFIDSC PNHGPPVFVK DSVVDRGHPN HSVLSLPPGL
260 270 280 290 300
RIGPSGIPEA GLGVWNEASD LPVGLHFGPY KGQITEDEEA ANSGYSWLIT
310 320 330 340 350
KGRNCYEYVD GQDESQANWM RYVNCARDDE EQNLVAFQYH RKIFYRTCRV
360 370 380 390 400
IRPGRELLVW YGDEYGQELG IKWGSKMKKG FTAGRELRTE IHPCFLCSLA
410 420 430 440 450
FSSQKFLTQH VEWNHRTEIF PGASARINPK PGDPCPDQLQ EHFDSQNKND
460 470 480 490 500
KASNEVKRKS KPRHKWTRQR ISTAFSSTLK EQMRSEESKR TVEEELRTGQ
510 520 530 540 550
TTNIEDTAKS FIASETSRIE RQCGQCFSDK SNVSEHQRTH TGEKPYICRE
560 570 580 590 600
CGRGFSQKSD LIKHQRTHTE EKPYICRECG RGFTQKSDLI KHQRTHTEEK
610 620 630 640 650
PYICRECGRG FTQKSDLIKH QRTHTGEKPY ICRECGRGFT QKSDLIKHQR
660 670 680 690 700
THTEEKPYIC RECGRGFTQK SSLIRHQRTH TGEKPYICRE CGLGFTQKSN
710 720 730 740 750
LIRHLRTHTG EKPYICRECG LGFTRKSNLI QHQRTHTGEK PYICRECGQG
760 770 780 790
LTWKSSLIQH QRTHTGEKPY ICRECGRGFT WKSSLIQHQR THTVEK
Length:796
Mass (Da):92,579
Last modified:February 10, 2009 - 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:i7FB5104B805F87D9
GO
Isoform 2 (identifier: P0C6Y7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.
     386-408: ELRTEIHPCFLCSLAFSSQKFLT → GGYHYDSLKEKEKMDFSLRIFIF
     409-796: Missing.

Show »
Length:283
Mass (Da):32,406
Checksum:iAE2D191116075BA2
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0363791 – 125Missing in isoform 2. CuratedAdd BLAST125
Alternative sequenceiVSP_036380386 – 408ELRTE…QKFLT → GGYHYDSLKEKEKMDFSLRI FIF in isoform 2. CuratedAdd BLAST23
Alternative sequenceiVSP_036381409 – 796Missing in isoform 2. CuratedAdd BLAST388

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
CH474033 Genomic DNA Translation: EDL99813.1

NCBI Reference Sequences

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RefSeqi
NP_001102373.2, NM_001108903.2 [P0C6Y7-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000066370; ENSRNOP00000060531; ENSRNOG00000021493 [P0C6Y7-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
365155

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:365155

UCSC genome browser

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UCSCi
RGD:1305247, rat [P0C6Y7-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
CH474033 Genomic DNA Translation: EDL99813.1
RefSeqiNP_001102373.2, NM_001108903.2 [P0C6Y7-1]

3D structure databases

SMRiP0C6Y7
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060531

Proteomic databases

PaxDbiP0C6Y7
PRIDEiP0C6Y7

Genome annotation databases

EnsembliENSRNOT00000066370; ENSRNOP00000060531; ENSRNOG00000021493 [P0C6Y7-1]
GeneIDi365155
KEGGirno:365155
UCSCiRGD:1305247, rat [P0C6Y7-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
56979
RGDi1305247, Prdm9

Phylogenomic databases

eggNOGiKOG1721, Eukaryota
KOG2461, Eukaryota
GeneTreeiENSGT00940000158211
HOGENOMiCLU_002678_32_0_1
InParanoidiP0C6Y7
KOiK20796
OMAiRSCNDKT
OrthoDBi1318335at2759
PhylomeDBiP0C6Y7
TreeFamiTF338096

Enzyme and pathway databases

ReactomeiR-RNO-212436, Generic Transcription Pathway
R-RNO-3214841, PKMTs methylate histone lysines

Miscellaneous databases

Protein Ontology

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PROi
PR:P0C6Y7

Gene expression databases

BgeeiENSRNOG00000021493, Expressed in testis and 21 other tissues

Family and domain databases

CDDicd07765, KRAB_A-box, 1 hit
InterProiView protein in InterPro
IPR001909, KRAB
IPR036051, KRAB_dom_sf
IPR003655, Krueppel-associated_box-rel
IPR001214, SET_dom
IPR019041, SSXRD_motif
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type
PfamiView protein in Pfam
PF01352, KRAB, 1 hit
PF00856, SET, 1 hit
PF09514, SSXRD, 1 hit
PF00096, zf-C2H2, 8 hits
SMARTiView protein in SMART
SM00349, KRAB, 1 hit
SM00317, SET, 1 hit
SM00355, ZnF_C2H2, 11 hits
SUPFAMiSSF109640, SSF109640, 1 hit
SSF57667, SSF57667, 5 hits
PROSITEiView protein in PROSITE
PS50806, KRAB_RELATED, 1 hit
PS50280, SET, 1 hit
PS00028, ZINC_FINGER_C2H2_1, 10 hits
PS50157, ZINC_FINGER_C2H2_2, 10 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_RAT
<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: P0C6Y7
<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: February 10, 2009
Last modified: August 12, 2020
This is version 94 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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