Terminology Service < Semantic Lookup Platform

All terms in GO

Label	Id	Description
glutathione oxidoreductase activity	GO_0097573	[Catalysis of the reaction: protein-S-S-glutathione + glutathione-SH = protein-SH + glutathione-S-S-glutathione.]
protein disulfide oxidoreductase activity	GO_0015035	[Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.]
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.]
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.]
cellular copper ion homeostasis	GO_0006878	[Any process involved in the maintenance of an internal steady state of copper ions at the level of 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.]
maintenance of location in cell	GO_0051651	[Any process in which a substance or cellular entity, such as a protein complex or organelle, is maintained in a specific location within, or in the membrane of, a cell, and is prevented from moving elsewhere.]
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.]