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| ARHGDIG | Rho GDP-dissociation inhibitor 3; Inhibits GDP/GTP exchange reaction of RhoB. Interacts specifically with the GDP- and GTP-bound forms of post- translationally processed Rhob and Rhog proteins, both of which show a growth-regulated expression in mammalian cells. Stimulates the release of the GDP-bound but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange of RhoB but shows less ability to inhibit the dissociation of prebound GTP (225 aa) | |||
| SUGP1 | SURP and G-patch domain-containing protein 1; Plays a role in pre-mRNA splicing; G-patch domain containing (645 aa) | |||
| MRPL53 | Mitochondrial ribosomal protein L53 (112 aa) | |||
| SDHA | Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial; Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily (664 aa) | |||
| TIMM44 | Mitochondrial import inner membrane translocase subunit TIM44; 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. Recruits mitochondrial HSP70 to drive protein translocation into the matrix using ATP as an energy source; Belongs to the Tim44 family (452 aa) | |||
| ATP6V1A | V-type proton ATPase catalytic subunit A; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation; Belongs to the ATPase alpha/beta chains family (617 aa) | |||
| TXNDC16 | Thioredoxin domain containing 16 (825 aa) | |||
| PDIA4 | Protein disulfide-isomerase A4; Protein disulfide isomerase family A member 4; Belongs to the protein disulfide isomerase family (645 aa) | |||
| RBMS1 | RNA-binding motif, single-stranded-interacting protein 1; Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5’-[AT]CT[AT][AT]T-3’. Probably has a role in DNA replication (406 aa) | |||
| HSP90B1 | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity; Belongs to the heat shock protein 90 family (803 aa) | |||
| PPIB | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (216 aa) | |||
| PDIA3 | Protein disulfide-isomerase A3; Protein disulfide isomerase family A member 3; Belongs to the protein disulfide isomerase family (505 aa) | |||
| ENO3 | Beta-enolase; Appears to have a function in striated muscle development and regeneration; Belongs to the enolase family (434 aa) | |||
| P4HB | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] (508 aa) | |||
| ACAA1 | 3-ketoacyl-CoA thiolase, peroxisomal; acetyl-CoA acyltransferase 1 (424 aa) | |||
| ISYNA1 | Inositol-3-phosphate synthase 1; Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (558 aa) | |||
| SFN | 14-3-3 protein sigma; Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53; Belongs to the 14-3-3 family (248 aa) | |||
| MRRF | Ribosome-recycling factor, mitochondrial; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (By similarity) (262 aa) | |||
| CISD1 | CDGSH iron-sulfur domain-containing protein 1; Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions; Belongs to the CISD protein family (108 aa) | |||
| UCHL3 | Ubiquitin carboxyl-terminal hydrolase isozyme L3; Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards ’Lys-48’-linked ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 [...] (230 aa) | |||
| PCNA | Proliferating cell nuclear antigen; Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase’s processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3’- 5’ exonuclease and 3’-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA re [...] (261 aa) | |||
| FKBP2 | Peptidyl-prolyl cis-trans isomerase FKBP2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; FKBP prolyl isomerases (142 aa) | |||
| FKBP1A | Peptidyl-prolyl cis-trans isomerase FKBP1A; Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the FKBP-type PPIase family. FKBP1 subfamily (108 aa) | |||
| TAGLN | Transgelin; Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence; Belongs to the calponin family (201 aa) | |||
| ZC3H11A | Zinc finger CCCH domain-containing protein 11A; Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex; Zinc fingers CCCH-type (810 aa) | |||
| LSM4 | U6 snRNA-associated Sm-like protein LSm4; Binds specifically to the 3’-terminal U-tract of U6 snRNA; Belongs to the snRNP Sm proteins family (139 aa) | |||
