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STRINGSTRING
RNF212 RNF212 ZNF783 ZNF783 ZNF773 ZNF773 CENPBD1 CENPBD1 TRIM28 TRIM28 PRDM7 PRDM7 ZNF419 ZNF419 PLOD1 PLOD1 PLOD3 PLOD3 CAMKMT CAMKMT PLOD2 PLOD2
"PRDM7" - Probable histone-lysine N-methyltransferase PRDM7 in Homo sapiens
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
PRDM7Probable histone-lysine N-methyltransferase PRDM7; Probable histone methyltransferase; PR/SET domain family (492 aa)    
Predicted Functional Partners:
TRIM28
Transcription intermediary factor 1-beta; Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at ’Lys-9’ (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 ’Lys-9 and ’Lys-14’ acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression [...] (835 aa)
          
    0.900
CAMKMT
Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing (323 aa)
          
  0.703
PLOD2
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (758 aa)
          
    0.650
PLOD3
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (738 aa)
          
    0.650
PLOD1
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1; Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (By similarity). Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (Probable) (727 aa)
          
    0.650
RNF212
Probable E3 SUMO-protein ligase RNF212; SUMO E3 ligase that acts as a regulator of crossing-over during meiosis- required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11. May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to enhance their binding to recombination sites. Acts as a limiting factor for crossover designation and/or reinforcement and plays an antagonist role with [...] (297 aa)
            
  0.626
CENPBD1
CENPB DNA-binding domain-containing protein 1; Helix-turn-helix CENPB type domain containing (187 aa)
            
  0.556
ZNF783
Protein ZNF783; May be involved in transcriptional regulation; Zinc fingers C2H2-type (546 aa)
        
 
  0.542
ZNF419
Zinc finger protein 419; May be involved in transcriptional regulation; Belongs to the krueppel C2H2-type zinc-finger protein family (511 aa)
        
 
  0.540
ZNF773
Zinc finger protein 773; May be involved in transcriptional regulation; Zinc fingers C2H2-type (442 aa)
        
 
  0.540
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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