STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ZNF770Zinc finger protein 770; May be involved in transcriptional regulation; Belongs to the krueppel C2H2-type zinc-finger protein family. (691 aa)    
Predicted Functional Partners:
NOL12
Nucleolar protein 12; May bind to 28S rRNA; Belongs to the RRP17 family.
    
   0.598
NUP58
Nucleoporin p58/p45; Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. Belongs to the NUP58 family.
   
 
 0.564
NIFK
Nucleolar protein interacting with the FHA domain of MKI67.
   
   0.559
SIKE1
Suppressor of IKBKE 1; Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3- mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and DDX58/RIG-I. Does not inhibit NF-kappa-B activation pathways; Belongs to the SIKE family.
   
   0.538
NUS1
Dehydrodolichyl diphosphate synthase complex subunit NUS1; With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stabilit [...]
   
  
 0.533
LRRC2
Leucine-rich repeat-containing protein 2; Leucine rich repeat containing 2.
    
 
 0.532
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 [...]
   
 0.524
ZNF654
Zinc finger protein 654; May be involved in transcriptional regulation; Belongs to the krueppel C2H2-type zinc-finger protein family.
   
  
 0.507
SMARCAD1
ATP-dependent helicase 1; DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double- strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restorat [...]
   
 
 0.505
METAP1
Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle.
   
 
 0.491
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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