STRINGSTRING
CHGG_08244 CHGG_08244 CHGG_08243 CHGG_08243 CHGG_08189 CHGG_08189 CHGG_06927 CHGG_06927 CHGG_06680 CHGG_06680 CHGG_03653 CHGG_03653 CHGG_03307 CHGG_03307 CHGG_01954 CHGG_01954 cnxG cnxG CHGG_01044 CHGG_01044
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:
CHGG_08244Uncharacterized protein; Belongs to the actin family. (573 aa)
CHGG_08243Uncharacterized protein. (873 aa)
CHGG_08189CAP-Gly domain-containing protein. (1351 aa)
CHGG_06927Uncharacterized protein. (198 aa)
CHGG_06680CDH-cyt domain-containing protein. (353 aa)
CHGG_03653Uncharacterized protein. (630 aa)
CHGG_03307Uncharacterized protein. (1176 aa)
CHGG_01954RRN9 domain-containing protein. (800 aa)
cnxGMolybdopterin synthase sulfur carrier subunit; Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by UBA4. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin. (541 aa)
CHGG_01044F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. (287 aa)
Your Current Organism:
Chaetomium globosum
NCBI taxonomy Id: 306901
Other names: C. globosum CBS 148.51, Chaetomium globosum CBS 148.51
Server load: low (16%) [HD]