• Version:
  • 11.0 [archived version]
STRINGSTRING
DEFA4 DEFA4 COL6A2 COL6A2 DEFA5 DEFA5 DEFA3 DEFA3 DEFB108B DEFB108B DEFB128 DEFB128 TCTEX1D2 TCTEX1D2 DEFB121 DEFB121 DEFB124 DEFB124 DEFB135 DEFB135 IL27RA IL27RA DEFB118 DEFB118 DEFB129 DEFB129 DEFB110 DEFB110 NHLRC3 NHLRC3 DEFB112 DEFB112 DEFB131 DEFB131 VWDE VWDE DEFB114 DEFB114 DEFB123 DEFB123 FSTL1 FSTL1 DEFB1 DEFB1 DEFB119 DEFB119 PVRL4 PVRL4 LAYN LAYN TMEM67 TMEM67
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:
DEFB129Beta-defensin 129; Has antibacterial activity; Defensins, beta (183 aa)
DEFB118Beta-defensin 118; Has antibacterial activity; Defensins, beta (123 aa)
IL27RAInterleukin-27 receptor subunit alpha; Receptor for IL27. Requires IL6ST/gp130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1- type immune responses. Also appears to be involved in innate defense mechanisms; Fibronectin type III domain containing (636 aa)
VWDEVon Willebrand factor D and EGF domains (1590 aa)
FSTL1Follistatin-related protein 1; May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity); SPARC family (308 aa)
DEFA4Neutrophil defensin 4; Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Protects blood cells against infection with HIV-1 (in vitro). Inhibits corticotropin (ACTH)-stimulated corticosterone production; Defensins, alpha (97 aa)
DEFB1Beta-defensin 1; Has bactericidal activity. May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility; Belongs to the beta-defensin family (68 aa)
COL6A2Collagen alpha-2(VI) chain; Collagen VI acts as a cell-binding protein; Collagens (1019 aa)
DEFB114Beta-defensin 114; Has a salt-sensitive antimicrobial activity against Gram-negative bacteria, including E.coli, Gram-positive, including S.aureus, and fungi, including C.albicans. Binds to and neutralizes bacterial lipopolysaccharides (LPS), abolishing TNF production by macrophages challenged with LPS. Rescues the LPS- induced reduction of sperm motility in vitro and may protect from LPS-induced lethality; Defensins, beta (69 aa)
DEFB112Beta-defensin 112; Has antibacterial activity; Defensins, beta (113 aa)
TCTEX1D2Tctex1 domain-containing protein 2; Required for proper retrograde ciliary transport; Belongs to the dynein light chain Tctex-type family (142 aa)
DEFB124Beta-defensin 124; Has antibacterial activity; Defensins, beta (71 aa)
DEFA3Neutrophil defensin 3; Defensin 2 and defensin 3 have antibiotic, fungicide and antiviral activities. Has antimicrobial activity against Gram- negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane; Defensins, alpha (94 aa)
DEFA5Defensin-5; Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing; Defensins, alpha (94 aa)
DEFB108BBeta-defensin 108B; Has antibacterial activity; Defensins, beta (73 aa)
DEFB128Beta-defensin 128; Has antibacterial activity; Defensins, beta (93 aa)
DEFB131Beta-defensin 131A; Has antibacterial activity (Probable). Upon stimulation with lipoteichoic acid, promotes cytokines and chemokines production and secretion; Belongs to the beta-defensin family (70 aa)
PVRL4Nectin-4; Seems to be involved in cell adhesion through trans- homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells (510 aa)
DEFB110Beta-defensin 110; Has antibacterial activity; Defensins, beta (67 aa)
LAYNLayilin; Receptor for hyaluronate; C-type lectin domain containing (382 aa)
DEFB123Beta-defensin 123; Has antibacterial activity; Belongs to the beta-defensin family (67 aa)
DEFB119Defensin beta 119 (88 aa)
NHLRC3NHL repeat containing 3 (347 aa)
DEFB135Beta-defensin 135; Has antibacterial activity; Defensins, beta (77 aa)
TMEM67Meckelin; Required for ciliary structure and function. Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Involved in centrosome migration to the apical cell surface during early ciliogenesis. Involved in the regulation of cilia length and appropriate number through the control of centrosome duplication. Required for cell branching morphology. Essential for endoplasmic reticulum-associated degradation (ERAD) of surfactant protein C (SFTPC) (995 aa)
DEFB121Beta-defensin 121; Has antibacterial activity; Belongs to the beta-defensin family (76 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
Server load: low (0%) [HD]