[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/kinesin-associated-protein-3-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/kinesin-associated-protein-3-wikipedia\/","headline":"Kinesin-associated protein 3 – Wikipedia","name":"Kinesin-associated protein 3 – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens Kinesin-associated protein 3 (KAP3) is a","datePublished":"2015-10-12","dateModified":"2015-10-12","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/www.wikimedia.org\/static\/images\/wmf-logo.png","url":"https:\/\/www.wikimedia.org\/static\/images\/wmf-logo.png","height":"101","width":"135"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/kinesin-associated-protein-3-wikipedia\/","wordCount":6421,"articleBody":" (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensKinesin-associated protein 3 (KAP3) is a protein that in humans is encoded by the KIFAP3 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] (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsFunction[edit]Interactions[edit]References[edit]Further reading[edit]Function[edit]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] It has also been proposed to act as a clamp, stabilizing the C-terminal half [9] of the otherwise unstable stalk coiled-coil.Interactions[edit]KIFAP3 has been shown to interact with APC,[10]SMC3[11] and RAP1GDS1.[5] (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000075945 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026585 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ a b 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\u20137. doi:10.1074\/jbc.271.43.27013. PMID\u00a08900189.^ a b “Entrez Gene: KIFAP3 kinesin-associated protein 3”.^ 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\u201380. doi:10.1083\/jcb.132.3.371. PMC\u00a02120715. PMID\u00a08636215.^ 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\u20138. Bibcode:1996PNAS…93.8443Y. doi:10.1073\/pnas.93.16.8443. PMC\u00a038690. PMID\u00a08710890.^ Ahmed Z, Mazumdar S, Ray K (February 2020). “Kinesin associated protein, DmKAP, binding harnesses the C-terminal ends of the Drosophila kinesin-2 stalk heterodimer”. Biochem Biophys Res Commun. 522 (2): 506\u2013511. doi:10.1016\/j.bbrc.2019.11.111. PMC\u00a08407544. PMID\u00a031784087.^ 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\u20137. doi:10.1038\/ncb779. PMID\u00a011912492. S2CID\u00a010745049.^ 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\u20134. doi:10.1074\/jbc.273.12.6591. PMID\u00a09506951.Further reading[edit]ul{margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li{margin-left:0;padding-left:3.2em;text-indent:-3.2em}.mw-parser-output .refbegin-hanging-indents ul,.mw-parser-output .refbegin-hanging-indents ul li{list-style:none}@media(max-width:720px){.mw-parser-output .refbegin-hanging-indents>ul>li{padding-left:1.6em;text-indent:-1.6em}}.mw-parser-output .refbegin-columns{margin-top:0.3em}.mw-parser-output .refbegin-columns ul{margin-top:0}.mw-parser-output .refbegin-columns li{page-break-inside:avoid;break-inside:avoid-column}]]>Nagata K, Puls A, Futter C, et\u00a0al. (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\u201358. doi:10.1093\/emboj\/17.1.149. PMC\u00a01170366. PMID\u00a09427749.Shimizu K, Shirataki H, Honda T, et\u00a0al. (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\u20134. doi:10.1074\/jbc.273.12.6591. PMID\u00a09506951.Strausberg RL, Feingold EA, Grouse LH, et\u00a0al. (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\u2013903. Bibcode:2002PNAS…9916899M. doi:10.1073\/pnas.242603899. PMC\u00a0139241. PMID\u00a012477932.Ota T, Suzuki Y, Nishikawa T, et\u00a0al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40\u20135. doi:10.1038\/ng1285. PMID\u00a014702039.Gerhard DS, Wagner L, Feingold EA, et\u00a0al. (2004). “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121\u20137. doi:10.1101\/gr.2596504. PMC\u00a0528928. PMID\u00a015489334.Khanna H, Hurd TW, Lillo C, et\u00a0al. (2005). “RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with SMC1, SMC3, and microtubule transport proteins”. J. Biol. Chem. 280 (39): 33580\u20137. doi:10.1074\/jbc.M505827200. PMC\u00a01249479. PMID\u00a016043481.Rual JF, Venkatesan K, Hao T, et\u00a0al. (2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173\u20138. Bibcode:2005Natur.437.1173R. doi:10.1038\/nature04209. PMID\u00a016189514. S2CID\u00a04427026.Brown CL, Maier KC, Stauber T, et\u00a0al. (2006). “Kinesin-2 is a motor for late endosomes and lysosomes”. Traffic. 6 (12): 1114\u201324. doi:10.1111\/j.1600-0854.2005.00347.x. PMID\u00a016262723.Haraguchi K, Hayashi T, Jimbo T, et\u00a0al. (2006). “Role of the kinesin-2 family protein, KIF3, during mitosis”. J. Biol. Chem. 281 (7): 4094\u20139. doi:10.1074\/jbc.M507028200. PMID\u00a016298999.Gregory SG, Barlow KF, McLay KE, et\u00a0al. (2006). “The DNA sequence and biological annotation of human chromosome 1”. Nature. 441 (7091): 315\u201321. Bibcode:2006Natur.441..315G. doi:10.1038\/nature04727. PMID\u00a016710414.Lim J, Hao T, Shaw C, et\u00a0al. (2006). “A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration”. Cell. 125 (4): 801\u201314. doi:10.1016\/j.cell.2006.03.032. PMID\u00a016713569. S2CID\u00a013709685.Kuraguchi M, Wang XP, Bronson RT, et\u00a0al. (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\u00a01564426. PMID\u00a017002498.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\u201351. doi:10.1016\/j.cub.2006.09.060. PMID\u00a017113389. S2CID\u00a09739953.Wikimedia ErrorOur servers are currently under maintenance or experiencing a technical problem.Please try again in a few\u00a0minutes.See the error message at the bottom of this page for more\u00a0information. (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/kinesin-associated-protein-3-wikipedia\/#breadcrumbitem","name":"Kinesin-associated protein 3 – Wikipedia"}}]}]