• Version:
  • 11.0 [archived version]
STRINGSTRING
SMARCC1 SMARCC1 SMARCC2 SMARCC2 EOGT EOGT SAMD9 SAMD9 EEA1 EEA1 PFKP PFKP KARS KARS TPT1 TPT1 RSRP1 RSRP1
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:
some 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 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:
RSRP1Arginine and serine rich protein 1; Belongs to the RSRP family (290 aa)
SMARCC1SWI/SNF complex subunit SMARCC1; Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. May stimulate the ATPase activity of the catalytic subunit of the complex. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF [...] (1105 aa)
SMARCC2SWI/SNF complex subunit SMARCC2; Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. Belongs to the neural progenitors-s [...] (1214 aa)
EEA1Early endosome antigen 1; Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking; Zinc fingers FYVE-type (1411 aa)
KARSLysine--tRNA ligase; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction- the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity; Belongs to the class-I [...] (625 aa)
SAMD9Sterile alpha motif domain-containing protein 9; May play a role in the inflammatory response to tissue injury and the control of extra-osseous calcification, acting as a downstream target of TNF-alpha signaling. Involved in the regulation of EGR1, in coordination with RGL2. May be involved in endosome fusion; Sterile alpha motif domain containing (1589 aa)
PFKPATP-dependent 6-phosphofructokinase, platelet type; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis; Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily (784 aa)
EOGTEGF domain-specific O-linked N-acetylglucosamine transferase; Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N- acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains; O-linked N-acetylglucosaminyltransferases (527 aa)
TPT1Translationally-controlled tumor protein; Involved in calcium binding and microtubule stabilization (197 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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