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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 the two- and three-domain systems, this puts them into a separate domain. There is a great deal of diversity in the domain Bacteria. That diversity is further confounded by the exchange of genes between different bacterial lineages. The occurrence of duplicate genes between otherwise distantly-related bacteria makes it nearly impossible to ...
The etymology of the word "morphology" is from the Ancient Greek μορφή (morphḗ), meaning "form", and λόγος (lógos), meaning "word, study, research". [2] [3]While the concept of form in biology, opposed to function, dates back to Aristotle (see Aristotle's biology), the field of morphology was developed by Johann Wolfgang von Goethe (1790) and independently by the German anatomist ...
The extracellular domain is just externally from the cell or organelle. If the polypeptide chain crosses the bilayer several times, the external domain comprises loops entwined through the membrane. By definition, a receptor's main function is to recognize and respond to a type of ligand.
There are numerous coated vesicles and coated pits along the basolateral domain of the podocytes which indicate a high rate of vesicular traffic. Podocytes possess a well-developed endoplasmic reticulum and a large Golgi apparatus , indicative of a high capacity for protein synthesis and post-translational modifications .
They are referred to as coiled coils unless they are proven to be important for protein function. If that is the case, then they are annotated in the “domain” subsection, which would be the bZIP domain. [9] Two different types of such a-helices can pair up to form a heterodimeric leucine zipper.
Caveolae have a role in cell signaling, too. Caveolins associate with some signaling molecules (e.g. eNOS) through their scaffolding domain and so they can regulate their signaling. Caveolae are also involved in regulation of channels and in calcium signaling. [15] Caveolae also participate in lipid regulation.