STRINGSTRING
CG42335 CG42335 CG9581 CG9581 CG2111 CG2111 CG9806 CG9806 Psa Psa CG6071 CG6071 S-Lap4 S-Lap4 S-Lap1 S-Lap1 S-Lap2 S-Lap2 CG32454 CG32454 und und CG5188 CG5188 DppIII DppIII CG8774 CG8774 CG5849 CG5849 CG31343 CG31343 CG31198 CG31198 CG11951 CG11951 CG46339 CG46339 CG13630 CG13630 superdeath superdeath SP1029 SP1029 CG13423 CG13423 S-Lap8 S-Lap8 S-Lap5 S-Lap5 S-Lap7 S-Lap7 TppII TppII CG40470 CG40470 loopin-1 loopin-1 CG3502 CG3502 CG8773 CG8773 ApepP ApepP CG31445 CG31445 S-Lap3 S-Lap3 CG1440 CG1440 grsm grsm CG31233 CG31233
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:
CG42335Aminopeptidase; Peptide binding; zinc ion binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (924 aa)
CG9581GH19483p; Peptidase activity; aminopeptidase activity; manganese ion binding. (545 aa)
CG2111Aminopeptidase; Zinc ion binding; peptide binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (931 aa)
CG9806Metalloaminopeptidase activity; peptide binding; zinc ion binding. It is involved in the biological process described with: multicellular organism reproduction; peptide catabolic process; proteolysis. (911 aa)
PsaPuromycin sensitive aminopeptidase, isoform C; Peptide binding; zinc ion binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (1075 aa)
CG6071Aminopeptidase; Peptide binding; zinc ion binding; metalloaminopeptidase activity. It is involved in the biological process described with: multicellular organism reproduction; proteolysis; peptide catabolic process. (962 aa)
S-Lap4Sperm-Leucylaminopeptidase 4; Metalloexopeptidase activity; aminopeptidase activity; manganese ion binding. It is involved in the biological process described with: proteolysis. (524 aa)
S-Lap1Sperm-Leucylaminopeptidase 1; Aminopeptidase activity; metalloexopeptidase activity; manganese ion binding. It is involved in the biological process described with: mushroom body development; proteolysis. (555 aa)
S-Lap2Sperm-Leucylaminopeptidase 2; Aminopeptidase activity; metalloexopeptidase activity; manganese ion binding. It is involved in the biological process described with: proteolysis. (552 aa)
CG32454AMP_N domain-containing protein; Aminopeptidase activity; manganese ion binding. (534 aa)
undMethionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). (448 aa)
CG5188Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). (317 aa)
DppIIIDipeptidyl peptidase 3; Degrades neuropeptide proctolin (RYLPT) by cleavage between Tyr and Leu residues; Belongs to the peptidase M49 family. (786 aa)
CG8774Metalloaminopeptidase activity; zinc ion binding; peptide binding. It is involved in the biological process described with: proteolysis; peptide catabolic process. (942 aa)
CG5849Metalloaminopeptidase activity; peptide binding; zinc ion binding. It is involved in the biological process described with: proteolysis; peptide catabolic process. (968 aa)
CG31343Aminopeptidase; Zinc ion binding; peptide binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (961 aa)
CG31198Aminopeptidase; Peptide binding; zinc ion binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (940 aa)
CG11951Aminopeptidase; Zinc ion binding; peptide binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (924 aa)
CG46339Uncharacterized protein, isoform D; Peptide binding; aminopeptidase activity; zinc ion binding; metalloaminopeptidase activity. (1194 aa)
CG13630Methionine aminopeptidase; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). (374 aa)
superdeathAminopeptidase; Zinc ion binding; peptide binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (999 aa)
SP1029Metalloaminopeptidase activity; peptide binding; zinc ion binding. It is involved in the biological process described with: proteolysis; peptide catabolic process. (932 aa)
CG13423Bleomycin hydrolase; Cysteine-type peptidase activity; cysteine-type endopeptidase activity. It is involved in the biological process described with: homocysteine catabolic process; response to toxic substance; proteolysis. (476 aa)
S-Lap8Sperm-Leucylaminopeptidase 8; Aminopeptidase activity; metalloexopeptidase activity; manganese ion binding. It is involved in the biological process described with: proteolysis. (534 aa)
S-Lap5Sperm-Leucylaminopeptidase 5; Metalloexopeptidase activity; aminopeptidase activity; manganese ion binding. It is involved in the biological process described with: proteolysis; mesoderm development. (549 aa)
S-Lap7Sperm-Leucylaminopeptidase 7, isoform A; Manganese ion binding; metalloexopeptidase activity; aminopeptidase activity. It is involved in the biological process described with: proteolysis; multicellular organism reproduction. (527 aa)
TppIITripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited (By similarity). Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala-polypeptide, Val-Leu-Lys- polypeptide only at high concentration. Does not cleave Ala-Phe-Pro- polypeptide nor Pro-Leu-Gly-polypeptide; Belongs to the peptidase S8 family. (1441 aa)
CG40470Metalloaminopeptidase activity; zinc ion binding; peptide binding. It is involved in the biological process described with: peptide catabolic process; proteolysis. (941 aa)
loopin-1Loopin-1, isoform A; Loopin-1 (loopin-1) encodes a testis-specific protein with homology to several leucine aminopeptidases. Sequence analysis suggest that it doesn't have enzymatic activity. It accumulates inside the axoneme-associated mitochondrial derivative in mature sperms. (526 aa)
CG3502Aminopeptidase; Peptide binding; zinc ion binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (912 aa)
CG8773Metalloaminopeptidase activity; peptide binding; zinc ion binding. It is involved in the biological process described with: dsRNA transport; peptide catabolic process; proteolysis. (994 aa)
ApepPXaa-Pro aminopeptidase ApepP; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Belongs to the peptidase M24B family. (613 aa)
CG31445Aminopeptidase; Peptide binding; zinc ion binding; metalloaminopeptidase activity. It is involved in the biological process described with: peptide catabolic process; proteolysis. (927 aa)
S-Lap3Sperm-Leucylaminopeptidase 3, isoform B; Manganese ion binding; metalloexopeptidase activity; aminopeptidase activity. It is involved in the biological process described with: proteolysis. (535 aa)
CG1440Uncharacterized protein, isoform D; Cysteine-type peptidase activity; cysteine-type endopeptidase activity. It is involved in the biological process described with: homocysteine catabolic process; response to toxic substance; proteolysis. (551 aa)
grsmGranny smith (grsm) encodes a member of the M17 family of leucine aminopeptidases, a family of proteases broadly involved in a number of cellular processes. High throughput transcriptomic and proteomic analyses have implicated the product of grsm in the regulation of immune-, nervous- and immune-related processes. (655 aa)
CG31233Metalloaminopeptidase activity; zinc ion binding; peptide binding. It is involved in the biological process described with: peptide catabolic process; proteolysis. (952 aa)
Your Current Organism:
Drosophila melanogaster
NCBI taxonomy Id: 7227
Other names: D. melanogaster, Diptera sp. DNAS-2A9-224646, Sophophora melanogaster, fruit fly
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