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Dynein light intermediate chain (DLIC)
This family consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organisation, and function of centrosomes and mitotic spindles when bound to pericentrin [1,2]. DLIC2 is a subunit of cytoplasmic dynein 2 that may play a role in maintaining Golgi organisation by binding cytoplasmic dynein 2 to its Golgi-associated cargo [3]. [1]. 10545494. Direct interaction of pericentrin with cytoplasmic dynein light intermediate chain contributes to mitotic spindle organization. Purohit A, Tynan SH, Vallee R, Doxsey SJ;. J Cell Biol 1999;147:481-492. [2]. 10893222. Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein which binds to pericentrin. Tynan SH, Purohit A, Doxsey SJ, Vallee RB;. J Biol Chem 2000;275:32763-32768. [3]. 11907264. Identification of a novel light intermediate chain (D2LIC) for mammalian cytoplasmic dynein 2. Grissom PM, Vaisberg EA, McIntosh JR;. Mol Biol Cell 2002;13:817-829. [4]. 20298435. Contribution of dynein light intermediate and intermediate chains to subcellular localization of the dynein-dynactin motor complex in Schizosaccharomyces pombe. Fujita I, Yamashita A, Yamamoto M;. Genes Cells. 2010;15:359-372. (from Pfam)
ATP-binding cassette domain-containing protein
ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain Pfam:PF00664. These four domains may belong to a single polypeptide as in Swiss:P13569, or belong in different polypeptide chains. [1]. 1864505. Homology between proteins controlling Streptomyces fradiae tylosin resistance and ATP-binding transport. Rosteck PR Jr, Reynolds PA, Hershberger CL;. Gene 1991;102:27-32. [2]. 1977073. Structure and function of haemolysin B,P-glycoprotein and other members of a novel family of membrane translocators. Blight MA, Holland IB;. Mol Microbiol 1990;4:873-880. [3]. 2229036. Binding protein-dependent transport systems. Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher MP;. J Bioenerg Biomembr 1990;22:571-592. [4]. 9872322. Crystal structure of the ATP-binding subunit of an ABC transporter. Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH;. Nature 1998;396:703-707. (from Pfam)
ribosomal protection-like ABC-F family protein
ABC-F family ATP-binding cassette domain-containing protein
ABC-F family ATP-binding cassette domain-containing protein similar to Bacillus subtilis VmlR, a ribosomal protection protein that confers resistance to lincomycin (Lnc), the streptogramin A (SA) antibiotic virginiamycin M (VgM) and the pleuromutilin antibiotic tiamulin
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