STRINGSTRING
adm-4 adm-4 nep-1 nep-1 ZK550.3 ZK550.3 nep-26 nep-26 nep-25 nep-25 nas-30 nas-30 Y67H2A.7 Y67H2A.7 Y50D7A.13 Y50D7A.13 unc-71 unc-71 Y19D10B.6 Y19D10B.6 nep-24 nep-24 nep-23 nep-23 zmp-4 zmp-4 nep-22 nep-22 toh-1 toh-1 nas-5 nas-5 nas-27 nas-27 zmp-6 zmp-6 adt-3 adt-3 nep-21 nep-21 nas-22 nas-22 nas-21 nas-21 nas-20 nas-20 nep-20 nep-20 nep-2 nep-2 nas-15 nas-15 nas-32 nas-32 dpy-31 dpy-31 nas-23 nas-23 nas-11 nas-11 nas-10 nas-10 nas-3 nas-3 nas-33 nas-33 nas-19 nas-19 nas-18 nas-18 nas-17 nas-17 nas-16 nas-16 nep-18 nep-18 zmp-5 zmp-5 zmp-2 zmp-2 nas-31 nas-31 nas-29 nas-29 nas-38 nas-38 mig-17 mig-17 nas-2 nas-2 nep-17 nep-17 nas-25 nas-25 nas-1 nas-1 nep-16 nep-16 F42G10.1 F42G10.1 nas-28 nas-28 hch-1 hch-1 nep-15 nep-15 nep-13 nep-13 nas-13 nas-13 nas-39 nas-39 F27D9.7 F27D9.7 gon-1 gon-1 nas-24 nas-24 nep-11 nep-11 nep-10 nep-10 nep-9 nep-9 nep-8 nep-8 nep-6 nep-6 nep-5 nep-5 nas-14 nas-14 adt-2 adt-2 zmp-1 zmp-1 sup-17 sup-17 nep-4 nep-4 nep-3 nep-3 nas-9 nas-9 tag-275 tag-275 nas-8 nas-8 zmp-3 zmp-3 nas-36 nas-36 nas-12 nas-12 nas-37 nas-37 nas-7 nas-7 nas-4 nas-4 adm-2 adm-2 adt-1 adt-1 C01F1.5 C01F1.5 nas-6 nas-6
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.
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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:
adm-4Disintegrin and metalloproteinase domain-containing protein 17 homolog; Metalloprotease (By similarity). Acts together with protease sup-17 to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision. By modulating lin-12/Notch signaling, plays a role in germline development. (686 aa)
nep-1Neprilysin-1; Probable cell surface protease. Required to control the neuronal innervation of pharyngeal pumping. Belongs to the peptidase M13 family. (754 aa)
ZK550.3Peptidase_M3 domain-containing protein. (772 aa)
nep-26NEPrilysin metallopeptidase family. (807 aa)
nep-25Peptidase_M13 domain-containing protein. (515 aa)
nas-30Zinc metalloproteinase nas-30; Metalloprotease. (525 aa)
Y67H2A.7Peptidase_M3 domain-containing protein. (692 aa)
Y50D7A.13ZnMc domain-containing protein. (194 aa)
unc-71Disintegrin and metalloproteinase domain-containing protein unc-71; Involved in the migration of sex myoblasts (progenitors of egg-laying muscles), Q neuroblasts and BDU interneurons during development. Involved in axon branching and guidance of neurons including GABAergic type D motor neurons. Promotes sex myoblast migration and positioning independently of gonad attraction cues. May act downstream of mig-13 in order to promote the guidance, migration and positioning of Q neuroblasts and their descendants along the anteroposterior body axis. Required for coordinated movements. (1042 aa)
Y19D10B.6Uncharacterized protein. (492 aa)
nep-24NEPrilysin metallopeptidase family. (567 aa)
nep-23NEPrilysin metallopeptidase family. (714 aa)
zmp-4ZnMc domain-containing protein. (472 aa)
nep-22NEPrilysin metallopeptidase family. (798 aa)
toh-1Zinc metalloproteinase nas-26; Metalloprotease. (414 aa)
nas-5Zinc metalloproteinase nas-5; Metalloprotease. (360 aa)
nas-27Zinc metalloproteinase nas-27; Metalloprotease. (428 aa)
zmp-6ZnMc domain-containing protein. (279 aa)
adt-3Peptidase M12B domain-containing protein. (940 aa)
nep-21Neprilysin-21; Probable cell surface protease. (856 aa)
nas-22Zinc metalloproteinase nas-22; Metalloprotease. (367 aa)
nas-21Zinc metalloproteinase-like protein nas-21; May lack metalloprotease activity. (380 aa)
nas-20Zinc metalloproteinase nas-20; Metalloprotease. (379 aa)
nep-20NEPrilysin metallopeptidase family. (834 aa)
nep-2Neprilysin-2; Required for olfactory plasticity, which is the change from positive chemotaxis to dispersal after prolonged exposure to an odorant. Thought to antagonise snet-1 by degrading excess snet-1 peptides and thus enabling olfactory plasticity. (736 aa)
nas-15Zinc metalloproteinase nas-15; Metalloprotease. (571 aa)
nas-32Zinc metalloproteinase nas-32; Metalloprotease. (653 aa)
dpy-31Zinc metalloproteinase dpy-31; Metalloprotease which cleaves the carboxyl terminus of procollagens, such as sqt-3, to mature collagens (By similarity). Involved in cuticular collagen maturation. (592 aa)
nas-23Zinc metalloproteinase nas-23; Metalloprotease. (537 aa)
nas-11Zinc metalloproteinase nas-11; Metalloprotease. (579 aa)
nas-10Zinc metalloproteinase nas-10; Metalloprotease. (560 aa)
nas-3Zinc metalloproteinase nas-3; Metalloprotease. (292 aa)
nas-33Zinc metalloproteinase nas-33; Metalloprotease. (644 aa)
nas-19Zinc metalloproteinase nas-19; Metalloprotease. (396 aa)
nas-18Zinc metalloproteinase nas-18; Metalloprotease. (240 aa)
nas-17Zinc metalloproteinase nas-17; Metalloprotease. (448 aa)
nas-16Zinc metalloproteinase nas-16; Metalloprotease. (337 aa)
nep-18NEPrilysin metallopeptidase family. (701 aa)
zmp-5ZnMc domain-containing protein. (405 aa)
zmp-2Matrix metalloproteinase-B; Metalloprotease involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. Plays a role in thermotolerance probably by preventing the accumulation of oxidized lipoproteins and cholesterol. (519 aa)
nas-31Zinc metalloproteinase nas-31; Metalloprotease. (611 aa)
nas-29Zinc metalloproteinase nas-29; Metalloprotease. (532 aa)
nas-38Zinc metalloproteinase nas-38; Metalloprotease. (745 aa)
mig-17Metalloprotease mig-17; Metalloprotease. Acts in the basement membrane to control directional migration of distal tip cells (DTCs) along the body wall basement membranes, a key step that promotes gonad morphogenesis. Regulates DTC migration probably by recruiting fibulin fbl-1, type IV collagen let-2 and nidogen nid-1 to the gonad basement membrane thereby promoting the remodeling of the basement membrane. During larval development and probably upstream of basement membrane proteins fbl-1, let-2 and nid-1, regulates pharynx length, probably by regulating pharyngeal cell length. Does no [...] (509 aa)
nas-2Zinc metalloproteinase nas-2; Metalloprotease. (272 aa)
nep-17NEPrilysin metallopeptidase family. (1589 aa)
nas-25Zinc metalloproteinase nas-25; Metalloprotease. (399 aa)
nas-1Zinc metalloproteinase nas-1; Metalloprotease. (270 aa)
nep-16Peptidase_M13_N domain-containing protein. (868 aa)
F42G10.1Uncharacterized protein. (587 aa)
nas-28Zinc metalloproteinase nas-28; Metalloprotease. (497 aa)
hch-1Zinc metalloproteinase nas-34; Metalloprotease (By similarity). Required for normal hatching and migration of neuroblasts. May act by degrading eggshell proteins at hatching. (605 aa)
nep-15Peptidase_M13 domain-containing protein. (267 aa)
nep-13NEPrilysin metallopeptidase family. (732 aa)
nas-13Zinc metalloproteinase nas-13; Metalloprotease. (450 aa)
nas-39Zinc metalloproteinase nas-39; Metalloprotease. (951 aa)
F27D9.7Peptidase M12B domain-containing protein. (386 aa)
gon-1A disintegrin and metalloproteinase with thrombospondin motifs gon-1; Secreted metalloprotease required for distal tip cell (DTC) migration along the body wall basement membranes, a key step that promotes gonad morphogenesis. Probably acts by remodeling the basement membrane during cell migration. Required to restrict presynaptic growth at the neuromuscular junctions (NMJ) in late larval stage and in adult motor neurons, probably by controlling collagen IV emb-9 degradation, a component of the synapse basement membrane. Also involved in the organization of adult muscle morphology. Has [...] (2165 aa)
nas-24Zinc metalloproteinase nas-24; Metalloprotease. (396 aa)
nep-11Neprilysin-11; Probable cell surface protease; Belongs to the peptidase M13 family. (848 aa)
nep-10NEPrilysin metallopeptidase family. (711 aa)
nep-9NEPrilysin metallopeptidase family. (700 aa)
nep-8Peptidase_M13 domain-containing protein. (686 aa)
nep-6NEPrilysin metallopeptidase family. (726 aa)
nep-5NEPrilysin metallopeptidase family. (655 aa)
nas-14Zinc metalloproteinase nas-14; Metalloprotease. (503 aa)
adt-2A disintegrin and metalloproteinase with thrombospondin motifs adt-2; Regulates body size probably independently of the TGF beta- like dbl-1 pathway. However, may regulate some dbl-1-mediated transcription. Plays a role in cuticle collagen fibril organization. Required for embryonic development. (1020 aa)
zmp-1Matrix metalloproteinase-A; Metalloprotease which, together with cadherin cdh-3 and hemicentin him-4, plays a role in anchor cell (AC) invasion during postembryonic vulval development probably by promoting the degradation of the basement membrane separating the gonad from the vulva epithelium. (521 aa)
sup-17Disintegrin and metalloproteinase domain-containing protein 10 homolog; Metalloprotease (By similarity). Acts together with protease adm-4 and in a cell autonomous manner to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision and vulva precursor cell specification. By modulating lin-12/Notch signaling, plays a role in germline development. Probably by modulating BMP-like Sma/Mab signaling via the shedding of unc-40 ectodomain, involved in the regulation of body size and mesoderm development. Probably b [...] (922 aa)
nep-4Peptidase_M13 domain-containing protein. (437 aa)
nep-3NEPrilysin metallopeptidase family. (634 aa)
nas-9Zinc metalloproteinase nas-9; Metalloprotease. (546 aa)
tag-275Peptidase M12B domain-containing protein. (472 aa)
nas-8Zinc metalloproteinase nas-8; Metalloprotease. (403 aa)
zmp-3Matrix metalloproteinase-C; Metalloproteinase. (579 aa)
nas-36Zinc metalloproteinase nas-36; Metalloprotease (By similarity). Involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. (617 aa)
nas-12Zinc metalloproteinase nas-12; Metalloprotease. (384 aa)
nas-37Zinc metalloproteinase nas-37; Metalloprotease (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. Required during ecdysis, the opening of the cuticle to allow the worm to escape. (765 aa)
nas-7Zinc metalloproteinase nas-7; Metalloprotease. (382 aa)
nas-4Zinc metalloproteinase nas-4; Metalloprotease (By similarity). May be involved in digestion. (365 aa)
adm-2ADAM (Disintegrin plus metalloprotease) family. (952 aa)
adt-1A disintegrin and metalloproteinase with thrombospondin motifs adt-1; Plays a role in ray morphogenesis in the male tail, probably by remodeling the extracellular matrix (ECM) in the cuticle. (1461 aa)
C01F1.5Uncharacterized protein. (308 aa)
nas-6Zinc metalloproteinase nas-6; Metalloprotease. (344 aa)
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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