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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 ...
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 general purpose of the Pfam database is to provide a complete and accurate classification of protein families and domains. [5] Originally, the rationale behind creating the database was to have a semi-automated method of curating information on known protein families to improve the efficiency of annotating genomes. [6]
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.
Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases.These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe 2+, and ascorbate.
Arginylglycylaspartic acid (RGD) is the most common peptide motif responsible for cell adhesion to the extracellular matrix (ECM), found in species ranging from Drosophila to humans.
EH domain-containing protein 1, also known as testilin or PAST homolog 1 (PAST1), is a protein that in humans is encoded by the EHD1 gene [5] belonging to the EHD protein family. Function [ edit ]
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 ...