STRINGSTRING
GRPEL1 GRPEL1 TIMM8A TIMM8A ENSMFAP00000045795 ENSMFAP00000045795 CHORDC1 CHORDC1 CCT3 CCT3 VBP1 VBP1 CANX CANX CCT4 CCT4 PSMG1 PSMG1 ENSMFAP00000013972 ENSMFAP00000013972 ENSMFAP00000013176 ENSMFAP00000013176 ENSMFAP00000012410 ENSMFAP00000012410 G7PJL0_MACFA G7PJL0_MACFA LOC102121674 LOC102121674 ENSMFAP00000009917 ENSMFAP00000009917 PSMG2 PSMG2 ENSMFAP00000006494 ENSMFAP00000006494 CCT6A CCT6A PFDN4 PFDN4 DNAJC18 DNAJC18 ENSMFAP00000002612 ENSMFAP00000002612 CRYAA CRYAA TSACC TSACC TBCA TBCA CALR CALR TIMM13 TIMM13 ENSMFAP00000035554 ENSMFAP00000035554 CRYAB CRYAB RBBP7 RBBP7 CCT6B CCT6B SDHAF2 SDHAF2 TOR1A TOR1A HSP90AB1 HSP90AB1 CCT5 CCT5 ENSMFAP00000042652 ENSMFAP00000042652 CCT7 CCT7 HSPA1L HSPA1L PSMD5 PSMD5 TCP1 TCP1 HSP90AA1 HSP90AA1 ENSMFAP00000032474 ENSMFAP00000032474 HSP90B1 HSP90B1 DNAJB6 DNAJB6 PDILT PDILT MDN1 MDN1 ENSMFAP00000029034 ENSMFAP00000029034 LOC102147033 LOC102147033 DNAJC2 DNAJC2 CLGN CLGN GRPEL2 GRPEL2 TIMM8B TIMM8B ENSMFAP00000025746 ENSMFAP00000025746 HSPA14 HSPA14 CCT2 CCT2 ENSMFAP00000022029 ENSMFAP00000022029 RSAD1 RSAD1 CCT8 CCT8 ENSMFAP00000021488 ENSMFAP00000021488
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:
GRPEL1GrpE protein homolog; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner; Belongs to the GrpE family. (217 aa)
TIMM8Azf-Tim10_DDP domain-containing protein; Belongs to the small Tim family. (97 aa)
ENSMFAP00000045795Uncharacterized protein; Belongs to the TCP-1 chaperonin family. (209 aa)
CHORDC1Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity). (333 aa)
CCT3T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (545 aa)
VBP1Prefoldin subunit 3; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins; Belongs to the prefoldin subunit alpha family. (197 aa)
CANXCalnexin. (592 aa)
CCT4T-complex protein 1 subunit delta. (539 aa)
PSMG1Proteasome assembly chaperone 1; Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with psmg2. (288 aa)
ENSMFAP00000013972zf-Tim10_DDP domain-containing protein; Belongs to the small Tim family. (97 aa)
ENSMFAP00000013176zf-Tim10_DDP domain-containing protein; Belongs to the small Tim family. (83 aa)
ENSMFAP00000012410Uncharacterized protein; Belongs to the GroES chaperonin family. (102 aa)
G7PJL0_MACFAUncharacterized protein; Belongs to the GroES chaperonin family. (102 aa)
LOC102121674zf-Tim10_DDP domain-containing protein; Belongs to the small Tim family. (94 aa)
ENSMFAP00000009917Proteasome assembly chaperone 2; Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. Belongs to the PSMG2 family. (264 aa)
PSMG2Proteasome assembly chaperone 2; Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. Belongs to the PSMG2 family. (264 aa)
ENSMFAP00000006494Uncharacterized protein. (536 aa)
CCT6AUncharacterized protein. (570 aa)
PFDN4Prefoldin subunit 4; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins; Belongs to the prefoldin subunit beta family. (134 aa)
DNAJC18DnaJ homolog subfamily C member 18. (358 aa)
ENSMFAP00000002612Uncharacterized protein; Belongs to the TCP-1 chaperonin family. (151 aa)
CRYAASHSP domain-containing protein; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. (172 aa)
TSACCTSSK6-activating co-chaperone protein; Co-chaperone that facilitates HSP-mediated activation of TSSK6; Belongs to the TSACC family. (100 aa)
TBCATubulin-specific chaperone A; Belongs to the TBCA family. (131 aa)
CALRCalreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. (417 aa)
TIMM13Translocase of inner mitochondrial membrane 13; Belongs to the small Tim family. (95 aa)
ENSMFAP00000035554Uncharacterized protein. (514 aa)
CRYABAlpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. (175 aa)
RBBP7Histone-binding protein RBBP7; Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and [...] (469 aa)
CCT6BChaperonin containing TCP1 subunit 6B. (531 aa)
SDHAF2Succinate dehydrogenase assembly factor 2, mitochondrial; Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SDHA of the SDH catalytic dimer. (166 aa)
TOR1ATorsin-1A; Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular traffickin [...] (315 aa)
HSP90AB1Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...] (724 aa)
CCT5T-complex protein 1 subunit epsilon; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (541 aa)
ENSMFAP00000042652Uncharacterized protein; Belongs to the GroES chaperonin family. (95 aa)
CCT7T-complex protein 1 subunit 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. (543 aa)
HSPA1LHeat shock 70 kDa protein 1-like; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis an [...] (643 aa)
PSMD526S proteasome non-ATPase regulatory subunit 5; Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5 (By similarity). (508 aa)
TCP1T-complex protein 1 subunit alpha; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (556 aa)
HSP90AA1Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] (831 aa)
ENSMFAP00000032474Uncharacterized protein. (524 aa)
HSP90B1Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Belongs to the heat shock protein 90 family. (804 aa)
DNAJB6DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). (334 aa)
PDILTProtein disulfide-isomerase-like protein of the testis; Probable redox-inactive chaperone involved in spermatogenesis; Belongs to the protein disulfide isomerase family. (583 aa)
MDN1Midasin; Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits; Belongs to the midasin family. (5605 aa)
ENSMFAP00000029034Uncharacterized protein; Belongs to the GroES chaperonin family. (88 aa)
LOC102147033Uncharacterized protein; Belongs to the GroES chaperonin family. (108 aa)
DNAJC2DnaJ homolog subfamily C member 2; Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histo [...] (621 aa)
CLGNCalmegin. (619 aa)
GRPEL2GrpE protein homolog; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner; Belongs to the GrpE family. (225 aa)
TIMM8Bzf-Tim10_DDP domain-containing protein; Belongs to the small Tim family. (98 aa)
ENSMFAP00000025746Uncharacterized protein; Belongs to the TCP-1 chaperonin family. (146 aa)
HSPA14Heat shock 70 kDa protein 14; Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding- competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (By similarity). (509 aa)
CCT2T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (589 aa)
ENSMFAP00000022029Uncharacterized protein. (350 aa)
RSAD1Radical S-adenosyl methionine domain-containing protein; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (442 aa)
CCT8T-complex protein 1 subunit theta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. (553 aa)
ENSMFAP00000021488Uncharacterized protein. (535 aa)
Your Current Organism:
Macaca fascicularis
NCBI taxonomy Id: 9541
Other names: M. fascicularis, Macaca cynomolgus, Macaca irus, crab eating macaque, crab-eating macaque, cynomolgus macaque, cynomolgus monkey, cynomolgus monkeys, long-tailed macaque
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