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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 .
Eps15 homology domain-containing protein 3, abbreviated as EHD3 and also known as PAST3, is a protein encoded by the EHD3 gene. It has been observed in humans, mice and rats. It has been observed in humans, mice and rats.
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]
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Schematic representation of the three top levels of the CATH classification scheme. [2]The CATH Protein Structure Classification database is a free, publicly available online resource that provides information on the evolutionary relationships of protein domains.
The transactivation domain or trans-activating domain (TAD) is a transcription factor scaffold domain which contains binding sites for other proteins such as transcription coregulators. These binding sites are frequently referred to as activation functions (AFs). [1] TADs are named after their amino acid composition.
Another commonly found domain is an armadillo repeat region (ARR) located in the FH3 domain. The FH2 domain, has been shown by X-ray crystallography to have an elongated, crescent shape containing three helical subdomains. [17] [18] Formins also directly bind to microtubules via their FH2 domain. This interaction is important in promoting the ...