BP

GO:0000302

response to reactive oxygen species

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.

TAS

BP

GO:0006457

protein folding

The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

TAS

BP

GO:0006464

cellular protein modification process

The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).

TAS

BP

GO:0009266

response to temperature stimulus

Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a temperature stimulus.

TAS

BP

GO:0010260

animal organ senescence

The process that occurs in an animal organ near the end of its active life that is associated with the dismantling of cell components and membranes, and an overall decline in metabolism.

IEA

BP

GO:0019471

4-hydroxyproline metabolic process

The chemical reactions and pathways involving 4-hydroxyproline, C5H9NO3, a derivative of the amino acid proline. The presence of hydroxyproline is essential to produce stable triple helical tropocollagen, hence the problems caused by ascorbate deficiency in scurvy. This unusual amino acid is also present in considerable amounts in the major glycoprotein of primary plant cell walls.

IEA

BP

GO:0022417

protein maturation by protein folding

The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that results in the attainment of the full functional capacity of a protein.

IEA

BP

GO:0030198

extracellular matrix organization

A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.

IEA

BP

GO:0030968

endoplasmic reticulum unfolded protein response

The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.

IEA

BP

GO:0034975

protein folding in endoplasmic reticulum

A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation).

IBA

BP

GO:0034976

response to endoplasmic reticulum stress

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.

ISS

BP

GO:0045454

cell redox homeostasis

Any process that maintains the redox environment of a cell or compartment within a cell.

IEA

BP

GO:0050873

brown fat cell differentiation

The process in which a relatively unspecialized cell acquires specialized features of a brown adipocyte, an animal connective tissue cell involved in adaptive thermogenesis. Brown adipocytes contain multiple small droplets of triglycerides and a high number of mitochondria.

IEA

BP

GO:0051085

chaperone mediated protein folding requiring cofactor

The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.

IDA

BP

GO:0051209

release of sequestered calcium ion into cytosol

The process in which calcium ions sequestered in the endoplasmic reticulum, Golgi apparatus or mitochondria are released into the cytosolic compartment.

ISS

BP

GO:0055114

oxidation-reduction process

A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.

IEA

BP

GO:0070059

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.

ISS

BP

GO:0071456

cellular response to hypoxia

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.

IEA

CC

GO:0005783

endoplasmic reticulum

The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).

IDA

CC

GO:0005788

endoplasmic reticulum lumen

The volume enclosed by the membranes of the endoplasmic reticulum.

TAS

CC

GO:0005789

endoplasmic reticulum membrane

The lipid bilayer surrounding the endoplasmic reticulum.

IBA

CC

GO:0016020

membrane

A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

IDA

CC

GO:0030425

dendrite

A neuron projection that has a short, tapering, often branched, morphology, receives and integrates signals from other neurons or from sensory stimuli, and conducts a nerve impulse towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.

IEA

CC

GO:0043231

intracellular membrane-bounded organelle

Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.

TAS

MF

GO:0003756

protein disulfide isomerase activity

Catalysis of the rearrangement of both intrachain and interchain disulfide bonds in proteins.

IBA

MF

GO:0015035

protein disulfide oxidoreductase activity

Catalysis of the reaction: a protein with reduced sulfide groups = a protein with oxidized disulfide bonds.

IBA

MF

GO:0015036

disulfide oxidoreductase activity

Catalysis of the reaction: substrate with reduced sulfide groups = substrate with oxidized disulfide bonds.

TAS

MF

GO:0016491

oxidoreductase activity

Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

IDA

MF

GO:0016671

oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor

Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces disulfide.

IEA