• Version:
  • 11.0 [archived version]
STRINGSTRING
DEFA4 DEFA4 DEFA5 DEFA5 DEFA3 DEFA3 DEFB108B DEFB108B FAM172A FAM172A DEFB119 DEFB119 DEFB112 DEFB112 NMT1 NMT1 DEFB124 DEFB124 DEFB123 DEFB123 DEFB118 DEFB118 DEFB129 DEFB129 DEFB131 DEFB131 DEFB128 DEFB128 DEFB114 DEFB114 DEFB136 DEFB136 DEFB110 DEFB110 DEFB135 DEFB135 FBXW5 FBXW5 DEFB1 DEFB1 NMT2 NMT2 IDE IDE PM20D2 PM20D2 ASPH ASPH PMPCB PMPCB PMPCA PMPCA
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)
PMPCBMitochondrial-processing peptidase subunit beta; Cleaves presequences (transit peptides) from mitochondrial protein precursors; M16 metallopeptidases (489 aa)
DEFB118Beta-defensin 118; Has antibacterial activity; Defensins, beta (123 aa)
IDEInsulin-degrading enzyme; Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia; M16 metallopeptidases (1019 aa)
PM20D2Peptidase M20 domain containing 2 (436 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)
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)
FBXW5F-box/WD repeat-containing protein 5; Substrate recognition component of both SCF (SKP1-CUL1- F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. Substrate recognition component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SASS6 during S phase, leading to prevent centriole reduplication. The SCF(FBXW5) complex also mediates ubiquitination and degradation of actin-regulator EPS8 during G2 phase, leading to the transient degradation of EPS8 and subsequent cell shape changes re [...] (566 aa)
DEFB112Beta-defensin 112; Has antibacterial activity; Defensins, beta (113 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)
DEFB110Beta-defensin 110; Has antibacterial activity; Defensins, beta (67 aa)
PMPCAMitochondrial-processing peptidase subunit alpha; Cleaves presequences (transit peptides) from mitochondrial protein precursors; Belongs to the peptidase M16 family (525 aa)
DEFB123Beta-defensin 123; Has antibacterial activity; Belongs to the beta-defensin family (67 aa)
DEFB119Defensin beta 119 (88 aa)
NMT2Glycylpeptide N-tetradecanoyltransferase 2; Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins (498 aa)
ASPHAspartyl/asparaginyl beta-hydroxylase; Isoform 1- specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins; Belongs to the aspartyl/asparaginyl beta-hydroxylase family (758 aa)
DEFB135Beta-defensin 135; Has antibacterial activity; Defensins, beta (77 aa)
DEFB136Beta-defensin 136; Has antibacterial activity; Defensins, beta (78 aa)
FAM172AProtein FAM172A; Family with sequence similarity 172 member A; Belongs to the UPF0528 family (416 aa)
NMT1Glycylpeptide N-tetradecanoyltransferase 1; Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins (496 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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