Coatomer Protein
A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
Coat Protein Complex I
Golgi Apparatus
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Coated Vesicles
COP-Coated Vesicles
TRANSPORT VESICLES formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of COP (coat protein complex) proteins, either COPI or COPII. COPI coated vesicles transport backwards from the cisternae of the GOLGI APPARATUS to the rough endoplasmic reticulum (ENDOPLASMIC RETICULUM, ROUGH), while COPII coated vesicles transport forward from the rough endoplasmic reticulum to the Golgi apparatus.
ADP-Ribosylation Factor 1
ADP-Ribosylation Factors
Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. (1/266)
COPI-coated vesicle budding from lipid bilayers whose composition resembles mammalian Golgi membranes requires coatomer, ARF, GTP, and cytoplasmic tails of putative cargo receptors (p24 family proteins) or membrane cargo proteins (containing the KKXX retrieval signal) emanating from the bilayer surface. Liposome-derived COPI-coated vesicles are similar to their native counterparts with respect to diameter, buoyant density, morphology, and the requirement for an elevated temperature for budding. These results suggest that a bivalent interaction of coatomer with membrane-bound ARF[GTP] and with the cytoplasmic tails of cargo or putative cargo receptors is the molecular basis of COPI coat assembly and provide a simple mechanism to couple uptake of cargo to transport vesicle formation. (+info)Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. (2/266)
The crystal structure of the complex of ARF1 GTPase bound to GDP and the catalytic domain of ARF GTPase-activating protein (ARFGAP) has been determined at 1.95 A resolution. The ARFGAP molecule binds to switch 2 and helix alpha3 to orient ARF1 residues for catalysis, but it supplies neither arginine nor other amino acid side chains to the GTPase active site. In the complex, the effector-binding region appears to be unobstructed, suggesting that ARFGAP could stimulate GTP hydrolysis while ARF1 maintains an interaction with its effector, the coatomer complex of COPI-coated vesicles. Biochemical experiments show that coatomer directly participates in the GTPase reaction, accelerating GTP hydrolysis a further 1000-fold in an ARFGAP-dependent manner. Thus, a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats. (+info)Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. (3/266)
The Saccharomyces cerevisiae maltose transporter is a 12-transmembrane segment protein that under certain physiological conditions is degraded in the vacuole after internalization by endocytosis. Previous studies showed that endocytosis of this protein is dependent on the actin network, is independent of microtubules, and requires the binding of ubiquitin. In this work, we attempted to determine which coat proteins are involved in this endocytosis. Using mutants defective in the heavy chain of clathrin and in several subunits of the COPI and the COPII complexes, we found that clathrin, as well as two cytosolic subunits of COPII, Sec23p and Sec24p, could be involved in internalization of the yeast maltose transporter. The results also indicate that endocytosis of the maltose transporter and of the alpha-factor receptor could have different requirements. (+info)Inhibition of secretion by 1,3-Cyclohexanebis(methylamine), a dibasic compound that interferes with coatomer function. (4/266)
We noted previously that certain aminoglycoside antibiotics inhibit the binding of coatomer to Golgi membranes in vitro. The inhibition is mediated in part by two primary amino groups present at the 1 and 3 positions of the 2-deoxystreptamine moiety of the antibiotics. These two amines appear to mimic the epsilon-amino groups present in the two lysine residues of the KKXX motif that is known to bind coatomer. Here we report the effects of 1, 3-cyclohexanebis(methylamine) (CBM) on secretion in vivo, a compound chosen for study because it contains primary amino groups that resemble those in 2-deoxystreptamine and it should penetrate lipid bilayers more readily than antibiotics. CBM inhibited coatomer binding to Golgi membranes in vitro and in vivo and inhibited secretion by intact cells. Despite depressed binding of coatomer in vivo, the Golgi complex retained its characteristic perinuclear location in the presence of CBM and did not fuse with the endoplasmic reticulum (ER). Transport from the ER to the Golgi was also not blocked by CBM. These data suggest that a full complement of coat protein I (COPI) on membranes is not critical for maintenance of Golgi integrity or for traffic from the ER to the Golgi but is necessary for transport through the Golgi to the plasma membrane. (+info)Nef-induced CD4 degradation: a diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes. (5/266)
The Nef protein of primate lentiviruses downregulates the cell surface expression of CD4 through a two-step process. First, Nef connects the cytoplasmic tail of CD4 with adaptor protein complexes (AP), thereby inducing the formation of CD4-specific clathrin-coated pits that rapidly endocytose the viral receptor. Second, Nef targets internalized CD4 molecules for degradation. Here we show that Nef accomplishes this second task by acting as a connector between CD4 and the beta subunit of COPI coatomers in endosomes. A sequence encompassing a critical acidic dipeptide, located nearby but distinct from the AP-binding determinant of HIV-1 Nef, is responsible for beta-COP recruitment and for routing to lysosomes. A novel class of endosomal sorting motif, based on acidic residues, is thus revealed, and beta-COP is identified as its downstream partner. (+info)p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway. (6/266)
COPI-coated vesicles that bud off the Golgi complex contain two major transmembrane proteins, p23 and p24. We have localized the protein at the Golgi complex and at COPI-coated vesicles. Transport from the intermediate compartment (IC) to the Golgi can be blocked at 15 degrees C, and under these conditions p24 accumulates in peripheral punctated structures identified as IC. Release from the temperature block leads to a redistribution of p24 to the Golgi, showing that p24, similar to p23, cycles between the IC and Golgi complex. Immunoprecipitations of p24 from cell lysates and from detergent-solubilized Golgi membranes and COPI-coated vesicles show that p24 and p23 interact with each other to form a complex. Transient transfection of p23 in HeLa cells shows that p23 and p24 colocalize in structures induced by the overexpression of p23. Taken together p24 interacts with p23 and constitutively cycles between the organelles of the early secretory pathway. (+info)Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COPI dissociation. (7/266)
Physiological conditions that impinge on constitutive traffic and affect organelle structure are not known. We report that osmotically induced cell volume changes, which are known to occur under a variety of conditions, rapidly inhibited endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells. Both ER export and ER Golgi intermediate compartment (ERGIC)-to-Golgi trafficking steps were blocked, but retrograde transport was active, and it mediated ERGIC and Golgi collapse into the ER. Extensive tubulation and relatively rapid Golgi resident redistribution were observed under hypo-osmotic conditions, whereas a slower redistribution of the same markers, without apparent tubulation, was observed under hyperosmotic conditions. The osmotic stress response correlated with the perturbation of COPI function, because both hypo- and hyperosmotic conditions slowed brefeldin A-induced dissociation of betaCOP from Golgi membranes. Remarkably, Golgi residents reemerged after several hours of sustained incubation in hypotonic or hypertonic medium. Reemergence was independent of new protein synthesis but required PKC, an activity known to mediate cell volume recovery. Taken together these results indicate the existence of a coupling between cell volume and constitutive traffic that impacts organelle structure through independent effects on anterograde and retrograde flow and that involves, in part, modulation of COPI function. (+info)GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23. (8/266)
A site-directed photocross-linking approach was employed to determine components that act downstream of ADP-ribosylation factor (ARF). To this end, a photolabile phenylalanine analog was incorporated at various positions of the putative effector region of the ARF molecule. Depending on the position of incorporation, we find specific and GTP-dependent interactions of ARF with two subunits of the coatomer complex, beta-COP and gamma-COP, as well as an interaction with a cytosolic protein (approximately 185 kDa). In addition, we observe homodimer formation of ARF molecules at the Golgi membrane. These data suggest that the binding site of ARF to coatomer is at the interface of its beta- and gamma-subunits, and this is in close proximity to the second site of interaction of coatomer with the Golgi membrane, the binding site within gamma-COP for cytosolic dibasic/diphenylalanine motifs. (+info)Coatomer protein is a complex of eight coat proteins (alpha, beta, beta prime, gamma, delta, epsilon, zeta, and theta) that play a crucial role in the formation of vesicular coats in the early secretory pathway, facilitating the budding of transport vesicles from the Golgi apparatus and endoplasmic reticulum.
Coatomer is a protein complex that plays a role in the formation of transport vesicles within cells. These vesicles are responsible for carrying proteins and other cargo between different cellular compartments. Coatomer gets its name from the coat-like structure it forms on the surface of budding vesicles. It is composed of several individual protein subunits, known as α-COP, β-COP, γ-COP, δ-COP, ε-COP, ζ-COP, and η-COP. These subunits work together to help recognize and bind to specific proteins, curvature the membrane, and ultimately pinch off the vesicle from the donor compartment.
Coatomer protein is primarily involved in transport between the endoplasmic reticulum (ER) and the Golgi apparatus, but it also plays a role in other intracellular transport processes. Mutations or dysfunction in coatomer proteins have been linked to various diseases, including neurological disorders and cancer.
Coat Protein Complex I (COPI), in cell biology, is a protein complex that functions in the intracellular vesicular transport of proteins, primarily within the Golgi apparatus, where it facilitates the retrograde transport of cargo from the Golgi to the endoplasmic reticulum.
Coat Protein Complex I (CPCI or COPI) is a protein complex involved in the intracellular transport of proteins within eukaryotic cells. It functions primarily in the retrograde transport of proteins from the Golgi apparatus to the endoplasmic reticulum (ER). The complex is composed of seven subunits, known as alpha, beta, gamma, delta, epsilon, zeta, and eta COPs (coat proteins), which form a cage-like structure around transport vesicles. This coat assists in the selection of cargo proteins, vesicle budding, and subsequent fusion with target membranes during the recycling of ER-derived proteins.
The Golgi apparatus, also known as the Golgi complex, is a cellular organelle composed of a series of stacked membrane pouches involved in the post-translational modification, sorting, and packaging of proteins and lipids for transport to their final destinations within or outside the cell.
The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.
The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.
The Golgi apparatus performs several essential functions in the cell:
1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.
In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.
Coated vesicles are membrane-bound, transport structures characterized by the presence of a coat protein complex (such as clathrin or COP) on their cytoplasmic surface, which facilitate intracellular cargo sorting, packaging, and budding from donor membranes during vesicular trafficking.
Coated vesicles are membrane-bound compartments found within cells that are characterized by a coat of proteins on their cytoplasmic surface. These vesicles play a crucial role in intracellular transport and membrane trafficking, particularly in the process of endocytosis and exocytosis.
Endocytosis is the process by which cells engulf extracellular material, such as nutrients or molecules like receptors, into vesicles that are formed from the plasma membrane. During this process, coated vesicles called clathrin-coated vesicles form around the region of the plasma membrane where endocytosis is taking place. Clathrin, a protein involved in the formation of these vesicles, polymerizes to form a lattice-like structure that curves the membrane into a spherical shape and pinches it off from the plasma membrane.
Exocytosis, on the other hand, is the process by which cells release molecules or vesicles containing molecules to the extracellular space. In this case, coated vesicles called COP-coated vesicles are involved. These vesicles have a different protein coat, composed of coatomer proteins (COP), and they mediate the transport of proteins and lipids between the endoplasmic reticulum, Golgi apparatus, and the plasma membrane.
Coated vesicles are essential for maintaining cellular homeostasis by controlling the movement of molecules in and out of the cell, as well as the proper sorting and targeting of proteins within the cell. Dysfunctions in coated vesicle formation or trafficking have been implicated in various diseases, including neurodegenerative disorders and cancer.
COP-coated vesicles are membrane-bound transport carriers characterized by the presence of coat proteins (COPs), including clathrin and adaptor protein complexes, which facilitate the formation, cargo selection, and intracellular trafficking of these vesicles during secretion, endocytosis, and organelle biogenesis.
COP-coated vesicles refer to transport vesicles that are coated with coat proteins (COPs) during their formation and play a crucial role in intracellular trafficking. These vesicles are involved in the transport of proteins and lipids between different cellular compartments, such as the endoplasmic reticulum, Golgi apparatus, and plasma membrane.
There are two main types of COP-coated vesicles: COPI (coat protein I) and COPII (coat protein II) coated vesicles.
COPI-coated vesicles are involved in the retrograde transport of proteins from the Golgi apparatus to the endoplasmic reticulum, as well as intra-Golgi trafficking. They are formed by the assembly of coatomer proteins (COPs) around a budding membrane, which then pinches off to form a vesicle. The COPI coat is disassembled upon arrival at the target membrane, releasing the cargo and allowing for fusion with the target membrane.
On the other hand, COPII-coated vesicles are involved in the anterograde transport of proteins from the endoplasmic reticulum to the Golgi apparatus. They are formed by the assembly of Sar1, Sec23/24, and Sec13/31 coat proteins around a budding membrane, which then pinches off to form a vesicle. The COPII coat is disassembled upon arrival at the target membrane, releasing the cargo and allowing for fusion with the target membrane.
Overall, COP-coated vesicles are essential components of the intracellular transport machinery that enables cells to regulate their protein and lipid composition in a precise and coordinated manner.
ADP-Ribosylation Factor 1 (ARF1) is a small, ubiquitous G protein that plays a crucial role in intracellular membrane traffic, actin dynamics, and signal transduction pathways by cycling between GTP-bound active and GDP-bound inactive states.
ADP-Ribosylation Factor 1 (ARF1) is a small GTP-binding protein that belongs to the ADP-ribosylation factor family. It plays a crucial role in intracellular membrane traffic, actin dynamics, and signal transduction pathways. ARF1 functions as a molecular switch by cycling between an active GTP-bound state and an inactive GDP-bound state.
In the active state, ARF1 regulates the recruitment of coat proteins to membranes, which facilitates vesicle formation and transport. It also activates phospholipase D, which generates second messengers that regulate various cellular processes. In contrast, in the inactive state, ARF1 is bound to GDP and cannot participate in these functions.
Mutations or dysregulation of ARF1 have been implicated in several human diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the structure, function, and regulation of ARF1 is essential for developing new therapeutic strategies to treat these conditions.
ADP-Ribosylation Factors (ARFs) are small, ubiquitous GTP-binding proteins that play crucial roles in regulating intracellular membrane traffic, actin dynamics, and nuclear export.
ADP-ribosylation factors (ARFs) are a family of small GTP-binding proteins that play a crucial role in intracellular membrane traffic, actin dynamics, and signal transduction. They function as molecular switches, cycling between an active GTP-bound state and an inactive GDP-bound state.
ARFs are involved in the regulation of vesicle formation, budding, and transport, primarily through their ability to activate phospholipase D and recruit coat proteins to membranes. There are six isoforms of ARFs (ARF1-6) that share a high degree of sequence similarity but have distinct cellular functions and subcellular localizations.
ADP-ribosylation factors get their name from the fact that they were originally identified as proteins that become ADP-ribosylated by cholera toxin, an enzyme produced by Vibrio cholerae bacteria. However, this post-translational modification is not required for their cellular functions.
Defects in ARF function have been implicated in various human diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the regulation and function of ARFs is an important area of research in biology and medicine.
Coatomer
The coatomer protein complex is made up of seven nonidentical protein subunits. These seven nonidentical protein subunits are ... The coatomer is a protein complex that coats membrane-bound transport vesicles. Two types of coatomers are known: COPI ( ... Coatomer+Protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Boehm, Markus; Bonifacino, Juan S. ( ... COP II is a coatomer that coats the vesicles transporting proteins from the ER to the golgi complex. This pathway is referred ...
COPE (gene)
The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds ... "Entrez Gene: COPE coatomer protein complex, subunit epsilon". Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene. ...
COPG
Coatomer subunit gamma is a protein that in humans is encoded by the COPG gene. It is one of seven proteins in the COPI ... "Entrez Gene: COPG coatomer protein complex, subunit gamma". Bermak, Jason C; Li Ming; Bullock Clayton; Weingarten Paul; Zhou ... 2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi: ... "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex" (PDF). J. Cell ...
COPA (gene)
Coatomer subunit alpha is a protein that in humans is encoded by the COPA gene. In eukaryotic cells, protein transport between ... "Entrez Gene: COPA coatomer protein complex, subunit alpha". Gerich B, Orci L, Tschochner H, Lottspeich F, Ravazzola M, Amherdt ... 1997). "Association of coatomer proteins with the beta-receptor for platelet-derived growth factor". Biochem. Biophys. Res. ... 1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell ...
COPG2
Coatomer subunit gamma-2 is a protein that in humans is encoded by the COPG2 gene. COPG2 has been shown to interact with ... "Entrez Gene: COPG2 coatomer protein complex, subunit gamma 2". Bermak JC, Li M, Bullock C, Weingarten P, Zhou QY (Feb 2002). " ... Waters MG, Serafini T, Rothman JE (1991). "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/ ...
COPZ1
Coatomer subunit zeta-1 is a protein that in humans is encoded by the COPZ1 gene. COPZ1 has been shown to interact with COPG. ... "Entrez Gene: COPZ1 coatomer protein complex, subunit zeta 1". Futatsumori M, Kasai K, Takatsu H, Shin HW, Nakayama K (November ... "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex" (PDF). J. Cell ... Overview of all the structural information available in the PDB for UniProt: P61923 (Human Coatomer subunit zeta-1) at the PDBe ...
COPB2
"The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase Cepsilon". J. Biol. Chem. 272 (46): 29200 ... Coatomer subunit beta is a protein that is encoded by the COPB2 gene in humans. The Golgi coatomer complex (see MIM 601924) ... "Entrez Gene: COPB2 coatomer protein complex, subunit beta 2 (beta prime)". Eugster A, Frigerio G, Dale M, Duden R (August 2000 ... "Assignment of the cellular retinol-binding protein 1 gene (RBP1) and of the coatomer beta subunit gene (COPB2) to human ...
COPI
... is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to ... 1994). "Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum". Cell. 79 (7): 1199-207. ... Luminal proteins: Proteins found in the lumen of the Golgi complex that need to be transported to the lumen of the ER contain ... 1996). "A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding". J Cell Biol. 135 (5 ...
COPB1
Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene. COPI coatomer, a protein complex GRCh38: ... 1997). "Association of coatomer proteins with the beta-receptor for platelet-derived growth factor". Biochem. Biophys. Res. ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Pavel J, Harter C, Wieland FT (1998). "Reversible dissociation of coatomer: Functional characterization of a β/δ-coat protein ...
Chylomicron retention disease
Though PCTV does not require COPII coatomer proteins for budding from the ER, association with the coatomer is necessary for ... Without the fully functional sar1B protein, the COPll coatomer proteins engulf pre-chylomicrons exiting the ER but are unable ... Sar1B is a GTPase and one of the five proteins of the COPll coatomer. A mutation in the sar1B gene and subsequently the sar1B ... Before the PCTV leaves the ER, it is incorporated into a COPII coatomer of five proteins. The PCTV undergoes a similar ...
ARF5
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... 2000). "A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. Bibcode: ... The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ...
ARF4
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... The gene products include 5 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ... ADP-ribosylation factor 4 is a protein that in humans is encoded by the ARF4 gene. ADP-ribosylation factor 4 (ARF4) is a member ... Shin OH, Ross AH, Mihai I, Exton JH (1999). "Identification of arfophilin, a target protein for GTP-bound class II ADP- ...
ARF3
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (1999). "Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a ... Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (October 1999). "Arf proteins bind to mitotic kinesin-like protein 1 ( ... The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ...
Beta2-adaptin C-terminal domain
These vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction ... AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ...
ARF6
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... ARF6+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Human ARF6 genome location and ... D'Souza-Schorey C, Boshans RL, McDonough M, Stahl PD, Van Aelst L (1997). "A role for POR1, a Rac1-interacting protein, in ARF6 ... ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety ...
Clathrin adaptor protein
Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between ... Protein pages needing a picture, Peripheral membrane proteins, Protein families). ... Adaptor protein (AP) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to ...
Alpha solenoid
They are also common in membrane coat proteins known as coatomers, such as clathrin, and in regulatory proteins that form ... The protein-protein interaction capacity of alpha solenoid proteins also makes them well suited to function as regulatory ... extended protein-protein interaction surfaces or to form deep concave areas for binding globular proteins. Because they are ... "When protein folding is simplified to protein coiling: the continuum of solenoid protein structures". Trends in Biochemical ...
COPE
... a human gene that encodes the protein coatomer subunit epsilon COPE (film), a 2007 psychological thriller/horror independent ...
Copa
... a human gene that encodes the coatomer subunit alpha protein Controlling Profitability Analysis, Profitability Analysis (SAP) ...
Vesicular transport adaptor protein
Components of COPI (cop one) a coatomer, and TSET (T-set) a membrane trafficking complex have similar heterotetramers of the AP ... In the AP complexes, there are two large proteins (~100 kD) and two smaller proteins. One of the large proteins is termed β ( ... Protein complexes, Protein families, Molecular evolution, Vesicular transport proteins). ... PTBs are protein domains that include NUMB, DAB1 and DAB2. Epsin and AP180 in the ANTH domain are other adaptor proteins that ...
RBP1
1999). "Assignment of the cellular retinol-binding protein 1 gene (RBP1) and of the coatomer beta subunit gene (COPB2) to human ... Retinol binding protein 1, cellular, also known as RBP1, is a protein that in humans is encoded by the RBP1 gene. RBP1 is the ... "The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane ... Alteration of relative protein amounts is linked to the state of differentiation". Biochem. J. 287. ( Pt 2) (2): 383-9. doi: ...
TMEM267
The coatomer subunit delta (delta-COP) is a cytosolic protein complex that binds to motifs and associates with vesicles ... Role of Mammalian Vacuolar Protein-sorting Proteins in Endocytic Trafficking of a Non-ubiquitinated G Protein-coupled Receptor ... There is no evidence of post-translational modifications of the TMEM267 protein found in tissues. According to protein sequence ... The protein was identified as a member of a large group of proteins that comprise a filter in mammalian cells which allow ...
SCYL1
2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. ... Scyl1 localizes to the cis-Golgi and ER-Golgi Intermediate Compartment (ERGIC). Scyl1 binds to Coatomer I (COPI) and ... This gene encodes a transcriptional regulator belonging to the SCY1-like family of kinase-like proteins. The protein has a ... The FL protein contains HEAT repeats and a C-terminal coiled coil domain that also contains multiple dibasic motifs, and ends ...
Archain
... is a human protein that is encoded by gene which is located on chromosome 11. Also known as ARCN1, it plays a role in ... It is part of the COPI coatomer complex. Xu X, Kedlaya R, Higuchi H, et al. (2010). "Mutation in archain 1, a subunit of COPI ... Protein pages needing a picture, Genes on human chromosome 11, Accuracy disputes from September 2020, All accuracy disputes, ... Peripheral membrane proteins, All stub articles, Human chromosome 11 gene stubs). ...
Adipocyte
The SREBF1-SCAP complex is retained in the ER membrane by INSIG1 (insulin-induced gene 1 protein). When sterol levels are ... depleted, INSIG1 releases SCAP and the SREBF1-SCAP complex can be sorted into transport vesicles coated by the coatomer COPII ... In the Golgi apparatus, SREBF1 is cleaved and released as a transcriptionally active mature protein. It is then free to ... White fat cells secrete many proteins acting as adipokines such as resistin, adiponectin, leptin and apelin. An average human ...
SACM1L
2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs ... 2004). "The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex". J. Biol. Chem. 278 (52): 52689- ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (6): 355-64. doi: ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (6): 347-55. doi: ...
Nucleoporin
The proteins lining the inner pore make up the NUP62 complex. On the nucleoplasm side, extra proteins associated with the ring ... the ancestral coatomer elements (ACE). To date, two classes of ACEs have been identified. ACE1 is a 28-helix domain found in ... Different sets of proteins associate on either ring, and some transmembrane proteins anchor the assembly to the lipid bilayer. ... Karyopherins can serve as an importin (transporting proteins into the nucleus) or an exportin (transporting proteins out of the ...
ARF1
... including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized ... Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions ... The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively ... ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene. ADP-ribosylation factor 1 (ARF1) is a member ...
TMED2
Transmembrane emp24 domain-containing protein 2 is a protein that in humans is encoded by the TMED2 gene. TMED2 has been shown ... Fiedler K, Veit M, Stamnes MA, Rothman JE (September 1996). "Bimodal interaction of coatomer with the p24 family of putative ... two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular ... Majoul I, Straub M, Hell SW, Duden R, Söling HD (July 2001). "KDEL-cargo regulates interactions between proteins involved in ...
RGS2
Regulator of G-protein signaling 2 is a protein that in humans is encoded by the RGS2 gene. It is part of a larger family of ... 2000). "RGS4 and RGS2 bind coatomer and inhibit COPI association with Golgi membranes and intracellular transport". Mol. Biol. ... Nlend MC, Bookman RJ, Conner GE, Salathe M (2002). "Regulator of G-protein signaling protein 2 modulates purinergic calcium and ... 1999). "Regulators of G protein signaling exhibit distinct patterns of gene expression and target G protein specificity in ...
OMIM - COATOMER PROTEIN COMPLEX, SUBUNIT BETA-2; COPB2 - OMIM - NCBI
Coatomer - Wikipedia
The coatomer protein complex is made up of seven nonidentical protein subunits. These seven nonidentical protein subunits are ... The coatomer is a protein complex that coats membrane-bound transport vesicles. Two types of coatomers are known: COPI ( ... Coatomer+Protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Boehm, Markus; Bonifacino, Juan S. ( ... COP II is a coatomer that coats the vesicles transporting proteins from the ER to the golgi complex. This pathway is referred ...
Copb2 COPI coat complex subunit beta 2 [Mus musculus (house mouse)] - Gene - NCBI
coatomer subunit beta. Names. beta-COP. beta-coat protein. coatomer protein complex, subunit beta 2 (beta prime). p102. ... mRNA and Protein(s) * NM_015827.2 → NP_056642.1 coatomer subunit beta. See identical proteins and their annotated locations ... General protein information Go to the top of the page Help Preferred Names. ... protein coding. RefSeq status. PROVISIONAL. Organism. Mus musculus Lineage. Eukaryota; Metazoa; Chordata; Craniata; Vertebrata ...
MMRRC:042420-MU
Difficulties in Differentiating Coronaviruses from Subcellular Structures in Human Tissues by Electron Microscopy - Volume 27,...
These clathrin and coatomer proteins, however, are in direct contact with the cell cytosol (Figure 1, panel D; Figure 2, panel ... Coatomer proteins mediate transport within the Golgi complex and between the Golgi complex and ER (42). Although the sizes of ... Coat proteins: shaping membrane transport. Nat Rev Mol Cell Biol. 2003;4:409-14. DOIPubMedGoogle Scholar ... The SARS coronavirus nucleocapsid protein-forms and functions. Antiviral Res. 2014;103:39-50. DOIPubMedGoogle Scholar ...
SEC27 - SSH1 Interaction Summary | BioGRID
Essential beta-coat protein of the COPI coatomer; involved in ER-to-Golgi and Golgi-to-ER transport; contains WD40 domains ... SRP-dependent cotranslational protein targeting to membrane [IGI, IMP]. Gene Ontology Molecular Function. *protein ... Search BioGRID for SARS-CoV-2 Protein Interactions , Download SARS-CoV-2 and Coronavirus-Related Interactions ... Subunit of the Ssh1 translocon complex; Sec61p homolog involved in co-translational pathway of protein translocation; not ...
COP Coated Vesicles | Cell Biology | JoVE
COPI and COPII vesicles are composed of similar coat protein complexes called coatomers. These bend the membrane to form a bud ... Specific coat proteins cover their cytosolic surface.. Based on the type of protein coats, these vesicles can be of three types ... Proteins selected by COPII-coated vesicles include enzymes that act in the biosynthetic pathways, membrane proteins involved in ... The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their ...
A dissection of SARS‑CoV2 with clinical implications (Review)
The strongest proviral activation was seen in the β2 subunit of the coatomer protein complex (COPB2) followed by inositol ... nucleocapsid protein (N), spike surface glycoprotein (S), matrix protein (M), and small envelope protein (E). The N-protein ... RNA encodes for 27 viral proteins, of which 16 are non-structural proteins (nsps), and 11 are accessory and structural proteins ... The S protein is a class I viral fusion protein like the influenza virus hemagglutinin (HA); SARS-CoV2 also has an S1/S2 ...
Prof. Dr. Julien Béthune, HAW Hamburg
Béthune, J., Kol, M., Hoffmann, J., Reckmann, I., Brugger, B. and Wieland, F. (2006) Coatomer, the coat protein of COPI ... Béthune, J. and Wieland, F.T. (2018) Assembly of COPI and COPII Vesicular Coat Proteins on Membranes. Annual Reviews of ... Langer, J.D., Stoops, E.H., Béthune, J. and Wieland, F.T. (2007) Conformational changes of coat proteins during vesicle ... Schopp, I.M. and Béthune, J. (2018) Split-BioID - Proteomic Analysis of Context-specific Protein Complexes in Their Native ...
ADARB1 | Cancer Genetics Web
... coatomer protein complex, subunit α), are closely associated with HCC pathogenesis. In vitro and in vivo functional assays ... Rho GTPase activating protein 26 (ARHGAP26) is a negative regulator of the Rho family that converts the small G proteins RhoA ... negative regulation of protein kinase activity by regulation of protein phosphorylation - nucleolus - nucleoplasm - nucleus - ... What does this gene/protein do?. Show (22). ADARB1 is implicated in:. - adenosine deaminase activity - adenosine to inosine ...
CoP: Co-expressed Biological Processes
Coatomer gamma subunit (Gamma-coat protein)(Gamma-COP). 1e-25. At4g34450. coatomer gamma-2 subunit, putative / gamma-2 coat ... WD40-like domain containing protein. 3e-8. At3g63460. WD-40 repeat family protein. O.I.. H.G.. S.X.. Please select. KEGG ( ... unknown protein. O.I.. H.G.. S.X.. Please select. 0.67. 86.1. 0.99. Gma.8460.1.S1_at. AF404404.1. acyl-CoA oxidase. -. 7e-39. ... Ribophorin II family protein. 1e-6. At4g21150. HAP6 (HAPLESS 6). O.I.. H.G.. S.X.. Please select. KEGG (integral). Gramene ( ...
Jared D Evans, PhD | Editor | SciTechnol | Journal of Virology &
Role of Coatomer Protein I in Virus Replication. Review Article: J Virol Antivir Res 2012, 1:2 DOI: 10.4172/2324-8955.1000102. ... Viral Proteomics: Decoding the Intricate World of Viral Proteins. Opinion Article: J Virol Antivir. DOI: Stephan Phillips *Full ... Virus-Induced FOXO Protein Facilitates Viral Replication of Human Cytomegalovirus. Annual Meeting Abstract: J Virol Antivir Res ... Diversity of and Implications from the Viral Genomes and Viral Proteins of Zika Virus. Short Communication: J Virol Antivir Res ...
Pharos : Target Details - COPE
The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds ... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be ... which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer ... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Coatomer complex consists of at least ...
PlanMine: Keyword Search
Scott D Emr - Google Scholar
Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. F Letourneur, EC Gaynor, S ... Protein Sorting in Saccharomyces cerevisiae: Isolation of Mutants Defective in the Delivery and Processing of Multiple Vacuolar ... Phosphatidylinositol 3-Kinase Encoded by Yeast VPS34 Gene Essential for Protein Sorting. PV Schu, K Takegawa, MJ Fry, JH Stack ... The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. M Babst, B ...
The evolutionary history of effectors downstream of Cdc42 and Rac | Genome Biology | Full Text
... a comparison of effector proteins from evolutionarily diverse organisms suggests that six groups of proteins serve as the core ... Although dozens of proteins act downstream of these GTPases, ... actin-bundling proteins; coatomers (vesicle coat proteins); ... scaffold protein IRSp53, and the Borg proteins. Interestingly, the CRIB motif also makes an appearance in plant proteins, but ... This motif is found in Cdc42/Rac-associated proteins such as the protein kinases Pak, MRCK and Ack, the adaptor proteins Spec ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
DeCS - New terms
COATOMER PROTEIN PROTEINA COATOMERA PROTEÍNA COATOMER COILED BODIES CUERPOS ENROLLADOS CORPOS ESPIRALADOS ... PROTEIN RENATURATION RENATURACION DE PROTEINA RENATURAÇÃO PROTÉICA PROTEIN STRUCTURE, QUATERNARY ESTRUCTURA CUATERNARIA DE ... SOS1 PROTEIN PROTEINA SOS1 PROTEÍNA SOS1 SPERM INJECTIONS, INTRACYTOPLASMIC INYECCIONES DE ESPERMA INTRACITOPLASMATICAS ... CDC42 GTP-BINDING PROTEIN, YEAST PROTEINA DE ENLACE-GTP CDC42 DE LEVADURA PROTEÍNA CDC42 DE LEVEDURA DE LIGAÇÃO A GTP ...
Computational identification of protein-protein interactions in model plant proteomes | Scientific Reports
A PPI network provides crucial information on how biological pathways are structured and coordinated from individual protein ... Our method considers a variety of features including protein sequences, gene co-expression, functional association, and ... Protein-protein interactions (PPIs) play essential roles in many biological processes. ... Our predicted PPIs also included some subunits of known complexes such as coatomer, RNA polymerase, DNA directed RNA polymerase ...