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STRINGSTRING
CCT3 CCT3 TOMM22 TOMM22 MKKS MKKS CCT4 CCT4 YARS YARS TECRL TECRL BBS10 BBS10 CCT5 CCT5 CCT2 CCT2 TCP1 TCP1 HSPD1 HSPD1 CCT7 CCT7 TECR TECR FARS2 FARS2 G3BP2 G3BP2 AIMP1 AIMP1 PIKFYVE PIKFYVE PHB PHB USP45 USP45 SLMO2 SLMO2 TRIAP1 TRIAP1 SLMO1 SLMO1 CDIPT CDIPT PRELID1 PRELID1 CRLS1 CRLS1
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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 each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
TECRtrans-2,3-enoyl-CoA reductase; Reduces trans-2,3-stearoyl-CoA to stearoyl-CoA of long and very long chain fatty acids (308 aa)
TOMM22translocase of outer mitochondrial membrane 22 homolog (yeast); Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore (142 aa)
CDIPTCDP-diacylglycerol--inositol 3-phosphatidyltransferase; Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns-inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme (213 aa)
MKKSMcKusick-Kaufman syndrome; Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis (570 aa)
CCT7chaperonin containing TCP1, subunit 7 (eta); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity) (543 aa)
PIKFYVEphosphoinositide kinase, FYVE finger containing; The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo- inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes (2098 aa)
FARS2phenylalanyl-tRNA synthetase 2, mitochondrial; Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins (451 aa)
CCT5chaperonin containing TCP1, subunit 5 (epsilon); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (541 aa)
CCT3chaperonin containing TCP1, subunit 3 (gamma); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (545 aa)
CCT2chaperonin containing TCP1, subunit 2 (beta); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (535 aa)
PHBprohibitin; Prohibitin inhibits DNA synthesis. It has a role in regulating proliferation. As yet it is unclear if the protein or the mRNA exhibits this effect. May play a role in regulating mitochondrial respiration activity and in aging (272 aa)
PRELID1PRELI domain containing 1; May be important for the development of vital and immunocompetent organs (219 aa)
TCP1t-complex 1; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (556 aa)
USP45ubiquitin specific peptidase 45 (814 aa)
SLMO1slowmo homolog 1 (Drosophila) (172 aa)
HSPD1heat shock 60kDa protein 1 (chaperonin); Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (573 aa)
SLMO2slowmo homolog 2 (Drosophila) (194 aa)
G3BP2GTPase activating protein (SH3 domain) binding protein 2; Probable scaffold protein that may be involved in mRNA transport (Potential) (482 aa)
YARStyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (By similarity) (528 aa)
CRLS1cardiolipin synthase 1; Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol (301 aa)
TECRLtrans-2,3-enoyl-CoA reductase-like (363 aa)
BBS10Bardet-Biedl syndrome 10; Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation (723 aa)
CCT4chaperonin containing TCP1, subunit 4 (delta); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (539 aa)
AIMP1aminoacyl tRNA synthetase complex-interacting multifunctional protein 1; Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90 [...] (336 aa)
TRIAP1TP53 regulated inhibitor of apoptosis 1; Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis (76 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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