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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 ...
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 ...
A Ramachandran plot generated from human PCNA, a trimeric DNA clamp protein that contains both β-sheet and α-helix (PDB ID 1AXC). The red, brown, and yellow regions represent the favored, allowed, and "generously allowed" regions, respectively, as defined by ProCheck
Created Date: 8/30/2012 4:52:52 PM
The protein-binding EH domain was first noted in EPS15, a substrate for the epidermal growth factor receptor. The EH domain has been shown to be an important motif in proteins involved in protein-protein interactions and in intracellular sorting. The protein encoded by this gene is thought to play a role in the endocytosis of IGF1 receptors. [5]
Most of the 3000 types of proteins are involved in a variety of processes other than ATP production, such as porphyrin synthesis. Only about 3% of them code for ATP production proteins. This means most of the genetic information coding for the protein makeup of mitochondria is in chromosomal DNA and is involved in processes other than ATP ...
These multiple forms (isoforms or subtypes) of phosphodiesterase were isolated from rat brain using polyacrylamide gel electrophoresis in the early 1970s by Weiss and coworkers, [1] [2] and were soon afterward shown to be selectively inhibited by a variety of drugs in brain and other tissues, also by Weiss and coworkers.
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 ...