STRINGSTRING
petE petE coxB coxB AFW94339.1 AFW94339.1 AFW95418.1 AFW95418.1 coxB-2 coxB-2 coxB-3 coxB-3
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:
petEPlastocyanin; Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. (139 aa)
coxBCytochrome c oxidase subunit II protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (311 aa)
AFW94339.1Copper-binding protein. (149 aa)
AFW95418.1Multicopper oxidase, types 2 and 3. (334 aa)
coxB-2Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (321 aa)
coxB-3Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (308 aa)
Your Current Organism:
Anabaena sp. 90
NCBI taxonomy Id: 46234
Other names: A. sp. 90, Anabaena circinalis 90, Anabaena sp. strain 90
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