KLC3

Kinesin light chain 3 is a protein that in humans is encoded by the KLC3 gene.[5]

KLC3
Identifiers
Aliases	KLC3, KLC2, KLC2L, KLCt, KNS2B, kinesin light chain 3
External IDs	OMIM: 601334 MGI: 1277971 HomoloGene: 14899 GeneCards: KLC3
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19q13.32 Start 45,333,434 bp[1] End 45,351,520 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 A3|7 9.62 cM Start 19,394,437 bp[2] End 19,404,104 bp[2]
Gene ontology Molecular function • microtubule binding • microtubule motor activity • GO:0001948 protein binding • kinesin binding Cellular component • cytoplasm • neuron projection • motile cilium • microtubules • cytoskeleton • kinesin complex • ciliary rootlet Biological process • axo-dendritic transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	147700	232943
Ensembl	ENSG00000104892	ENSMUSG00000040714
UniProt	Q6P597	Q91W40
RefSeq (mRNA)	NM_145275 NM_177417	NM_001286038 NM_001286039 NM_146182
RefSeq (protein)	NP_803136	NP_001272967 NP_001272968 NP_666294
Location (UCSC)	Chr 19: 45.33 – 45.35 Mb	Chr 7: 19.39 – 19.4 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the kinesin light chain gene family. Kinesins are molecular motors involved in the transport of cargo along microtubules, and are composed of two kinesin heavy chain (KHC) and two kinesin light chain (KLC) molecules. KLCs are thought to typically be involved in binding cargo and regulating kinesin activity. In the rat, a protein similar to this gene product is expressed in post-meiotic spermatids, where it associates with structural components of sperm tails and mitochondria.[5]

Interactions

KLC3 has been shown to interact with YWHAH.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000104892 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040714 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: KLC3 kinesin light chain 3".
6. Ichimura T, Wakamiya-Tsuruta A, Itagaki C, Taoka M, Hayano T, Natsume T, Isobe T (Apr 2002). "Phosphorylation-dependent interaction of kinesin light chain 2 and the 14-3-3 protein". Biochemistry. 41 (17): 5566–72. doi:10.1021/bi015946f. PMID 11969417.

Further reading

• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Zhang Y, Oko R, van der Hoorn FA (Nov 2004). "Rat kinesin light chain 3 associates with spermatid mitochondria". Developmental Biology. 275 (1): 23–33. doi:10.1016/j.ydbio.2004.07.014. PMC 3138780. PMID 15464570.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• Bhullar B, Zhang Y, Junco A, Oko R, van der Hoorn FA (May 2003). "Association of kinesin light chain with outer dense fibers in a microtubule-independent fashion". The Journal of Biological Chemistry. 278 (18): 16159–68. doi:10.1074/jbc.M213126200. PMC 3178653. PMID 12594206.
• Yang J, Liu X, Yue G, Adamian M, Bulgakov O, Li T (Nov 2002). "Rootletin, a novel coiled-coil protein, is a structural component of the ciliary rootlet". The Journal of Cell Biology. 159 (3): 431–40. doi:10.1083/jcb.200207153. PMC 2173070. PMID 12427867.
• Ichimura T, Wakamiya-Tsuruta A, Itagaki C, Taoka M, Hayano T, Natsume T, Isobe T (Apr 2002). "Phosphorylation-dependent interaction of kinesin light chain 2 and the 14-3-3 protein". Biochemistry. 41 (17): 5566–72. doi:10.1021/bi015946f. PMID 11969417.
• Junco A, Bhullar B, Tarnasky HA, van der Hoorn FA (May 2001). "Kinesin light-chain KLC3 expression in testis is restricted to spermatids". Biology of Reproduction. 64 (5): 1320–30. doi:10.1095/biolreprod64.5.1320. PMC 3161965. PMID 11319135.
• Rahman A, Kamal A, Roberts EA, Goldstein LS (Sep 1999). "Defective kinesin heavy chain behavior in mouse kinesin light chain mutants". The Journal of Cell Biology. 146 (6): 1277–88. doi:10.1083/jcb.146.6.1277. PMC 2156125. PMID 10491391.
• Rahman A, Friedman DS, Goldstein LS (Jun 1998). "Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins". The Journal of Biological Chemistry. 273 (25): 15395–403. doi:10.1074/jbc.273.25.15395. PMID 9624122.
• Lamerdin JE, Stilwagen SA, Ramirez MH, Stubbs L, Carrano AV (Jun 1996). "Sequence analysis of the ERCC2 gene regions in human, mouse, and hamster reveals three linked genes". Genomics. 34 (3): 399–409. doi:10.1006/geno.1996.0303. PMID 8786141.