Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. (updated: April 1, 2015)
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
No sequence conservation computed yet.
Total structural coverage: 54%
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The reference OMIM entry for this protein is 600025
Kinesin light chain 1; klc1
Kinesin 2; kns2
Kns2a
Klc
DESCRIPTION
Kinesins are tubulin (see
191130) molecular motors that transport organelles within cells and move chromosomes along microtubules during cell division. In sea urchin and mammalian cells, kinesins have been characterized as tetrameric proteins containing 2 heavy (alpha) chains of approximately 120 kD and 2 light (beta) chains of approximately 70 kD. The alpha chains provide the tubulin binding site and the ATPase domains, whereas the beta chains are responsible for the specific attachment of the organelle to be moved by the kinesin tetramer. Kinesins transport their bound organelle to the plus end of the microtubule (summary by Chernajovsky et al., 1996).
CLONING
Chernajovsky et al. (1996) noted that differential splicing occurs for the kinesin beta (light chain) cDNA sequences at the 3-prime end of the rat kinesin mRNA, producing kinesins having different C-terminal ends that seem to confer the kinesin specificity for organelle binding. Cabeza-Arvelaiz et al. (1993) isolated and sequenced a cDNA encoding the human kinesin light chain protein (KLC). The cDNA encodes a deduced polypeptide of 569 amino acids with a predicted molecular mass of 64,789 Da. The predicted secondary internal structure of the KLC molecule consists of about 27 contiguous repeats, each of approximately 21 amino acids, and could be divided into 3 domains. Rahman et al. (1998) cloned mouse Klc1. The deduced 581-amino acid protein has an N-terminal coiled-coil region of about 100 amino acids and 6 imperfect tetratricopeptide repeats of about 34 amino acids each. Northern and Western blot analyses detected Klc1 predominantly in mouse central and peripheral neuronal tissues. Immunofluorescence analysis of cultured rat hippocampal precursor cells showed that Klc1 levels increased with differentiation. In situ hybridization of mouse brain showed that both Klc1 and Klc2 (
611729) were enriched in olfactory bulb, hippocampus, dentate gyrus, and the granular layer of cerebellum. Klc1 was expressed in a subset of cells in the sciatic nerve and showed diffuse axonal staining. Fractionation of whole mouse brain extracts revealed Klc1 and Klc2 in the cytosolic fraction and Klc2 in the microsomal fraction.
GENE FUNCTION
Chernajovsky et al. (1996) characterized the human KNS2 gene product of a differentially spliced, T-cell-derived mRNA and cloned its promoter region. The promoter region transcribes constitutively. In permanently transfected human HeLa and NB100 neuroblastoma cells, a reporter gene containing the promoter and part of the first exon of beta kinesin was 75-fold more active than the HSV-tk promoter. The first exon contains a 5-prime untranslated sequence capable of forming a stable double-hairpin loop, which functions as a translational enhancer. Its deletion decreases the efficiency of in vitro translation of beta kinesin mRNA. Kamal et al. (2000) demonstrated that the axonal transport of APP (
104760) in neurons is mediated by the direct binding of APP to the light chain subunit of kinesin-1. Using anti-mouse Klc1 antibodies to immunoprecipitate proteins from mouse brain lysates, Rahman et al. (1998) showed that Klc1 associated with Nkhc (KIF5A;
602821) and Ukhc (KIF5B;
602809), but not with Klc2. In the presence of a nonhydrolyzable ATP analog, both Klc1 and Klc2 cosedimented with taxol-stabilized mouse brain microtubules. Using a yeast 2-hybrid screen of a rat brain cDNA library with rat Arms (KIDINS220;
615759) as bait, ...
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Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600025 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed