| Name | UniProt ID Gene Name |
Species Category Species |
Specific function |
|---|---|---|---|
| Fumarate reductase iron-sulfur subunit | P17596 ![]() frdB |
bacterial Wolinella succinogenes |
The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor |
| Fumarate reductase cytochrome b subunit | P17413 ![]() frdC |
bacterial Wolinella succinogenes |
The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor |
| Poly [ADP-ribose] polymerase 3 | Q9Y6F1 ![]() PARP3 |
human Homo sapiens |
Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing |
| Lactaldehyde dehydrogenase | P25553 ![]() aldA |
bacterial Escherichia coli |
Acts on lactaldehyde as well as other aldehydes |
| Cytochrome c oxidase subunit 1 | P33517 ![]() ctaD |
bacterial Rhodobacter sphaeroides |
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer |
| Cytochrome c oxidase subunit 2 | Q03736 ![]() ctaC |
bacterial Rhodobacter sphaeroides |
Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B) |
| Nuclear receptor coactivator 5 | Q9HCD5 ![]() NCOA5 |
human Homo sapiens |
Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC/c-myc in response to 17-beta-estradiol (E2) |
| Type I polyketide synthase PikAIV | Q9ZGI2 ![]() pikAIV |
bacterial Streptomyces venezuelae |
|
| Putative cytochrome P450 130 | Q11062 ![]() cyp130 |
bacterial Mycobacterium tuberculosis |
|
| Pol polyprotein | Q88016 ![]() |
viral Primate lentivirus group Simian immunodeficiency virus |
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1) |
| Hemagglutinin | P26137 ![]() |
viral Influenzavirus A Influenza A virus |
Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore |
| MAP kinase-activated protein kinase 3 | Q16644 ![]() MAPKAPK3 |
human Homo sapiens |
Modulator of polycomb-mediated repression, which can be activated either by ERK, p38 and JNK. Substrate of CSBP. In vitro, phosphorylates HSPB1, BMI1/PCGF4 and TCF3 |
| Hydroxymethylglutaryl-CoA synthase, cytoplasmic | Q01581 ![]() HMGCS1 |
human Homo sapiens |
This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase |
| Guanine nucleotide-binding protein G(T) subunit gamma-T1 | P63211 ![]() GNGT1 |
human Homo sapiens |
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | P62873 ![]() GNB1 |
human Homo sapiens |
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction |
| Phosducin | P20941 ![]() PDC |
human Homo sapiens |
May participate in the regulation of visual phototransduction or in the integration of photoreceptor metabolism |
| GTPase KRas | P01116 ![]() KRAS |
human Homo sapiens |
Ras proteins bind GDP/GTP and possess intrinsic GTPase activity |
| Rab proteins geranylgeranyltransferase component A 1 | P24386 ![]() CHM |
human Homo sapiens |
Binds unprenylated Rab proteins, presents it to the catalytic Rab GGTase dimer, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane |
| Serine/threonine-protein kinase PCTAIRE-1 | Q00536 ![]() CDK16 |
human Homo sapiens |
May play a role in signal transduction cascades in terminally differentiated cells |
| Endo-1,4-beta-xylanase Z | P10478 ![]() xynZ |
bacterial Clostridium thermocellum |
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans |
| Est1e | D2YW37 ![]() |
bacterial Clostridium proteoclasticum |
|
| Neocarzinostatin | P0A3R9 ![]() ncsA |
bacterial Streptomyces carzinostaticus |
NCS has antibiotic activity (for Gram-positive bacteria) and antitumor activity (for certain mouse tumors). NCS binds non- covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks |
| 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | Q8EBR3 ![]() ispF |
bacterial Shewanella oneidensis |
Converts 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate into 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) and CMP (By similarity) |
| Lantibiotic nisin-Z | P29559 ![]() nisZ |
bacterial Lactococcus lactis subsp. |
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores |
| D-alanine--D-alanine ligase | Q5HEB7 ![]() ddl |
bacterial Staphylococcus aureus |
Cell wall formation (By similarity) |