Kinesins (Homo sapiens)

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3, 10, 21, 2716, 224-6, 14, 17...20, 238, 2611215, 19, 251, 12, 17137, 9, 24cytosolKIFAP3 KIF18B KIF5B KIF3C KIF18A dimerKLC4 KIF15 KIF22 KIF16B KIFAP3Kinesin-6KLC2 KLC3 KIFC1 KIF3A partnersKinesin-13 dimersKIF3B KIF18A KLC3 Chromokinesin dimers KIF18B KIF3B KLC4 Kinesin-13 monomersKIFC1RACGAP1 KIF21B KIF11 KIF3A ATPCENPE KIF16B KIF21A KIF28P KIF1C KIF15 KIF5B KIF26B Kinesin-3 dimers Kinesin-13 dimers KIF3C KIF15Chromokinesin dimers Kinesins:microtubuleKIF5A KIF15 KIF22 KLC2 KIF9 KIFC1 KIFAP3 KIF5A KIF23 KIF13B KLC4 KIF3A KIF3B ChromokinesinmonomersKIF23 CENPE KIFC1 KLC1 KIFC2 CentralspindlinKIF3B RACGAP1 Kinesin-3 monomersKIF9 KIF5B(1-?) KIF3B KinesinsKIF26B KLC3 KIF15 dimerKinesin-13 dimers KIF15 CENPE Kinesin-5homotetramerKIFC2 KIF1A KIF5A KIF5C(?-?) KIFAP3 KIF23 KIF2B Chromokinesin dimers KIF3B KIF11KLC3 KIF25 KLC1,KLC2,KLC3,KLC4KIF4 KLC4 KLC3 KIF9KIF23 KLC1 KIF18AKLC2 KIF27 Chromokinesin dimersKinesin-3 dimers RACGAP1 KIF1B KIF20A KIFAP3 KIF1A KIF6 Kinesin-13 dimers KIF3C KIF18A CENPE KIF3C KIF11 KIF5C(?-?) KIF11 KIF20A Kinesin-3 dimers RACGAP1 KIF20A KIF3B KIF2B KIF1C KIF5A KIF25 KIF6 Kinesin-4 homodimers CENPEKIF27 Kinesin-1 heavychainKLC1 Kinesin-2KIF3C KIF3A MicrotubuleKIF12 KIF5B KIF26A KIF18A Kinesin-14KIF20B KIF11 KIF2A KIF3A KIF18A Microtubule protofilament KIF3A KLC4 ADPKIF21B KLC2 Kinesin-3 dimersKIF13B KIF20A KIF5B KIF9 KIF3A RACGAP1KIF20A KIF19 KIF26A KIF28P KIF5B(1-?) KLC1 KLC2 KIF23 KIF12 KIF2C KIF26A Microtubule protofilament KIF21A KIF2C Kinesin-1CENP-E dimerKLC1 KIF5A KIF2A KIF9 dimerKIF1B KIF20B KinesinsKIF3AKIF19 KIF5B


Kinesins are a superfamily of microtubule-based motor proteins that have diverse functions in transport of vesicles, organelles and chromosomes, and regulate microtubule dynamics. There are 14 families of kinesins, all reprsented in humans. A standardized nomenclature was published in 2004 (Lawrence et al.). View original pathway at:Reactome.


Pathway is converted from Reactome ID: 983189
Reactome version: 63
Reactome Author 
Reactome Author: Akkerman, Jan Willem N

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  1. Nangaku M, Sato-Yoshitake R, Okada Y, Noda Y, Takemura R, Yamazaki H, Hirokawa N.; ''KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria.''; PubMed Europe PMC Scholia
  2. Nislow C, Lombillo VA, Kuriyama R, McIntosh JR.; ''A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles.''; PubMed Europe PMC Scholia
  3. Sindelar CV, Budny MJ, Rice S, Naber N, Fletterick R, Cooke R.; ''Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy.''; PubMed Europe PMC Scholia
  4. Navone F, Niclas J, Hom-Booher N, Sparks L, Bernstein HD, McCaffrey G, Vale RD.; ''Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells.''; PubMed Europe PMC Scholia
  5. Yang JT, Saxton WM, Stewart RJ, Raff EC, Goldstein LS.; ''Evidence that the head of kinesin is sufficient for force generation and motility in vitro.''; PubMed Europe PMC Scholia
  6. Wordeman L, Mitchison TJ.; ''Identification and partial characterization of mitotic centromere-associated kinesin, a kinesin-related protein that associates with centromeres during mitosis.''; PubMed Europe PMC Scholia
  7. Endow SA, Kull FJ, Liu H.; ''Kinesins at a glance.''; PubMed Europe PMC Scholia
  8. Kuznetsov SA, Vaisberg YA, Rothwell SW, Murphy DB, Gelfand VI.; ''Isolation of a 45-kDa fragment from the kinesin heavy chain with enhanced ATPase and microtubule-binding activities.''; PubMed Europe PMC Scholia
  9. Tokai N, Fujimoto-Nishiyama A, Toyoshima Y, Yonemura S, Tsukita S, Inoue J, Yamamota T.; ''Kid, a novel kinesin-like DNA binding protein, is localized to chromosomes and the mitotic spindle.''; PubMed Europe PMC Scholia
  10. Yang JT, Laymon RA, Goldstein LS.; ''A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses.''; PubMed Europe PMC Scholia
  11. Hammond JW, Cai D, Blasius TL, Li Z, Jiang Y, Jih GT, Meyhofer E, Verhey KJ.; ''Mammalian Kinesin-3 motors are dimeric in vivo and move by processive motility upon release of autoinhibition.''; PubMed Europe PMC Scholia
  12. Bloom GS, Wagner MC, Pfister KK, Brady ST.; ''Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide.''; PubMed Europe PMC Scholia
  13. Cai S, Weaver LN, Ems-McClung SC, Walczak CE.; ''Kinesin-14 family proteins HSET/XCTK2 control spindle length by cross-linking and sliding microtubules.''; PubMed Europe PMC Scholia
  14. Lawrence CJ, Dawe RK, Christie KR, Cleveland DW, Dawson SC, Endow SA, Goldstein LS, Goodson HV, Hirokawa N, Howard J, Malmberg RL, McIntosh JR, Miki H, Mitchison TJ, Okada Y, Reddy AS, Saxton WM, Schliwa M, Scholey JM, Vale RD, Walczak CE, Wordeman L.; ''A standardized kinesin nomenclature.''; PubMed Europe PMC Scholia
  15. Sekine Y, Okada Y, Noda Y, Kondo S, Aizawa H, Takemura R, Hirokawa N.; ''A novel microtubule-based motor protein (KIF4) for organelle transports, whose expression is regulated developmentally.''; PubMed Europe PMC Scholia
  16. Blangy A, Lane HA, d'Hérin P, Harper M, Kress M, Nigg EA.; ''Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo.''; PubMed Europe PMC Scholia
  17. Mazumdar M, Sundareshan S, Misteli T.; ''Human chromokinesin KIF4A functions in chromosome condensation and segregation.''; PubMed Europe PMC Scholia
  18. Vale RD, Funatsu T, Pierce DW, Romberg L, Harada Y, Yanagida T.; ''Direct observation of single kinesin molecules moving along microtubules.''; PubMed Europe PMC Scholia
  19. Verhey KJ, Hammond JW.; ''Traffic control: regulation of kinesin motors.''; PubMed Europe PMC Scholia
  20. Okada Y, Yamazaki H, Sekine-Aizawa Y, Hirokawa N.; ''The neuron-specific kinesin superfamily protein KIF1A is a unique monomeric motor for anterograde axonal transport of synaptic vesicle precursors.''; PubMed Europe PMC Scholia
  21. Manning AL, Ganem NJ, Bakhoum SF, Wagenbach M, Wordeman L, Compton DA.; ''The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles during mitosis in human cells.''; PubMed Europe PMC Scholia
  22. Hirokawa N, Noda Y.; ''Intracellular transport and kinesin superfamily proteins, KIFs: structure, function, and dynamics.''; PubMed Europe PMC Scholia
  23. Mayr MI, Hümmer S, Bormann J, Grüner T, Adio S, Woehlke G, Mayer TU.; ''The human kinesin Kif18A is a motile microtubule depolymerase essential for chromosome congression.''; PubMed Europe PMC Scholia
  24. Mishima M, Kaitna S, Glotzer M.; ''Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity.''; PubMed Europe PMC Scholia
  25. Brown CL, Maier KC, Stauber T, Ginkel LM, Wordeman L, Vernos I, Schroer TA.; ''Kinesin-2 is a motor for late endosomes and lysosomes.''; PubMed Europe PMC Scholia
  26. Espeut J, Gaussen A, Bieling P, Morin V, Prieto S, Fesquet D, Surrey T, Abrieu A.; ''Phosphorylation relieves autoinhibition of the kinetochore motor Cenp-E.''; PubMed Europe PMC Scholia
  27. Kuznetsov SA, Vaisberg EA, Shanina NA, Magretova NN, Chernyak VY, Gelfand VI.; ''The quaternary structure of bovine brain kinesin.''; PubMed Europe PMC Scholia


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101313view11:20, 1 November 2018ReactomeTeamreactome version 66
100850view20:51, 31 October 2018ReactomeTeamreactome version 65
100391view19:26, 31 October 2018ReactomeTeamreactome version 64
99939view16:10, 31 October 2018ReactomeTeamreactome version 63
99495view14:43, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99144view12:40, 31 October 2018ReactomeTeamreactome version 62
93827view13:39, 16 August 2017ReactomeTeamreactome version 61
93377view11:21, 9 August 2017ReactomeTeamreactome version 61
86463view09:18, 11 July 2016ReactomeTeamreactome version 56
83275view10:37, 18 November 2015ReactomeTeamVersion54
81393view12:55, 21 August 2015ReactomeTeamVersion53
76861view08:13, 17 July 2014ReactomeTeamFixed remaining interactions
76566view11:55, 16 July 2014ReactomeTeamFixed remaining interactions
75899view09:55, 11 June 2014ReactomeTeamRe-fixing comment source
75599view10:44, 10 June 2014ReactomeTeamReactome 48 Update
74954view13:47, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74598view08:38, 30 April 2014ReactomeTeamReactome46
71654view19:36, 17 October 2013MaintBotUpdated data sources
71187view15:46, 11 October 2013EgonwReplaced DataSource Uniprot with Uniprot/TrEMBL.
44882view10:09, 6 October 2011MartijnVanIerselOntology Term : 'transport pathway' added !
42003view21:30, 4 March 2011MaintBotAutomatic update
39868view05:53, 21 January 2011MaintBotNew pathway

External references


View all...
NameTypeDatabase referenceComment
ADPMetaboliteCHEBI:16761 (ChEBI)
ATPMetaboliteCHEBI:15422 (ChEBI)
CENP-E dimerComplexR-HSA-984773 (Reactome)
CENPE ProteinQ02224 (Uniprot-TrEMBL)
CENPEProteinQ02224 (Uniprot-TrEMBL)
CentralspindlinComplexR-HSA-984587 (Reactome)
Chromokinesin monomersComplexR-HSA-984725 (Reactome)
Chromokinesin dimers R-HSA-984722 (Reactome)
Chromokinesin dimersComplexR-HSA-984722 (Reactome)
KIF11 ProteinP52732 (Uniprot-TrEMBL)
KIF11ProteinP52732 (Uniprot-TrEMBL)
KIF12 ProteinQ96FN5 (Uniprot-TrEMBL)
KIF13B ProteinQ9NQT8 (Uniprot-TrEMBL)
KIF15 ProteinQ9NS87 (Uniprot-TrEMBL)
KIF15 dimerComplexR-HSA-984823 (Reactome)
KIF15ProteinQ9NS87 (Uniprot-TrEMBL)
KIF16B ProteinQ96L93 (Uniprot-TrEMBL)
KIF18A ProteinQ8NI77 (Uniprot-TrEMBL)
KIF18A dimerComplexR-HSA-984631 (Reactome)
KIF18AProteinQ8NI77 (Uniprot-TrEMBL)
KIF18B ProteinQ86Y91 (Uniprot-TrEMBL)
KIF19 ProteinQ2TAC6 (Uniprot-TrEMBL)
KIF1A ProteinQ12756 (Uniprot-TrEMBL)
KIF1B ProteinO60333 (Uniprot-TrEMBL)
KIF1C ProteinO43896 (Uniprot-TrEMBL)
KIF20A ProteinO95235 (Uniprot-TrEMBL)
KIF20B ProteinQ96Q89 (Uniprot-TrEMBL)
KIF21A ProteinQ7Z4S6 (Uniprot-TrEMBL)
KIF21B ProteinO75037 (Uniprot-TrEMBL)
KIF22 ProteinQ14807 (Uniprot-TrEMBL)
KIF23 ProteinQ02241 (Uniprot-TrEMBL)
KIF25 ProteinQ9UIL4 (Uniprot-TrEMBL)
KIF26A ProteinQ9ULI4 (Uniprot-TrEMBL) KIF26A is atypical as it lacks ATPase activity.
KIF26B ProteinQ2KJY2 (Uniprot-TrEMBL)
KIF27 ProteinQ86VH2 (Uniprot-TrEMBL)
KIF28P ProteinB7ZC32 (Uniprot-TrEMBL)
KIF2A ProteinO00139 (Uniprot-TrEMBL)
KIF2B ProteinQ8N4N8 (Uniprot-TrEMBL)
KIF2C ProteinQ99661 (Uniprot-TrEMBL)
KIF3A ProteinQ9Y496 (Uniprot-TrEMBL)
KIF3A partnersComplexR-HSA-984629 (Reactome)
KIF3AProteinQ9Y496 (Uniprot-TrEMBL)
KIF3B ProteinO15066 (Uniprot-TrEMBL)
KIF3C ProteinO14782 (Uniprot-TrEMBL)
KIF4 R-HSA-445000 (Reactome)
KIF5A ProteinQ12840 (Uniprot-TrEMBL)
KIF5B ProteinP33176 (Uniprot-TrEMBL)
KIF5B(1-?) ProteinQ66K46 (Uniprot-TrEMBL)
KIF5C(?-?) ProteinQ6PKD1 (Uniprot-TrEMBL)
KIF6 ProteinQ6ZMV9 (Uniprot-TrEMBL)
KIF9 ProteinQ9HAQ2 (Uniprot-TrEMBL)
KIF9 dimerComplexR-HSA-984777 (Reactome)
KIF9ProteinQ9HAQ2 (Uniprot-TrEMBL)
KIFAP3 ProteinQ92845 (Uniprot-TrEMBL)
KIFAP3ProteinQ92845 (Uniprot-TrEMBL)
KIFC1 ProteinQ9BW19 (Uniprot-TrEMBL)
KIFC1ProteinQ9BW19 (Uniprot-TrEMBL)
KIFC2 ProteinQ96AC6 (Uniprot-TrEMBL)
KLC1 ProteinQ07866 (Uniprot-TrEMBL)
KLC1,KLC2,KLC3,KLC4ComplexR-HSA-983226 (Reactome)
KLC2 ProteinQ9H0B6 (Uniprot-TrEMBL)
KLC3 ProteinQ6P597 (Uniprot-TrEMBL)
KLC4 ProteinQ9NSK0 (Uniprot-TrEMBL)
Kinesin-1 heavy chainComplexR-HSA-983211 (Reactome)
Kinesin-13 dimers R-HSA-990485 (Reactome)
Kinesin-13 dimersComplexR-HSA-990485 (Reactome)
Kinesin-13 monomersComplexR-HSA-990510 (Reactome)
Kinesin-14ComplexR-HSA-1015869 (Reactome)
Kinesin-1ComplexR-HSA-983227 (Reactome)
Kinesin-2ComplexR-HSA-984619 (Reactome)
Kinesin-3 dimers R-HSA-984608 (Reactome)
Kinesin-3 dimersComplexR-HSA-984608 (Reactome)
Kinesin-3 monomersComplexR-HSA-984739 (Reactome)
Kinesin-4 homodimers R-HSA-984704 (Reactome)
Kinesin-5 homotetramerComplexR-HSA-984691 (Reactome)
Kinesin-6ComplexR-HSA-984628 (Reactome)
Kinesins:microtubuleComplexR-HSA-983245 (Reactome)
KinesinsComplexR-HSA-8849364 (Reactome)
KinesinsComplexR-HSA-984770 (Reactome)
Microtubule protofilament R-HSA-8982424 (Reactome)
MicrotubuleComplexR-HSA-190599 (Reactome)
RACGAP1 ProteinQ9H0H5 (Uniprot-TrEMBL)
RACGAP1ProteinQ9H0H5 (Uniprot-TrEMBL)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
ADPArrowR-HSA-983259 (Reactome)
ATPR-HSA-983259 (Reactome)
CENP-E dimerArrowR-HSA-984689 (Reactome)
CENPER-HSA-984689 (Reactome)
CentralspindlinArrowR-HSA-984648 (Reactome)
Chromokinesin monomersR-HSA-984671 (Reactome)
Chromokinesin dimersArrowR-HSA-984671 (Reactome)
KIF11R-HSA-984606 (Reactome)
KIF15 dimerArrowR-HSA-984821 (Reactome)
KIF15R-HSA-984821 (Reactome)
KIF18A dimerArrowR-HSA-984609 (Reactome)
KIF18AR-HSA-984609 (Reactome)
KIF3A partnersR-HSA-984708 (Reactome)
KIF3AR-HSA-984708 (Reactome)
KIF9 dimerArrowR-HSA-984775 (Reactome)
KIF9R-HSA-984775 (Reactome)
KIFAP3R-HSA-984708 (Reactome)
KIFC1R-HSA-990478 (Reactome)
KLC1,KLC2,KLC3,KLC4R-HSA-983194 (Reactome)
Kinesin-1 heavy chainR-HSA-983194 (Reactome)
Kinesin-13 dimersArrowR-HSA-990489 (Reactome)
Kinesin-13 monomersR-HSA-990489 (Reactome)
Kinesin-14ArrowR-HSA-990478 (Reactome)
Kinesin-1ArrowR-HSA-983194 (Reactome)
Kinesin-2ArrowR-HSA-984708 (Reactome)
Kinesin-3 dimersArrowR-HSA-984733 (Reactome)
Kinesin-3 monomersR-HSA-984733 (Reactome)
Kinesin-5 homotetramerArrowR-HSA-984606 (Reactome)
Kinesin-6R-HSA-984648 (Reactome)
Kinesins:microtubuleArrowR-HSA-983259 (Reactome)
Kinesins:microtubuleArrowR-HSA-983266 (Reactome)
Kinesins:microtubuleR-HSA-983259 (Reactome)
KinesinsR-HSA-983266 (Reactome)
MicrotubuleR-HSA-983266 (Reactome)
R-HSA-983194 (Reactome) Kinesin-1 is a heterotetramer of two heavy chains (HCs) and two light chains (LCs). The HC tail binds microtubules and inhibits ATPase activity by interacting with the enzymatic HC heads. LCs regulate the head and microtubule-binding activities of the HC tail by reducing the affinity of the head-tail interaction over tenfold. By a separate mechanism LCs inhibit microtubule binding.
R-HSA-983259 (Reactome) Kinesins consume ATP to power the motor which allows them to move along microtubules. The motor region contains highly conserved Switch 1 (SSRSH) and 2 (DLAGSE) motifs which change conformation during ATP hydrolysis (Rice et al. 1999). These form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves & Holmes 1999). This closed conformation has now been seen by cryo-electron microscopy in human conventional kinesin (Sindelar & Downing 2010) and in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).
R-HSA-983266 (Reactome) All kinesins contain a motor domain or head, the position varies but it is structurally highly conserved (Kull et al. 1996, Sablin et al. 1996). The microtubule-binding site includes structural elements which interact with tubulin and undergo movement between the ADP and ATP bound states. The highly conserved switch I (SSRSH) and II (DLAGSE) motifs, which change in conformation during the ATP hydrolysis cycle, form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves & Holmes 1999). This closed conformation has now been seen in a crystal structure of the frog kinesin-5 Eg5 (Parke et al. 2010).
R-HSA-984606 (Reactome) Kinesin-5 motors are bipolar homotetramers with two motor domains at each end, separated by a stalk/tail region (Cole et al. 1994). During mitosis, Kinesin-5 motors function near the spindle midzone to maintain pole to pole distance. Motor domains attach to microtubules from opposite poles and translocate towards the plus ends, thereby pushing the spindle poles apart (Kapitein et al. 2005). Kinesin-5 is also involved in axon growth (Myers & Baas 2007).
R-HSA-984609 (Reactome) Kinesin-8 is a plus-end-directed dimeric kinesin with an internal motor domain (Loughlin et al. 2008) that can depolymerize stable microtubuless specifically at their plus-ends (Pereira et al. 1997) in a length-dependent manner (Varga et al. 2006). Human kinesin-8 KIF18A is believed to promote chromosome congression by attenuating chromosome oscillation magnitudes (Stumpff et al. 2008).
R-HSA-984648 (Reactome) Cytokinesis requires the central spindle, which forms during anaphase by the bundling of antiparallel nonkinetochore microtubules. Microtubule bundling and completion of cytokinesis require MKLP1, a kinesin-6 family member, and RACGAP1 (MgcRacGap), which contains a RhoGAP domain. These form a heterotetrameric complex known as centralspindlin. Centralspindlin, but not its individual components, strongly promotes microtubule bundling in vitro.
R-HSA-984671 (Reactome) Chromokinesins consist of the kinesin-4 and kinesin-10 families.They act in various steps of mitosis, including chromosome condensation, metaphase alignment, chromosome segregation and cytokinesis (Mazumdar & Misteli 2005). Both families consist of homodimeric microtubule-based plus-end directed motor proteins (Sekine et al. 1994, Yajima et al. 2003).
R-HSA-984689 (Reactome) Human kinesin-7, or CENP-E was one of the first kinesins to be discovered (Yen et al. 1991). It is essential for mammalian development, having a role in stabilizing kinetochore-microtubule capture (Putkey et al. 2002), CENP-E is an integral component of kinetochore corona fibers that link centromeres to spindle microtubules and localizes to kinetochores throughout all phases of mitotic chromosome movement (early premetaphase through anaphase A). Though originally reported to be minus-end-directed it is now believed to be a plus-end-directed dimeric kinesin (Espeut et al. 2008). It is sequestered in the cytoplasm until nuclear envelope breakdown and then localizes to its chromosomal cargo at the kinetochores (Brown et al. 1996).
R-HSA-984708 (Reactome) Kinesin-2 is a heterotrimer with two different motor subunits and an accessory protein that is believed to interact with the cargo, or possibly regulate motor activity (Marszalek & Goldstein 2002). The motor domain interacts with microtubules and contains the ATPase used to translocate the holoenzyme along the microtubule. The coiled-coil stalk is where the two motor subunits interact with each other to form a stable heterodimer. The tail domains interact with the KAP3 non-motor accessory subunit. Kinesin-2 is a plus-end directed kinesin involved in photoreceptor cell function (Jimeno et al. 2006) and normal steady-state localization of late endosomes/lysosomes (Brown et al. 2005).
R-HSA-984733 (Reactome) Kinesin-3 drives the transport of synaptic vesicle precursors to axon terminals. Loss of the Caenorhabditis elegans protein Unc104, eqivalent to human KIF1A, results in decreased synaptic vesicles in axonal growth cones. In mice loss of KIF1A caused severe motor and sensory abnormalities associated with neuronal cell death (Yonekawa et al. 1998). Kinesin-3 is often described as monomeric, but has recently been shown to be functionally dimeric (Hammond et al. 2009).
R-HSA-984775 (Reactome) KIF9 has the coiled-coil domain typical of the dimeric kinesins and is believed to function as a dimer.
R-HSA-984821 (Reactome) Kif15 (human kinesin-12) is by analogy with orthologous proteins believed to be a plus-end-directed motor. It cooperates with kinesin-5 to promote bipolar spindle assembly during cell division (Tanenbaum et al. 2009), with a mechanism that is distinct from that of kinesin-5 (Vanneste et al. 2009).
R-HSA-990478 (Reactome) Kinesin-14 proteins have a C-terminal motor domain. At least four members of the group (Dm Ncd, Sc KAR3, Cg CHO2, At KCBP) have been demonstrated to be minus-end directed motors (Walker et al. 1990), in contrast to the usual plus-end directed motility of other kinesin proteins.

During spindle formation, Kinesin-14 cross-links antiparallel microtubules and slides them together (thereby generating inward forces) to balance the outward forces generated by plus-end-directed kinesins of the Kinesin-5 family. Kinesin-14 family members also gather microtubule minus-ends and focus them into spindle poles. Mutation or inhibition of Kinesin-14 family members often results in disordered or splayed meiotic spindle poles (Ambrose et al. 2005).
R-HSA-990489 (Reactome) Kinesin-13 proteins are homodimeric with the kinesin motor in the middle of the amino acid sequence. They induce microtubule depolymerization by disassembling tubulin subunits from the polymer end (Desai et al. 1999).
RACGAP1R-HSA-984648 (Reactome)
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