Search results
Results from the WOW.Com Content Network
98878 Ensembl ENSG00000103966 ENSMUSG00000027293 UniProt Q9H223 Q9EQP2 RefSeq (mRNA) NM_139265 NM_133838 RefSeq (protein) NP_644670 NP_598599 Location (UCSC) Chr 15: 41.9 – 41.97 Mb Chr 2: 119.92 – 119.99 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse EH-domain containing 4, also known as EHD4, is a human gene belonging to the EHD protein family. References ^ a b c GRCh38 ...
The EHD protein family is a relatively small group of proteins which have been shown to play a role in several physiological functions, the most notable being the regulation of endocytotic vesicles. This family is recognized by its highly conserved EH ( Eps15 homology) [ 1 ] domain, a structural motif that has been shown to facilitate ...
The EH domain is a common motif in a family of proteins involved in endocytic trafficking. This family of four paralogs (EHD1-EHD4) has been implicated in receptor intracellular trafficking, particularly in internalization and recycling to the plasma membrane. The list of functions of EHD proteins is just starting to be populated. [8]
Clathrin is a protein that plays a role in the formation of coated vesicles.Clathrin was first isolated by Barbara Pearse in 1976. [1] It forms a triskelion shape composed of three clathrin heavy chains and three light chains.
Retromer is a complex of proteins that has been shown to be important in recycling transmembrane receptors from endosomes to the trans-Golgi network (TGN) and directly back to the plasma membrane. Mutations in retromer and its associated proteins have been linked to Alzheimer's and Parkinson's diseases. [1] [2] [3] [4]
Small GTPases (EC 3.6.5.2), also known as small G-proteins, are a family of hydrolase enzymes that can bind and hydrolyze guanosine triphosphate (GTP). They are a type of G-protein found in the cytosol that are homologous to the alpha subunit of heterotrimeric G-proteins, but unlike the alpha subunit of G proteins, a small GTPase can function independently as a hydrolase enzyme to bind to and ...
The Drosophila protein Slimb is part of an SCF complex that targets proteins for ubiquitylation. Slimb binds to phosphorylated Ci protein. In the absence of Hh (Figure 3), a cell-surface transmembrane protein called Patched (PTCH) acts to prevent high expression and activity of a 7 membrane spanning receptor [ 10 ] called Smoothened (SMO).
The Sec1/Munc18 protein family is known to bind to Syntaxin and regulate Syntaxins machinery. Munc18-1 binds to Syntaxin 1A via two distinct sites referred as N-terminus binding and "closed" conformation that incorporates both the central Habc domain and the SNARE core domain. Munc18-1 binding to the N-terminus of Syntaxin-1 is thought to ...