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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 ATP binding domain shows impressive structural and functional similarity to the Dynamin GTP binding domain which is known to facilitate clathrin-coated vesicle budding. Given this resemblance, several researchers tend to consider the EHD protein family a sub-group that falls within the Dynamin protein superfamily. When ATP binds to this ...
In biological taxonomy, a domain (/ d ə ˈ m eɪ n / or / d oʊ ˈ m eɪ n /) (Latin: regio [1]), also dominion, [2] superkingdom, realm, or empire, is the highest taxonomic rank of all organisms taken together. It was introduced in the three-domain system of taxonomy devised by Carl Woese, Otto Kandler and Mark Wheelis in 1990. [1]
Mechanism of clathrin-dependent endocytosis. Receptor-mediated endocytosis (RME), also called clathrin-mediated endocytosis, is a process by which cells absorb metabolites, hormones, proteins – and in some cases viruses – by the inward budding of the plasma membrane (invagination).
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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] Dynamin-type guanine nucleotide-binding (G) domain, between the 56th and 286th
The full extent of the role of DUBs in diseases remains to be elucidated. Their involvement in disease is predicted due to known roles in physiological processes that are involved in disease states; including cancer and neurological disorders.
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