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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 ...
EHD3 protein is formed of four different domains: EH domain-containing protein N-terminal, between the 24th and 56th amino acid. This is a short domain that can be found at the beginning of a protein, also known as N-terminus, of many dynamins and EF-hand domain-containing proteins. [3]
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 ...
PhosphoSitePlus is a database of observed post-translational modifications in human and mouse proteins; an online systems biology resource providing comprehensive information and tools for the study of protein post-translational modifications (PTMs) including phosphorylation, ubiquitination, acetylation and methylation.
The Chou–Fasman method is an empirical technique for the prediction of secondary structures in proteins, originally developed in the 1970s by Peter Y. Chou and Gerald D. Fasman. [ 1 ] [ 2 ] [ 3 ] The method is based on analyses of the relative frequencies of each amino acid in alpha helices , beta sheets , and turns based on known protein ...
As protein detection technologies have increased in sensitivity, such as with improvements in mass spectrometry techniques, more numerous proteins have been attributed to the PSD. Current estimates are greater than several hundred proteins are found at PSDs among brain regions and during different states of development and synaptic activity.