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Kinectin 1 (kinesin receptor)
Symbols KTN1 ; CG1; KNT; MU-RMS-40.19
External IDs OMIM600381 MGI109153 HomoloGene135663 GeneCards: KTN1 Gene
RNA expression pattern
PBB GE KTN1 214709 s at tn.png
PBB GE KTN1 200914 x at tn.png
PBB GE KTN1 200915 x at tn.png
More reference expression data
Species Human Mouse
Entrez 3895 16709
Ensembl ENSG00000126777 ENSMUSG00000021843
UniProt Q86UP2 Q61595
RefSeq (mRNA) NM_001079521 NM_008477
RefSeq (protein) NP_001072989 NP_032503
Location (UCSC) Chr 14:
56.03 – 56.17 Mb
Chr 14:
47.66 – 47.74 Mb
PubMed search [1] [2]

Kinectin is a protein that in humans is encoded by the KTN1 gene.[1][2]

Various cellular organelles and vesicles are transported along the microtubules in the cytoplasm. Likewise, membrane recycling of the endoplasmic reticulum (ER), Golgi assembly at the microtubule organizing center, and alignment of lysosomes along microtubules are all related processes. The transport of organelles requires a special class of microtubule-associated proteins (MAPs). One of these is the molecular motor kinesin (see MIM 148760 and MIM 600025), an ATPase that moves vesicles unidirectionally toward the plus end of the microtubule. Another such MAP is kinectin, a large integral ER membrane protein. Antibodies directed against kinectin have been shown to inhibit its binding to kinesin.[supplied by OMIM][2]


KTN1 has been shown to interact with EEF1D,[3] RhoG[4][5] and RHOA.[4][5][6][7]


  1. ^ Rao PN, Yu H, Hodge R, Pettenati MJ, Sheetz MP (Jun 1998). "Assignment of the human kinectin gene (KTN1), encoding a kinesin-binding protein, to chromosome 14 band q22.1 by in situ hybridization". Cytogenet Cell Genet 79 (3–4): 196–7. doi:10.1159/000134719. PMID 9605849. 
  2. ^ a b "Entrez Gene: KTN1 kinectin 1 (kinesin receptor)". 
  3. ^ Ong, Lee-Lee; Er Connie P N; Ho Andrea; Aung May T; Yu Hanry (Aug 2003). "Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum". J. Biol. Chem. (United States) 278 (34): 32115–23. doi:10.1074/jbc.M210917200. ISSN 0021-9258. PMID 12773547. 
  4. ^ a b Neudauer, C L; Joberty G; Macara I G (Jan 2001). "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10". Biochem. Biophys. Res. Commun. (United States) 280 (2): 541–7. doi:10.1006/bbrc.2000.4160. ISSN 0006-291X. PMID 11162552. 
  5. ^ a b Vignal, E; Blangy A; Martin M; Gauthier-Rouvière C; Fort P (Dec 2001). "Kinectin Is a Key Effector of RhoG Microtubule-Dependent Cellular Activity". Mol. Cell. Biol. (United States) 21 (23): 8022–34. doi:10.1128/MCB.21.23.8022-8034.2001. ISSN 0270-7306. PMC 99969. PMID 11689693. 
  6. ^ Riento, Kirsi; Guasch Rosa M; Garg Ritu; Jin Boquan; Ridley Anne J (Jun 2003). "RhoE Binds to ROCK I and Inhibits Downstream Signaling". Mol. Cell. Biol. (United States) 23 (12): 4219–29. doi:10.1128/MCB.23.12.4219-4229.2003. ISSN 0270-7306. PMC 156133. PMID 12773565. 
  7. ^ Hotta, K; Tanaka K; Mino A; Kohno H; Takai Y (Aug 1996). "Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor". Biochem. Biophys. Res. Commun. (UNITED STATES) 225 (1): 69–74. doi:10.1006/bbrc.1996.1132. ISSN 0006-291X. PMID 8769096. 

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