STRINGSTRING
enpep enpep dpp3 dpp3 metap1 metap1 AOPEP AOPEP lta4h lta4h lap3 lap3 lnpep lnpep erap2 erap2 ENSHBUP00000011621 ENSHBUP00000011621 LOC102301823 LOC102301823 xpnpep1 xpnpep1 xpnpep2 xpnpep2 trhde trhde rnpepl1 rnpepl1 LOC102293374 LOC102293374 ANPEP ANPEP LOC102313890 LOC102313890 mmp15 mmp15 LOC102310167 LOC102310167 npepl1 npepl1 LOC102302644 LOC102302644 npepps npepps LOC102294382 LOC102294382 LOC102299978 LOC102299978 LOC102302232 LOC102302232 LOC102302131 LOC102302131 metap1d metap1d xpnpep3 xpnpep3 LOC102310942 LOC102310942 LOC102303792 LOC102303792
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:
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:
enpepAminopeptidase. (957 aa)
dpp3Dipeptidyl peptidase 3; Belongs to the peptidase M49 family. (726 aa)
metap1Methionine 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). (412 aa)
AOPEPAminopeptidase O (putative). (873 aa)
lta4hLeukotriene A4 hydrolase. (673 aa)
lap3Leucine aminopeptidase 3. (520 aa)
lnpepLeucyl/cystinyl aminopeptidase. (1035 aa)
erap2Aminopeptidase. (945 aa)
ENSHBUP00000011621Uncharacterized protein. (53 aa)
LOC102301823Aminopeptidase. (825 aa)
xpnpep1X-prolyl aminopeptidase (aminopeptidase P) 1, soluble; Belongs to the peptidase M24B family. (689 aa)
xpnpep2X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound; Belongs to the peptidase M24B family. (710 aa)
trhdeAminopeptidase. (993 aa)
rnpepl1Arginyl aminopeptidase like 1. (712 aa)
LOC102293374Uncharacterized protein. (1199 aa)
ANPEPAminopeptidase. (968 aa)
LOC102313890Aminopeptidase. (964 aa)
mmp15Matrix metallopeptidase 15b. (657 aa)
LOC102310167Matrix metallopeptidase 14b (membrane-inserted). (664 aa)
npepl1Aminopeptidase like 1. (523 aa)
LOC102302644Methionine 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). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily. (477 aa)
npeppsAminopeptidase. (873 aa)
LOC102294382Methionine 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). Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily. (477 aa)
LOC102299978Aminopeptidase. (959 aa)
LOC102302232Zgc:152830. (525 aa)
LOC102302131Uncharacterized protein. (642 aa)
metap1dMethionine 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). (339 aa)
xpnpep3X-prolyl aminopeptidase 3, mitochondrial. (511 aa)
LOC102310942Aminopeptidase. (970 aa)
LOC102303792Peptidase D. (507 aa)
Your Current Organism:
Haplochromis burtoni
NCBI taxonomy Id: 8153
Other names: Astatotilapia burtoni, Chromis burtoni, H. burtoni
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