KIFAP3

Kinesin-associated protein 3 is a protein that in humans is encoded by the KIFAP3 (also known as KAP3) gene.[5][6] It is a non-motor, accessory subunit which co-oligomerizes with the motor subunits KIF3A and KIF3B or KIF3C, to form heterotrimeric kinesin-2 motor proteins. Kinesin-2 KAP subunits were initially characterized in echinoderms and mice.[7][8]

KIFAP3
Identifiers
Aliases	KIFAP3, FLA3, KAP-1, KAP-3, KAP3, SMAP, Smg-GDS, dJ190I16.1, kinesin associated protein 3
External IDs	OMIM: 601836 MGI: 107566 HomoloGene: 7799 GeneCards: KIFAP3
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q24.2 Start 169,921,326 bp[1] End 170,085,208 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 H2.1 Start 163,779,583 bp[2] End 163,917,109 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • kinesin binding • intraciliary transport particle B binding • protein phosphatase binding Cellular component • intraciliary transport particle • ciliary basal body • cytosol • centrosome • Golgi apparatus • kinesin complex • microtubule cytoskeleton • kinesin II complex • photoreceptor connecting cilium • condensed nuclear chromosome • ciliary tip • spindle microtubule • endoplasmic reticulum • periciliary membrane compartment • GO:0035085 axoneme • cilium Biological process • protein localization • plus-end-directed vesicle transport along microtubule • antigen processing and presentation of exogenous peptide antigen via MHC class II • negative regulation of apoptotic process • microtubule-based movement • positive regulation of calcium-dependent cell-cell adhesion • microtubule-based process • signal transduction • negative regulation of cell proliferation • retrograde vesicle-mediated transport, Golgi to ER • intraciliary transport involved in cilium assembly • macromolecular complex assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	22920	16579
Ensembl	ENSG00000075945	ENSMUSG00000026585
UniProt	Q92845	P70188
RefSeq (mRNA)	NM_001204514 NM_001204516 NM_001204517 NM_014970 NM_001375830 NM_001375831	NM_010629 NM_001305643
RefSeq (protein)	NP_001191443 NP_001191445 NP_001191446 NP_055785 NP_001362759 NP_001362760	NP_001292572 NP_034759
Location (UCSC)	Chr 1: 169.92 – 170.09 Mb	Chr 1: 163.78 – 163.92 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The small G protein GDP dissociation stimulator (smg GDS) is a regulator protein having two activities on a group of small G proteins including the Rho and Rap1 family members and Ki-Ras; one is to stimulate their GDP/GTP exchange reactions, and the other is to inhibit their interactions with membranes. The protein encoded by this gene contains 9 Armadillo repeats and interacts with the smg GDS protein through these repeats. This protein, which is highly concentrated around the endoplasmic reticulum, is phosphorylated by v-src, and this phosphorylation reduces the affinity of the protein for smg GDS. It is thought that this protein serves as a linker between human chromosome-associated polypeptide (HCAP) and KIF3A/B, a kinesin superfamily protein in the nucleus, and that it plays a role in the interaction of chromosomes with an ATPase motor protein.[6]

Interactions

KIFAP3 has been shown to interact with APC,[9] SMC3[10] and RAP1GDS1.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000075945 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026585 - 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. Shimizu K, Kawabe H, Minami S, Honda T, Takaishi K, Shirataki H, Takai Y (Dec 1996). "SMAP, an Smg GDS-associating protein having arm repeats and phosphorylated by Src tyrosine kinase". J Biol Chem. 271 (43): 27013–7. doi:10.1074/jbc.271.43.27013. PMID 8900189.
6. "Entrez Gene: KIFAP3 kinesin-associated protein 3".
7. Wedaman KP, Meyer DW, Rashid DJ, Cole DG, Scholey JM (February 1996). "Sequence and submolecular localization of the 115-kD accessory subunit of the heterotrimeric kinesin-II (KRP85/95) complex". J. Cell Biol. 132 (3): 371–80. doi:10.1083/jcb.132.3.371. PMC 2120715. PMID 8636215.
8. Yamazaki H, Nakata T, Okada Y, Hirokawa N (August 1996). "Cloning and characterization of KAP3: a novel kinesin superfamily-associated protein of KIF3A/3B". Proc. Natl. Acad. Sci. U.S.A. 93 (16): 8443–8. doi:10.1073/pnas.93.16.8443. PMC 38690. PMID 8710890.
9. Jimbo T, Kawasaki Y, Koyama R, Sato R, Takada S, Haraguchi K, Akiyama T (April 2002). "Identification of a link between the tumour suppressor APC and the kinesin superfamily". Nat. Cell Biol. 4 (4): 323–7. doi:10.1038/ncb779. PMID 11912492.
10. Shimizu K, Shirataki H, Honda T, Minami S, Takai Y (March 1998). "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide". J. Biol. Chem. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.

Further reading

• Nagata K, Puls A, Futter C, et al. (1998). "The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3". EMBO J. 17 (1): 149–58. doi:10.1093/emboj/17.1.149. PMC 1170366. PMID 9427749.
• Shimizu K, Shirataki H, Honda T, et al. (1998). "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide". J. Biol. Chem. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Khanna H, Hurd TW, Lillo C, et al. (2005). "RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with SMC1, SMC3, and microtubule transport proteins". J. Biol. Chem. 280 (39): 33580–7. doi:10.1074/jbc.M505827200. PMC 1249479. PMID 16043481.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Brown CL, Maier KC, Stauber T, et al. (2006). "Kinesin-2 is a motor for late endosomes and lysosomes". Traffic. 6 (12): 1114–24. doi:10.1111/j.1600-0854.2005.00347.x. PMID 16262723.
• Haraguchi K, Hayashi T, Jimbo T, et al. (2006). "Role of the kinesin-2 family protein, KIF3, during mitosis". J. Biol. Chem. 281 (7): 4094–9. doi:10.1074/jbc.M507028200. PMID 16298999.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
• Kuraguchi M, Wang XP, Bronson RT, et al. (2006). "Adenomatous Polyposis Coli (APC) Is Required for Normal Development of Skin and Thymus". PLoS Genet. 2 (9): e146. doi:10.1371/journal.pgen.0020146. PMC 1564426. PMID 17002498.
• Stauber T, Simpson JC, Pepperkok R, Vernos I (2007). "A role for kinesin-2 in COPI-dependent recycling between the ER and the Golgi complex". Curr. Biol. 16 (22): 2245–51. doi:10.1016/j.cub.2006.09.060. PMID 17113389.