All terms in GO

Label Id Description
right nucleus GO_0097572 [One of the two nuclei found in Giardia species (trophozoite stage). It is located on the right side of the cell when viewed from the dorsal side.]
obsolete glutathione oxidoreductase activity GO_0097573 [OBSOLETE. Catalysis of the reaction: protein-S-S-glutathione + glutathione-SH = protein-SH + glutathione-S-S-glutathione.]
lateral part of cell GO_0097574 [The region of a polarized cell other than its tips or ends (in some cell types, one end may be called the apex and the other the base). For example, in a polarized epithelial cell, the lateral part includes the cell sides which interface adjacent cells.]
lateral cell cortex GO_0097575 [The region directly beneath the plasma membrane of the lateral portion of the cell.]
vacuole fusion GO_0097576 [Merging of two or more vacuoles, or of vacuoles and vesicles within a cell to form a single larger vacuole.]
sequestering of iron ion GO_0097577 [The process of binding or confining iron ions such that they are separated from other components of a biological system.]
sequestering of copper ion GO_0097578 [The process of binding or confining copper ions such that they are separated from other components of a biological system.]
intracellular copper ion homeostasis GO_0006878 [A homeostatic process involved in the maintenance of a steady state level of copper ions within a cell.]
extracellular sequestering of copper ion GO_0097579 [The process of binding or confining copper ions in an extracellular area such that they are separated from other components of a biological system.]
intracellular sequestering of copper ion GO_0097580 [The process of binding or confining copper ions in an intracellular area such that they are separated from other components of a biological system.]
dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex GO_0097582 [A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt1p-Pmt2p.]
dolichyl-phosphate-mannose-protein mannosyltransferase complex GO_0031502 [A complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity; usually includes members of the PMT1 and PMT2 protein subfamilies.]
dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex GO_0097583 [A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt1p-Pmt3p.]
dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p dimer complex GO_0097584 [A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt5p-Pmt2p.]
dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt3p dimer complex GO_0097585 [A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt5p-Pmt3p.]
dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex GO_0097586 [A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt4p.]
MutLgamma complex GO_0097587 [A heterodimer involved in the recognition of base-base and small insertion/deletion mismatches. In S. cerevisiae the complex consists of two subunits, Mlh1 and Mlh3.]
archaeal or bacterial-type flagellum-dependent cell motility GO_0097588 [Cell motility due to movement of bacterial- or archaeal-type flagella.]
cilium or flagellum-dependent cell motility GO_0001539 [Cell motility due to movement of eukaryotic cilia or bacterial-type flagella or archaeal-type flagella.]
archaeal-type flagellum GO_0097589 [A non-membrane-bounded organelle superficially similar to a bacterial-type flagellum; they both consist of filaments extending outside the cell, and rotate to propel the cell, but the archaeal flagella (also called archaella) have a unique structure which lacks a central channel. Similar to bacterial type IV pilins, the archaeal flagellins (archaellins) are made with class 3 signal peptides and they are processed by a type IV prepilin peptidase-like enzyme. The archaellins are typically modified by the addition of N-linked glycans which are necessary for proper assembly and/or function.]