peripheral plasma membrane protein
extrinsic to plasma membrane

The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. [GOC:curators, GOC:dos]


Complex of peripheral cytoplasmic proteins (alpha-, beta- and gamma-catenin) that interact with the cytoplasmic region of uvomorulin/E-cadherin to connect it to the actin cytoskeleton. [ISBN:0198599323]


Any of a family of heterotrimeric GTP-binding and hydrolyzing proteins; they belong to a superfamily of GTPases that includes monomeric proteins such as EF-Tu and RAS. Heterotrimeric G-proteins consist of three subunits; the alpha subunit contains the guanine nucleotide binding site and possesses GTPase activity; the beta and gamma subunits are tightly associated and function as a beta-gamma heterodimer; extrinsic plasma membrane proteins (cytoplasmic face) that function as a complex to transduce signals from G protein-coupled receptors to an effector protein. [ISBN:0198547684]

heterotrimeric G-protein complex location


inaD signalling complex
inaD signalling complex location
inaD signaling complex location

A complex of proteins that are involved in phototransduction and attached to the transient receptor potential (TRP) channel. The protein connections are mediated through inaD. [GOC:hb, PMID:9010208, PMID:9796815]


The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. [GOC:dos, GOC:go_curators]


ATP-sensitive potassium channel complex location

A protein complex that comprises four pore-forming (Kir6.x) and four regulatory sulphonylurea receptor (SURx) subunits and forms a transmembrane channel through which ions may pass. The opening and closing of the channel is regulated by ATP: binding of ATP to the Kir6.x subunit inhibits channel activity, whereas binding of Mg2+-complexed ATP or ADP to the SURx subunit stimulates channel activity. [GOC:bhm, PMID:16308567, PMID:16956886]


glycine-gated chloride channel complex location

A protein complex that forms a transmembrane channel through which chloride ions may pass in response to glycine binding to the channel complex or one of its constituent parts. [GOC:mah]


granulocyte macrophage colony stimulating factor receptor complex location

granulocyte macrophage colony-stimulating factor receptor complex location

The heterodimeric receptor for granulocyte macrophage colony-stimulating factor. [GOC:mah]


histamine-gated chloride channel complex location

A protein complex that forms a transmembrane channel through which chloride ions may pass in response to histamine binding to the channel complex or one of its constituent parts. [GOC:mah]


hydrogen/potassium-exchanging ATPase complex location

potassium:proton exchanging ATPase complex location

hydrogen:potassium-exchanging ATPase complex location

A protein complex that possesses hydrogen:potassium-exchanging ATPase activity; characterized in animal cells, where it maintains ionic gradients of K+ at the expense of ATP hydrolysis; The complex contains two obligatory subunits, the catalytic alpha subunit and a glycosylated beta subunit; two additional subunits, gamma and channel-inducing factor (CHIF), may also be present. [PMID:11756431]


A disulfide-bonded, heterotetrameric receptor complex. The alpha chains are entirely extracellular, while each beta chain has one transmembrane domain. The ligand binds to the alpha subunit extracellular domain and the kinase is associated with the beta subunit intracellular domain. [ISBN:0198506732]


A protein complex that is composed of one alpha subunit and one beta subunit, both of which are members of the integrin superfamily of cell adhesion receptors; the complex spans the plasma membrane and binds to extracellular matrix ligands, cell-surface ligands, and soluble ligands. [PMID:17543136]


IL-1 receptor complex
interleukin-1 receptor complex location
IL-1 receptor complex location

A protein complex that binds interleukin-1; comprises an alpha and a beta subunit. [GOC:mah, InterPro:IPR004075]


interleukin-12 receptor complex location

A protein complex that binds interleukin-12 and that consists of, at a minimum, a dimeric interleukin and its two receptor subunits as well as optional additional kinase subunits. [GOC:ebc, GOC:mah, PMID:10971505]


interleukin-13 receptor complex location

A protein complex that binds interleukin-13; consists of two chains, interleukin-13 receptor alpha1 chain and interleukin-4 receptor alpha chain. [PMID:8552669, PMID:9013879]


interleukin-18 receptor complex location

A protein complex that binds interleukin-18; comprises an alpha and a beta subunit. [GOC:mah, PMID:12759435]


IL-2 receptor complex
IL-2 receptor complex location
interleukin-2 receptor complex location

A protein complex that binds interleukin-2; comprises alpha, beta, and gamma subunits. [GOC:mah, PMID:3116143, PMID:8266078]


interleukin-3 receptor complex location
IL-3 receptor complex
IL-3 receptor complex location

A protein complex that binds interleukin-3; comprises an alpha and a beta subunit. The alpha chain is specific to the interleukin-3 receptor, whereas the beta chain is shared with the receptors for granulocyte-macrophage colony-stimulating factor and interleukin-5. [PMID:11839579]


IL-4 receptor complex
interleukin-4 receptor complex location
IL-4 receptor complex location

A protein complex that binds interleukin-4 (IL-4) and consists of an alpha chain that binds IL-4 with high affinity and a gamma common chain that also forms part of the interleukin-2 receptor. [PMID:10358772]


interleukin-5 receptor complex location
IL-5 receptor complex location
IL-5 receptor complex

A protein complex that binds interleukin-3; comprises an alpha and a beta subunit. The alpha chain is specific to the interleukin-5 receptor, whereas the beta chain is shared with the receptors for granulocyte-macrophage colony-stimulating factor and interleukin-3. [GOC:mah, PMID:11312115, PMID:11839579]


IL-6 receptor complex location
interleukin-6 receptor complex location
IL-6 receptor complex

A hexameric protein complex consisting of two molecules each of interleukin-6, interleukin-6 receptor alpha chain, and gp-130. [PMID:8083235]


IL-9 receptor complex
IL-9 receptor complex location
interleukin-9 receptor complex location

A protein complex that binds interleukin-9; comprises an alpha and a beta subunit. The alpha chain is specific to the interleukin-9 receptor, whereas the beta chain is shared with the receptors for several other interleukins. [GOC:mah, PMID:10642536]


ionotropic glutamate receptor complex location

A multimeric assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand-gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex. [http://www.bris.ac.uk/Depts/Synaptic/info/glutamate.html]


NMDA selective glutamate receptor complex location

N-methyl-D-aspartate selective glutamate receptor complex location

An assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex. NMDA receptors are composed of assemblies of NR1 subunits (Figure 3) and NR2 subunits, which can be one of four separate gene products (NR2A-D). Expression of both subunits are required to form functional channels. The glutamate binding domain is formed at the junction of NR1 and NR2 subunits. NMDA receptors are permeable to calcium ions as well as being permeable to other ions. Thus NMDA receptor activation leads to a calcium influx into the post-synaptic cells, a signal thought to be crucial for the induction of NMDA-receptor dependent LTP and LTD. [http://www.bris.ac.uk/Depts/Synaptic/info/glutamate.html]


acetylcholine-gated channel complex location

nicotinic acetylcholine-gated receptor-channel complex location

A homo- or hetero-pentameric protein complex that forms a transmembrane channel through which ions may pass in response to acetylcholine binding. [GOC:bf, GOC:mah, PMID:12381728, PMID:15579462]


A heterodimeric receptor for the cytokine oncostatin-M (OSM). In humans the receptor complex is made up of the gene products gp130 and OSMR-beta. [GOC:jl, PMID:8999038]


sodium:potassium-exchanging ATPase complex location

sodium/potassium-exchanging ATPase complex location

Sodium:potassium-exchanging ATPases are tetrameric proteins, consisting of two large alpha subunits and two smaller beta subunits. The alpha subunits bear the active site and penetrate the membrane, while the beta subunits carry oligosaccharide groups and face the cell exterior. [ISBN:0198506732]


voltage-sensitive calcium channel complex location

voltage-dependent calcium channel complex location

voltage-gated calcium channel complex location

voltage gated calcium channel complex location

A protein complex that forms a transmembrane channel through which calcium ions may pass in response to changes in membrane potential. [GOC:mah]


light-activated voltage-gated calcium channel complex location

light-activated voltage-sensitive calcium channel complex location

light-activated voltage-dependent calcium channel complex location

light-activated voltage gated calcium channel complex location

A protein complex that forms a transmembrane channel through which calcium ions may cross a cell membrane in response to changes in membrane potential generated in response to a light stimulus. [GOC:mah, PMID:9223679]


voltage-sensitive potassium channel complex location

voltage-gated potassium channel complex location

voltage gated potassium channel complex location

voltage-dependent potassium channel complex location

A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential. [GOC:mah]


voltage gated sodium channel complex location

voltage-gated sodium channel complex location

voltage-dependent sodium channel complex location

voltage-sensitive sodium channel complex location

A sodium channel in a cell membrane whose opening is governed by the membrane potential. [ISBN:0198506732]


internal leaflet of plasma membrane
internal side of plasma membrane

The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface. [GOC:dos, GOC:tb]


The portion of the plasma membrane at the lateral side of the cell. In epithelial cells, lateral plasma membranes are on the sides of cells which lie at the interface of adjacent cells. [GOC:hb, GOC:mah, GOC:pr]


Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. [PMID:16645198, PMID:20044567]


plasma membrane proton-transporting ATP synthase complex location, catalytic core F(1)

The catalytic sector of the plasma membrane hydrogen-transporting ATP synthase; it comprises the catalytic core and central stalk, and is peripherally associated with the plasma membrane when the entire ATP synthase is assembled. Examples of this component are found in Bacterial species. [GOC:mah, GOC:mtg_sensu, PMID:10838056]

plasma membrane proton-transporting ATP synthase complex, catalytic core F(1)


plasma membrane proton-transporting ATP synthase, catalytic core

The hexamer that possesses the catalytic activity of the plasma membrane hydrogen-transporting ATP synthase. Examples of this component are found in Bacterial species. [GOC:mtg_sensu, PMID:10838056]


plasma membrane proton-transporting ATP synthase, central stalk

One of two stalks that connect the catalytic core of the hydrogen-transporting ATP synthase to the plasma membrane-associated Fo proteins; rotates within the catalytic core during catalysis. Examples of this component are found in Bacterial species. [GOC:mtg_sensu, PMID:10838056]


plasma membrane proton-transporting ATP synthase complex, coupling factor F(o)

hydrogen-transporting ATP synthase, coupling factor CF(0)

hydrogen-transporting ATP synthase, F0 sector

hydrogen-transporting ATP synthase complex, coupling factor F(o)

proton-transporting ATP synthase complex location, coupling factor F(0)

plasma membrane proton-transporting ATP synthase complex location, coupling factor F(o)

hydrogen-transporting ATP synthase complex location, coupling factor F(o)

All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins. [PMID:10838056]

proton-transporting ATP synthase complex, coupling factor F(0)


A subcomplex of the respiratory chain located in the plasma membrane. It contains about 25 different polypeptide subunits, including NADH dehydrogenase (ubiquinone), flavin mononucleotide and several different iron-sulfur clusters containing non-heme iron. The iron undergoes oxidation-reduction between Fe(II) and Fe(III), and catalyzes proton translocation linked to the oxidation of NADH by ubiquinone. Examples of this component are found in bacterial species. [GOC:mtg_sensu, ISBN:0198547684]

plasma membrane respiratory chain complex I location


plasma membrane respiratory chain complex II location

A part of the respiratory chain located in the plasma membrane, containing the four polypeptide subunits of succinate dehydrogenase, flavin-adenine dinucleotide and iron-sulfur. Catalyzes the oxidation of succinate by ubiquinone. Connects the TCA cycle with the respiratory chain. Examples of this component are found in bacterial species. [GOC:mtg_sensu, ISBN:0198547684]


plasma membrane fumarate reductase complex location

A membrane-bound flavoenzyme complex consisting of four subunits, A, B, C, and D. A and B comprise the membrane-extrinsic catalytic domain and C (InterPro:IPR003510; InterPro:IPR00224) and D (InterPro:IPR003418) link the catalytic centers to the electron-transport chain. In some species, the complex has only three subunits, and in these cases, there is only one membrane anchor instead of two. This family consists of the 13 kDa hydrophobic subunit D. This component may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalyzed by the related complex II of the respiratory chain (succinate dehydrogenase-(ubiquinone)). Examples of this component are found in bacterial species. [GOC:mtg_sensu, InterPro:IPR003418, InterPro:IPR004224]


A multimeric complex which consists of flavoprotein (subunit A ; InterPro:IPR003952), iron-sulfur protein (subunit B) and membrane-bound cytochrome b560 (subunit C; InterPro:IPR000701). In some Archaea, the membrane-bound subunits (C or C and D) do not necessarily contain heme. Membrane-bound subunits can bind/react with quinones. Examples of this component are found in Bacterial species. [GOC:kd, GOC:mtg_sensu, InterPro:IPR000701]

plasma membrane succinate dehydrogenase complex location


plasma membrane coenzyme Q-cytochrome c oxidoreductase complex location

plasma membrane ubiquinol-cytochrome-c reductase complex location

plasma membrane coenzyme Q-cytochrome c reductase complex location

plasma membrane respiratory chain complex III location

plasma membrane cytochrome bc1 complex location

A part of the respiratory chain located in the plasma membrane, containing about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1. Examples of this component are found in bacterial species. [GOC:mtg_sensu, ISBN:0198547684]


plasma membrane respiratory chain complex IV location

A part of the respiratory chain located in the plasma membrane, containing the 13 polypeptide subunits of cytochrome c oxidase, including cytochrome a and cytochrome a3. Catalyzes the oxidation of reduced cytochrome c by dioxygen (O2). Examples of this component are found in bacterial species. [GOC:mtg_sensu, ISBN:0198547684]


The specialized microvilli-containing organelle on the apical surfaces of a photoreceptor cell containing the visual pigment rhodopsin and most of the proteins involved in phototransduction. [GOC:hb, GOC:sart, PMID:8646774]


A membrane-bounded compartment that is found at the base of the rhabdomere and contains stored calcium, InsP3 receptors and smooth endoplasmic reticulum Ca2+-ATPase. [PMID:11707492, PMID:8646774]


Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. [ISBN:0124325653]


plasma membrane succinate dehydrogenase complex location (ubiquinone)

plasma membrane succinate dehydrogenase complex (ubiquinone)

The enzyme, located in the plasma membrane, that catalyzes the oxidation of succinate and ubiquinone to fumarate and ubiquinol; involved in aerobic respiration, repressed in anaerobic respiration. [GOC:kd, GOC:mtg_sensu, ISBN:0198547684]


A thylakoid that is derived from and attached to, but not necessarily continuous with, the plasma membrane, and is not enclosed in a plastid. It bears the photosynthetic pigments in photosynthetic cyanobacteria. [GOC:mah, GOC:mtg_sensu]


light-harvesting complex, core complex location

Light harvesting complex associated with the reaction complex of photosynthetic purple bacteria. [GOC:lr]


LH1 complex location
B875 antenna complex location
LH1 complex
light harvesting complex I location
light harvesting complex I

Protein complex that surrounds and transfers excitation energy directly to the bacterial reaction center; binds bacteriochlorophyll a and has a single absorption band between 870 and 890 nm. [GOC:kd]


light-harvesting complex, peripheral complex location

Bacteriochlorophyll a binding complex that is peripherally associated to the bacterial reaction center. [GOC:lr]


LH3 complex
B800-820 antenna complex location
LH3 complex location
light harvesting complex III
light harvesting complex III location

Protein-pigment complex that absorbs light at 800 and 820 nm; is peripherally associated to the bacterial reaction center; transfers excitation energy to the B875 antenna complex. [GOC:kd, GOC:lr]


light harvesting complex II location
B800-850 antenna complex location
light harvesting complex II
LH2 complex
LH2 complex location

Protein-pigment complex that absorbs light at 800 and 850 nm; is peripherally associated to the bacterial reaction center; transfers excitation energy to the B875 antenna complex. [GOC:kd, GOC:lr]


type I protein secretion system complex location

A complex of three secretory proteins that carry out secretion in the type I secretion system: an inner membrane transport ATPase (termed ABC protein for ATP-binding cassette), which provides the energy for protein secretion; an outer membrane protein, which is exported via the sec pathway; and a membrane fusion protein, which is anchored in the inner membrane and spans the periplasmic space. [PMID:9618447]


type III protein secretion system complex location

A complex of approximately 20 proteins, most of which are located in the cytoplasmic membrane that carries out protein secretion in the bacterial type III secretion system; type III secretion also requires a cytoplasmic, probably membrane-associated ATPase. [PMID:9618447]


plasma membrane proton-transporting ATP synthase complex location

plasma membrane hydrogen-translocating F-type ATPase complex location

hydrogen-transporting ATP synthase complex location

A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient. [ISBN:0198547684, ISBN:0716743663]


proton-transporting ATP synthase, catalytic core

hydrogen-transporting ATP synthase, catalytic core

The hexamer that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase. [PMID:10838056]


proton-transporting ATP synthase, central stalk

hydrogen-transporting ATP synthase, central stalk

One of two stalks that connect the catalytic core of the hydrogen-transporting ATP synthase to the membrane-associated Fo proteins; rotates within the catalytic core during catalysis. [PMID:10838056]


hydrogen-transporting ATP synthase, stator stalk

proton-transporting ATP synthase location, stator stalk

hydrogen-transporting ATP synthase location, stator stalk

proton-transporting ATP synthase, stator stalk

One of two stalks that connect the catalytic core of the hydrogen-transporting ATP synthase to the membrane-associated Fo proteins; is thought to prevent futile rotation of the catalytic core. [PMID:10838056]


pyruvate dehydrogenase (lipoamide) phosphatase complex location

A complex of a regulatory and catalytic subunit that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. [PMID:9395502]


pyruvate dehydrogenase complex location (lipoamide)

pyruvate dehydrogenase complex (lipoamide)

Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA; comprises subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). [ISBN:0716720094]


NADH dehydrogenase (ubiquinone) complex location

NADH dehydrogenase complex location (ubiquinone)

Respiratory chain complex I is an enzyme of the respiratory chain. It consists of several polypeptide chains and is L-shaped, with a horizontal arm lying in the membrane and a vertical arm that projects into the matrix. The electrons of NADH enter the chain at this complex. [GOC:imk, GOC:jid, ISBN:0716749556]


electron transport complex II location
respiratory chain complex II
electron transport complex II

A part of the respiratory chain, containing the four polypeptide subunits of succinate dehydrogenase, flavin-adenine dinucleotide and iron-sulfur. Catalyzes the oxidation of succinate by ubiquinone. Connects the TCA cycle with the respiratory chain. [ISBN:0198547684]


A membrane-bound flavoenzyme complex consisting of four subunits, A, B, C, and D. A and B comprise the membrane-extrinsic catalytic domain and C (InterPro:IPR003510; InterPro:IPR004224) and D (InterPro:IPR003418) link the catalytic centers to the electron-transport chain. This family consists of the 13 kDa hydrophobic subunit D. This component may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalyzed by the related complex II of the respiratory chain (succinate dehydrogenase-(ubiquinone)). [InterPro:IPR003418, InterPro:IPR004224]


succinate dehydrogenase complex location

A multimeric complex which consists of flavoprotein (subunit A ; InterPro:IPR003952), iron-sulfur protein (subunit B) and membrane-bound cytochrome b560 (subunit C; InterPro:IPR000701). In some Archaea, the membrane-bound subunits (C or C and D) do not necessarily contain heme. Membrane-bound subunits can bind or react with quinones. [GOC:kd, InterPro:IPR000701]


ubiquinol-cytochrome-c reductase complex location

ubiquinol-cytochrome c oxidoreductase complex location

A protein complex that transfers electrons from ubiquinol to cytochrome c and translocates two protons across a membrane. The complex contains a core structure of three catalytic subunits: cytochrome b, the Rieske iron sulfur protein (ISP), and cytochrome c1, which are arranged in an integral membrane-bound dimeric complex; additional subunits are present, and vary among different species. [PMID:16228398, PMID:16352458, PMID:17200733]


electron transport complex IV
respiratory chain complex IV
electron transport complex IV location
cytochrome c oxidase complex
respiratory chain complex IV location

A part of the respiratory chain, containing the 13 polypeptide subunits of cytochrome c oxidase, including cytochrome a and cytochrome a3. Catalyzes the oxidation of reduced cytochrome c by dioxygen (O2). [ISBN:0198547684]


RNP
RNA-protein complex location
protein-RNA complex location
protein-RNA complex
RNA-protein complex
ribonucleoprotein complex

A macromolecular complex that contains both RNA and protein molecules. [GOC:krc, GOC:vesicles]


succinate dehydrogenase complex location (ubiquinone)

succinate dehydrogenase complex (ubiquinone)

The enzyme that catalyzes the oxidation of succinate and ubiquinone to fumarate and ubiquinol; involved in aerobic respiration, repressed in anaerobic respiration. [GOC:kd, ISBN:0198547684]


tricarboxylic acid cycle enzyme complex location

Any of the heteromeric enzymes that act in the TCA cycle. [GOC:mah]


isocitrate dehydrogenase complex location (NAD+)

Complex that possesses isocitrate dehydrogenase (NAD+) activity. [GOC:mah]


succinate-CoA ligase complex location (GDP-forming)

succinate-CoA ligase complex (GDP-forming)

A heterodimeric enzyme complex, usually composed of an alpha and beta chain. Functions in the TCA cycle, hydrolyzing succinyl-CoA into succinate and CoA, thereby forming GTP. [GOC:jl, PMID:27487822]


plasma membrane light-harvesting complex location

A plasma membrane protein-pigment complex that may be closely or peripherally associated to photosynthetic reaction centers that participate in harvesting and transferring radiant energy to the reaction center. Examples of this complex are found in bacterial species. [GOC:mah, GOC:mtg_sensu]


cytochrome b6-f complex
cyt b(6)f complex location
cyt b6f complex
cytochrome b(6)f complex
cytochrome b6f complex location
cyt b6-f complex
cytochrome b6-f complex location
cyt b6f complex location
cyt b(6)f complex
cytochrome b(6)f complex location
cyt b6/f complex
cyt b6/f complex location
cytochrome b6f complex
cytochrome b6/f complex location
cytochrome b6/f complex

Complex that transfers electrons from reduced plastoquinone to oxidized plastocyanin and translocates protons from the stroma to the lumen. The complex contains a core structure of three catalytic subunits: cytochrome b, the Rieske iron sulfur protein (ISP), and cytochrome f, which are arranged in an integral membrane-bound dimeric complex; additional subunits are present, and vary among different species. [ISBN:0943088399, PMID:16228398, PMID:16352458]


The antenna complex of photosystem I. A photosystem has two closely linked components, an antenna containing light-absorbing pigments and a reaction center. Each antenna contains one or more light-harvesting complexes (LHCs). [GOC:jid, ISBN:0716731363]


A photochemical system containing P700, the chlorophyll a dimer that functions as a primary electron donor. Functioning as a light-dependent plastocyanin-ferredoxin oxidoreductase, it transfers electrons from plastocyanin to ferredoxin. [GOC:kd, ISBN:0943088399]


photosystem II oxygen evolving complex location

A complex, composed of a cluster of manganese, calcium and chloride ions bound to extrinsic proteins, that catalyzes the splitting of water to O2 and 4 H+. In cyanobacteria there are five extrinsic proteins in OEC (PsbO, PsbP-like, PsbQ-like, PsbU and PsbV), while in plants there are only three (PsbO, PsbP and PsbQ). [GOC:cjm, InterPro:IPR002683]


The antenna complex of photosystem II. A photosystem has two closely linked components, an antenna containing light-absorbing pigments and a reaction center. Each antenna contains one or more light-harvesting complexes (LHCs). [GOC:jid, ISBN:0716731363]


An integral membrane complex containing P680, the chlorophyll a molecule that functions as a primary electron donor. In the light, functioning as a water-plastoquinone oxidoreductase, it transfers electrons from water to plastoquinone. [GOC:kd, ISBN:0943088399]


A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex. [GOC:jh2, PMID:9529603]


A vesicle used to transport the partial or complete virion between cellular compartments. [GOC:vesicles, PMID:7933124]


A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles. [GOC:lh]


nuclear envelope-endoplasmic reticulum continuum

nuclear envelope-endoplasmic reticulum network


The lipid bilayer surrounding any membrane-bounded vesicle in the cell. [GOC:mah, GOC:vesicle]


extrinsic to membrane
peripheral membrane protein

The component of a membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. [GOC:dos, GOC:jl, GOC:mah]


integral component of membrane
integral to membrane

The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. [GOC:dos, GOC:go_curators]


hydrogen-transporting two-sector ATPase complex location

proton-transporting two-sector ATPase complex location

A large protein complex that catalyzes the synthesis or hydrolysis of ATP by a rotational mechanism, coupled to the transport of protons across a membrane. The complex comprises a membrane sector (F0, V0, or A0) that carries out proton transport and a cytoplasmic compartment sector (F1, V1, or A1) that catalyzes ATP synthesis or hydrolysis. Two major types have been characterized: V-type ATPases couple ATP hydrolysis to the transport of protons across a concentration gradient, whereas F-type ATPases, also known as ATP synthases, normally run in the reverse direction to utilize energy from a proton concentration or electrochemical gradient to synthesize ATP. A third type, A-type ATPases have been found in archaea, and are closely related to eukaryotic V-type ATPases but are reversible. [GOC:mah, ISBN:0716743663, PMID:16691483]


intracellular cyclic nucleotide activated cation channel complex location

A protein complex that forms a transmembrane channel through which cations ions may pass in response to an intracellular cyclic nucleotide binding to the channel complex or one of its constituent parts. [GOC:mah]


lipopolysaccharide receptor complex location

A multiprotein complex that consists of at least three proteins, CD14, TLR4, and MD-2, each of which is glycosylated and which functions as a lipopolysaccharide (LPS) receptor that primes the innate immune response against bacterial pathogens. [PMID:11706042, PMID:9665271]


PABA peptide hydrolase complex location
meprin A complex location
PABA peptide hydrolase complex

A protein complex that is located in the cell membrane, and is involved in the metabolism of peptides, including neuropeptides. The complex has metalloendopeptidase activity that catalyzes the hydrolysis of protein and peptide substrates, preferentially on carboxyl side of hydrophobic residues. [GOC:mah, MEROPS_fam:M12]


sodium-transporting two-sector ATPase complex location

sodium ion-transporting two-sector ATPase complex location

A large protein complex that catalyzes the synthesis or hydrolysis of ATP by a rotational mechanism, coupled to the transport of sodium ions across a membrane. The complex comprises a membrane sector (F0 or V0) that carries out ion transport and a cytoplasmic compartment sector (F1 or V1) that catalyzes ATP synthesis or hydrolysis. [GOC:mah, PMID:14656431]


sodium ion-transporting F-type ATPase complex location

sodium-translocating F-type ATPase complex location

A sodium ion-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism. [GOC:mah, PMID:14656431]


sodium-translocating V-type ATPase complex location

sodium ion-transporting V-type ATPase complex location

A sodium ion-transporting two-sector ATPase complex that couples ATP hydrolysis to the transport of sodium ions across a concentration gradient. The complex comprises a membrane sector (V0) that carries out proton transport and a cytoplasmic compartment sector (V1) that catalyzes ATP hydrolysis. [GOC:mah, PMID:15802565]


The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites. [GOC:go_curators]


A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis. [ISBN:0815316194]


shmoo tip
mating projection
conjugation tube

The projection formed by unicellular fungi in response to mating pheromone. [GOC:mcc]


Any part of a cell where non-isotropic growth takes place. [GOC:mah]


outer membrane-enclosed periplasmic space

outer membrane bounded periplasmic space

The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. [GOC:mlg, GOC:mtg_sensu]

outer membrane-bounded periplasmic space


A protective structure outside the cytoplasmic membrane composed of peptidoglycan (also known as murein), a molecule made up of a glycan (sugar) backbone of repetitively alternating N-acetylglucosamine and N-acetylmuramic acid with short, attached, cross-linked peptide chains containing unusual amino acids. An example of this component is found in Escherichia coli. [GOC:mlg, ISBN:0815108893]


20-80nm peptidoglycan-based cell wall
Gram-positive-bacterium-type cell wall

A layer of peptidoglycan found outside of the cytoplasmic membrane. The peptidoglycan is relatively thick (20-80nm) and retains the primary stain of the Gram procedure, thus cells appear blue after Gram stain. The cell walls often contain teichoic acids (acidic anionic polysaccharides) bound to the peptidoglycan. Examples of this component are found in Gram-positive bacteria. [GOC:mlg, ISBN:0815108893]


A rigid yet dynamic structure surrounding the plasma membrane that affords protection from stresses and contributes to cell morphogenesis, consisting of extensively cross-linked glycoproteins and carbohydrates. The glycoproteins may be modified with N- or O-linked carbohydrates, or glycosylphosphatidylinositol (GPI) anchors; the polysaccharides are primarily branched glucans, including beta-linked and alpha-linked glucans, and may also include chitin and other carbohydrate polymers, but not cellulose or pectin. Enzymes involved in cell wall biosynthesis are also found in the cell wall. Note that some forms of fungi develop a capsule outside of the cell wall under certain circumstances; this is considered a separate structure. [GOC:mcc, GOC:mtg_sensu, ISBN:3540601864, PMID:11283274, PMID:16927300, PMID:3319422]


The cell wall surrounding a fungal hypha. [GOC:mah]


The wall surrounding a cell of a dimorphic fungus growing in the single-cell budding yeast form, in contrast to the filamentous or hyphal form. [GOC:mah, GOC:mcc]


cellulose and pectin-containing cell wall

A more or less rigid stucture lying outside the cell membrane of a cell and composed of cellulose and pectin and other organic and inorganic substances. [ISBN:0471245208]


A plant cell wall that is still able to expand, permitting cell growth. Primary cell walls contain more pectin than secondary walls and no lignin is present. [GOC:jid, PMID:9442872]


A microfibril composed of cellulose arranged in orthogonal layers. Cellulose is a straight chain polysaccharide composed of B(14) linked glucose subunits. It is a major component of plant cell walls. Higher plant microfibrils are about 10nm in diameter and extremely long in relation to their width. The cellulose molecules are oriented parallel to the long axis of the microfibril in a paracrystalline array, which provides great tensile strength. The microfibrils are held in place by the wall matrix and their orientation is closely controlled by the cell. [GOC:jid, ISBN:0943088399]


A plant cell wall that is no longer able to expand and so does not permit growth. Secondary cell walls contain less pectin that primary cell walls. The secondary cell is mostly composed of cellulose and is strengthened with lignin. [GOC:jid, ISBN:0943088399]


A crystalline protein layer surrounding some bacteria. [GOC:mlg, ISBN:0815108893]


A slime layer is an easily removed, diffuse, unorganized layer of extracellular material that surrounds a cell. Specifically this consists mostly of exopolysaccharides, glycoproteins, and glycolipids. [GOC:mlg, Wikipedia:Slime_layer]


laminin-121 complex
laminin-3 complex location
laminin-121 complex location

A laminin complex composed of alpha1, beta2 and gamma1 polypeptide chains. [MEDLINE:95005761]


laminin-4 complex location
laminin-221 complex location
laminin-221 complex

A laminin complex composed of alpha2, beta2 and gamma1 polypeptide chains. [GOC:jl, PMID:10842354]


A collagen heterotrimer containing type IV alpha chains; [alpha1(IV)]2alpha2(IV) trimers are commonly observed, although more type IV alpha chains exist and may be present in type IV trimers; type IV collagen triple helices associate to form 3 dimensional nets within basement membranes. [ISBN:0721639976, PMID:19693541, PMID:21421911]


A protein complex consisting of three collagen chains assembled into a left-handed triple helix. These trimers typically assemble into higher order structures. [GOC:dos, GOC:mah, ISBN:0721639976, PMID:19693541, PMID:21421911]


A collagen heterotrimer containing type VI alpha chains in alpha1(VI)alpha2(VI)alpha3(VI) trimers; type VI collagen triple helices associate to form beaded fibrils. [ISBN:0721639976, PMID:19693541, PMID:21421911]


A collagen homotrimer of alpha1(VII) chains; type VII collagen triple helices form antiparallel dimer, which in turn associate laterally to form anchoring fibrils that connect type IV collagen in the basal lamina to plaques in the underlying connective tissue. It binds laminin. [ISBN:0721639976, PMID:19693541]


A collagen homotrimer of alpha1(XIII) chains; type XIII collagen triple helices span the plasma membrane. [GOC:bhm, GOC:dos, ISBN:0721639976]


A collagen homotrimer of alpha1(XV) chains; a chondroitin sulfate proteoglycan often found in specialized basement membranes where it bridges between fibrils. [PMID:11158616, PMID:11937714, PMID:21421911]


A collagen trimer that associates with collagen fibrils and consists of collagen monomers that contain two or more relatively short triple-helical domains connected by non-triple-helical sequences. [ISBN:0198599587, PMID:21421911]


A collagen heterotrimer containing type IX alpha chains in alpha1(IX)alpha2(IX)alpha3(IX) trimers; type IX collagen triple helices associate to form a structure that links glycosaminoglycans to type II collagen fibrils. [ISBN:0721639976]


A collagen homotrimer of alpha1(XII) chains; type XII collagen triple helices may link sheet-forming or fibrillar collagens to other structures. [ISBN:0721639976]


A collagen homotrimer of alpha1(XIV) chains; type XIV collagen triple helices may link sheet-forming or fibrillar collagens to other structures. [ISBN:0721639976]


A collagen trimer containing alpha(XVI) chains; type XVI trimers can associate with microfibrils. [GOC:mah, PMID:12782140]


Any triple helical collagen trimer that forms fibrils. [GOC:mah, ISBN:0721639976, PMID:21421911]


A collagen trimer containing alpha(I) chains. The most common form of type I collagen is a heterotrimer containing two alpha1(I) chains and one alpha2(I) chain; homotrimers containing three alpha1(I) chains are also found. Type I collagen triple helices associate to form banded fibrils. [GOC:mah, GOC:sl, ISBN:0721639976]


A collagen homotrimer of alpha1(II) chains; type II collagen triple helices associate to form fibrils. [ISBN:0721639976]


A collagen homotrimer of alpha1(III) chains; type III collagen triple helices associate to form fibrils. [ISBN:0721639976]


A collagen heterotrimer containing type V alpha chains; [alpha1(V)]2alpha2(V) and alpha1(V)alpha2(V)alpha3(V) trimers have been observed; type V collagen triple helices associate to form fibrils. [ISBN:0721639976]


A collagen heterotrimer containing type XI alpha chains in alpha1(XI)alpha2(XI)alpha3(XI) trimers; type XI collagen triple helices associate to form fibrils. [ISBN:0721639976]


Any collagen trimer that does not form fibrils and that is relatively short compared to the collagen trimers that do form fibrils. [ISBN:0198599587]


A collagen heterotrimer containing type VIII alpha chains; [alpha1(VIII)2]alpha2(VIII) and alpha1(VIII)[alpha2(VIII)]2 trimers have been observed; type VIII collagen triple helices associate to form regular hexagonal nets. [ISBN:0721639976, PMID:21421911]


A collagen homotrimer of alpha1(X) chains; type X collagen triple helices form hexagonal networks (sheets). [ISBN:0721639976, PMID:21421911]


terminal complement complex
TCC
MAC
terminal complement complex location
membrane attack complex location

A protein complex produced by sequentially activated components of the complement cascade inserted into a target cell membrane and forming a pore leading to cell lysis via ion and water flow. [GOC:add, ISBN:0198547684, ISBN:068340007X, ISBN:0781735149]


A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane. [ISBN:0198506732]


classical-complement-pathway C3/C5 convertase complex location

A heterodimeric protein complex that catalyzes the cleavage of complement components C3 and C5, and acts in the classical pathway of complement activation; consists of one monomer of C2a and one monomer of C4b; C2a is the catalytic subunit, but cannot catalyze cleavage alone. [BRENDA:3.4.21.43, GOC:mah, http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/C/Complement.html]


complement component C1q complex location

A protein-containing complex composed of six subunits of each of the three homologous polypeptide chains C1QA, C1QB, and C1QB. It is a subunit of the complement C1 complex. In addition to complement activation, C1q appears to have roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning. [PMID:29449492]


insulin-like growth factor binding protein complex location

A complex of proteins which includes the insulin-like growth factor (IGF) and a number of IGF-binding proteins. The complex plays a role in growth and development. [GOC:jl]


insulin-like growth factor binary complex location

A complex of two proteins, which in animals is 50kDa and consists of the insulin-like growth factor (IGF) and one of the insulin-like growth factor binding protein-1 (IGFBP-1), -2 (IGFBP-2), -4 (IGFBP-4) and -6 (IGFBP-6). The complex plays a role in growth and development. [GOC:jl, PMID:12239079]


insulin-like growth factor ternary complex location

A complex of three proteins, which in animals is approximately 150kDa and consists of the insulin-like growth factor (IGF), the insulin-like growth factor binding protein-3 (IGFBP-3), or -5 (IGFBP-5) and an acid-labile subunit (ALS). The complex plays a role in growth and development. [GOC:jl, PMID:12239079]


A multisubunit protein complex which, in Drosophila, is a heterohexamer of three subunits, alpha, beta and gamma. The complex is thought to store amino acids for synthesis of adult proteins. [GOC:jl, PMID:6781759]


Layer of intercellular material, chiefly pectic substances, cementing together the primary walls of contiguous cells. [ISBN:0471245208]


fibrinogen complex location
fibrinogen complex

A highly soluble, elongated protein complex found in blood plasma and involved in clot formation. It is converted into fibrin monomer by the action of thrombin. In the mouse, fibrinogen is a hexamer, 46 nm long and 9 nm maximal diameter, containing two sets of nonidentical chains (alpha, beta, and gamma) linked together by disulfide bonds. [ISBN:0198547684]


An organism that nourishes and supports another but does not benefit by the association; recipient of transplanted tissue or organ from a donor.


A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction. [GOC:pamgo_curators]


The plasma membrane surrounding a host cell. [GOC:mb]


The lipid bilayer of a virion that surrounds the protein capsid. May also contain glycoproteins. [GOC:bf, GOC:bm, GOC:jl, ISBN:0781718325, Wikipedia:Viral_envelope]


Protrusion that develops in the plasma membrane of a parasitized erythrocyte. An example of this component is found in Plasmodium species. [GOC:mb]


A disk-like structure that appears at the periphery of a red blood cell infected by an apicomplexan parasite, characterized by a translucent lumen and an electron-dense coat of variable thickness; often appears to be tethered to the host cell membrane by fibrous connections with the erythrocyte cytoskeleton. [PMID:16705161]


A direct connection between the cytoplasm of two cells that is formed following the completion of cleavage furrow ingression during cell division. They are usually present only briefly prior to completion of cytokinesis. However, in some cases, such as the bridges between germ cells during their development, they become stabilised. [PMID:9635420]


A type of extracellular matrix found in interstitial connective tissue, characterized by the presence of fibronectins, proteoglycans, and types I, III, V, VI, VII and XII collagens. [PMID:8450001]


Specific locations and structures in the virus infected cell involved in assembling new virions. [ISBN:0781718325]


pre-integration complex
pre-integration complex location
viral integration complex
PIC

A nucleoprotein complex containing viral genetic material and the viral integrase, required for genome integration into the host's genome. May contain other proteins. [PMID:21037296, PMID:2721960, PMID:29900498]


Specific locations and structures in the virus infected cell involved in transcribing the viral genome. [ISBN:0781718325]


A protein complex that in its canonical form is composed of two identical immunoglobulin heavy chains and two identical immunoglobulin light chains, held together by disulfide bonds and sometimes complexed with additional proteins. An immunoglobulin complex may be embedded in the plasma membrane or present in the extracellular space, in mucosal areas or other tissues, or circulating in the blood or lymph. [GOC:add, GOC:jl, ISBN:0781765196]


1-phosphatidylinositol-4-phosphate kinase, class IA complex location

1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex location

phosphatidylinositol 3-kinase complex location, class IA

phosphoinositide 3-kinase complex, class IA

phosphoinositide 3-kinase complex location, class IA

phosphatidylinositol 3-kinase complex, class IA

A class I phosphatidylinositol 3-kinase complex that possesses 1-phosphatidylinositol-4-phosphate 3-kinase activity; comprises a catalytic class IA phosphoinositide 3-kinase (PI3K) subunit and an associated SH2 domain-containing regulatory subunit that is a member of a family of related proteins often called p85 proteins. Through the interaction with the SH2-containing adaptor subunits, Class IA PI3K catalytic subunits are linked to tyrosine kinase signaling pathways. [PMID:9255069, PMID:9759495]


1-phosphatidylinositol-4-phosphate kinase, class IB complex location


platelet-activating factor acetylhydrolase complex location

1-alkyl-2-acetylglycerophosphocholine esterase complex location

2-acetyl-1-alkylglycerophosphocholine esterase complex location

An enzyme complex composed of two catalytic alpha subunits, which form a catalytic dimer, and a non-catalytic, regulatory beta subunit; the catalytic dimer may be an alpha1/alpha1 or alpha2/alpha2 homodimer, or an alpha1/alpha2 heterodimer. Modulates the action of platelet-activating factor (PAF). [GOC:jl, PMID:10542206]


isopropylmalate isomerase complex location

3-isopropylmalate dehydratase complex location

A heterodimeric enzyme complex composed of subunits leuC and leuD. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. [BRENDA:4.2.1.33, GOC:jl, MetaCyc:3-ISOPROPYLMALISOM-CPLX, PMID:7026530]


3-phenylpropionate dioxygenase complex location

Enzyme complex consisting of four proteins: the two subunits of the hydroxylase component (hcaE and hcaF), a ferredoxin (hcaC) and a ferredoxin reductase (hcaD). Converts 3-phenylpropionic acid (PP) into cis-3-(3-carboxyethyl)-3,5-cyclohexadiene-1,2-diol (PP-dihydrodiol). [GOC:jl, MetaCyc:HCAMULTI-CPLX, PMID:9603882]


acetate CoA-transferase complex location

A heterotetrameric enzyme complex made up of two alpha subunits and two beta subunits. Part of the acetyl-CoA carboxylase complex. Catalyzes the transfer of a carboxyl group to form malonyl-CoA. [GOC:jl, PMID:2719476, PMID:8423010]


acetohydroxyacid synthase complex location

A dimeric (a large and a small chain) or tetrameric (two large and two small chains) enzyme complex. Catalyzes the formation of acetolactate from pyruvate. [BRENDA:2.2.1.6, GOC:jl, PMID:16458324, PMID:8756689]


ACCase complex location
ACCase complex
acetyl-CoA carboxylase complex location

A protein complex that catalyzes the first step in long-chain fatty acid biosynthesis. For example, in E. coli the complex is heterohexameric and composed of biotin carbonyl carrier protein, biotin carboxylase and the acetate CoA-transferase complex. [GOC:jl, GOC:mah, PMID:12121720]


alkyl hydroperoxide reductase complex location

An enzyme complex, usually a homodimer, which directly reduces cellular levels of organic hydroperoxides. [GOC:jl, PMID:2649484]


trehalose-6-phosphate synthase complex location

UDP-glucose-glucosephosphate glucosyltransferase complex location

alpha,alpha-trehalose-phosphate synthase complex location (UDP-forming)

alpha,alpha-trehalose-phosphate synthase complex (UDP-forming)

A protein complex that possesses alpha,alpha-trehalose-phosphate synthase (UDP-forming) and trehalose-phosphatase activities, and thus catalyzes two reactions in trehalose biosynthesis. In the complex identified in Saccharomyces, Tps1p has alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity, Tps2p has trehalose 6-phosphate phosphatase activity; Tps3p is a regulatory subunit, and an additional subunit, Tsl1p, may be present. [PMID:9837904]


aminoacyl-tRNA synthetase multienzyme complex location

aminoacyl-tRNA synthetase complex location

A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates. [GOC:jl, PMID:16169847]


A heterotetrameric enzyme complex made up of two components I and two components II. Catalyzes the formation of anthranilate, pyruvate and L-glutamate from chorismate and L-glutamine. [EC:4.1.3.27, MetaCyc:ANTHRANSYN-CPLX, PMID:4886290]


aspartate carbamoyltransferase complex location

A multienzyme complex that catalyzes the formation N-carbamoyl-L-aspartate from carbamoyl phosphate and L-aspartate. It exhibits a variety of architectural organizations, but in all microorganisms the core catalytic component is a homotrimer of approximately 34 kDa polypeptides. [PMID:10447693]


A protein complex that possesses beta-galactosidase activity, i.e. catalyzes the hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. In E. coli, the complex is a homotetramer; dimeric and hexameric beta-galactosidase complexes have been observed in other species. [PMID:15950161]


An enzyme complex that catalyzes the formation of carboxybiotin-carboxyl-carrier protein from biotin-carboxyl-carrier protein and carbon dioxide (CO2). [EC:6.3.4.14]


CAAX-protein geranylgeranyltransferase complex location

A heterodimeric enzyme, composed of an alpha and a beta subunit. Participates in the post-translational C-terminal modification of several small GTPases, allowing their targeting to the membrane. [PMID:9781874]


calcium/calmodulin-dependent protein kinase complex location

calcium- and calmodulin-dependent protein kinase complex location

An enzyme complex which in eukaryotes is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Catalyzes the phosphorylation of proteins to O-phosphoproteins. [EC:2.7.11.17]


3',5' cAMP-dependent protein kinase complex location

cyclic AMP-dependent protein kinase complex location

adenosine 3',5'-cyclophosphate-dependent protein kinase complex location

An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer. [EC:2.7.11.11, ISBN:0198506732]

3',5'-cAMP-dependent protein kinase complex location


carbamoyl phosphate synthase complex location

carbamoyl-phosphate synthase complex location

A protein complex that catalyzes the formation of carbamoyl phosphate; comprises a small subunit that binds and cleaves glutamine, and a large subunit that accepts the ammonia group cleaved from glutamine, binds all of the remaining substrates and effectors, and carries out all of the other catalytic events. [PMID:8626695]


cysteine-type endopeptidase complex location

A protein complex that contains one or more cysteine-type endopeptidases (also called caspases), which give the complex a peptidase activity with specificity for the hydrolysis of aspartyl bonds. These complexes may be involved e.g. in apoptotic or inflammation processes. [GOC:cna, GOC:mtg_apoptosis, PMID:15569692]


Cysteine synthase is a multienzyme complex made up, in E. coli, of the heteromeric hexamer serine acetyltransferase and the homodimer O-acetylserine (thiol)-lyase A. [EC:4.2.99.8, MetaCyc:CYSSYNMULTI-CPLX]


cytochrome o ubiquinol oxidase complex location

A protein complex that possesses cytochrome o ubiquinol oxidase activity; consists of four polypeptide subunits and associated prosthetic groups. [GOC:mah, MetaCyc:CYT-O-UBIOX-CPLX, PMID:11017202, PMID:3052268]


D-amino-acid dehydrogenase complex location

A protein complex that possesses D-amino-acid dehydrogenase activity. [GOC:mah]


alpha-ketoglutarate dehydrogenase complex location

2-oxoglutarate dehydrogenase complex location

A protein complex that possesses alpha-ketoglutarate dehydrogenase activity. [GOC:mah]

dihydrolipoyl dehydrogenase complex location


dimethyl sulphoxide reductase complex location

dimethyl sulfoxide reductase complex location

An enzyme complex that catalyzes the formation of dimethyl sulfide from dimethyl sulfoxide. [UM-BBD_enzymeID:e0188]


DNA polymerase III holoenzyme complex location

The DNA polymerase III holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential sub-assemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core carries out the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. [PMID:11525729, PMID:12940977, UniProt:P06710]


A DNA polymerase complex that contains two UmuD' and one UmuC subunits, and acts in translesion DNA synthesis. [PMID:10430871, PMID:10542196]


DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex location

Complex that possesses DNA topoisomerase II (double strand cut, ATP-hydrolyzing) activity. [GOC:bhm, GOC:krc, GOC:mah, WikiPedia:Type_II_topoisomerase]


A heterodimeric enzyme, which in most bacterial species is composed of two subunits, ParC and ParE. Functions in chromosome segregation and can relax supercoiled DNA. [GOC:jl, PMID:7783632]


enterochelin synthetase complex location

enterobactin synthetase complex location

A multienzyme complex usually composed of four proteins, EntB, EntD, EntE and EntF. Plays a role in the enterobactin biosynthesis pathway. [MetaCyc:ENTMULTI-CPLX, PMID:9485415]


ethanolamine ammonia-lyase complex location

An enzyme complex that catalyzes the breakdown of ethanolamine to form acetaldehyde and ammonia. [EC:4.3.1.7]


excinuclease ABC complex
excinuclease repair complex location
excinuclease ABC complex location
UvrABC excinuclease complex
UvrABC excinuclease complex location

Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap. [GOC:mah, GOC:mlg, PMID:12145219, PMID:15192705]


An enzyme complex that catalyzes exonucleolytic cleavage (in the presence of ATP) in either 5' to 3' or 3' to 5' direction to yield 5'-phosphooligonucleotides. Exodeoxyribonuclease V shows a preference for double-stranded DNA and possesses DNA-dependent ATPase activity. It acts endonucleolytically on single-stranded circular DNA. [EC:3.1.11.5]


exodeoxyribonuclease VII complex location

An enzyme complex that catalyzes exonucleolytic cleavage in either 5' to 3' or 3' to 5' direction to yield nucleoside 5'-phosphates; it prefers single-stranded DNA. [EC:3.1.11.6]


follicle stimulating hormone complex location

follicle-stimulating hormone complex location

A gonadotrophic glycoprotein hormone secreted, in mammals, by the anterior pituitary gland; consists of alpha and beta subunits, the latter of which confers hormonal specificity. [ISBN:0198547684]


An enzyme complex that catalyzes the dehydrogenation of formate to produce carbon dioxide (CO2). [PMID:1504073, PMID:8566699]


glutamate synthase complex location (NADPH)

A complex that possesses glutamate synthase (NADPH) activity. [EC:1.4.1.13, GOC:mah]


gamma-glutamylcysteine synthetase complex location

glutamate-cysteine ligase complex location

An enzyme complex that catalyzes the ligation of glutamate to cysteine, forming glutamylcysteine. [EC:6.3.2.2]


An enzyme complex that catalyzes the ligation of glutamate and tRNA(Glu) to form glutamyl-tRNA(Glu). [EC:6.1.1.17]


glycerol-3-phosphate dehydrogenase complex location

An enzyme complex that catalyzes the dehydrogenation of sn-glycerol 3-phosphate to form glycerone phosphate. [EC:1.1.5.3]


glycine-tRNA synthetase complex location

A multimeric enzyme complex which, in bacteria, is usually a tetramer of two alpha and two beta chains and in eukaryotes, is usually a homodimer. Functions in the ligation of glycine and tRNA(Gly) to form glycyl-tRNA(Gly). [EC:6.1.1.14, GOC:jl, PMID:15733854]


An enzyme complex that catalyzes the oxidation of 2-hydroxy acid to form 2-oxo acid and hydrogen peroxide (H2O2). The enzyme is a flavoprotein (FMN). [EC:1.1.3.15]


guanylate cyclase complex location, soluble

Complex that possesses guanylate cyclase activity and is not bound to a membrane. [GOC:mah]


Holliday junction helicase complex location

A DNA helicase complex found at Holliday junctions where the helicase activity is involved in the migration of the junction branch point. The best-characterized example is the E. coli RuvAB complex, in which a hexamer of RuvB subunits possesses helicase activity that is modulated by association with RuvA. [PMID:16935884, PMID:9442895]


holo-[acyl-carrier-protein] synthase complex location

OBSOLETE. An enzyme complex that catalyzes the formation of holo-[acyl-carrier protein] from CoA and apo-[acyl-carrier protein]. [EC:2.7.8.7]


ClpYQ protease complex location
ClpYQ protease complex
HslUV protease complex location

A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. [GOC:bhm, PMID:12670962, UniProt:P0A6H5]


imidazoleglycerol phosphate synthase complex location

imidazoleglycerol-phosphate synthase complex location

Complex that possesses imidazoleglycerol-phosphate synthase activity. [GOC:mah]


magnesium-dependent protein serine/threonine phosphatase complex location

An enzyme complex that catalyzes the removal of serine- or threonine-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase. [PMID:17517611, PMID:22343722]


A protein complex that possesses methane monooxygenase activity; dimeric and trimeric complexes have been characterized. [BRENDA:1.14.13.25, GOC:mah]


methionyl glutamyl tRNA synthetase complex location

A complex consisting of methionyl- and glutamyl-tRNA synthetases. The tRNA synthetases present in the complex bind to their cognate tRNAs more efficiently than they do as monomers. [GOC:mcc, PMID:11069915]


molybdopterin converting factor complex location

A protein complex that possesses molybdopterin synthase activity. In E. coli, the complex is a heterotetramer consisting of two MoaD and two MoaE subunits. [GOC:mah, PMID:12571227, PMID:15709772]


NAD(P)+ transhydrogenase complex location (AB-specific)

NAD(P)+ transhydrogenase complex (AB-specific)

A protein complex that possesses NAD(P)+ transhydrogenase (AB-specific) activity. Homodimeric, trimeric, and heterotetrameric complexes have been identified. [BRENDA:1.6.1.2, GOC:mah]


An enzyme complex that catalyzes the formation of nitrate from nitrite with the concomitant reduction of an acceptor. [EC:1.7.99.4]


nitrite reductase complex location [NAD(P)H]

Complex that possesses nitrite reductase [NAD(P)H] activity. [GOC:mah]


An enzyme complex composed of two proteins, dinitrogenase and nitrogenase reductase; dinitrogenase is tetrameric with an alpha2-beta2 structure and nitrogenase reductase is a homodimer, and both are associated with metal ions, which differ between species. Both proteins are required for the enzyme activity of the complex, the formation of oxidized ferredoxin and ammonia from reduced ferredoxin and nitrogen. [EC:1.18.6.1, MetaCyc:CPLX-186, MetaCyc:CPLX-525]


An enzyme complex containing an iron-iron cluster found in species such as the photosynthetic bacterium Rhodobacter capsulatus. It is composed of two main subunits, dinitrogenase and nitrogenase reductase. Dinitrogenase, the iron-iron containing subunit, has an alpha1-beta2 or alpha2-beta2 structure, and the nitrogenase reductase subunit is a homodimer. Functions in the catalysis of the formation of oxidized ferredoxin and ammonia from reduced ferredoxin and nitrogen. [EC:1.18.6.1, GOC:jl, PMID:11848850]


molybdenum-iron nitrogenase complex location

An enzyme complex containing a molybdenum-iron cluster found in many species. It is composed of two proteins, dinitrogenase and nitrogenase reductase; dinitrogenase, the molybdenum-iron protein, is tetrameric with an alpha2-beta2 structure, and nitrogenase reductase is a homodimer. [EC:1.18.6.1]


vanadium-iron nitrogenase complex location

An enzyme complex containing a vanadium-iron cluster found in some species, such as Azotobacter vinelandii. It is composed of two proteins, dinitrogenase and nitrogenase reductase; dinitrogenase, the vanadium-iron protein, is tetrameric with an alpha2-beta2 structure, and nitrogenase reductase is a homodimer. [EC:1.18.6.1, PMID:3474027]


ornithine carbamoyltransferase complex location

A homotrimeric protein complex that catalyzes the transfer of a carbamoyl group to ornithine, forming citrulline. [EC:2.1.3.3, GOC:mah]


p-aminobenzoate synthetase complex location


phenylalanine-tRNA ligase complex location

An enzyme complex that catalyzes the ligation of phenylalanine to tRNA(Phe), forming L-phenylalanyl-tRNA(Phe). [EC:6.1.1.20]


phosphoribosylaminoimidazole carboxylase complex location

A protein complex that possesses phosphoribosylaminoimidazole carboxylase activity. [GOC:mah]


An enzyme complex that catalyzes the phosphorylation of phosphorylase b to form phosphorylase a. [EC:2.7.11.19]


photoreceptor cyclic-nucleotide phosphodiesterase complex location


A protein complex that possesses polyphosphate kinase activity. [GOC:mah]


procollagen-proline, 2-oxoglutarate-4-dioxygenase complex location

procollagen-proline 4-dioxygenase complex location

A protein complex that catalyzes the formation of procollagen trans-4-hydroxy-L-proline and succinate from procollagen L-proline and 2-oxoglutarate, requiring Fe2+ and ascorbate. Contains two alpha subunits that contribute to most parts of the catalytic sites, and two beta subunits that are identical to protein-disulfide isomerase. [PMID:14500733, PMID:7753822]


protein farnesyltransferase complex location

A protein complex that possesses protein farnesyltransferase activity. [GOC:mah]


protein histidine kinase complex location

A complex that possesses protein histidine kinase activity. [GOC:mah]


casein kinase II complex location
casein kinase II complex
protein kinase CK2 complex location

A protein complex that possesses protein serine/threonine kinase activity, and contains two catalytic alpha subunits and two regulatory beta subunits. Protein kinase CK2 complexes are found in nearly every subcellular compartment, and can phosphorylate many protein substrates in addition to casein. [GOC:mah, PMID:10994779]


protein serine/threonine phosphatase complex location

A complex, normally consisting of a catalytic and a regulatory subunit, which catalyzes the removal of a phosphate group from a serine or threonine residue of a protein. [GOC:bf]


calcium-dependent protein serine/threonine phosphatase complex location


An enzyme complex that catalyzes the removal of the phosphate group from phosphomyosin. Composed of a PP1 catalytic subunit (PP1c/PPP1CB) and a myosin phosphatase targeting subunit (MYPT1/PPP1R12A). [PMID:30076859]


A protein serine/threonine phosphatase complex formed by the catalytic subunit of protein phosphatase 4 plus one or more regulatory subunits. [GOC:bhm, PMID:10026142]


protein phosphatase type 1 complex location

A protein complex that possesses magnesium-dependent protein serine/threonine phosphatase (AMD phosphatase) activity, and consists of a catalytic subunit and one or more regulatory subunits that dictates the phosphatase's substrate specificity, function, and activity. [GOC:mah, GOC:ssd]


protein phosphatase type 2A complex location

A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. [GOC:mah, ISBN:0198547684, PMID:17245430]


protein-N(PI)-phosphohistidine-sugar phosphotransferase complex location

An enzyme complex that catalyzes the transfer of a phosphate from protein N(PI)-phosphohistidine to a sugar molecule. It is enzyme II of the phosphotransferase system. [EC:2.7.1.69]


Rab-protein geranylgeranyltransferase complex location

Rab geranylgeranyltransferase complex location

An protein-containing complex which catalyzes of the transfer of a geranyl-geranyl group from geranylgeranyl pyrophosphate to a Rab protein. In mammals it is composed of an alpha and a beta subunit, and associates with an accessory protein Rep (Rab escort protein). [GOC:jl, PMID:11886217]


An flavoprotein that catalyzes the reaction the breakdown of dimethyl(ribityl)lumazine to form riboflavin and ribitylamino-amino-dihydroxypyrimidine. [EC:2.5.1.9]


ribonucleoside-diphosphate reductase complex location

ribonucleotide reductase complex location

An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor. [BRENDA:1.17.4.1]


RISC complex
RISC complex location
RNA-induced silencing complex

A ribonucleoprotein complex that contains members of the Argonaute family of proteins, small interfering RNAs (siRNAs) or microRNAs (miRNAs), and miRNA or siRNA-complementary mRNAs, in addition to a number of accessory factors. The RISC complex is involved in posttranscriptional repression of gene expression through downregulation of translation or induction of mRNA degradation. [PMID:10749213, PMID:15145345]


serine-pyruvate aminotransferase, type 1 complex location


serine-pyruvate aminotransferase, type 2B complex location


succinate-CoA ligase complex location (ADP-forming)

succinate-CoA ligase complex (ADP-forming)

A heterodimeric enzyme complex, composed of an alpha and beta chain, most usually found in (but not limited to) bacteria. Functions in the TCA cycle, hydrolyzing succinyl-CoA into succinate and CoA, thereby forming ATP. [GOC:jl, PMID:9874242]


sulphate adenylyltransferase complex location (ATP)

sulfate adenylyltransferase complex location (ATP)

sulphate adenylyltransferase complex (ATP)

sulfate adenylyltransferase complex (ATP)

An enzyme complex that catalyzes the formation adenylylsulfate from sulfate and ATP. [EC:2.7.7.4]


sulphite reductase complex location (NADPH)

sulfite reductase complex location (NADPH)

A multisubunit iron flavoprotein, which in yeast is composed of 2 alpha and 2 beta subunits. Catalyzes the reduction of sulfite to sulfide. [BRENDA:1.8.1.2, GOC:jl]


translation release factor complex location

A heterodimeric complex involved in the release of a nascent polypeptide chain from a ribosome. [ISBN:0198547684]


trimethylamine-N-oxide reductase complex location

An enzyme complex that catalyzes the reduction of trimethylamine N-oxide to trimethylamine. [GOC:curators]


type I site-specific deoxyribonuclease complex location

type I restriction enzyme complex location

A multisubunit complex composed of two copies of a restriction (R) subunit, two copies of a methylation (M) subunit, and one copy of a specificity (S) subunit. This complex recognizes specific short DNA sequences (through the S subunit), and binds to them. If the recognition site is hemimethylated, the complex acts as a methyltransferase which modifies the recognition site, using S-adenosylmethionine as the methyl donor. Only the M and S subunits are required for this reaction. If the complex binds to an unmethylated recognition site, then the complex translocates the DNA bidirectionally in an ATP-dependent manner. When the translocation is stalled by impact with another complex or unusual DNA structure, the enzyme functions as an endonuclease and cleavage of the DNA will occur, hundreds or thousands of base pairs away from the recognition site. These DNA restriction systems are used by bacteria to defend against phage and other foreign DNA that may enter a cell. [PMID:12654995, PMID:15788748]


type II site-specific deoxyribonuclease complex location

type II restriction enzyme complex location

A protein complex that functions as an endonuclease to cleave DNA at or near a specific recognition site, when that site is unmethylated. These complexes may be dimers or tetramers; it is also possible for the endonuclease to be in a complex with the corresponding methyltransferase that methylates the recognition site. DNA restriction systems such as this are used by bacteria to defend against phage and other foreign DNA that may enter a cell. [PMID:12654995]


type III site-specific deoxyribonuclease complex location

type III restriction enzyme complex location

A heterodimeric enzyme complex composed of two subunits, Res and Mod, that functions as an endonuclease and cleaves DNA. Cleavage will only occur when there are two un-methylated copies of a specific recognition site in an inverse orientation on the DNA. Cleavage occurs at a specific distance away from one of the recognition sites. The Mod subunit can act alone as a methyltansferase. DNA restriction systems such as this are used by bacteria to defend against phage and other foreign DNA that may enter a cell. [PMID:12654995]


protein N-acetylglucosaminyltransferase complex location

A protein complex capable of protein N-acetylglucosaminyltransferase activity, the addition of nucleotide-activated sugars onto the polypeptide according to reaction: UDP-N-acetyl-D-glucosamine + protein = UDP + 4-N-(N-acetyl-D-glucosaminyl)-protein. The complex has different compositions in different species: In mammals it is often a homotrimer, in bacteria a heterotetramer of 2 different subunits. [PMID:15247246]


The complete protein-nucleic acid complex that is the packaged form of the genome in a virus particle. [ISBN:0781702534]


The protein coat that surrounds the infective nucleic acid in some virus particles. It comprises numerous regularly arranged subunits, or capsomeres. [GOC:mtg_sensu, ISBN:0198506732]


Any of the protein subunits that comprise the closed shell or coat (capsid) of certain viruses. [ISBN:0198506732]


The protein coat that surrounds the infective nucleic acid in some virus particles; the subunits are arranged to form a protein helix with the genetic material contained within. Tobacco mosaic virus has such a capsid structure. [ISBN:071673706X, UniProtKB-KW:KW-1139, VZ:885]


The protein coat that surrounds the infective nucleic acid in some virus particles; the subunits are arranged to form an icosahedron, a solid with 20 faces and 12 vertices. Icosahedral capsids have 12 pentamers plus 10(T-1) hexamers, where T is the triangulation number. Tobacco satellite necrosis virus has such a capsid structure. [GOC:bm, ISBN:0198506732, ISBN:071673706X, VZ:885, Wikipedia:Capsid]


A multimeric ring of proteins through which the DNA enters and exits the viral capsid. [PMID:11602732]


A complex of proteins that form a scaffold around which the viral capsid is constructed. [ISBN:0072370319]


A stable empty viral capsid produced during the assembly of viruses. [ISBN:0072370319, ISBN:1555811272]


A structure lying between the capsid and envelope of a virus, varying in thickness and often distributed asymmetrically. [ISBN:0721662544]


ethanol breakdown
ethanol catabolism
ethanol degradation

The chemical reactions and pathways resulting in the breakdown of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation. [GOC:ai, ISBN:0198506732]


The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. [GOC:ceb, GOC:mah, ISBN:0198506732]


The process whose specific outcome is the progression of the kidney over time, from its formation to the mature structure. The kidney is an organ that filters the blood and/or excretes the end products of body metabolism in the form of urine. [GOC:dph, GOC:mtg_kidney_jan10, ISBN:0124020607, ISBN:0721662544]


immunological synapse
supramolecular activation cluster

An area of close contact between a lymphocyte (T-, B-, or natural killer cell) and a target cell formed through the clustering of particular signaling and adhesion molecules and their associated membrane rafts on both the lymphocyte and the target cell and facilitating activation of the lymphocyte, transfer of membrane from the target cell to the lymphocyte, and in some situations killing of the target cell through release of secretory granules and/or death-pathway ligand-receptor interaction. [GOC:mgi_curators, PMID:11244041, PMID:11376300]


The morphological, biochemical and genetic changes that induce the differentiation of non-pathogenic parasites into pathogenic metacyclic parasites in the Trypanosomatidae species. The pathogenic parasites are known as metacyclic trypomastigotes in Trypanosoma and metacyclic promastigotes in Leishmania. [PMID:12152483, PMID:21514274, PMID:2659372, PMID:29091711, PMID:29409544]


cyclosome
anaphase-promoting complex location
anaphase-promoting complex
anaphase promoting complex
APC

A ubiquitin ligase complex that degrades mitotic cyclins and anaphase inhibitory protein, thereby triggering sister chromatid separation and exit from mitosis. Substrate recognition by APC occurs through degradation signals, the most common of which is termed the Dbox degradation motif, originally discovered in cyclin B. [GOC:jh, GOC:vw, PMID:10465783, PMID:10611969]


The sequence of enzymatic reactions by which a cap structure is added to the 5' end of nascent RNA polymerase transcripts. Examples of RNA capping include 7-methyl-G caps found on all RNA polymerase II transcripts and nucleotide-containing cofactor caps, such as NAD(H) or FAD, found on bacterial trancripts. [GOC:bf, GOC:krc, GOC:mah, PMID:18775984, PMID:27383794, PMID:29681497, PMID:30353673]


The directed movement of a motile cell or organism in response to an external stimulus. [GOC:jl, ISBN:0192801023]

directed movement in response to stimulus


The controlled shedding of a body part. [ISBN:0140514031]


Any of the smaller branches of an axon that emanate from the main axon cylinder. [NIF_Subcellular:sao1470140754]


A specialized neuron projection which is the site of synaptic transmission produced by retinal rod cells. Rod spherules are small round enlargements of the axon (3-5 micrometers diameter) or even extensions of the cell body. [PMID:26930660]


A specialized axon terminus which is produced by retinal cone cells. Pedicles are large, conical, flat end-feet (8-10 micrometers diameter) of the retinal cone axon that lie more or less side by side on the same plane at the outer edge of the outer plexiform layer (OPL). [PMID:10939333]


Protein complex that links the outer microtubule doublet of the ciliary or flagellum axoneme with the sheath that surrounds the central pair of microtubules. Composed of a stalk that attaches to each doublet microtubule and a globular structure (spoke head) that projects toward the central pair of microtubules. [ISBN:0124325653, PMID:9450971]


A cytoskeleton-like structure, originating from the basal body at the proximal end of a cilium, and extending proximally toward the cell nucleus. Rootlets are typically 80-100 nm in diameter and contain cross striae distributed at regular intervals of approximately 55-70 nm. [GOC:cilia, PMID:12427867]


Filaments formed of actin and associated proteins; attached to Z discs at either end of sarcomeres in myofibrils. [ISBN:0815316194]


Invagination of the plasma membrane of a muscle cell that extends inward from the cell surface around each myofibril. The ends of T-tubules make contact with the sarcoplasmic reticulum membrane. [GOC:mtg_muscle, ISBN:0815316194]


Regions within compact myelin in which the cytoplasmic faces of the enveloping myelin sheath are not tightly juxtaposed, and include cytoplasm from the cell responsible for making the myelin. Schmidt-Lanterman incisures occur in the compact myelin internode, while lateral loops are analogous structures found in the paranodal region adjacent to the nodes of Ranvier. [GOC:dgh]


A supramolecular assembly of fibrillar collagen complexes in the form of a long fiber (fibril) with transverse striations (bands). [GOC:dos, PMID:21421911]


A type of synapse occurring between an axon and a dendritic spine or dendritic shaft. Asymmetric synapses, the most abundant synapse type in the central nervous system, involve axons that contain predominantly spherical vesicles and contain a thickened postsynaptic density. Most or all synapses of this type are excitatory. [GOC:dgh, GOC:ef]


Type of synapse characterized by an electron-dense ribbon, lamella (bar) or spherical body in the presynaptic process cytoplasm. [NIF_Subcellular:sao1884931180, PMID:15626493]


The network of interconnected tubular and cisternal structures located at the convex side of the Golgi apparatus, which abuts the endoplasmic reticulum. [ISBN:0198506732, ISBN:0815316194]


Specialized junctions between NEURONS which connect the cytoplasm of one neuron to another allowing direct passage of an ion current.


mitochondrial envelope lumen
mitochondrial membrane lumen

The region between the inner and outer lipid bilayers of the mitochondrial envelope. [GOC:mah]


The lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex. [GOC:ecd, GOC:mah]


The volume enclosed by the nuclear inner membrane. [GOC:mah, GOC:pz]


The lipid bilayer surrounding a peroxisome. [GOC:mah]


The lipid bilayer surrounding an endosome. [GOC:mah]


The volume enclosed by the membrane of an endosome. [GOC:mah]


A ribosome that is not associated with the membrane of the rough endoplasmic reticulum.


The portion of the plasma membrane surrounding a cilium. [GOC:cilia, GOC:dph, GOC:rph]


The portion of the plasma membrane surrounding an axon; it is a specialized trilaminar random mosaic of protein molecules floating within a fluid matrix of highly mobile phospholipid molecules, 7-8 nm in thickness. [http://www.medik.sk/clanky/bio_jun.htm, ISBN:0124325653]


Any of a group of intermediate-filament proteins that form the fibrous matrix on the inner surface of the nuclear envelope. They are classified as lamins A, B and C. [ISBN:0198547684]


A nonmotile primary cilium that is found at the apical surface of auditory receptor cells. The kinocilium is surrounded by actin-based stereocilia. [GOC:cilia, GOC:dph, PMID:15882574]


The space bounded by the mitochondrial cristae membranes, continuous with the intermembrane space. [NIF_Subcellular:sao508958414]


Portion of the axon proximal to the neuronal cell body, at the level of the axon hillock. The action potentials that propagate along the axon are generated at the level of this initial segment. [GOC:nln, GOC:sl, PMID:1754851, PMID:21551097]


A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix. [ISBN:0815332181]


A subcompartment of the smooth endoplasmic reticulum consisting of lumenal expansion into a flattened, disc-shaped cavity. [GOC:sl, PMID:12112448]


A subcompartment of the rough endoplasmic reticulum consisting of lumenal expansion into a flattened, disc-shaped cavity. [GOC:sl, PMID:12112448]


growing microtubule plus end
microtubule plus-end

The growing (plus) end of a microtubule. In vitro, microtubules polymerize more quickly at the plus end than at the minus end. In vivo, microtubule growth occurs only at the plus end, and the plus end switches between periods of growth and shortening, a behavior known as dynamic instability. [GOC:bf, GOC:lb, PMID:12700769, PMID:16643273]


The end of a microtubule that does not preferentially grow (polymerize). [GOC:lb, PMID:23169647]


Part of the cilium where the axoneme ends. The ciliary tip has been implicated in ciliary assembly and disassembly, as well as signal transduction. [GOC:cilia, PMID:23970417]


flagellum shaft
ciliary shaft
cilial shaft
cilium shaft

The mid part of a cilium between the ciliary base and ciliary tip that extends into the extracellular space. [GOC:cilia, GOC:krc, PMID:19866682]


cilial basal body
ciliary basal body
kinetosome
microtubule basal body

A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport. [GOC:cilia, GOC:clt, PMID:21750193]


A ribosome located in the cytosol. [GOC:mtg_sensu]


A microtubule in the axoneme of a eukaryotic cilium or flagellum; an axoneme contains nine modified doublet microtubules, which may or may not surround a pair of single microtubules. [GOC:cilia, ISBN:0815316194]


Any (proper) part of the cytoplasm of a single cell of sufficient size to still be considered cytoplasm. [GOC:dos]


The region of a cell situated near the base. For example, in a polarized epithelial cell, the basal surface rests on the basal lamina that separates the epithelium from other tissue. [GOC:mah, ISBN:0815316194]


The lipid bilayer surrounding an endocytic vesicle. [GOC:mah]


The lipid bilayer surrounding a late endosome. [GOC:pz]


An electron dense layer within the basement membrane.


The developmental process in which a skeletal muscle attaches to its target (such as bone or body wall). [GOC:isa_complete, GOC:sart]


The regulated release of proinsulin from secretory granules accompanied by cleavage of proinsulin to form mature insulin. In vertebrates, insulin is secreted from B granules in the B cells of the vertebrate pancreas and from insulin-producing cells in insects. [GOC:mah, ISBN:0198506732]


RNA catabolism
RNA breakdown
RNA degradation

The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. [ISBN:0198506732]


mRNA catabolism
mRNA catabolic process
mRNA degradation

The chemical reactions and pathways resulting in the breakdown of mRNA, messenger RNA, which is responsible for carrying the coded genetic 'message', transcribed from DNA, to sites of protein assembly at the ribosomes. [ISBN:0198506732]


Lymph vessel formation when new vessels emerge from the proliferation of pre-existing vessels. [GOC:dph, PMID:11596157]


An extracellular multi-enzyme complex containing up to 11 different enzymes aligned on a non-catalytic scaffolding glycoprotein. Functions to hydrolyze cellulose. [GOC:jl, PMID:11601609, PMID:15197390, PMID:20373916]


Class I-restricted activation of CD8-POSITIVE LYMPHOCYTES resulting from ANTIGEN PRESENTATION of exogenous ANTIGENS (cross-presentation). This is in contrast to normal activation of these lymphocytes (direct-priming) which results from presentation of endogenous antigens.


Transfer of exogenous ANTIGEN to the ANTIGEN-PRESENTING CELLS for presentation to naive CD8-POSITIVE LYMPHOCYTES.


establishment of chromosome localisation

establishment of chromosome localization

The directed movement of a chromosome to a specific location. [GOC:ai]


The pairwise union of individuals for the purpose of sexual reproduction, ultimately resulting in the formation of zygotes. [GOC:jl, ISBN:0387520546]


A cellular process in which two or more cells combine together, their plasma membrane fusing, producing a single cell. In some cases, nuclei fuse, producing a polyploid cell, while in other cases, nuclei remain separate, producing a syncytium. [Wikipedia:Cell_fusion]


A nuclear body that is enriched in the lymphoid cell-specific protein LYSp100B; LANDs are globular, electron-dense structures and are morphologically distinct from the annular structures characteristic of PML bodies. [PMID:10921892, PMID:8695863]


The opening of an anther, fruit or other structure, which permits the escape of reproductive bodies contained within it. [ISBN:0879015322]


The process where mineral crystals are formed and deposited in an organized fashion in a matrix (either cellular or extracellular) by living organisms. This gives rise to inorganic compound-based structures such as skeleton, teeth, ivory, shells, cuticle, and corals as well as bacterial biomineralization products. [GOC:aa, PMID:24395694, PMID:28229486]


OGC
2-oxoglutarate carboxylase activity
oxalosuccinate synthetase activity

Catalysis of the reaction: 2-oxoglutarate + ATP + bicarbonate = ADP + 2 H(+) + oxalosuccinate + phosphate. [EC:6.4.1.7, RHEA:20425]


The movement of a monocyte in response to an external stimulus. [GOC:add, PMID:11696603, PMID:15173832]


The beginning of development of the breasts in the female. [GOC:curators, PMID:19117864]


Aggressive behavior performed in defence of a fixed area against intruders, typically conspecifics. [GOC:hjd]


The dense covering of microvilli on the apical surface of an epithelial cell in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell. [GOC:sl, ISBN:0815316194]


Binding to an acyl group, any group formally derived by removal of the hydroxyl group from the acid function of a carboxylic acid. [GOC:curators, ISBN:0198506732]


Binding to a lipid antigen. [PMID:14500461]


Binding to an endogenous cellular lipid antigen. [PMID:14500461]


Binding to an exogenous lipid antigen (examples include microbial lipids and glycolipids). [PMID:14500461]


Binding to an antigen peptide. [GOC:add, GOC:jl, GOC:rv]


Interacting selectively and non-covalently, in a non-covalent manner, with peptidoglycan, any of a class of glycoconjugates found in bacterial cell walls. [GOC:go_curators, PMID:14698226]


Binding to calcium oxalate, CaC2O4, a salt of oxalic acid. In animals, it may be excreted in urine or retained in the form of urinary calculi. [ISBN:0721662544]


Binding to a simple or complex galacturonan. Galacturonan is any glycan composed solely of galacturonic acid residues, a specific type of glycuronan, and a constituent of some pectins. [GOC:jid]


Binding to a disaccharide. Disaccharides are sugars composed of two monosaccharide units. [GOC:jid]


Binding to a monosaccharide. Monosaccharides are the simplest carbohydrates; they are polyhydroxy aldehydes H[CH(OH)]nC(=O)H or polyhydroxy ketones H[CHOH]nC(=O)[CHOH]mH with three or more carbon atoms. They form the constitutional repeating units of oligo- and polysaccharides. [GOC:jid]


Binding to fucose, the pentose 6-deoxygalactose. [ISBN:0582227089]


Binding to a galacturonate. Galacturonate is the anion of galacturonic acid, the uronic acid formally derived from galactose by oxidation of the hydroxymethylene group at C-6 to a carboxyl group. [GOC:jid]


Binding to N-acetylgalactosamine, 2-acetamido-2-deoxygalactopyranose, the n-acetyl derivative of galactosamine. [GOC:ai, PMID:18384150]


Binding to a trisaccharide. Trisaccharides are sugars composed of three monosaccharide units. [GOC:jid]


flavine-adenine dinucleotide binding
FAD or FADH2 binding

Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. [GOC:ai, GOC:imk, ISBN:0198506732]


Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. [GOC:tb]


nicotinamide adenine dinucleotide phosphate binding

Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. [GOC:ai]


Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds. [ISBN:0198506732]


Binding to ubiquinone, a quinone derivative with a tail of isoprene units. [GOC:jid, ISBN:0582227089]


Binding to diazepam, one of the most widely used benzodiazepine drugs. It is used as an anti-anxiety-hypnotic agent and has the proprietary name Valium. [ISBN:0198506732]


Binding to N-1-naphthylphthalamic acid, an auxin transport inhibitor. [GOC:sm]


extracellular matrix constituent binding

Binding to a component of the extracellular matrix. [GOC:ai]


Binding to auxin, a plant hormone that regulates aspects of plant growth. [GOC:sm]


ecdysis-triggering hormone receptor activity

Combining with ecdysis-triggering hormone to initiate a change in cell activity. [GOC:ma]


Binding to 20-hydroxyecdysone (ecdysone). Ecdysone is an ecdysteroid produced by the prothoracic glands of immature insects and the ovaries of adult females, which stimulates growth and molting. [GOC:bf, ISBN:0198506732, ISBN:0582227089]


Binding to hydroxyapatite, the calcium phosphate mineral of formula Ca10(PO4)6(OH)2 found both in rocks of nonorganic origin and as a component of bone and dentin. [PMID:2438276]


Binding to 3,4-didehydroretinal, a form of retinal that plays a role in the visual process in freshwater fish and some amphibians analogous to that of all-trans retinal in other vertebrates. 3,4-didehydro-11-cis-retinal combines with an opsin to form cyanopsin (cone) or porphyropsin (rod). [GOC:ai, ISBN:0198506732]


Binding to icosanoids, any C20 polyunsaturated fatty acids or their derivatives, including the leukotrienes and the prostanoids. [ISBN:0198506732]


Binding to icosatetraenoic acid, any straight-chain fatty acid with twenty carbon atoms and four double bonds per molecule. [ISBN:0198506732]


Binding to 5(S)-hydroxyperoxy-6E,8Z,11Z,14Z-icosatetraenoic acid, a straight-chain fatty acid with twenty carbon atoms and four double bonds. [GOC:ai]


Binding to 5-hydroxy-6E,8Z,11Z,14Z-icosatetraenoic acid, a straight-chain fatty acid with twenty carbon atoms and four double bonds. [GOC:ai]


Binding to 5-oxo-6E,8Z,11Z,14Z-icosatetraenoic acid, a straight-chain fatty acid with twenty carbon atoms and four double bonds. [GOC:ai]


Binding to arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer. [GOC:ai]


Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine. [ISBN:0198506732, PMID:12000961]


Binding to a transition metal ions; a transition metal is an element whose atom has an incomplete d-subshell of extranuclear electrons, or which gives rise to a cation or cations with an incomplete d-subshell. Transition metals often have more than one valency state. Biologically relevant transition metals include vanadium, manganese, iron, copper, cobalt, nickel, molybdenum and silver. [ISBN:0198506732]


Binding to a microfibril, any small fibril occurring in biological material. [GOC:ai]


Binding to single-stranded telomere-associated DNA. [GOC:jl, ISBN:0321000382]


Binding to a 5S ribosomal RNA, the smallest RNA constituent of a ribosome. [GOC:jl, ISBN:0321000382]


Binding to an unprocessed 5S ribosomal RNA transcript. [GOC:jl]


Binding to a BRE RNA element (Bruno response element). [PMID:10893231]


Binding to an mRNA molecule at its 5' untranslated region. [GOC:jid]


Binding to a pre-mRNA 3' splice site sequence. [GOC:jl]


Binding to a pre-mRNA 5' splice site sequence. [GOC:jl]


Binding to a pre-mRNA branch point sequence, located upstream of the 3' splice site. [PMID:11691992, PMID:9722632]


adenosine 3'-phosphate 5'-phosphosulfate binding

Binding to 3'-phosphoadenosine 5'-phosphosulfate (PAPS), a naturally occurring mixed anhydride. It is an intermediate in the formation of a variety of sulfo compounds in biological systems. [GOC:ai]


adenyl-nucleotide exchange factor activity

Binds to and stimulates the hydrolysis and exchange of adenyl nucleotides by other proteins. [GOC:kd]


Interacting selectively and non-covalently and stoichiometrically with neuropeptides, peptides with direct synaptic effects (peptide neurotransmitters) or indirect modulatory effects on the nervous system (peptide neuromodulators). [http://www.wormbook.org/chapters/www_neuropeptides/neuropeptides.html]


Interacting selectively and non-covalently and stoichiometrically with neuromedin U, a hypothalamic peptide involved in energy homeostasis and stress responses. [GOC:jl, PMID:12584108]


Combining with the peptide myosuppressin to initiate a change in cell activity. [GOC:bf]


Binding to a signal sequence, a specific peptide sequence found on protein precursors or mature proteins that dictates where the mature protein is localized. [GOC:ai]


endoplasmic reticulum retention sequence binding

Binding to an endoplasmic reticulum (ER) retention sequence, a specific peptide sequence that ensures a protein is retained within the ER. [GOC:ai]


Binding to a vacuolar sorting signal, a specific peptide sequence that acts as a signal to localize the protein within the vacuole. [GOC:mah]


Binding to actinin, any member of a family of proteins that crosslink F-actin. [GOC:jl, ISBN:0198506732]