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Gene Ontology Classifications
kinesin light chain 1

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Klc1. (This text reflects annotations as of Tuesday, May 26, 2015.)
Summary from NCBI RefSeq

Conventional kinesin is a tetrameric molecule composed of two heavy chains and two light chains, and transports various cargos along microtubules toward their plus ends. The heavy chains provide the motor activity, while the light chains bind to various cargos. This gene encodes a member of the kinesin light chain family. It associates with kinesin heavy chain through an N-terminal domain, and six tetratricopeptide repeat (TPR) motifs are thought to be involved in binding of cargos such as vesicles, mitochondria, and the Golgi complex. Thus, kinesin light chains function as adapter molecules and not motors per se. Although previously named "kinesin 2", this gene is not a member of the kinesin-2 / kinesin heavy chain subfamily of kinesin motor proteins. Extensive alternative splicing produces isoforms with different C-termini that are proposed to bind to different cargos; however, the full-length nature of some of these variants has not been determined. [provided by RefSeq, Jul 2008]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
  1. Araki Y et al. (2007) The novel cargo Alcadein induces vesicle association of kinesin-1 motor components and activates axonal transport. EMBO J, 26:1475-86. (PubMed:17332754)
  2. Bowman AB et al. (2000) Kinesin-dependent axonal transport is mediated by the sunday driver (SYD) protein. Cell, 103:583-94. (PubMed:11106729)
  3. Dodding MP et al. (2011) A kinesin-1 binding motif in vaccinia virus that is widespread throughout the human genome. EMBO J, 30:4523-38. (PubMed:21915095)
  4. Kamal A et al. (2001) Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature, 414:643-8. (PubMed:11740561)
  5. Kelkar N et al. (2000) Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3. Mol Cell Biol, 20:1030-43. (PubMed:10629060)
  6. Loschi M et al. (2009) Dynein and kinesin regulate stress-granule and P-body dynamics. J Cell Sci, 122:3973-82. (PubMed:19825938)
  7. Muresan Z et al. (2005) Coordinated transport of phosphorylated amyloid-beta precursor protein and c-Jun NH2-terminal kinase-interacting protein-1. J Cell Biol, 171:615-25. (PubMed:16301330)
  8. Pigino G et al. (2003) Alzheimer's presenilin 1 mutations impair kinesin-based axonal transport. J Neurosci, 23:4499-508. (PubMed:12805290)
  9. Rahman A et al. (1998) Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins. (Erratum pg. 24280) J Biol Chem, 273:15395-403. (PubMed:9624122)
  10. Roux KJ et al. (2009) Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization. Proc Natl Acad Sci U S A, 106:2194-9. (PubMed:19164528)
  11. Sun F et al. (2011) Sunday Driver/JIP3 binds kinesin heavy chain directly and enhances its motility. EMBO J, 30:3416-29. (PubMed:21750526)
  12. Terada S et al. (2010) Kinesin-1/Hsc70-dependent mechanism of slow axonal transport and its relation to fast axonal transport. EMBO J, 29:843-54. (PubMed:20111006)
  13. Verhey KJ et al. (2001) Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules. J Cell Biol, 152:959-70. (PubMed:11238452)
  14. Yang J et al. (2005) The ciliary rootlet interacts with kinesin light chains and may provide a scaffold for kinesin-1 vesicular cargos. Exp Cell Res, 309:379-89. (PubMed:16018997)

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Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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