|
Your Input:
|
||||
| OXCT1 | Succinyl-CoA-3-ketoacid coenzyme A transferase 1, mitochondrial; Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate; Belongs to the 3-oxoacid CoA-transferase family (520 aa) | |||
| IDH3G | Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial; Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers (393 aa) | |||
| OGDH | 2-oxoglutarate dehydrogenase, mitochondrial; The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components- 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (1023 aa) | |||
| RIF1 | Telomere-associated protein RIF1; Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage- acts by promoting non-homologous end joining (NHEJ)- mediated repair of DSBs. In response to DNA damage, interacts with ATM-phosphorylated TP53BP1. Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs. Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs. In the [...] (2472 aa) | |||
| AARS2 | Alanine--tRNA ligase, mitochondrial; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain; Belongs to the class-II aminoacyl-tRNA synthetase family (985 aa) | |||
| ACLY | ATP-citrate synthase; ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine; In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family (1101 aa) | |||
| SEPT11 | Septin-11; Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy; Septins (429 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) | |||
| ZMYND15 | Zinc finger MYND domain-containing protein 15; Acts as a transcriptional repressor through interaction with histone deacetylases (HDACs). May be important for spermiogenesis; Zinc fingers MYND-type (750 aa) | |||
| SETDB1 | Histone-lysine N-methyltransferase SETDB1; Histone methyltransferase that specifically trimethylates ’Lys-9’ of histone H3. H3 ’Lys-9’ trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 ’Lys-9’ trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone ’Lys-9’ t [...] (1291 aa) | |||
| IDH3A | Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial; Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers (366 aa) | |||
| SMYD4 | SET and MYND domain containing 4; Belongs to the class V-like SAM-binding methyltransferase superfamily (804 aa) | |||
| POLR3C | DNA-directed RNA polymerase III subunit RPC3; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the subcomplex RNA Pol III binding to the TFIIIB- DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during [...] (534 aa) | |||
| SMYD2 | N-lysine methyltransferase SMYD2; Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 ’Lys-4’ (H3K4me) and dimethylates histone H3 ’Lys-36’ (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates ’Lys-370’ of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at ’Lys-860’ (433 aa) | |||
| SERPINC1 | Antithrombin-III; Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin; Serpin peptidase inhibitors (464 aa) | |||
| S100A16 | Protein S100-A16; Calcium-binding protein. Binds one calcium ion per monomer. Can promote differentiation of adipocytes (in vitro) (By similarity). Overexpression in preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake (By similarity); Belongs to the S-100 family (103 aa) | |||
| SDHB | Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial; Iron-sulfur protein (IP) 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) (280 aa) | |||
| SUCLA2 | Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial; ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity) (463 aa) | |||
| SMYD5 | SET and MYND domain-containing protein 5; Zinc fingers MYND-type; Belongs to the class V-like SAM-binding methyltransferase superfamily (418 aa) | |||
| SUCLG1 | Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits (346 aa) | |||
| SEPT9 | Septin-9; Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- like GTPase superfamily. Septin GTPase family (586 aa) | |||
| SMYD1 | Histone-lysine N-methyltransferase SMYD1; Methylates histone H3 at ’Lys-4’ (H3K4me), seems able to perform both mono-, di-, and trimethylation. Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis; Belongs to the class V-like SAM-binding methyltransferase superfamily (490 aa) | |||
| SELENBP1 | Selenium-binding protein 1; Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similarity) (514 aa) | |||
| LARS2 | Probable leucine--tRNA ligase, mitochondrial; leucyl-tRNA synthetase 2, mitochondrial; Aminoacyl tRNA synthetases, Class I (903 aa) | |||
| SMYD3 | Histone-lysine N-methyltransferase SMYD3; Histone methyltransferase. Specifically methylates ’Lys- 4’ of histone H3, inducing di- and tri-methylation, but not monomethylation. Also methylates ’Lys-5’ of histone H4. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5’- CCCTCC-3’ or 5’-GAGGGG-3’ sequences; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family (369 aa) | |||
| SUCLG2 | Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial; GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (440 aa) | |||
