STRING protein interaction network
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 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
protein homology
Your Input:
Gene Fusion
CLEC1AC-type lectin domain family 1 member A (280 aa)    
Predicted Functional Partners:
Interleukin-10; Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells; Belongs to the IL-10 family
Lithostathine-1-beta; Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration; C-type lectin domain containing
NKG2-F type II integral membrane protein; May play a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells; Killer cell lectin like receptors
C-type lectin domain family 2 member D; Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon-gamma. Binds high molecular weight sulfated glycosaminoglycans; C-type lectin domain containing
Asialoglycoprotein receptor 1; Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface; C-type lectin domain containing
Podoplanin; Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation. Interaction with CD9, on the contrary, attenuates platelet aggregation induced by PDPN. Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness. Interaction with CD44 promo [...]
C-type lectin domain family 12 member A; Cell surface receptor that modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases; C-type lectin domain containing
Lithostathine-1-alpha; Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration; C-type lectin domain containing
C-type lectin domain containing 14A
C-type lectin domain family 4 member E; C-type lectin that functions as cell-surface receptor for a wide variety of ligands such as damaged cells, fungi and mycobacteria. Plays a role in the recognition of pathogenic fungi, such as Candida albicans. The detection of mycobacteria is via trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid. Specifically recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia. Recognizes also SAP130, a nuclear protein, that is released by dead or dying cells. Transduces signals through an ITAM-containing adapter protein, Fc recept [...]
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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