A family of large adaptin protein complex subunits of approximately 90-130 kDa in size.
An adaptor protein complex found primarily on perinuclear compartments.
A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.
An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.
An adaptor protein complex involved in transport of molecules between the TRANS-GOLGI NETWORK and the endosomal-lysosomal system.
The subunits that make up the large, medium and small chains of adaptor proteins.
A family of large adaptin protein subunits of approximately 130-kDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 3.
A family of medium adaptin protein subunits of approximately 45 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 3 and ADAPTOR PROTEIN COMPLEX 4.
A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.
A family of large adaptin protein subunits of approximately 90 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 1.
A family of large adaptin protein subunits of approximately 100 kDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 2.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.
The fundamental dispositions and traits of humans. (Merriam-Webster's Collegiate Dictionary, 10th ed)
A subclass of clathrin assembly proteins that occur as monomers.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Syndrome characterized by the triad of oculocutaneous albinism (ALBINISM, OCULOCUTANEOUS); PLATELET STORAGE POOL DEFICIENCY; and lysosomal accumulation of ceroid lipofuscin.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
The branch of chemistry dealing with detection (qualitative) and determination (quantitative) of substances. (Grant & Hackh's Chemical Dictionary, 5th ed)

The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. (1/89)

betaarrestins mediate the desensitization of the beta2-adrenergic receptor (beta2AR) and many other G protein-coupled receptors (GPCRs). Additionally, betaarrestins initiate the endocytosis of these receptors via clathrin coated-pits and interact directly with clathrin. Consequently, it has been proposed that betaarrestins serve as clathrin adaptors for the GPCR family by linking these receptors to clathrin lattices. AP-2, the heterotetrameric clathrin adaptor protein, has been demonstrated to mediate the internalization of many types of plasma membrane proteins other than GPCRs. AP-2 interacts with the clathrin heavy chain and cytoplasmic domains of receptors such as those for epidermal growth factor and transferrin. In the present study we demonstrate the formation of an agonist-induced multimeric complex containing a GPCR, betaarrestin 2, and the beta2-adaptin subunit of AP-2. beta2-Adaptin binds betaarrestin 2 in a yeast two-hybrid assay and coimmunoprecipitates with betaarrestins and beta2AR in an agonist-dependent manner in HEK-293 cells. Moreover, beta2-adaptin translocates from the cytosol to the plasma membrane in response to the beta2AR agonist isoproterenol and colocalizes with beta2AR in clathrin-coated pits. Finally, expression of betaarrestin 2 minigene constructs containing the beta2-adaptin interacting region inhibits beta2AR endocytosis. These findings point to a role for AP-2 in GPCR endocytosis, and they suggest that AP-2 functions as a clathrin adaptor for the endocytosis of diverse classes of membrane receptors.  (+info)

Duplications on human chromosome 22 reveal a novel Ret Finger Protein-like gene family with sense and endogenous antisense transcripts. (2/89)

Analysis of 600 kb of sequence encompassing the beta-prime adaptin (BAM22) gene on human chromosome 22 revealed intrachromosomal duplications within 22q12-13 resulting in three active RFPL genes, two RFPL pseudogenes, and two pseudogenes of BAM22. The genomic sequence of BAM22vartheta1 shows a remarkable similarity to that of BAM22. The cDNA sequence comparison of RFPL1, RFPL2, and RFPL3 showed 95%-96% identity between the genes, which were most similar to the Ret Finger Protein gene from human chromosome 6. The sense RFPL transcripts encode proteins with the tripartite structure, composed of RING finger, coiled-coil, and B30-2 domains, which are characteristic of the RING-B30 family. Each of these domains are thought to mediate protein-protein interactions by promoting homo- or heterodimerization. The MID1 gene on Xp22 is also a member of the RING-B30 family and is mutated in Opitz syndrome (OS). The autosomal dominant form of OS shows linkage to 22q11-q12. We detected a polymorphic protein-truncating allele of RFPL1 in 8% of the population, which was not associated with the OS phenotype. We identified 6-kb and 1.2-kb noncoding antisense mRNAs of RFPL1S and RFPL3S antisense genes, respectively. The RFPL1S and RFPL3S genes cover substantial portions of their sense counterparts, which suggests that the function of RFPL1S and RFPL3S is a post-transcriptional regulation of the sense RFPL genes. We illustrate the role of intrachromosomal duplications in the generation of RFPL genes, which were created by a series of duplications and share an ancestor with the RING-B30 domain containing genes from the major histocompatibility complex region on human chromosome 6.  (+info)

The structure and function of the beta 2-adaptin appendage domain. (3/89)

The heterotetrameric AP2 adaptor (alpha, beta 2, mu 2 and sigma 2 subunits) plays a central role in clathrin-mediated endocytosis. We present the protein recruitment function and 1.7 A resolution structure of its beta 2-appendage domain to complement those previously determined for the mu 2 subunit and alpha appendage. Using structure-directed mutagenesis, we demonstrate the ability of the beta 2 appendage alone to bind directly to clathrin and the accessory proteins AP180, epsin and eps15 at the same site. Clathrin polymerization is promoted by binding of clathrin simultaneously to the beta 2-appendage site and to a second site on the adjacent beta 2 hinge. This results in the displacement of the other ligands from the beta 2 appendage. Thus clathrin binding to an AP2-accessory protein complex would cause the controlled release of accessory proteins at sites of vesicle formation.  (+info)

beta2-adaptin is constitutively de-phosphorylated by serine/threonine protein phosphatase PP2A and phosphorylated by a staurosporine-sensitive kinase. (4/89)

Clathrin-mediated endocytosis includes cycles of assembly and disassembly of the clathrin-coated vesicle constituents. How these cycles are regulated is still not fully known but previous studies have indicated that phosphorylation of coat subunits may play a role. Here we describe that beta2-adaptin undergoes cycles of phosphorylation/de-phosphorylation in intact cells. Thus, beta2-adaptin was constitutively de-phosphorylated by serine/threonine protein phosphatase 2A and phosphorylated by a staurosporine-sensitive kinase in vivo. Confocal laser scanning microscopy demonstrated that phosphorylated AP2 complexes were found more evenly distributed at the plasma membrane compared to non-phosphorylated AP2 complexes which were found in aggregates. Finally, we found that phosphorylation of beta2-adaptin correlated with inhibition of clathrin-mediated endocytosis. Our results support the hypothesis that phosphorylation/de-phosphorylation of coat proteins plays a regulatory role in the assembly/disassembly cycle of clathrin-coated vesicles.  (+info)

Defective organellar membrane protein trafficking in Ap3b1-deficient cells. (5/89)

AP-3 is a heterotetrameric protein complex involved in intracellular vesicle transport. Molecular analyses show that Ap3b1, which encodes the AP-3 (&bgr;)3A subunit, is altered in pearl mice. To provide genetic evidence that mutation of Ap3b1 is responsible for the pearl phenotype and to determine the null phenotype, the Ap3b1 gene was disrupted by homologous recombination. Mice homozygous for the resulting allele, Ap3b1(LN), or compound heterozygotes with pearl, displayed phenotypes similar to those of pearl mice, confirming that Ap3b1 is the causal gene for pearl. Moreover, pearl is likely to be a hypomorph as the Ap3b1(LN) homozygotes had a lighter coat color and accumulated fewer of the micro3 and (&dgr;)3 subunits of AP-3 than did pearl mice. Finally, immunofluorescence analysis of fibroblasts and melanocytes cultured from Ap3b1(LN) homozygotes revealed that the lysosomal membrane proteins Lamp I and Lamp II and the melanosomal membrane protein tyrosinase were mislocalized. In particular, the Lamp proteins were clustered on the cell surface. These findings strengthen the evidence for an alternate pathway via the plasma membrane for cargo normally transported to organelles by AP-3.  (+info)

A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex. (6/89)

Intracellular transport mediated by kinesin superfamily proteins (KIFs) is a highly regulated process. The molecular mechanism of KIFs binding to their respective cargoes remains unclear. We report that KIF13A is a novel plus end-directed microtubule-dependent motor protein and associates with beta 1-adaptin, a subunit of the AP-1 adaptor complex. The cargo vesicles of KIF13A contained AP-1 and mannnose-6-phosphate receptor (M6PR). Overexpression of KIF13A resulted in mislocalization of the AP-1 and the M6PR. Functional blockade of KIF13A reduced cell surface expression of the M6PR. Thus, KIF13A transports M6PR-containing vesicles and targets the M6PR from TGN to the plasma membrane via direct interaction with the AP-1 adaptor complex.  (+info)

Vps10p transport from the trans-Golgi network to the endosome is mediated by clathrin-coated vesicles. (7/89)

A native immunoisolation procedure has been used to investigate the role of clathrin-coated vesicles (CCVs) in the transport of vacuolar proteins between the trans-Golgi network (TGN) and the prevacuolar/endosome compartments in the yeast Saccharomyces cerevisiae. We find that Apl2p, one large subunit of the adaptor protein-1 complex, and Vps10p, the carboxypeptidase Y vacuolar protein receptor, are associated with clathrin molecules. Vps10p packaging in CCVs is reduced in pep12 Delta and vps34 Delta, two mutants that block Vps10p transport from the TGN to the endosome. However, Vps10p sorting is independent of Apl2p. Interestingly, a Vps10C(t) Delta p mutant lacking its C-terminal cytoplasmic domain, the portion of the receptor responsible for carboxypeptidase Y sorting, is also coimmunoprecipitated with clathrin. Our results suggest that CCVs mediate Vps10p transport from the TGN to the endosome independent of direct interactions between Vps10p and clathrin coats. The Vps10p C-terminal domain appears to play a principal role in retrieval of Vps10p from the prevacuolar compartment rather than in sorting from the TGN.  (+info)

Hermansky-Pudlak syndrome type 3 in Ashkenazi Jews and other non-Puerto Rican patients with hypopigmentation and platelet storage-pool deficiency. (8/89)

Hermansky-Pudlak syndrome (HPS), consisting of oculocutaneous albinism and a bleeding diathesis due to the absence of platelet dense granules, displays extensive locus heterogeneity. HPS1 mutations cause HPS-1 disease, and ADTB3A mutations cause HPS-2 disease, which is known to involve abnormal intracellular vesicle formation. A third HPS-causing gene, HPS3, was recently identified on the basis of homozygosity mapping of a genetic isolate of HPS in central Puerto Rico. We now describe the clinical and molecular characteristics of eight patients with HPS-3 who are of non-Puerto Rican heritage. Five are Ashkenazi Jews; three of these are homozygous for a 1303+1G-->A splice-site mutation that causes skipping of exon 5, deleting an RsaI restriction site and decreasing the amounts of mRNA found on northern blotting. The other two are heterozygous for the 1303+1G-->A mutation and for either an 1831+2T-->G or a 2621-2A-->G splicing mutation. Of 235 anonymous Ashkenazi Jewish DNA samples, one was heterozygous for the 1303+1G-->A mutation. One seven-year-old boy of German/Swiss extraction was compound heterozygous for a 2729+1G-->C mutation, causing skipping of exon 14, and resulting in a C1329T missense (R396W), with decreased mRNA production. A 15-year-old Irish/English boy was heterozygous for an 89-bp insertion between exons 16 and 17 resulting from abnormal splicing; his fibroblast HPS3 mRNA is normal in amount but is increased in size. A 12-year-old girl of Puerto Rican and Italian background has the 3,904-bp founder deletion from central Puerto Rico on one allele. All eight patients have mild symptoms of HPS; two Jewish patients had received the diagnosis of ocular, rather than oculocutaneous, albinism. These findings expand the molecular diagnosis of HPS, provide a screening method for a mutation common among Jews, and suggest that other patients with mild hypopigmentation and decreased vision should be examined for HPS.  (+info)

Adaptor protein complex beta subunits are a group of proteins that play a crucial role in the formation and function of adaptor protein complexes (APCs). These complexes are involved in various cellular processes, including endocytosis, signal transduction, and vesicle trafficking. The beta subunits of APCs are characterized by their ability to bind to specific proteins, such as clathrin, and to interact with other components of the APC. They are typically composed of a single membrane-spanning domain and a cytoplasmic tail that contains a number of conserved motifs, including an SH3 domain and a phosphotyrosine-binding domain. In the medical field, defects in the genes encoding adaptor protein complex beta subunits have been linked to a number of diseases, including neurodevelopmental disorders, immunodeficiencies, and cancer. For example, mutations in the APBB1 gene, which encodes the beta-1 subunit of the adaptor protein complex 2 (AP-2), have been associated with the neurodegenerative disorder frontotemporal dementia. Similarly, mutations in the APBB2 gene, which encodes the beta-2 subunit of AP-2, have been linked to the development of certain types of cancer.

Adaptor Protein Complex 3 (AP-3) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: μ1A, μ1B, μ2A, and μ2B, which are encoded by different genes. AP-3 is involved in the sorting of cargo molecules destined for lysosomes, endosomes, and the plasma membrane. It recognizes specific sorting signals on the cargo molecules and mediates their binding to vesicles that transport them to their final destinations. Mutations in the genes encoding AP-3 subunits have been associated with several human diseases, including Hermansky-Pudlak syndrome, Chediak-Higashi syndrome, and a form of retinitis pigmentosa. These diseases are characterized by defects in the immune system, bleeding disorders, and vision problems, respectively.

Adaptor Protein Complex 1 (AP-1) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: AP-1A, AP-1B, AP-1C, and AP-1D, which are encoded by different genes. AP-1 is involved in the formation of coated vesicles, which are small vesicles that bud off from the plasma membrane and transport cargo to various cellular compartments. AP-1 recognizes specific signals on the cargo proteins and helps to sort them into the correct vesicles for transport. Disruptions in AP-1 function have been linked to a number of human diseases, including neurodegenerative disorders, lysosomal storage diseases, and cancer. Therefore, understanding the role of AP-1 in cellular trafficking is important for developing new treatments for these diseases.

Adaptor Protein Complex 2 (AP-2) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: alpha, beta, mu, and sigma, which together form a heterotetramer. AP-2 is involved in the recognition and sorting of cargo molecules destined for different cellular compartments, such as the plasma membrane, lysosomes, and endosomes. It recognizes specific sorting signals on the cargo molecules, such as tyrosine-based motifs, and binds to them through its alpha and beta subunits. Once bound to the cargo molecule, AP-2 recruits other proteins, such as clathrin, to form a coated pit on the plasma membrane. This coated pit then pinches off to form a vesicle that contains the cargo molecule, which is transported to its final destination within the cell. Disruptions in AP-2 function have been linked to various diseases, including neurodegenerative disorders, lysosomal storage diseases, and cancer.

Adaptor Protein Complex 4 (AP-4) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits, each with distinct functions, and is involved in the formation of vesicles that transport cargo from the Golgi apparatus to the plasma membrane or to other organelles within the cell. In the medical field, AP-4 is implicated in several diseases, including neurodegenerative disorders such as Parkinson's disease and Alzheimer's disease, as well as certain types of cancer. Mutations in the genes encoding AP-4 subunits have been linked to these conditions, suggesting that the proper functioning of AP-4 is essential for maintaining cellular health. Additionally, AP-4 has been proposed as a potential therapeutic target for the treatment of these diseases.

Adaptor protein complex subunits are proteins that are involved in the formation and function of adaptor protein complexes. These complexes play a crucial role in various cellular processes, including endocytosis, signal transduction, and vesicle trafficking. Adaptor protein complexes are composed of multiple subunits, each with a specific function. These subunits include adaptor proteins, which link the complexes to other proteins, and protein modules, which mediate specific protein-protein interactions. There are several types of adaptor protein complexes, including the AP-1, AP-2, and AP-3 complexes. These complexes are involved in the recognition and sorting of cargo molecules for transport to different cellular compartments, such as the plasma membrane, endosomes, and lysosomes. Disruptions in the function of adaptor protein complexes can lead to various diseases, including neurodegenerative disorders, lysosomal storage diseases, and immune system disorders. Therefore, understanding the structure and function of adaptor protein complexes is important for the development of new therapeutic strategies for these diseases.

Adaptor protein complex delta subunits are a group of proteins that are involved in the regulation of various cellular processes, including endocytosis, signal transduction, and vesicle trafficking. These proteins are part of a larger family of adaptor protein complexes, which are multi-subunit complexes that play a critical role in the sorting and transport of proteins and lipids within cells. The adaptor protein complex delta subunits are composed of several different proteins, including AP-1, AP-2, and AP-3. These proteins are characterized by the presence of a common set of domains, including a clathrin-binding domain, a membrane-binding domain, and a sorting motif. These domains allow the adaptor protein complex delta subunits to interact with other proteins and lipids within the cell, and to mediate the sorting and transport of specific cargo molecules. In the medical field, the adaptor protein complex delta subunits are of interest because they are involved in the regulation of several important cellular processes, including endocytosis and signal transduction. Mutations in the genes encoding these proteins have been linked to a number of human diseases, including neurodegenerative disorders, immune system disorders, and developmental disorders. As such, understanding the function and regulation of the adaptor protein complex delta subunits is an important area of ongoing research in the medical field.

Adaptor protein complex mu subunits, also known as AP-μ subunits, are a type of protein that plays a role in the sorting and transport of proteins and lipids within cells. They are part of a larger family of adaptor proteins called AP complexes, which are involved in the formation of vesicles that transport cargo between different compartments within cells. The AP-μ subunits are composed of four different proteins, each with a specific role in the vesicle formation process. These proteins are encoded by genes located on different chromosomes and are highly conserved across different species. Mutations in the genes encoding AP-μ subunits have been associated with a number of human diseases, including a type of inherited lysosomal storage disorder called Chediak-Higashi syndrome. This disorder is characterized by the accumulation of large, abnormal lysosomes within cells, which can lead to a range of symptoms including immune deficiency, bleeding disorders, and neurological problems.

Adaptor proteins, vesicular transport are a class of proteins that play a crucial role in the process of vesicular transport in cells. These proteins function as molecular adaptors that link cargo molecules to the vesicles that transport them within the cell. In vesicular transport, cargo molecules are packaged into vesicles and transported to their destination within the cell or to other cells. Adaptor proteins help to recognize and bind to specific cargo molecules, and then link them to the vesicles that will transport them. This process is essential for the proper functioning of cells, as it allows for the transport of a wide variety of molecules, including proteins, lipids, and carbohydrates. Adaptor proteins, vesicular transport are involved in a number of different types of vesicular transport, including endocytosis, exocytosis, and intracellular trafficking. They are also involved in the regulation of a number of cellular processes, including signal transduction and the regulation of gene expression. In the medical field, adaptor proteins, vesicular transport are the subject of ongoing research, as they play a critical role in many cellular processes and are involved in a number of diseases and disorders. For example, defects in adaptor proteins have been implicated in a number of neurological disorders, including Alzheimer's disease and Parkinson's disease. Additionally, alterations in the expression or function of adaptor proteins have been linked to a number of cancers, including breast cancer and prostate cancer.

Adaptor protein complex gamma subunits, also known as AP-3 subunits, are a group of proteins that play a crucial role in the sorting and transport of proteins within cells. These subunits are part of a larger protein complex called the adaptor protein complex 3 (AP-3), which is involved in the formation of vesicles that transport specific cargo from the Golgi apparatus to lysosomes or other cellular compartments. The AP-3 complex is composed of four subunits: mu1A, mu1B, sigma2, and mu2A. These subunits interact with each other to form a stable complex that recognizes specific sorting signals on the cargo proteins and mediates their transport to the appropriate cellular compartment. Mutations in the genes encoding AP-3 subunits have been associated with a number of human diseases, including Hermansky-Pudlak syndrome, Chediak-Higashi syndrome, and Griscelli syndrome. These disorders are characterized by defects in the immune system, bleeding disorders, and other abnormalities, and are thought to result from impaired trafficking of specific proteins within cells.

Adaptor protein complex (AP) alpha subunits are a group of proteins that play a crucial role in the endocytic pathway of cells. These proteins are part of a larger protein complex called the AP-1 complex, which is involved in the sorting and transport of membrane proteins from the trans-Golgi network to endosomes. The AP-1 complex is composed of four subunits: alpha, beta, mu, and sigma. The alpha subunit is the largest subunit and is responsible for recognizing and binding to specific sorting signals on membrane proteins. There are four different isoforms of the alpha subunit, each of which is specific to a different subset of membrane proteins. The AP-1 complex is essential for the proper functioning of the endocytic pathway, which is responsible for the internalization and recycling of membrane proteins and lipids. Mutations in the genes encoding the AP-1 complex alpha subunits have been linked to a number of human diseases, including Hermansky-Pudlak syndrome and Chediak-Higashi syndrome.

Adaptor proteins, signal transducing are a class of proteins that play a crucial role in transmitting signals from the cell surface to the interior of the cell. These proteins are involved in various cellular processes such as cell growth, differentiation, and apoptosis. Adaptor proteins function as molecular bridges that connect signaling receptors on the cell surface to downstream signaling molecules inside the cell. They are characterized by their ability to bind to both the receptor and the signaling molecule, allowing them to transmit the signal from the receptor to the signaling molecule. There are several types of adaptor proteins, including SH2 domain-containing adaptor proteins, phosphotyrosine-binding (PTB) domain-containing adaptor proteins, and WW domain-containing adaptor proteins. These proteins are involved in a wide range of signaling pathways, including the insulin, growth factor, and cytokine signaling pathways. Disruptions in the function of adaptor proteins can lead to various diseases, including cancer, diabetes, and immune disorders. Therefore, understanding the role of adaptor proteins in signal transduction is important for the development of new therapeutic strategies for these diseases.

Clathrin is a protein that plays a crucial role in the process of endocytosis, which is the process by which cells take in substances from their environment. Clathrin forms a lattice-like structure that surrounds and helps to shape the plasma membrane as it buds inward to form a vesicle. This vesicle then pinches off from the plasma membrane and is transported into the cell, where it can be processed and used by the cell. Clathrin is also involved in the transport of certain molecules within the cell, such as the transport of proteins from the Golgi apparatus to the plasma membrane. In the medical field, clathrin is often studied in relation to diseases such as cancer, where it has been implicated in the formation of abnormal blood vessels and the spread of cancer cells.

Monomeric clathrin assembly proteins (mCAPs) are a group of proteins that play a crucial role in the assembly of clathrin-coated vesicles in the endocytic pathway. Clathrin-coated vesicles are small membrane-bound structures that are involved in the internalization of proteins and other molecules from the cell surface into the cell interior. mCAPs are monomeric proteins that interact with clathrin and other components of the endocytic machinery to promote the assembly of clathrin lattices on the membrane. They are thought to function by stabilizing the clathrin triskelion, which is the basic building block of the clathrin lattice, and by facilitating the assembly of additional triskelia into a lattice. mCAPs are found in a variety of organisms, including humans, and are involved in a wide range of cellular processes, including endocytosis, intracellular trafficking, and signal transduction. Mutations in mCAP genes have been linked to a number of human diseases, including neurodegenerative disorders and immune system disorders.

In the medical field, a protein subunit refers to a smaller, functional unit of a larger protein complex. Proteins are made up of chains of amino acids, and these chains can fold into complex three-dimensional structures that perform a wide range of functions in the body. Protein subunits are often formed when two or more protein chains come together to form a larger complex. These subunits can be identical or different, and they can interact with each other in various ways to perform specific functions. For example, the protein hemoglobin, which carries oxygen in red blood cells, is made up of four subunits: two alpha chains and two beta chains. Each of these subunits has a specific structure and function, and they work together to form a functional hemoglobin molecule. In the medical field, understanding the structure and function of protein subunits is important for developing treatments for a wide range of diseases and conditions, including cancer, neurological disorders, and infectious diseases.

Hermanski-Pudlak Syndrome (HPS) is a rare genetic disorder that affects the body's ability to produce certain proteins that are necessary for the proper functioning of the immune system, as well as for the formation of certain structures in the eye and skin. It is caused by mutations in the HPS1, HPS2, or HPS3 genes, which are located on different chromosomes. Symptoms of HPS can vary widely depending on the specific type of the disorder and the severity of the mutations. Common symptoms include vision problems, such as decreased visual acuity and night blindness, as well as skin abnormalities, such as light-colored spots on the skin and abnormal pigmentation. Other symptoms may include bleeding disorders, immune system problems, and developmental delays. There is currently no cure for HPS, but treatment is focused on managing the symptoms and complications of the disorder. This may include medications to treat bleeding disorders, surgery to correct vision problems, and supportive care to manage other symptoms.

In the medical field, "Analytic Chemistry" refers to the branch of chemistry that deals with the measurement and identification of the chemical components of biological samples, such as blood, urine, and tissue. Analytical chemistry is used to determine the concentration of various substances in a sample, including drugs, hormones, and toxins, and to identify the presence of specific molecules or compounds. Analytical chemistry techniques used in the medical field include chromatography, mass spectrometry, spectroscopy, and immunoassays. These techniques allow for the precise measurement and identification of specific molecules in biological samples, which is essential for the diagnosis and treatment of diseases. In addition to its role in disease diagnosis and treatment, analytical chemistry is also used in drug development, quality control of pharmaceuticals, and environmental monitoring. Overall, analytical chemistry plays a critical role in advancing medical research and improving patient care.

"Entrez Gene: AP3B1 adaptor-related protein complex 3, beta 1 subunit". GeneReviews/NCBI/NIH/UW entry on Hermansky-Pudlak ... AP-3 complex subunit beta-1 is a protein that in humans is encoded by the AP3B1 gene. This gene encodes a protein that may play ... The encoded protein is part of the heterotetrameric AP-3 protein complex which interacts with the scaffolding protein clathrin ... trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor". ...
"Entrez Gene: AP3B2 adaptor-related protein complex 3, beta 2 subunit". Human AP3B2 genome location and AP3B2 gene details page ... AP-3 complex subunit beta-2 is a protein that in humans is encoded by the AP3B2 gene. GRCm38: Ensembl release 89: ... 1997). "AP-3: an adaptor-like protein complex with ubiquitous expression". EMBO J. 16 (5): 917-28. doi:10.1093/emboj/16.5.917. ... Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS (1998). "Association of the AP-3 adaptor complex with clathrin". ...
"Entrez Gene: AP2B1 adaptor-related protein complex 2, beta 1 subunit". Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, ... AP-2 complex subunit beta is a protein that in humans is encoded by the AP2B1 gene. The protein encoded by this gene is one of ... Gallusser A, Kirchhausen T (Dec 1993). "The beta 1 and beta 2 subunits of the AP complexes are the clathrin coat assembly ... Kim YM, Benovic JL (Aug 2002). "Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein- ...
AP-1 complex subunit beta-1 is a protein that in humans is encoded by the AP1B1 gene. Adaptor protein complex 1 is found at the ... "Entrez Gene: AP1B1 adaptor-related protein complex 1, beta 1 subunit". Nakagawa, T; Setou M; Seog D; Ogasawara K; Dohmae N; ... The protein encoded by this gene serves as one of the large subunits of this complex and is a member of the adaptin protein ... 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using ...
AP-4 complex subunit beta-1 is a protein that in humans is encoded by the AP4B1 gene. The heterotetrameric adaptor protein (AP ... "Entrez Gene: AP4B1 adaptor-related protein complex 4, beta 1 subunit". Hirst J, Bright NA, Rous B, Robinson MS (August 1999). " ... 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using ... PDBe-KB provides an overview of all the structure information available in the PDB for Human AP-4 complex subunit beta-1 Hirst ...
The family routinely lies on the clathrin adaptor complex 3 beta-1 subunit proteins. The exact function of DUF 1682 is unclear ... The final protein is thought to be translated from the endoplasmic reticulum into the cytoplasm of the cell. The protein is ... The portion of the protein which extends into the cytosol is predicted to be highly phosphorylated as the protein's ... cAMP-responsive element binding protein (CREB), PAR b ZIP family and Sp4 Transcription Factor. NRF1 encodes a protein which ...
... either directly or through adaptor proteins. This gene encodes an alpha subunit of the heteromeric SEC61 complex, which also ... contains beta and gamma subunits. GRCh38: Ensembl release 89: ENSG00000058262 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... Protein transport protein Sec61 subunit alpha isoform 1 is a protein that in humans is encoded by the SEC61A1 gene. The protein ... 2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi: ...
This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles ... alpha or beta), a medium adaptin (mu), and a small adaptin (sigma). The complex is part of the protein coat on the cytoplasmic ... "Entrez Gene: AP2A1 adaptor-related protein complex 2, alpha 1 subunit". Nishimura, Takashi; Fukata Yuko; Kato Katsuhiro; ... Adaptor-related protein complex 2, alpha 1 has been shown to interact with DPYSL2 and NUMB. GRCh38: Ensembl release 89: ...
In molecular biology, the adaptor complexes medium subunit domain is a protein domain found at the C-terminus of the mu subunit ... The C-terminal domain has an immunoglobulin-like beta-sandwich fold consisting of 9 strands in 2 sheets with a Greek key ... "Study of the interaction of the medium chain mu 2 subunit of the clathrin-associated adapter protein complex 2 with cytotoxic T ... "Bivalent Motif-Ear Interactions Mediate the Association of the Accessory Protein Tepsin with the AP-4 Adaptor Complex". The ...
AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). ... beta-1-adaptin, mu-1 and sigma-1, while in AP2 they are alpha-adaptin, beta-2-adaptin, mu-2 and sigma-2. Each subunit has a ... Adaptor protein (AP) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ...
Adaptor related protein complex 2 subunit beta (AP2B1) helps establish a link between clathrin and receptors in coated vesicles ... c12orf71 protein has been found to be present in a protein-protein interaction (PPI) network of the Carboxypeptidase M (CPM) ... c12orf71 protein is 269 amino acids long and the unmodified precursor protein has a predicted molecular weight of 30.4 kDa and ... c12orf71 protein has multiple predicted phosphorylation sites, which can have an impact on the protein interactions and sub- ...
Adaptins are clustered subunits of adaptor protein (AP) complexes. There are several types of adaptin, each related to a ... beta and one other depending on the complex), a medium adaptin (mu), and a small adaptin (sigma): complex 1 AP1B1 AP1G1 AP1G2 ... 2011). "The Fifth Adaptor Protein Complex". PLOS Biology. 9 (10): e1001170. doi:10.1371/journal.pbio.1001170. PMC 3191125. PMID ... Clathrin adaptor proteins, also known as adaptins, are proteins that mediate the formation of vesicles for intracellular ...
... and some of the adapter proteins, such as talin, paxillin and tensin. Many of these focal complexes fail to mature and are ... Integrins are heterodimers which are formed from one beta and one alpha subunit. These subunits are present in different forms ... bind to and associate with this integrin-adapter protein-cytoskeleton complex, and this forms the basis of a focal adhesion. ... However, some focal complexes mature into larger and stable focal adhesions, and recruit many more proteins such as zyxin. ...
... an adaptor or scaffolding protein by permitting the recruitment of the inhibitor of nuclear factor-kappa-B kinase subunit beta ... The link between these two protein within the JAK1-SNX8 complex allows JAK1 to catalyse SNX8's tyrosines phosphorylation in ... are involved in protein-protein interactions. The SNX8 protein, even though is very similar to the other sorting nexins, ... It is suggested that it acts as an adaptor protein in events related to immune response and cholesterol regulation, for example ...
"Entrez Gene: AP2M1 adaptor-related protein complex 2, mu 1 subunit". Follows ER, McPheat JC, Minshull C, Moore NC, Pauptit RA, ... "Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, ... AP-2 complex subunit mu is a protein that in humans is encoded by the AP2M1 gene. This gene encodes a subunit of the ... heterotetrameric coat assembly protein complex 2 (AP2), which belongs to the adaptor complexes medium subunits family. The ...
The protein encoded by this gene is the medium subunit of AP-3, which is an adaptor-related protein complex associated with the ... trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor". ... "Entrez Gene: AP3M1 adaptor-related protein complex 3, mu 1 subunit". Human AP3M1 genome location and AP3M1 gene details page in ... 2000). "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based ...
AP-4 complex subunit sigma-1 is a protein that in humans is encoded by the AP4S1 gene. The heterotetrameric adaptor protein (AP ... AP4 is composed of 2 large chains, beta-4 (AP4B1) and epsilon-4 (AP4E1), a medium chain, mu-4 (AP4M1), and a small chain, sigma ... "Entrez Gene: adaptor-related protein complex 4". Abou Jamra R, Philippe O, Raas-Rothschild A, Eck SH, Graf E, Buchert R, Borck ... Hirst J, Bright NA, Rous B, Robinson MS (1999). "Characterization of a fourth adaptor-related protein complex". Mol. Biol. Cell ...
AP-4 complex subunit epsilon-1 is a protein that in humans is encoded by the AP4E1 gene. The heterotetrameric adaptor protein ( ... AP4 is composed of 2 large chains, beta-4 (AP4B1) and epsilon-4 (AP4E1; this gene), a medium chain, mu-4 (AP4M1), and a small ... 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using ... "Entrez Gene: adaptor-related protein complex 4". Abou Jamra R, Philippe O, Raas-Rothschild A, Eck SH, Graf E, Buchert R, Borck ...
... and two smaller proteins. One of the large proteins is termed β (beta), with β1 in the AP-1 complex, β2 in the AP-2 complex, ... The two smaller proteins are a medium subunit named μ (mu ~50 kD) and a small subunit σ (sigma ~20 kD), and named 1 through 5 ... Most of the adaptor proteins are heterotetramers. In the AP complexes, there are two large proteins (~100 kD) ... Vesicular transport adaptor proteins are proteins involved in forming complexes that function in the trafficking of molecules ...
Kato Y, Habas R, Katsuyama Y, Näär AM, He X (Aug 2002). "A component of the ARC/Mediator complex required for TGF beta/Nodal ... Abraham S, Solomon WB (Sep 2000). "A novel glutamine-rich putative transcriptional adaptor protein (TIG-1), preferentially ... "A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology". Molecular ... "Entrez Gene: PCQAP PC2 (positive cofactor 2, multiprotein complex) glutamine/Q-rich-associated protein". Suzuki Y, Nogi Y, Abe ...
"Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery". ... Geyer M, Fackler OT, Peterlin BM (Jun 2002). "Subunit H of the V-ATPase involved in endocytosis shows homology to beta-adaptins ... The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain ... The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit ...
AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... a medium subunit (mu) and a small subunit (sigma). For example, in AP1 these subunits are gamma-1-adaptin, beta-1-adaptin, mu-1 ... The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ...
AP-5 complex subunit beta (AP5B1) is a protein that in humans is encoded by the AP5B1 gene. The protein encoded by this gene is ... In addition, damaging variants in the genes encoding two proteins that stably associate with the AP-5 adaptor complex are also ... Hirst, Jennifer; Irving, Carol; Borner, Georg H. H. (2012-11-21). "Adaptor protein complexes AP-4 and AP-5: new players in ... "The fifth adaptor protein complex". PLOS Biology. 9 (10): e1001170. doi:10.1371/journal.pbio.1001170. ISSN 1545-7885. PMC ...
... the plasma membrane the TCR receptor chains α and β associate with six additional adaptor proteins to form an octameric complex ... and beta (β) chains expressed as part of a complex with the invariant CD3 chain molecules. T cells expressing this receptor are ... The two main subunits of TCR (α- and β-chains) are twisted together. CD3 and zeta subunits are required to carry out the signal ... LAT associates with another scaffolding protein Slp-76 via the Grap2 adaptor protein, which provides additional binding sites. ...
... encoding protein Beta-soluble NSF attachment protein NDUFAF5: encoding protein NADH:ubiquinone oxidoreductase complex assembly ... encoding protein Serine incorporator 3 SHLD1: encoding protein Shieldin complex subunit 1 SLC17A9: encoding protein Solute ... encoding protein Kizuna centrosomal protein Kua-UEV: LIME1: encoding protein Lck-interacting transmembrane adapter 1 LZTS3: ... encoding protein Zinc finger protein 334 ZNF343: encoding protein Zinc finger protein 343 ZSWIM3: encoding protein Zinc finger ...
The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. This ... beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex ... "Entrez Gene: AP1G2 adaptor-related protein complex 1, gamma 2 subunit". Rost, Martina; Döring Tatjana; Prange Reinhild (Nov ... AP-1 complex subunit gamma-like 2 is a protein that in humans is encoded by the AP1G2 gene. Adaptins are important components ...
The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. Two ... beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex ... "Entrez Gene: AP1G1 adaptor-related protein complex 1, gamma 1 subunit". Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999 ... "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three- ...
"Entrez Gene: AP1M1 adaptor-related protein complex 1, mu 1 subunit". Hinners I, Wendler F, Fei H, Thomas L, Thomas G, Tooze SA ... The other components of this complex are beta-prime-adaptin, gamma-adaptin, and the small chain AP1S1. This complex is located ... AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene. The protein encoded by this gene is the ... Page LJ, Robinson MS (Nov 1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". The Journal ...
... of rRNA processing Protein Phosphorylation Ribosomal small subunit biogenesis RIOK1 is the only component of the PRMT5 complex ... used as a basis for synthesis of a macrocyclic inhibitor of protein-protein interactions between PRMT5 and its adaptor proteins ... and 7 beta strands (blue) (Protein Data Bank in Europe ) RIOK1 belongs to the serine/threonine-specific protein kinase family ... 6:7,389,496-7,418,037) Effects on modified protein - protein degradation, triggered by K411-m1; protein stabilization, ...
2001). "The Transmembrane Adaptor Protein Trim Regulates T Cell Receptor (Tcr) Expression and Tcr-Mediated Signaling via an ... "The implications of subunit interactions for the structure of the T cell receptor-CD3 complex". Eur. J. Immunol. 20 (2): 299- ... 1985). "Analysis of cDNA clones specific for human T cells and the alpha and beta chains of the T-cell receptor heterodimer ... v t e (Articles with short description, Short description matches Wikidata, Human genes, Proteins, All stub articles, Protein ...
"Entrez Gene: AP3B1 adaptor-related protein complex 3, beta 1 subunit". GeneReviews/NCBI/NIH/UW entry on Hermansky-Pudlak ... AP-3 complex subunit beta-1 is a protein that in humans is encoded by the AP3B1 gene. This gene encodes a protein that may play ... The encoded protein is part of the heterotetrameric AP-3 protein complex which interacts with the scaffolding protein clathrin ... trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor". ...
Name: adaptor-related protein complex 3, beta 1 subunit. Synonyms: rim2, recombination induced mutation 2, Hps2, beta3A, AP-3 ...
603401 Adaptor-related protein complex 3, beta-1 subunit; AP3B1. Cross references. Phenotypically related immunodeficiencies. ...
... a wiki resource centered on human protein-protein interactions ... adaptor related protein complex 2 subunit beta 1. SMAD family ... Positive Regulation Of Transforming Growth Factor Beta Receptor Signaling Pathway. *Positive Regulation Of BMP Signaling ...
Autosomal-Recessive Mutations in AP3B2, Adaptor-Related Protein Complex 3 Beta 2 Subunit, Cause an Early-Onset Epileptic ...
BCKDHB: branched chain keto acid dehydrogenase E1 subunit beta. *BCOR: BCL6 corepressor ... BMPR1A: bone morphogenetic protein receptor type 1A. *BMPR2: bone morphogenetic protein receptor type 2 ... BCS1L: BCS1 homolog, ubiquinol-cytochrome c reductase complex chaperone. *BDNF: brain derived neurotrophic factor ... BICD2: BICD cargo adaptor 2. *BIN1: bridging integrator 1. *BLM: BLM RecQ like helicase ...
Late endosomal/lysosomal adaptor, MAPK and MTOR activator 2. 0.8810. 29. AP2S1. Adaptor related protein complex 2 subunit sigma ... Thymosin beta 10. Predicted locationi All transcripts of all genes have been analyzed regarding the location(s) of ... The Human Protein Atlas project is funded. by the Knut & Alice Wallenberg Foundation. ... DNA polymerase epsilon 4, accessory subunit. 0.9048. 29. GCNT2. Glucosaminyl (N-acetyl) transferase 2 (I blood group). 0.9048. ...
Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter protein coupling the receptor to ... Subunit:. Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. ... Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Isoform 2 may act as an antagonist of ... The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. ...
... either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS ... Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex. ... the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm ... The protein encoded by this gene is a member of the importin beta family. Two transcript variants encoding different isoforms ...
NOP16 nucleolar protein [Source:HG.... NPRL3. 8131. NPRL3. NPR3 like, GATOR1 complex subunit .... ... adaptor related protein complex 4 .... ATR. 545. ATR. ATR serine/threonine kinase [Sourc.... ... syntrophin beta 1 [Source:HGNC Sym.... SPRYD4. 283377. SPRYD4. SPRY domain containing 4 [Source:H.... ... nucleolar protein 9 [Source:HGNC S.... NOP16. 51491. NOP16. ... F-box protein 28 [Source:HGNC Symb.... FBXO3. 26273. FBXO3. F- ...
Following signaling via the BCR, protein kinase C (PKC) beta-dependent serine phosphorylation within the CARD11 linker domain ... 20] Upon antigen stimulation, clustering of the BCRs occurs, leading to signal transduction via the CD79A and B subunits. [21] ... 15] The CBM complex is required for activation of the classic NFkB pathway downstream of the antigen receptors in B and T cells ... 16] CARD11 is a multidomain signaling adapter that contains (1) an amino-terminal CARD and coiled-coil domains, (2) an ...
Adaptor Protein Complex gamma Subunits 100% * Adaptor Protein Complex alpha Subunits 99% ... Molecular evolution of extended spectrum beta-lactam resistance. Gaszek, I. K., Kantarcioglu, I., Yildiz, M. S., Sari, L., ... Impact of Asp/Glu-ADP-ribosylation on protein-protein interaction and protein function. Pei, J., Zhang, J., Wang, X. D., Kim, C ... Recent advances in predicting and modeling protein-protein interactions. Durham, J., Zhang, J., Humphreys, I. R., Pei, J. & ...
Further characterization of the FE65-Mena complex may identify a physiological role for these proteins in beta-amyloid ... To understand the function of this adapter protein, we identified binding partners for the FE65 WW domain. Proline-rich ... By Far-Western blotting and yeast two-hybrid assay, we demonstrate that p45, the large subunit of NF-E2, is capable of binding ... The rsp5 protein is thought to interact with nuclear proteins but also contains a C2 domain typical for cytoplasmic proteins. ...
Vesicular TransportAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex 1AuxilinsAdaptor Protein Complex beta Subunits ... Shock ProteinsDynaminsAdaptor Protein Complex mu SubunitsAdaptor Protein Complex gamma SubunitsAdaptor Protein Complex 3Protein ... Heat-Shock ProteinsDynaminsAdaptor Protein Complex mu SubunitsAdaptor Protein Complex gamma SubunitsAdaptor Protein Complex 3 ... ProteinsPhosphoproteinsRecombinant Fusion ProteinsAdaptor Protein Complex sigma SubunitsCarrier ProteinsAdaptor Protein Complex ...
Activation of the Arp2/3 complex by the Listeria acta protein. Acta binds two actin monomers and three subunits of the Arp2/3 ... The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck. Antón, I.M., Lu, W., Mayer, B. ... Plant profilin induces actin polymerization from actin : beta-thymosin complexes and competes directly with beta-thymosins and ... Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and ...
The inflammasome is a large multiprotein complex which plays a key role in innate immunity by participating in the production ... It comprises the NLR protein NLRP3, the adapter ASC and pro-caspase-1. The general consensus is that maturation and release of ... The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol. 9(8):857-65.. 7. Dostert C. et ... The inflammasome is a large multiprotein complex which plays a key role in innate immunity by participating in the production ...
Human AP2m1(Adaptor Related Protein Complex 2 Mu 1) ELISA Kit. *Human APLP1(Amyloid Beta Precursor Like Protein 1) ELISA Kit ... Human ARHGDIb(Rho GDP Dissociation Inhibitor Beta) ELISA Kit. *Human ARPC2(Actin Related Protein 2/3 Complex Subunit 2) ELISA ... Human PPM1A(Protein Phosphatase, Mg2+/Mn2+ Dependent 1A) ELISA Kit. *Human PPP1R1B(Protein Phosphatase 1, Regulatory Subunit 1B ... Human PTPLA(Protein Tyrosine Phosphatase Like Protein A) ELISA Kit. *Human PTPN1(Protein Tyrosine Phosphatase, Non Receptor ...
CADASIL is reviewed by kinase and protein of tyrosine-based viral complex tumors from the P2 DNA, having taken ions to an ... Most linkages are post-translational absence creating from 17-beta-hydroxysteroid beta actin to asymmetric Recent gain. ... REV1( maturation) leaves a spherical cilium subunit that can refer a C bubble opposite an complex transport( Lin et al. ... Interaction with many PCNA at a DNA adaptor chromosome plays particular formation route( TLS)( Garg and Burgers 2005, Wood et ...
Hermansky-Pudlak syndrome-associated genes participate in at least 4 distinct protein complexes: the adaptor complex AP-3; BLOC ... Because the expression of the beta-3A subunit is normally ubiquitous, deficiency of the beta-3A subunit leads to a precise ... HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex (AP3BA), which ... Badolato R, Parolini S. Novel insights from adaptor protein 3 complex deficiency. J Allergy Clin Immunol. 2007 Oct. 120(4):735- ...
... mitochondrial ribosomal proteins (MRPS27, MRPS9, MRPS31), and DNA replication and repair (WRN). Those up-regulated in MP > 3 ... cows encoded immune defence proteins (LYZ, CTSZ, SREBF1, GRN, ANXA5, ADARB1). Genes and pathways associated with lactation ... Another cluster included genes encoding enzymes in the mitochondrial beta-oxidation pathway. Top clusters up-regulated in MP & ... These genes encode late endosomal/lysosomal adaptor, MAPK and MTOR activator-1, − 2 and − 3 respectively, all subunits of the ...
... and other scaffolding and adaptor proteins may also bind and help localize the AChR. To identify protein interaction domain(s) ... 2007) Synaptic differentiation is defective in mice lacking acetylcholine receptor beta-subunit tyrosine phosphorylation. ... Alternatively, another muscle protein might form a tertiary complex with rapsyn and the β loop and mediate their ... only those containing the intracellular loop of the β subunit loop were observed to cluster. The CD4-β subunit protein ...
Protein Kinase A, RII beta Subunit MH - G-Protein-Coupled Receptor Kinases UI - D054768 MN - D08.811.913.696.620.682.700.364 MN ... The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the ... A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A ... HN - 2008 BX - Protein Kinase A, Catalytic Subunits MH - Cyclic AMP-Dependent Protein Kinase RIalpha Subunit UI - D054756 MN - ...
Protein Kinase A, RII beta Subunit MH - G-Protein-Coupled Receptor Kinases UI - D054768 MN - D08.811.913.696.620.682.700.364 MN ... The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the ... A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A ... HN - 2008 BX - Protein Kinase A, Catalytic Subunits MH - Cyclic AMP-Dependent Protein Kinase RIalpha Subunit UI - D054756 MN - ...
Protein Kinase A, RII beta Subunit MH - G-Protein-Coupled Receptor Kinases UI - D054768 MN - D08.811.913.696.620.682.700.364 MN ... The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the ... A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A ... HN - 2008 BX - Protein Kinase A, Catalytic Subunits MH - Cyclic AMP-Dependent Protein Kinase RIalpha Subunit UI - D054756 MN - ...
Protein Kinase A, RII beta Subunit MH - G-Protein-Coupled Receptor Kinases UI - D054768 MN - D08.811.913.696.620.682.700.364 MN ... The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the ... A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A ... HN - 2008 BX - Protein Kinase A, Catalytic Subunits MH - Cyclic AMP-Dependent Protein Kinase RIalpha Subunit UI - D054756 MN - ...
FRET Reveals Novel Protein-Receptor Interaction of Bone Morphogenetic Proteins Receptors and Adaptor Protein 2 at the Cell ... Bone Morphogenetic Proteins (BMPs) are potent growth factors belonging to the Transforming Growth Factor Beta superfamily. To ... Casein Kinase 2 β-Subunit Is a Regulator of Bone Morphogenetic Protein 2 Signaling ... They signal through a hetero-oligomer complex of BMP receptors. Binding of the ligand to the receptors activates several ...
Hermansky-Pudlak syndrome-associated genes participate in at least 4 distinct protein complexes: the adaptor complex AP-3; BLOC ... Because the expression of the beta-3A subunit is normally ubiquitous, deficiency of the beta-3A subunit leads to a precise ... HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex (ADTB3A), which ... Badolato R, Parolini S. Novel insights from adaptor protein 3 complex deficiency. J Allergy Clin Immunol. 2007 Oct. 120(4):735- ...
... is the response of activity details as cholesterol protein from the complexes of JJ proteins. The atypical four constituents of ... is the ligand of rate processes in the er of the killer intermediate promoter beta in autosomal box, in the adapter of the ... immigrants that are secretory levels for Runx2 and Runx3 are a different subunit of complex development and, thus, several form ... The proteins by which rough kinase is introduced to coli and these serve illuminated up from the lysine complex into people ...
This enzyme is part of a complex of 3 electron-transporting proteins (methylamine dehydrogenase, blue copper protein amicyanin ... "dolichyl-phosphate-mannose-protein" and "1,3-beta-glucan synthase" found in T1 could be involved in the modulation of β-D- ... The second taxonomic analysis was based on the 16S and 18S ribosomal subunits. Using the reads merged by FLASH, the ribosomal ... Martin, M. (2011). Cutadapt removes adapter sequences from high-throughput sequencing reads. EMBnet J. 17, 1-10. doi: 10.14806/ ...
  • They preferentially bind and release hydrophobic peptides by an ATP-dependent process and are involved in post-translational PROTEIN TRANSLOCATION. (lookformedical.com)
  • This protein is a receptor for members of the epidermal growth factor family. (bioss.com.cn)
  • Binding of the protein to a ligand induces receptor dimerization and tyrosine autophosphorylation and leads to cell proliferation. (bioss.com.cn)
  • The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. (bioss.com.cn)
  • Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. (bioss.com.cn)
  • an adapter protein coupling the receptor to downstream signaling pathways. (bioss.com.cn)
  • Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. (nih.gov)
  • G protein-coupled receptor 155 [So. (gsea-msigdb.org)
  • POLK and POLZ have in the receptor of proteins reused multiple to such anions by POLK. (erik-mill.de)
  • At the neuromuscular junction, the acetylcholine receptor (AChR) is specifically clustered in the postsynaptic membrane via interactions with rapsyn and other scaffolding proteins. (jneurosci.org)
  • Together, these findings suggest that agrin-induced phosphorylation of the β subunit motif increases the stoichiometry of rapsyn binding to the AChR, thereby helping to stably cluster the receptor and anchor it at high density in the postsynaptic membrane. (jneurosci.org)
  • ELAC1 has been in the use and may as define as an RNase Z. In pyrophosphates subfamilies are transcribed from coupling tubules in the function by a two receptor chromatin that appears ultraviolet from protein threatening( reviewed in Popow et al. (evakoch.com)
  • Ligand binding to a receptor leads to the recruitment and activation of an IKK complex comprising IKK alpha and/or IKK beta catalytic subunits and two molecules of NEMO. (abcam.com)
  • In the canonical signaling pathway , binding of a ligand to a cell surface receptor such as a member of the Toll-like receptor superfamily leads to the recruitment of adaptors (such as TRAF) to the cytoplasmic domain of the receptor (Figure 1). (abcam.com)
  • The impaired function of specific organelles indicates that the causative genes encode protein complexes that regulate vesicle trafficking in the endolysosomal system including AP-3, BLOC-1, BLOC-2, and BLOC-3. (medscape.com)
  • Another cluster included genes encoding enzymes in the mitochondrial beta-oxidation pathway. (biomedcentral.com)
  • Differentially expressed candidate genes for ageing previously identified in the human blood transcriptome up-regulated in PP cows were mainly associated with T-cell function ( CCR7 , CD27 , IL7R , CAMK4 , CD28 ), mitochondrial ribosomal proteins ( MRPS27 , MRPS9 , MRPS31 ), and DNA replication and repair ( WRN ). (biomedcentral.com)
  • The impaired function of specific organelles indicates that the causative genes encode proteins operative in the formation of lysosomes and vesicles. (medscape.com)
  • Mapping of the genes encoding human protein matches to pathways point to targets that could explain the observed presentation of symptoms in COVID-19 disease. (danielsolis.cz)
  • AP-3 complex subunit beta-1 is a protein that in humans is encoded by the AP3B1 gene. (wikipedia.org)
  • This gene encodes a protein that may play a role in organelle biogenesis associated with melanosomes, platelet dense granules, and lysosomes. (wikipedia.org)
  • The beta3A subunit gene (Ap3b1) of the AP-3 adaptor complex is altered in the mouse hypopigmentation mutant pearl, a model for Hermansky-Pudlak syndrome and night blindness" (PDF). (wikipedia.org)
  • The protein encoded by this gene is a transmembrane glycoprotein that is a member of the protein kinase superfamily. (bioss.com.cn)
  • Multiple alternatively spliced transcript variants that encode different protein isoforms have been found for this gene. (bioss.com.cn)
  • Description of the protein which includes the UniProt Function and the NCBI Gene Summary. (nih.gov)
  • HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex ( AP3BA ), which assists in the vesicle formation from the trans-Golgi network or late endosome. (medscape.com)
  • HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex (ADTB3A), which resides on chromosome 5. (medscape.com)
  • other specificity is tiny gene activity and distribution browser through the kinase of the R-RasGAP complex ileal to suitable or through the functionality of RhoA. (evakoch.com)
  • This enables the active NF-κB transcription factor subunits to translocate to the nucleus and induce target gene expression. (abcam.com)
  • NF-κB activation leads to expression of the IκBα gene, which functions as a negative feedback loop to sequester NF-κB subunits, terminating signaling unless a persistent activation signal is present. (abcam.com)
  • After the XPC p16-INK4A and the UV-DDB hemolytic digestion substituted DNA, a separate localization adaptor TFIIH controls identified to the subunit recycling ubiquitin( many) dephosphorylation( Volker et al. (evakoch.com)
  • Ubiquitylation describes the covalent attachment of a small 76-amino acid protein, ubiquitin, to other proteins. (ddw-online.com)
  • A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane. (lookformedical.com)
  • Indeed, we have shown previously that mutation of a tyrosine phosphorylation site in the long cytoplasmic loop of the β subunit impairs agrin-induced cytoskeletal anchoring and aggregation of mutant AChR in muscle cells ( Borges and Ferns, 2001 ). (jneurosci.org)
  • Phosphorylation of the AChR β subunit is correlated with increased rapsyn/AChR binding, suggesting that the effect of βY390 phosphorylation on clustering is mediated by rapsyn. (jneurosci.org)
  • These adaptors in turn recruit the IKK complex, which leads to phosphorylation and degradation of the IκB inhibitor. (abcam.com)
  • L ike protein phosphorylation by kinases, protein ubiquitylation regulates many aspects of cell function and provides a wealth of drug target opportunities across many therapeutic areas including cancer, cardiovascular, metabolism, inflammation, neurodegeneration and infectious diseases. (ddw-online.com)
  • The encoded protein is part of the heterotetrameric AP-3 protein complex which interacts with the scaffolding protein clathrin. (wikipedia.org)
  • Moreover, FBP21 interacts directly with the U1 snRNP protein U1C, the core snRNP proteins SmB and SmB', and the branchpoint binding protein SF1/mBBP. (embl.de)
  • It interacts directly with MTOR to enhance its kinase activity and stabilizes the MTOR-RPTOR PROTEIN interaction in nutrient-poor conditions, favoring RPTOR inhibition of MTOR activity. (bvsalud.org)
  • The heavy chain subunits of clathrin. (lookformedical.com)
  • A subclass of clathrin assembly proteins that occur as monomers. (lookformedical.com)
  • The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN. (lookformedical.com)
  • Specialized regions of the cell membrane composed of pits coated with a bristle covering made of the protein CLATHRIN. (lookformedical.com)
  • An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE. (lookformedical.com)
  • A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK. (lookformedical.com)
  • The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS. (lookformedical.com)
  • A family of proteins that play a role as cofactors in the process of CLATHRIN recycling in cells. (lookformedical.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in tissue homogenates, cell lysates and other biological fluids. (1elisakits.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (1elisakits.com)
  • This download is the types and cells led from a human assembly target content soccer methylated alongside the set of two interaction localizing enzyme proteins in New Zealand. (evakoch.com)
  • The muscle AChR is a pentamer of homologous subunits, with the stoichiometry α(2), β, δ and γ (fetal) or ε (adult) subunits. (jneurosci.org)
  • SAR-CoV-2 spike proteins, and all other SARS-CoV-2 proteins, immunogenic epitopes in each SARS-CoV-2 protein were compared to human proteins in search of high local homologous matching. (danielsolis.cz)
  • If all of the parts of the epitopes that are homologous to human proteins are excluded from consideration due to risk of pathogenic priming, the remaining immunogenic parts of the epitopes may be still immunogenic and remain as potentially viable candidates for vaccine development. (danielsolis.cz)
  • Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported. (lookformedical.com)
  • After process membrane and during S mitosis, FANCD2 dissociates to viral such others that cycle with proteins taken in molecular type trans-membrane, neutral as BRCA1 and RAD51. (erik-mill.de)
  • The mechanism by which MuSK signaling regulates the interaction of the AChR with scaffolding proteins that localize it in the postsynaptic membrane, however, remain unknown. (jneurosci.org)
  • The communication in subunit: enabling lymphoid GT-domains preventing membrane as a subunits addition: A ATM identified to the Faculty of Graduate Studies and Research in isolated pore of the heterotrimers for the use of Master of Nursing. (evakoch.com)
  • Each subunit has a large intracellular loop between the third and fourth transmembrane domains that is the likely site for regulated interactions with postsynaptic scaffolding proteins. (jneurosci.org)
  • The non-canonical pathway is responsible for the activation of p100/RelB complexes and occurs during the development of lymphoid organs responsible for the generation of B and T lymphocytes (Figure 2). (abcam.com)
  • For this yeast to produce, s is oxidized from the subunits into the Golgi plasma, and B4GALT1 leads with LALBA( glycerol) to choose its transcription localization( Brew and Hill 1975). (erik-mill.de)
  • Using a proline-rich domain derived from formin (a product of the murine limb deformity locus), we have identified a family of murine formin binding proteins (FBP's), each of which contains one or more of a special class of tyrosine-rich WW domains. (embl.de)
  • WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif. (embl.de)
  • Interaction with many PCNA at a DNA adaptor chromosome plays particular formation route( TLS)( Garg and Burgers 2005, Wood et al. (erik-mill.de)
  • Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. (bioss.com.cn)
  • Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. (nih.gov)
  • In yeast, this bridging involves interactions between the WW domains in the splicing factor PRP40 and a proline-rich domain in the branchpoint binding protein, BBP. (embl.de)
  • At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. (nih.gov)
  • NF-κB proteins are inhibited by IκB proteins present in the cytoplasm. (abcam.com)
  • EGFR is a cell surface protein that binds to epidermal growth factor. (bioss.com.cn)
  • However, it remains unclear where these proteins bind on the AChR and how the interactions are regulated. (jneurosci.org)
  • A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. (lookformedical.com)
  • CDK5 regulatory subunit associated. (gsea-msigdb.org)
  • The common regulatory step in both of these cascades is activation of an IκB kinase ( IKK ) complex consisting of catalytic kinase subunits (IKKα and/or IKKβ) and the regulatory non-enzymatic scaffold protein NEMO (NF-κB essential modulator also known as IKKγ). (abcam.com)
  • Homology between human and viral proteins is an established factor in viral- or vaccine-induced autoimmunity. (danielsolis.cz)
  • The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. (lookformedical.com)
  • A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. (lookformedical.com)
  • Because the expression of the beta-3A subunit is normally ubiquitous, deficiency of the beta-3A subunit leads to a precise phenotype in cells with a large number of intracellular granules (eg, neutrophils, natural killer cells, cytotoxic T lymphocytes, platelets, melanocytes). (medscape.com)
  • Hermansky-Pudlak syndrome type 5 (HPS-5) results from a deficiency of the HPS5 protein, a component of BLOC-2. (medscape.com)
  • To be somatic nucleus nucleotide through coupled uracil kDa at such cancers, transporters serve a scaffold, replaced to as activation deficit( TLS), which translocates form protein to Get complex classes. (erik-mill.de)
  • A constitutively expressed subfamily of the HSP70 heat-shock proteins. (lookformedical.com)
  • Description: A sandwich ELISA kit for detection of Serine Palmitoyltransferase, Long Chain Base Subunit 3 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (1elisakits.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Mouse Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in samples from tissue homogenates, cell lysates or other biological fluids. (1elisakits.com)
  • There are currently seven identified IκB family members: IκBα, IκBβ, Bcl-3, IκBε, IκBγ, and the precursor proteins p100 and p105, which are characterized by the presence of ankyrin repeats. (abcam.com)
  • An adaptor protein, consisting of seven WD REPEATS along its length, that functions as a component of the MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1 and MTORC2 COMPLEX. (bvsalud.org)
  • Autosomal-Recessive Mutations in AP3B2, Adaptor-Related Protein Complex 3 Beta 2 Subunit, Cause an Early-Onset Epileptic Encephalopathy with Optic Atrophy. (bvsalud.org)
  • Prior studies of acute phosphate restriction during the endochondral phase of fracture healing showed delayed chondrocyte differentiation was mechanistically linked to decreased bone morphogenetic protein signaling. (researchgate.net)
  • Recombinant human bone morphogenetic protein 2 (rh. (researchgate.net)
  • Recombinant human bone morphogenetic protein 2 (rhBMP2) is a. (researchgate.net)
  • A family of large adaptin protein subunits of approximately 100 kDa in size. (lookformedical.com)
  • A family of large adaptin protein complex subunits of approximately 90-130 kDa in size. (lookformedical.com)
  • A family of medium adaptin protein subunits of approximately 45 KDa in size. (lookformedical.com)
  • The IKK complex then phosphorylates IκB leading to degradation by the proteasome. (abcam.com)
  • A large variety of proteins containing the WW domain are known. (embl.de)
  • The inflammasome is a large multiprotein complex which plays a key role in innate immunity by participating in the production of the pro-inflammatory cytokines interleukin-1β (IL-1β) and IL-18. (invivogen.com)
  • Using chimeric proteins in which CD4 is fused to the large intracellular loop of each of the AChR subunits we found that agrin induced clustering of only chimeras containing the β subunit loop. (jneurosci.org)
  • The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport. (lookformedical.com)
  • Cells have reading renewables like kinesin influenza and subunit I addition sites to hold the size of the cortisol. (erik-mill.de)
  • [ 6 ] Cells deficient in the HPS5 protein maintain early-stage melanosome formation and Pmel-17 trafficking. (medscape.com)
  • HPS1 is the most common subtype and involves the BLOC-3 protein complex. (medscape.com)
  • Similar to HPS1, HPS4 involves the BLOC-3 protein complex. (medscape.com)
  • An important part of this process takes place on the farm and involves the spontaneous fermentation of the cocoa pulp, by a complex microbial succession, which allows the removal of the pulp and creates specific conditions within the cotyledons. (frontiersin.org)
  • We show that FBP21 is present in highly purified spliceosomal complex A, is associated with U2 snRNPs, and colocalizes with splicing factors in nuclear speckle domains. (embl.de)
  • It is frequently associated with other domains typical for proteins in signal transduction processes. (embl.de)
  • Two of these WW domains, in the proteins FBP11 and FBP21, are strikingly similar to those found in the yeast splicing factor PRP40. (embl.de)
  • The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found. (lookformedical.com)
  • They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 2. (lookformedical.com)
  • An adaptor protein complex found primarily on perinuclear compartments. (lookformedical.com)