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Kinesin-like protein KIF11

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1534:– the ability of a kinesin to take multiple steps along the microtubule without dissociating. Kinesin-5 in this setup has shown bi-directionality. Thus it can "walk" in both direction. The switching of direction is controlled with high precision. In single molecule motility assays, velocities for Kinesin-5 were similar to those seen in microtubule gliding assays, and the motor was observed to be weakly processive. In optical trap experiments, Kinesin-5 molecules are attached to a bead that can be held in place by a finely focused laser. By moving the bead close to a microtubule, the kinesin can bind to the microtubule and begin stepping, pulling the bead along behind it. Since the bead is being held in place by the trap laser, it acts like a spring and exerts a force that resists the forward movement of the kinesin. This allows for the measurement of the stall force – the maximum amount of force that can be exerted by a motor before it releases from the microtubule. Optical trap experiments showed that Kinesin-5 generates a maximum of 7 picoNewtons of force before releasing, but that its behavior differs from that of other kinesins in that there was no observable plateau phase in which the motor "struggles" at its maximal force generation before letting go. Extrapolation of kinetic data suggests that the maximal observed force generated in the optical trap by Kinesin-5 is actually an underestimate and that it theoretically can exert up to 9 picoNewtons of force as a maximum, although further experimental work is required to test this. 1489:
studies on Kinesin-5 kinetics has been on the human protein. X-ray crystallography, cryo-electron microscopy, and real-time infrared spectroscopy have been used to measure the structure of Kinesin-5 in the different catalytic intermediate states. Changes in the secondary structure, or conformational switching, is required to convert and amplify biochemical changes in the catalytic active site into larger movements necessary for cellular motion. For example, the first step of ATP hydrolysis, which is the attack of the terminal phosphate of ATP by a water molecule, had not been observed by x-ray crystallography in any kinesin protein, until recently in Kinesin-5. This crystal structure showed that there was not one, but rather two, water molecules and they are in close association with each other. A two-water catalytic model was proposed and confirmed by an alternate method to track Kinesin-5 catalysis in real-time and in a kinesin protein in a different subfamily. Two-water catalytic models also are proposed in a divergent motor protein, myosin, and observed experimentally in one of its crystal structures.
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based on a predicted balance of motor forces acting in opposition within the spindle microtubules. Still, it is not clear whether all the structural elements required for spindle assembly are known, or how the motors, including Kinesin-5, might be regulated in space and time. Such caveats make assessment of such models difficult. Recent data, however, finds that aspects of the 'force balance' model that posit spindle length and stability to be mediated by a balance between the minus-end directed microtubule sliding and plus-end directed microtubule sliding by opposing motors in insect cells, seems not to be the case in mammalian cells. The process of self-assembly of the mitotic spindle remains a major unsolved question in cell biology, and a robust model awaits further details of the regulation and behavior of various microtubule motors and structural elements that compose this machinery.
1501:). Conventional kinesin dimerizes in such a manner that the catalytic (head) domains are together on one end of the complex to facilitate hand-over-hand movement along a microtubule that enables long-range, directed transport of cellular cargoes. The unique assembly of Kinesin-5 proteins not only organizes the protein complex for a different cellular function (antiparallel microtubule sliding, described above) but also made it difficult to study the mechanical properties of the motor using the classical experiments that were designed for dimeric kinesins. These obstacles have been overcome by either adapting the original experiments to analyze the tetrameric organization of Kinesin-5, or by working with shorter Kinesin-5 proteins that form dimers like conventional kinesin. 1632:). This syndrome is observed as an autosomal dominant disorder with variable expressivity but can also be sporadic. It is characterized by mild-to-severe microcephaly, often associated with developmental delay, ocular defects and lymphedema, usually on the dorsum of the feet. Phenotypic evaluation of patients (n = 87) revealed microcephaly in 91%, eye anomalies in 72%, intellectual disability in 67% and lymphedema in 47% of the patients. Unaffected carriers were rare (4 out of 87: 5%). Family history is not a requisite for diagnosis; 31% (16 out of 52) were de novo cases. All inherited cases, and 50% of sporadic cases of MCLMR are due to germline KIF11 mutations. 1416:
allosteric inhibitors has been used to probe the specific role of Kinesin-5 in mitotic spindle assembly as well as fine dissection of motor domain function. Through this work it was found that, in mammalian cells, Kinesin-5 is required for the initial assembly of the mitotic spindle during prophase and prometaphase, but is dispensable to traverse subsequent anaphase during a round of mitosis. Also, the binding of the Kinesin-5 inhibitors to an allosteric site on the motor interrupts the mechanism by which this enzyme converts the chemical energy of ATP hydrolysis into the mechanical work of moving microtubules, thus providing insight on how this enzyme works.
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within the superfamily. The L5 loop in human Kinesin-5 closes around the inhibitor and is open in the absence of inhibitor. These structural changes are correlated with other changes in the catalytic active site. Other sites of inhibitor binding have been identified in the human Kinesin-5 motor domain. For inhibitors that bind to the L5 pocket, the mechanism of inhibition is that they slow ADP release from the catalytic active site and inhibit ATP-dependent directional motion. However, a previously unknown diffusive motion by Kinesin-5 along microtubules was uncovered when monastrol inhibited the motor domain.
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mutations in the KIF11 gene convey resistance of mitotic cell lines to inhibitors such as monastrol and STLC. For example, point mutations in the inhibitor binding pocket, R119A, D130A, L132A, I136A, L214A and E215A confer resistance to monastrol, while R119A, D130A and L214A mutations confer resistance to STLC. In contrast to the loss-of-function experiments, a gain-of-function experiment using Drosophila Kinesin-5 showed that all L5-directed inhibitors do not allosterically communicate in the same way within the Kinesin-5 motor domain.
483: 380: 405: 512: 411: 1648: 1445:. In mature neurons, KIF11 restricts the movement of short microtubules in dendrites, contributing to the formation of characteristic shape of dendrites. KIF11 is also expressed in adult dorsal root ganglion neurons, although at a much diminished level. In adult neurons It has a similar effect on inhibiting the rate of short microtubule transport so pharmacological inhibition and 49: 1429:
dendrites. It has been shown, for example, that neurons remain fully viable in the background of a knock-down of Kinesin-5, but that changes in neuronal development and morphogenesis ensue. In developing neurons pharmacological inhibition and siRNA knockdown of KIF11 results in longer axons, more branches, fewer bouts of axon retraction and the inability of
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was indeed capable of carrying out the role that had been proposed for it in mitosis – sliding oppositely oriented microtubules in the mitotic spindle. To study the behavior of individual Kinesin-5 molecules, single molecule motility assays were performed by attaching microtubules to a glass surface, then adding a dilute solution of Kinesin-5 with a
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microtubule-associated Kinesin-5 is phosphorylated at this residues. While additional phosphosites or other post-translational modifications within the Kinesin-5 tail, stalk, and motor have been identified, no other modifications have been proven as necessary for Kinesin-5 to perform its necessary tasks in mitosis.
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Matthieu J SchlΓΆgel, Antonella Mendola, Elodie FastrΓ©, Pradeep Vasudevan, Koen Devriendt, Thomy JL de Ravel, Hilde Van Esch, Ingele Casteels, Ignacio Arroyo Carrera, Francesca Cristofoli, Karen Fieggen, Katheryn Jones, Mark Lipson, Irina Balikova, Ami Singer, Maria Soller, MarΓ­a Mercedes Villanueva,
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The majority of human Kinesin-5 inhibitors are selective, because they bind to a drug 'hot spot', composed of residues from the Ξ±2 and Ξ±3 helices and a flexible L5 loop on the surface of the motor domain. This L5 loop has high sequence variability amongst the Kinesin-5 orthologs and other kinesins
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Inhibitors of KIF11 have been developed as chemotherapeutic agents in the treatment of cancer. Drugs that specifically inhibit only human Kinesin-5 are alternatives to the taxanes and vinc alkaloids that target microtubules, and thus all cells, and that are currently used clinically. Inhibition of
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and binds to microtubules. Kinesin-5 motors assemble into a bipolar homotetrameric structure that is capable of sliding apart bundles of anti-parallel oriented microtubules. This motor is essential for mitosis in most organisms, wherein it participates in the self-assembly of the microtubule-based
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By attaching microtubules to the glass surface first, then adding Kinesin-5 with free microtubules in solution, it was possible to adapt the microtubule gliding assays to show that Kinesin-5 can crosslink two microtubules and move them in opposite directions. This experiment showed that Kinesin-5
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There are many models that attempt to explain the self-assembly of the mitotic spindle based upon microtubules as a structural element, and a set of microtubule motors, including Kinesin-5 to move and order them. Many of these models attempt to explain the steady state of the spindle at metaphase
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Cox CD, Breslin MJ, Mariano BJ, Coleman PJ, Buser CA, Walsh ES, Hamilton K, Huber HE, Kohl NE, Torrent M, Yan Y, Kuo LC, Hartman GD (2005). "Kinesin spindle protein (KSP) inhibitors. Part 1: The discovery of 3,5-diaryl-4,5-dihydropyrazoles as potent and selective inhibitors of the mitotic kinesin
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The most striking outcomes of the analysis of Kinesin-5 motility is that it is slow – about 10 times slower than conventional Kinesin-1 – with a velocity in the range of 50 nanometers per second and that it could generate very high levels of mechanical force (7-9 picoNewtons per molecule). These
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knockdown of adult KIF11 may be a potential therapeutic tool for the augmentation of adult axon regeneration. However, a clear in vivo role for Kinesin-5 in neurogenesis remains to be elucidated. Of note is that unusual peripheral neuropathies have not been observed in patients undergoing recent
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Although Kinesin-5 is required in all cells during cell division, it does not appear to play a major role in the metabolism of most non-dividing cells. Among non-dividing cells, Kinesin-5 is most enriched within neurons, wherein it decorates the large microtubule bundles extending into axons and
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A second purpose of mutational studies is to understand how drug resistance in cells is conferred from only changing one residue. These changes in the inhibitor-binding pocket are correlated with structural modification, or twist, of the central beta-sheet of the Kinesin-5 motor domain. In this
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Kinesin-5, like all motor proteins, breaks down ATP into ADP and inorganic phosphate, using a water molecule, and converts the chemical energy to force and motion along microtubules. Kinetic experiments reveal rates of how fast intermediate steps in catalysis occur and the most extensive set of
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The role of specific residues in the L5 pocket (L5, Ξ±2, and Ξ±3) in human Kinesin-5 has been tested, but not yet been systematically explored. The initial goal of these mutation experiments was to determine which residues had greatest pharmacological importance in drug development. For example,
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The discovery of small chemical inhibitors of human Kinesin-5 through a pioneering in vitro phenotypic screening on cancer cell lines has led to both the development of new anticancer therapeutic agents, and to novel tools to probe the mechanism of microtubule motor proteins. This toolkit of
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was discovered in a chemical screen of a large library of cell permeable compounds. Since then, over 100 different chemical classes of allosteric inhibitors have been identified in the scientific literature and they have a wide range in potency against human Kinesin-5. Common KIF11 inhibitors
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Loss of Kinesin-5 function from the onset of mitosis in most eukaryotic organisms examined, including animals, plants, and fungi, results in catastrophic failure of mitosis. This motor's function is crucial during the onset of mitosis, wherein its loss of function results in the collapse, or
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In most eukaryotic cells, Kinesin-5 is thought to form cross-bridges between pairs of oppositely oriented microtubules in prophase and prometaphase and drives apart duplicated centrosomes during the formation of the mitotic spindle. This permits the establishment of a steady-state bipolar
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assays. In microtubule gliding assays, kinesins are attached to a glass surface and microtubules are laid down over the top. Since the motors are attached to the glass, their motile behavior translates into movement of the microtubule across the anchored kinesins, akin to someone
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within its C-terminal tail. Once Kinesin-5 is phosphorylated at this residue in early prophase, it localizes to the mitotic spindle where it binds to microtubules. An additional phosphosite was identified on the Kinesin-5 tail in 2008, however, only approximately 3% of the total
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Small-molecule inhibitors are not only important tools for understanding nanomotors in cells; they are also have potential for serving as tools in the clinic. Induced by human Kinesin-5 inhibitors, mitotic arrest results in apoptosis in some tumor cell lines and
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manner, the L5 loop may be able to directly control nucleotide binding and beta-sheet twist can manipulate the adjacent microtubule-binding site. This may explain how tumor cells rapidly can become drug-resistant to KIF11 inhibitors.
1470:, associates with Kinesin-5 in mitosis. Their interaction is necessary for Kinesin-5 localization to the mitotic spindle, for stabilizing the spindle, and for spindle pole segregation. Kinesin-5 has been shown to interact with the 3499:
Yoon SY, Choi JE, Huh JW, Hwang O, Lee HS, Hong HN, Kim D (April 2005). "Monastrol, a selective inhibitor of the mitotic kinesin Eg5, induces a distinctive growth profile of dendrites and axons in primary cortical neuron cultures".
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inversion, of the spindle poles leaving centrally positioned centrosome pairs flanked by a radial array of microtubules with peripheral condensed chromosomes. The one exception to this effect is mitosis within the nematode,
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subunit p150Glued as well as many other cell cycle related proteins in vivo and in vitro, however, additional experimentation is needed to confirm that their association is necessary for Kinesin-5 to function normally.
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Haque SA, Hasaka TP, Brooks AD, Lobanov PV, Baas PW (2004). "Monastrol, a prototype anti-cancer drug that inhibits a mitotic kinesin, induces rapid bursts of axonal outgrowth from cultured postmitotic neurons".
1597:(LY2523355) (Eli Lilly) have entered into clinical trials. Although second-generation Kinesin-5 inhibitors have had better success, none have been fully developed and marketed as an anti-cancer treatment. 1497:
The antiparallel tetrameric organization of the Kinesin-5 family is fundamentally different from the majority of other kinesins that are dimers, such as the well-characterized conventional Kinesin-1 (
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attached. This experimental setup enables the observer to follow separate Kinesin-5 molecules as they "walk" along the microtubule, providing not only information about velocity, but also about
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Feuk L, McCarthy S, Andersson B, Prince JA, Brookes AJ (July 2005). "Mutation screening of a haplotype block around the insulin degrading enzyme gene and association with Alzheimer's disease".
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Yan Y, Sardana V, Xu B, Homnick C, Halczenko W, Buser CA, Schaber M, Hartman GD, Huber HE, Kuo LC (2004). "Inhibition of a mitotic motor protein: where, how, and conformational consequences".
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separation and establishing a bipolar spindle during cell mitosis. The human kinesin-5 protein has been actively studied for its role in mitosis and its potential as a therapeutic target for
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Khoury HJ, Garcia-Manero G, Borthakur G, Kadia T, Foudray MC, Arellano M, Langston A, Bethelmie-Bryan B, Rush S, Litwiler K, Karan S, Simmons H, Marcus AI, Ptaszynski M, Kantarjian H (2012).
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Wojcik EJ, Dalrymple NA, Alford SR, Walker RA, Kim S (2004). "Disparity in allosteric interactions of monastrol with Eg5 in the presence of ADP and ATP: a difference FT-IR investigation".
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Wilde A, Lizarraga SB, Zhang L, Wiese C, Gliksman NR, Walczak CE, Zheng Y (2001). "Ran stimulates spindle assembly by altering microtubule dynamics and the balance of motor activities".
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Brier S, Lemaire D, Debonis S, Forest E, Kozielski F (2004). "Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of the mitotic kinesin Eg5".
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to turn on contact with repulsive substrates. In migratory neurons, inhibition of KIF11 causes neurons to migrate in a random pattern and form shorter leading processes. KIF11, like
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Currently, there are over 70 different eukaryotic kinesin-5 proteins identified by sequence similarity. Members of this protein family are known to be involved in various kinds of
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Iwakiri Y, Kamakura S, Hayase J, Sumimoto H (2013). "Interaction of NuMA protein with the kinesin Eg5: its possible role in bipolar spindle assembly and chromosome alignment".
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Ulaganathan V, Talapatra SK, Rath O, Pannifer A, Hackney DD, Kozielski F (2013). "Structural insights into a unique inhibitor binding pocket in kinesin spindle protein".
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Tihy F, Kress M, Harper M, Dutrillaux B, Lemieux N (August 1992). "Localization of the human kinesin-related gene to band 10q24 by fluorescence in situ hybridization".
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mitotic spindle, but is not otherwise required for cell viability. The motor may also play a role in the proper development of mammalian neuronal processes, including
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Hotha S, Yarrow JC, Yang JG, Garrett S, Renduchintala KV, Mayer TU, Kapoor TM (May 2003). "HR22C16: a potent small-molecule probe for the dynamics of cell division".
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Sharp DJ, Yu KR, Sisson JC, Sullivan W, Scholey JM (May 1999). "Antagonistic microtubule-sliding motors position mitotic centrosomes in Drosophila early embryos".
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Sakowicz R, Finer JT, Beraud C, Crompton A, Lewis E, Fritsch A, Lee Y, Mak J, Moody R, Turincio R, Chabala JC, Gonzales P, Roth S, Weitman S, Wood KW (May 2004).
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Smith CA, Rayment I (1996). "X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution".
5436:"Quantitative live imaging of cancer and normal cells treated with Kinesin-5 inhibitors indicates significant differences in phenotypic responses and cell fate" 5293:
Kwok BH, Kapitein LC, Kim JH, Peterman EJ, Schmidt CF, Kapoor TM (2006). "Allosteric inhibition of kinesin-5 modulates its processive directional motility".
2651:"The Caenorhabditis elegans Aurora B kinase AIR-2 phosphorylates and is required for the localization of a BimC kinesin to meiotic and mitotic spindles" 1056: 1037: 341: 5626:
Purcell JW, Davis J, Reddy M, Martin S, Samayoa K, Vo H, Thomsen K, Bean P, Kuo WL, Ziyad S, Billig J, Feiler HS, Gray JW, Wood KW, Cases S (2010).
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Miller K, Ng C, Ang P, Brufsky AM, Lee SC, Dees EC, Piccart M, Verrill M, Wardley A, Loftiss J, Bal J, Yeoh S, Hodge J, Williams D, Dar M, Ho PT.
1441:, is thought to act as a restrictor of short microtubules moving bi-directionally along the axon, exerting forces antagonistically to cytoplasmic 1921:"Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo" 1337:, which are nanomotors that move along microtubule tracks in the cell. Named from studies in the early days of discovery, it is also known as 1412:, in which Kinesin-5 is not strictly essential for mitosis, but nonetheless has considerable impact on the overall fidelity of cell division. 6439: 2320:
Acar S, Carlson DB, Budamagunta MS, Yarov-Yarovoy V, Correia JJ, Ninonuevo MR, Jia W, Tao L, Leary JA, Voss JC, Evans JE, Scholey JM (2013).
1805: 1787: 6121:"Genetic variants in a haplotype block spanning IDE are significantly associated with plasma Abeta42 levels and risk for Alzheimer disease" 5892:"No evidence of locus heterogeneity in familial microcephaly with or without chorioretinopathy, lymphedema, or mental retardation syndrome" 5395:"Inhibition of the mitotic kinesin Eg5 up-regulates Hsp70 through the phosphatidylinositol 3-kinase/Akt pathway in multiple myeloma cells" 2168:
Sawin KE, LeGuellec K, Philippe M, Mitchison TJ (October 1992). "Mitotic spindle organization by a plus-end-directed microtubule motor".
505: 6078:"TOGp, the human homolog of XMAP215/Dis1, is required for centrosome integrity, spindle pole organization, and bipolar spindle assembly" 5873: 2564:
Sawin KE, Mitchison TJ, Wordeman LG (1992). "Evidence for kinesin-related proteins in the mitotic apparatus using peptide antibodies".
1518: 2024:"The bipolar kinesin, KLP61F, cross-links microtubules within interpolar microtubule bundles of Drosophila embryonic mitotic spindles" 1256: 1263: 482: 5246:"ATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrol" 5833: 6407: 1574: 5677:"A phase 1 dose-escalation study of ARRY-520, a kinesin spindle protein inhibitor, in patients with advanced myeloid leukemias" 1774: 1753: 3979:"Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150" 404: 379: 5834:"Mutations in the human kinesin Eg5 that confer resistance to monastrol and S-trityl-L-cysteine in tumor derived cell lines" 5583:
Kathman SJ, Williams DH, Hodge JP, Dar M (2007). "A Bayesian population PK-PD model of ispinesib-induced myelosuppression".
3161:"The functional antagonism between Eg5 and dynein in spindle bipolarization is not compatible with a simple push-pull model" 2467:
Enos AP, Morris NR (1990). "Mutation of a gene that encodes a kinesin-like protein blocks nuclear division in A. nidulans".
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Kinesin-5 causes cells to undergo mitotic arrest, undergo apoptosis and form monoaster spindles. The first KIF11 inhibitor,
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The 2013 version of this article was updated by an external expert under a dual publication model. The corresponding
518: 417: 3816:"Tyrosines in the kinesin-5 head domain are necessary for phosphorylation by Wee1 and for mitotic spindle integrity" 3726:"The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site necessary for mitotic spindle formation" 1668:
Edward J Wojcik, Rebecca S Buckley, Jessica Richard, Liqiong Liu, Thomas M Huckaba, Sunyoung Kim (1 December 2013).
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values come from three types of experimental data: microtubule gliding assays, single molecule motility assays, and
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El-Nassan HB (2012). "Advances in the discovery of kinesin spindle protein (Eg5) inhibitors as antitumor agents".
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Ertekin-Taner N, Allen M, Fadale D, Scanlin L, Younkin L, Petersen RC, Graff-Radford N, Younkin SG (April 2004).
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Kinesin-5 is also regulated through direct interaction with other proteins. The microtubule-associated protein,
3007:"Loop 5-directed compounds inhibit chimeric kinesin-5 motors: implications for conserved allosteric mechanisms" 1101: 329: 5500:"ZM336372 Induces Apoptosis Associated With Phosphorylation of GSK-3Ξ² in Pancreatic Adenocarcinoma Cell Lines" 5162:"NSC 622124 inhibits human Eg5 and other kinesins via interaction with the conserved microtubule-binding site" 4445:
Chan Q, Nitta R, Inoue S, Hirokawa N (2013). "Structural Basis for the ATP-Induced Isomerization of Kinesin".
3403:"Kinesin-12, a mitotic microtubule-associated motor protein, impacts axonal growth, navigation, and branching" 2703:"In vitro screening for inhibitors of the human mitotic kinesin Eg5 with antimitotic and antitumor activities" 4912:
Huszar D, Theoclitou ME, Skolnik J, Herbst R (2009). "Kinesin motor proteins as targets for cancer therapy".
4774:"Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro" 4611:"The rate of bipolar spindle assembly depends on the microtubule-gliding velocity of the mitotic kinesin Eg5" 3775:"Parkin regulates Eg5 expression by Hsp70 ubiquitination-dependent inactivation of c-Jun NH2-terminal kinase" 2510:
Hagan I, Yanagida M (1990). "Novel potential mitotic motor protein encoded by the fission yeast cut7+ gene".
1082: 2221:"Expression of the mitotic motor protein Eg5 in postmitotic neurons: implications for neuronal development" 2022:
Sharp DJ, McDonald KL, Brown HM, Matthies HJ, Walczak C, Vale RD, Mitchison TJ, Scholey JM (January 1999).
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Phase II, open label study of SB-715992 (ispinesib) in subjects with advanced or metastatic breast cancer
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KIF11 mutations have been widely described in cancer, and many trials with KIF11 inhibitors are ongoing.
1656: 393: 2757:"Probing spindle assembly mechanisms with monastrol, a small molecule inhibitor of the mitotic kinesin" 1360:
dynamics and essential for mitosis. The function of this gene product includes chromosome positioning,
5076:"Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker" 5958: 5737: 5349: 4857: 4821:
Zhang Y, Xu W (August 2008). "Progress on kinesin spindle protein inhibitors as anti-cancer agents".
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Kim ED, Buckley R, Learman S, Richard J, Parke C, Worthylake DK, Wojcik EJ, Walker RA, Kim S (2010).
2855: 2519: 2333: 2177: 1978: 5628:"Activity of the kinesin spindle protein inhibitor ispinesib (SB-715992) in models of breast cancer" 5129: 4660:"A nonmotor microtubule binding site in kinesin-5 is required for filament crosslinking and sliding" 4529: 3215: 2971: 308: 5393:
Liu M, Aneja R, Liu C, Sun L, Gao J, Wang H, Dong JT, Sarli V, Giannis A, Joshi HC, Zhou J (2006).
1334: 2908:"Allosteric drug discrimination is coupled to mechanochemical changes in the kinesin-5 motor core" 6306: 6150: 6029: 5608: 5375: 5318: 4980: 4937: 4887: 4396:"Real-time structural transitions are coupled to chemical steps in ATP hydrolysis by Eg5 kinesin" 4145: 4088: 3609: 3141: 2732: 2543: 2492: 2201: 2096: 1384:
to maintain spindle bipolarity. The motor domain or motor head is at the N-terminus and performs
353: 6043:"N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso" 2844:"The conserved L5 loop establishes the pre-powerstroke conformation of the Kinesin-5 motor, eg5" 2426:
Bannigan A, Scheible WR, Lukowitz W, Fagerstrom C, Wadsworth P, Somerville C, Baskin TI (2007).
1594: 1239: 1218: 1192: 1171: 2612:"Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen" 1582: 1578: 6298: 6269: 6224: 6179: 6142: 6107: 6064: 6021: 5986: 5923: 5856: 5814: 5763: 5706: 5657: 5600: 5565: 5529: 5465: 5416: 5367: 5310: 5275: 5226: 5191: 5142: 5097: 5056: 5015: 4972: 4929: 4879: 4838: 4803: 4754: 4697: 4640: 4591: 4542: 4497: 4462: 4427: 4376: 4325: 4284: 4235: 4186: 4137: 4080: 4045: 4000: 3959: 3910: 3853: 3796: 3755: 3706: 3647: 3601: 3566: 3517: 3481: 3432: 3383: 3334: 3277: 3228: 3182: 3133: 3090: 3038: 2984: 2939: 2881: 2824: 2786: 2724: 2701:
DeBonis S, Skoufias DA, Lebeau L, Lopez R, Robin G, Margolis RL, Wade RH, Kozielski F (2004).
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KIF11 (also known as kinesin-5 and Eg5) is a homotetramer which cross-links anti-parallel
1319: 573: 2273:"Kinesin-5, a mitotic microtubule-associated motor protein, modulates neuronal migration" 5962: 5741: 5353: 4732: 4675: 4626: 4123: 3888: 3831: 3682: 3354:"Microtubule redistribution in growth cones elicited by focal inactivation of kinesin-5" 3312: 3121: 2859: 2523: 2337: 2181: 2116:"A "slow" homotetrameric kinesin-related motor protein purified from Drosophila embryos" 1982: 6415: 6264: 6237: 6219: 6192: 5918: 5891: 5809: 5782: 5758: 5725: 5701: 5676: 5652: 5627: 5524: 5499: 5460: 5435: 5270: 5245: 5186: 5161: 4798: 4773: 4749: 4716: 4692: 4659: 4586: 4561: 4480:
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6302: 6273: 6254: 6228: 6209: 6146: 6111: 6068: 6025: 5990: 5971: 5927: 5860: 5818: 5767: 5710: 5661: 5604: 5569: 5533: 5469: 5420: 5411: 5394: 5371: 5314: 5279: 5230: 5195: 5146: 5101: 5092: 5075: 5060: 5019: 5011: 4976: 4933: 4883: 4842: 4807: 4758: 4701: 4644: 4595: 4501: 4466: 4431: 4380: 4329: 4239: 4190: 4141: 4084: 4049: 3963: 3914: 3857: 3800: 3791: 3774: 3759: 3651: 3605: 3570: 3521: 3485: 3436: 3387: 3338: 3281: 3232: 3186: 3137: 3094: 3042: 2988: 2943: 2885: 2828: 2790: 2728: 2684: 2635: 2453: 2363: 2306: 2092: 1883: 1713: 6183: 4577: 4562:"Microtubule cross-linking triggers the directional motility of kinesin-5" 4546: 4288: 4270: 4004: 3945: 3710: 3401:
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with or without chorioretinopathy, lymphedema, or mental retardation (
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Kinesin-like protein KIF11 is a member of the 528: 427: 3297:"Kinesin-5 is essential for growth-cone turning" 3625: 3623: 3000: 2998: 2901: 2899: 2897: 2895: 2802: 2800: 2750: 2748: 2746: 2696: 2694: 2605: 2603: 2601: 2599: 2597: 2595: 2266: 2264: 27:Protein-coding gene in the species Homo sapiens 2559: 2557: 2163: 2161: 1771:GRCm38: Ensembl release 89: ENSMUSG00000012443 4658:Weinger JS, Qiu M, Yang G, Kapoor TM (2011). 3814:Garcia K, Stumpff J, Duncan T, Su TT (2009). 1960: 1958: 1956: 1914: 1912: 1910: 8: 5244:Cochran JC, Krzysiak TC, Gilbert SP (2005). 4204:Cochran JC, Krzysiak TC, Gilbert SP (2006). 810:plus-end-directed microtubule motor activity 5035:"Antitumor activity of a kinesin inhibitor" 1750:GRCh38: Ensembl release 89: ENSG00000138160 917:regulation of mitotic centrosome separation 6283:Am. J. Med. Genet. B Neuropsychiatr. Genet 4163:Maliga Z, Kapoor TM, Mitchison TJ (2002). 997: 772: 569: 468: 365: 83: 6263: 6253: 6218: 6208: 6136: 6101: 6058: 6015: 5980: 5970: 5917: 5907: 5808: 5798: 5757: 5700: 5651: 5523: 5459: 5410: 5361: 5269: 5185: 5128: 5091: 5050: 4873: 4797: 4748: 4691: 4634: 4585: 4528: 4421: 4411: 4370: 4360: 4319: 4278: 4229: 4180: 4131: 4039: 3994: 3953: 3904: 3847: 3790: 3749: 3700: 3690: 3560: 3475: 3426: 3377: 3328: 3271: 3214: 3176: 3084: 3032: 3022: 2970: 2933: 2923: 2875: 2780: 2718: 2674: 2443: 2402: 2353: 2296: 2244: 2141: 2131: 2047: 1998: 1936: 1873: 1703: 2649:Bishop JD, Han Z, Schumacher JM (2005). 1895: 1893: 1329:. In humans it is coded for by the gene 34:Beltsville Information Management Center 6076:Cassimeris L, Morabito J (April 2004). 5336:Crevel IM, Alonso MC, Cross RA (2004). 3352:Nadar VC, Lin S, Baas PW (April 2012). 1901:"Entrez Gene: Kinesin family member 11" 1737: 38: 533: 494: 489: 432: 391: 386: 7: 4609:Kwok BH, Yang JG, Kapoor TM (2004). 3977:Blangy A, Arnaud L, Nigg EA (1997). 3246:Myers KA, Baas PW (September 2007). 2271:Falnikar A, Tole S, Baas PW (2011). 5874:Online Mendelian Inheritance in Man 2237:10.1523/JNEUROSCI.18-19-07822.1998 1593:(ARRY-520) (Array BioPharma), and 1229: 1208: 1182: 1161: 1137: 1118: 1092: 1073: 1047: 1028: 805:protein-containing complex binding 751: 669: 607: 586: 25: 5896:Orphanet Journal of Rare Diseases 3553:10.1111/j.1600-0854.2010.01152.x 1646: 1521:Microtubule gliding by Kinesin-5 517: 510: 504: 481: 416: 409: 403: 378: 47: 5787:Journal of Biological Chemistry 4715:Valentine MT, Block SM (2009). 3665:Sawin KE, Mitchison TJ (1995). 1581:(SB-715992; Cytokinetics/GSK), 1402:microtubule spindle structure. 3468:10.1523/JNEUROSCI.3070-12.2012 3419:10.1523/JNEUROSCI.3739-10.2010 3370:10.1523/JNEUROSCI.0144-12.2012 735:More reference expression data 1: 5644:10.1158/1078-0432.CCR-09-1498 5452:10.1158/1535-7163.MCT-08-0684 5052:10.1158/0008-5472.can-03-3839 4182:10.1016/S1074-5521(02)00212-0 2133:10.1016/S0021-9258(17)31593-4 957:mitotic centrosome separation 502: 401: 6440:Genes on human chromosome 10 6176:10.1016/0888-7543(92)90075-4 6060:10.1016/j.molcel.2003.08.008 5951:Proc. Natl. Acad. Sci. U.S.A 4969:10.1126/science.286.5441.913 4856:Gura T (21 September 2000). 3644:10.1016/j.ejmech.2013.01.031 3178:10.1016/j.celrep.2012.03.006 3159:Florian S, Mayer TU (2012). 2628:10.1126/science.286.5441.971 2481:10.1016/0092-8674(90)90350-N 1938:10.1016/0092-8674(95)90142-6 927:mitotic spindle organization 4862:Nature International Weekly 4835:10.2174/1871520610808060698 1678:. Gene Wiki Review Series. 1558:S-Trityl-L-cysteine (STLC), 1393:navigation and elongation. 655:stromal cell of endometrium 6466: 6356:"Tim Mitchison Laboratory" 5750:10.1016/j.jtbi.2011.08.017 5562:10.1016/j.bmcl.2005.02.055 5504:Cancer Chemother Pharmacol 5000:Angew. Chem. Int. Ed. Engl 4858:"A chemistry set for life" 4823:Anticancer Agents Med Chem 4302:Kull FJ, Endow SA (2002). 2720:10.1158/1535-7163.1079.3.9 1866:10.1016/j.gene.2013.08.004 1688:10.1016/J.GENE.2013.08.004 1538:Pharmacological inhibitors 1316:Kinesin-like protein KIF11 942:microtubule-based movement 891:protein-containing complex 790:microtubule motor activity 31: 5909:10.1186/s13023-015-0271-4 5853:10.1016/j.bcp.2009.11.001 5516:10.1016/j.jss.2009.06.013 5363:10.1016/j.cub.2004.05.030 5139:10.1016/j.jmb.2003.10.074 4926:10.1007/s10555-009-9185-8 4741:10.1016/j.bpj.2009.07.013 4684:10.1016/j.cub.2010.12.038 4636:10.1016/j.cub.2004.09.052 4459:10.1016/j.jmb.2013.03.004 4133:10.1016/j.cub.2006.03.056 3897:10.1016/j.cub.2008.02.077 3840:10.1016/j.cub.2009.08.013 3321:10.1016/j.cub.2008.11.021 2868:10.1016/j.bpj.2010.03.014 1806:"Mouse PubMed Reference:" 1788:"Human PubMed Reference:" 1659:article was published in 1302: 1297: 1293: 1286: 1270: 1251: 1236: 1215: 1204: 1189: 1168: 1157: 1144: 1140: 1125: 1121: 1112: 1099: 1095: 1080: 1076: 1067: 1054: 1050: 1035: 1031: 1022: 1007: 1000: 996: 980: 775: 771: 759: 754: 745: 732: 681: 672: 619: 610: 580: 572: 568: 551: 538: 501: 480: 471: 467: 450: 437: 400: 377: 368: 364: 319: 316: 306: 299: 294: 91: 86: 69: 64: 59: 55: 46: 41: 6389:"Patricia Wadsworth Lab" 3996:10.1074/jbc.272.31.19418 3671:Proc Natl Acad Sci U S A 3502:Cell Motil. Cytoskeleton 1264:Chr 19: 37.36 – 37.41 Mb 1257:Chr 10: 92.57 – 92.66 Mb 947:mitotic spindle assembly 6328:"Peter Baas Laboratory" 6094:10.1091/mbc.E03-07-0544 5800:10.1074/jbc.M110.192930 5597:10.1038/sj.clpt.6100021 4413:10.1074/jbc.C110.103762 4362:10.1074/jbc.M109.071233 3692:10.1073/pnas.92.10.4289 3203:Cell Motil Cytoskeleton 3130:10.1126/science.1063488 3024:10.1074/jbc.M110.154989 2925:10.1074/jbc.M109.092072 2667:10.1091/mbc.E04-08-0682 2289:10.1091/mbc.E10-11-0905 1585:from Cytokinetics/GSK, 6255:10.1074/jbc.M413140200 6210:10.1074/jbc.M404203200 5972:10.1073/pnas.111145398 5412:10.1074/jbc.M601324200 5093:10.1074/jbc.M100395200 5012:10.1002/anie.200351173 3792:10.1074/jbc.M806860200 1657:academic peer reviewed 1522: 922:chromosome segregation 820:protein kinase binding 4914:Cancer Metastasis Rev 4578:10.1083/jcb.200801145 4394:Jun B, Kim S (2010). 4271:10.1083/jcb.135.2.291 3946:10.1083/jcb.201106149 3264:10.1083/jcb.200702074 2773:10.1083/jcb.150.5.975 2578:10.1242/jcs.101.2.303 2395:10.1083/jcb.123.3.665 2040:10.1083/jcb.144.1.125 1617:Clinical significance 1575:human tumor xenograft 1520: 1493:Mechanical Properties 1454:Functional regulation 1325:that is essential in 496:Chromosome 19 (mouse) 394:Chromosome 10 (human) 6295:10.1002/ajmg.b.30172 5550:Bioorg Med Chem Lett 4321:10.1242/jcs.115.1.15 1665:and can be cited as: 952:spindle organization 87:List of PDB id codes 60:Available structures 6332:Research Laboratory 5963:2001PNAS...98.7004M 5742:2011JThBi.289..107H 5585:Clin Pharmacol Ther 5354:2004CBio...14.R411C 5307:10.1038/nchembio812 4733:2009BpJ....97.1671V 4676:2011CBio...21..154W 4627:2004CBio...14.1783K 4124:2006CBio...16..743K 3889:2008CBio...18..519E 3832:2009CBio...19.1670G 3683:1995PNAS...92.4289S 3313:2008CBio...18.1972N 3122:2001Sci...294..543K 2860:2010BpJ....98.2619L 2524:1990Natur.347..563H 2338:2013NatCo...4.1343A 2182:1992Natur.359..540S 1983:1996Natur.379..270K 1967:"A bipolar kinesin" 1479:Molecular mechanism 1424:Function in neurons 1397:Function in mitosis 1335:kinesin superfamily 861:spindle microtubule 800:microtubule binding 659:gingival epithelium 627:ganglionic eminence 6138:10.1002/humu.20016 6017:10.1002/humu.10282 5841:Biochem. Pharmacol 5693:10.1002/cncr.26664 4032:10.1042/BJ20121447 3742:10.1242/jcs.035360 3736:(Pt 23): 3912–21. 3077:10.1242/jcs.062208 3071:(Pt 20): 3435–45. 3059:, Craig E (2010). 2445:10.1242/jcs.009506 2438:(Pt 16): 2819–27. 2346:10.1038/ncomms2348 1622:Germline mutations 1523: 1102:ENSMUSG00000012443 972:mitotic cell cycle 905:Biological process 834:Cellular component 795:nucleotide binding 783:Molecular function 6408:"David Sharp Lab" 6402:Worthylake, David 6383:Rosenfeld, Steven 5262:10.1021/bi051724w 5223:10.1021/ja310377d 5178:10.1021/bi801291q 5086:(27): 25496–502. 4868:(6802): 282–284. 4539:10.1021/bi952633+ 4494:10.1021/bi040002m 4222:10.1021/bi0608562 3413:(44): 14896–906. 2981:10.1021/bi048982y 2821:10.1021/bi049264e 1730: 1729: 1313: 1312: 1309: 1308: 1282: 1281: 1247: 1246: 1226: 1225: 1200: 1199: 1179: 1178: 1153: 1152: 1134: 1133: 1108: 1107: 1089: 1088: 1063: 1062: 1044: 1043: 992: 991: 767: 766: 763: 762: 741: 740: 728: 727: 666: 665: 651:bone marrow cells 564: 563: 463: 462: 358:KIF11 - orthologs 290: 289: 286: 285: 70:Ortholog search: 16:(Redirected from 6457: 6426: 6424: 6423: 6414:. Archived from 6396: 6374: 6372: 6371: 6362:. Archived from 6350:Kozielski, Frank 6335: 6314: 6277: 6267: 6257: 6248:(13): 12658–67. 6232: 6222: 6212: 6203:(37): 38861–70. 6187: 6158: 6140: 6115: 6105: 6072: 6062: 6037: 6019: 5994: 5984: 5974: 5932: 5931: 5921: 5911: 5886: 5880: 5871: 5865: 5864: 5838: 5829: 5823: 5822: 5812: 5802: 5778: 5772: 5771: 5761: 5721: 5715: 5714: 5704: 5672: 5666: 5665: 5655: 5623: 5617: 5616: 5580: 5574: 5573: 5544: 5538: 5537: 5527: 5495: 5489: 5488: 5480: 5474: 5473: 5463: 5431: 5425: 5424: 5414: 5390: 5384: 5383: 5365: 5333: 5327: 5326: 5290: 5284: 5283: 5273: 5256:(50): 16633–48. 5241: 5235: 5234: 5206: 5200: 5199: 5189: 5157: 5151: 5150: 5132: 5112: 5106: 5105: 5095: 5071: 5065: 5064: 5054: 5030: 5024: 5023: 4995: 4989: 4988: 4952: 4946: 4945: 4920:(1–2): 197–208. 4909: 4903: 4902: 4900: 4898: 4877: 4875:10.1038/35030189 4853: 4847: 4846: 4818: 4812: 4811: 4801: 4769: 4763: 4762: 4752: 4712: 4706: 4705: 4695: 4655: 4649: 4648: 4638: 4606: 4600: 4599: 4589: 4557: 4551: 4550: 4532: 4512: 4506: 4505: 4477: 4471: 4470: 4442: 4436: 4435: 4425: 4415: 4391: 4385: 4384: 4374: 4364: 4340: 4334: 4333: 4323: 4299: 4293: 4292: 4282: 4253:Vale RD (1996). 4250: 4244: 4243: 4233: 4216:(40): 12334–44. 4201: 4195: 4194: 4184: 4160: 4154: 4153: 4135: 4103: 4097: 4096: 4077:10.1038/35060000 4060: 4054: 4053: 4043: 4015: 4009: 4008: 3998: 3989:(31): 19418–24. 3974: 3968: 3967: 3957: 3925: 3919: 3918: 3908: 3868: 3862: 3861: 3851: 3811: 3805: 3804: 3794: 3770: 3764: 3763: 3753: 3721: 3715: 3714: 3704: 3694: 3662: 3656: 3655: 3627: 3618: 3617: 3581: 3575: 3574: 3564: 3532: 3526: 3525: 3514:10.1002/cm.20057 3496: 3490: 3489: 3479: 3462:(40): 14033–49. 3447: 3441: 3440: 3430: 3398: 3392: 3391: 3381: 3349: 3343: 3342: 3332: 3292: 3286: 3285: 3275: 3243: 3237: 3236: 3225:10.1002/cm.10176 3218: 3197: 3191: 3190: 3180: 3156: 3150: 3149: 3105: 3099: 3098: 3088: 3053: 3047: 3046: 3036: 3026: 3002: 2993: 2992: 2974: 2954: 2948: 2947: 2937: 2927: 2918:(24): 18650–61. 2903: 2890: 2889: 2879: 2839: 2833: 2832: 2815:(41): 13072–82. 2804: 2795: 2794: 2784: 2752: 2741: 2740: 2722: 2698: 2689: 2688: 2678: 2646: 2640: 2639: 2607: 2590: 2589: 2572:(Pt 2): 303–13. 2561: 2552: 2551: 2532:10.1038/347563a0 2507: 2501: 2500: 2464: 2458: 2457: 2447: 2423: 2417: 2416: 2406: 2374: 2368: 2367: 2357: 2317: 2311: 2310: 2300: 2268: 2259: 2258: 2248: 2216: 2210: 2209: 2190:10.1038/359540a0 2165: 2156: 2155: 2145: 2135: 2111: 2105: 2104: 2068: 2062: 2061: 2051: 2019: 2013: 2012: 2002: 1991:10.1038/379270a0 1962: 1951: 1950: 1940: 1916: 1905: 1904: 1897: 1888: 1887: 1877: 1845: 1839: 1838: 1836: 1834: 1820: 1814: 1813: 1802: 1796: 1795: 1784: 1778: 1768: 1757: 1747: 1725: 1707: 1650: 1642: 1295: 1294: 1266: 1259: 1242: 1230: 1221: 1209: 1205:RefSeq (protein) 1195: 1183: 1174: 1162: 1138: 1119: 1093: 1074: 1048: 1029: 998: 937:spindle assembly 773: 752: 737: 717:secondary oocyte 693:ventricular zone 689:genital tubercle 677: 675:Top expressed in 670: 631:secondary oocyte 623:ventricular zone 615: 613:Top expressed in 608: 587: 570: 560: 547: 536: 521: 514: 508: 497: 485: 469: 459: 446: 435: 420: 413: 407: 396: 382: 366: 360: 311: 304: 281: 84: 78: 57: 56: 51: 39: 21: 6465: 6464: 6460: 6459: 6458: 6456: 6455: 6454: 6430: 6429: 6421: 6419: 6405: 6386: 6377:Moores, Carolyn 6369: 6367: 6353: 6325: 6322: 6317: 6280: 6235: 6190: 6161: 6118: 6082:Mol. Biol. Cell 6075: 6040: 5997: 5957:(13): 7004–11. 5944: 5940: 5938:Further reading 5935: 5888: 5887: 5883: 5872: 5868: 5836: 5831: 5830: 5826: 5780: 5779: 5775: 5723: 5722: 5718: 5687:(14): 3556–64. 5674: 5673: 5669: 5632:Clin Cancer Res 5625: 5624: 5620: 5582: 5581: 5577: 5546: 5545: 5541: 5497: 5496: 5492: 5482: 5481: 5477: 5440:Mol Cancer Ther 5433: 5432: 5428: 5405:(26): 18090–7. 5392: 5391: 5387: 5335: 5334: 5330: 5292: 5291: 5287: 5243: 5242: 5238: 5208: 5207: 5203: 5159: 5158: 5154: 5130:10.1.1.451.9558 5114: 5113: 5109: 5073: 5072: 5068: 5032: 5031: 5027: 5006:(21): 2379–82. 4997: 4996: 4992: 4963:(5441): 913–4. 4954: 4953: 4949: 4911: 4910: 4906: 4896: 4894: 4855: 4854: 4850: 4820: 4819: 4815: 4790:10.1038/ncb1394 4771: 4770: 4766: 4714: 4713: 4709: 4657: 4656: 4652: 4608: 4607: 4603: 4559: 4558: 4554: 4530:10.1.1.543.1030 4523:(17): 5404–17. 4514: 4513: 4509: 4488:(13): 3757–63. 4479: 4478: 4474: 4453:(11): 1869–80. 4444: 4443: 4439: 4406:(15): 11073–7. 4393: 4392: 4388: 4342: 4341: 4337: 4314:(Pt 1): 15–23. 4301: 4300: 4296: 4252: 4251: 4247: 4203: 4202: 4198: 4162: 4161: 4157: 4105: 4104: 4100: 4062: 4061: 4057: 4017: 4016: 4012: 3976: 3975: 3971: 3927: 3926: 3922: 3870: 3869: 3865: 3813: 3812: 3808: 3785:(51): 35783–8. 3772: 3771: 3767: 3723: 3722: 3718: 3677:(10): 4289–93. 3664: 3663: 3659: 3629: 3628: 3621: 3598:10.1038/nrc3310 3583: 3582: 3578: 3534: 3533: 3529: 3498: 3497: 3493: 3449: 3448: 3444: 3400: 3399: 3395: 3364:(17): 5783–94. 3351: 3350: 3346: 3294: 3293: 3289: 3245: 3244: 3240: 3216:10.1.1.507.5695 3199: 3198: 3194: 3158: 3157: 3153: 3116:(5542): 543–7. 3107: 3106: 3102: 3055: 3054: 3050: 3004: 3003: 2996: 2972:10.1.1.495.1844 2965:(31): 9939–49. 2956: 2955: 2951: 2905: 2904: 2893: 2854:(11): 2619–27. 2841: 2840: 2836: 2806: 2805: 2798: 2754: 2753: 2744: 2707:Mol Cancer Ther 2700: 2699: 2692: 2648: 2647: 2643: 2622:(5441): 971–4. 2609: 2608: 2593: 2563: 2562: 2555: 2518:(6293): 563–6. 2509: 2508: 2504: 2466: 2465: 2461: 2425: 2424: 2420: 2376: 2375: 2371: 2319: 2318: 2314: 2270: 2269: 2262: 2231:(19): 7822–35. 2218: 2217: 2213: 2176:(6395): 540–3. 2167: 2166: 2159: 2126:(37): 22913–6. 2113: 2112: 2108: 2070: 2069: 2065: 2021: 2020: 2016: 1977:(6562): 270–2. 1964: 1963: 1954: 1918: 1917: 1908: 1899: 1898: 1891: 1847: 1846: 1842: 1832: 1830: 1828:www.uniprot.org 1822: 1821: 1817: 1804: 1803: 1799: 1786: 1785: 1781: 1769: 1760: 1748: 1739: 1735: 1726: 1667: 1666: 1651: 1638: 1624:in KIF11 cause 1619: 1611: 1609:Human mutations 1540: 1481: 1456: 1426: 1399: 1382:mitotic spindle 1374: 1320:molecular motor 1304:View/Edit Mouse 1299:View/Edit Human 1262: 1255: 1252:Location (UCSC) 1238: 1217: 1191: 1170: 1083:ENSG00000138160 976: 900: 896:mitotic spindle 851:kinesin complex 829: 825:ATPase activity 733: 724: 719: 715: 711: 707: 703: 699: 695: 691: 687: 673: 662: 657: 653: 649: 647:trabecular bone 645: 641: 637: 633: 629: 625: 611: 555: 542: 534: 524: 523: 522: 515: 495: 472:Gene location ( 454: 441: 433: 423: 422: 421: 414: 392: 369:Gene location ( 320: 307: 300: 93: 71: 37: 28: 23: 22: 15: 12: 11: 5: 6463: 6461: 6453: 6452: 6447: 6442: 6432: 6431: 6428: 6427: 6403: 6400: 6399:Wojcik, Edward 6397: 6384: 6381: 6378: 6375: 6351: 6348: 6345: 6342: 6341:Gilbert, Susan 6339: 6336: 6321: 6320:External links 6318: 6316: 6315: 6278: 6233: 6188: 6159: 6116: 6088:(4): 1580–90. 6073: 6038: 5995: 5941: 5939: 5936: 5934: 5933: 5881: 5878:MCLMR - 152950 5866: 5824: 5793:(7): 5242–53. 5773: 5716: 5667: 5618: 5575: 5539: 5490: 5475: 5446:(11): 3480–9. 5426: 5385: 5348:(11): R411–2. 5328: 5285: 5236: 5217:(6): 2263–72. 5201: 5172:(8): 1754–62. 5152: 5107: 5066: 5045:(9): 3276–80. 5025: 4990: 4947: 4904: 4848: 4829:(6): 698–704. 4813: 4764: 4707: 4670:(2): 154–160. 4650: 4601: 4552: 4507: 4472: 4437: 4386: 4355:(8): 5859–67. 4335: 4294: 4265:(2): 291–302. 4245: 4196: 4155: 4098: 4055: 4026:(2): 195–204. 4010: 3969: 3920: 3863: 3826:(19): 1670–6. 3806: 3765: 3716: 3657: 3632:Eur J Med Chem 3619: 3586:Nat Rev Cancer 3576: 3527: 3491: 3442: 3393: 3344: 3307:(24): 1972–7. 3287: 3258:(6): 1081–91. 3238: 3192: 3151: 3100: 3048: 3017:(8): 6201–10. 2994: 2949: 2891: 2834: 2796: 2742: 2713:(9): 1079–90. 2690: 2641: 2591: 2553: 2502: 2475:(6): 1019–27. 2459: 2418: 2369: 2312: 2283:(9): 1561–74. 2260: 2211: 2157: 2106: 2073:Nat. Cell Biol 2063: 2014: 1952: 1931:(7): 1159–69. 1906: 1889: 1840: 1815: 1797: 1779: 1758: 1736: 1734: 1731: 1728: 1727: 1654: 1652: 1645: 1637: 1634: 1618: 1615: 1610: 1607: 1566: 1565: 1562: 1559: 1556: 1539: 1536: 1484:ATP hydrolysis 1480: 1477: 1460:phosphorylated 1455: 1452: 1425: 1422: 1398: 1395: 1386:ATP hydrolysis 1373: 1370: 1311: 1310: 1307: 1306: 1301: 1291: 1290: 1284: 1283: 1280: 1279: 1277: 1275: 1268: 1267: 1260: 1253: 1249: 1248: 1245: 1244: 1234: 1233: 1227: 1224: 1223: 1213: 1212: 1206: 1202: 1201: 1198: 1197: 1187: 1186: 1180: 1177: 1176: 1166: 1165: 1159: 1155: 1154: 1151: 1150: 1142: 1141: 1135: 1132: 1131: 1123: 1122: 1116: 1110: 1109: 1106: 1105: 1097: 1096: 1090: 1087: 1086: 1078: 1077: 1071: 1065: 1064: 1061: 1060: 1052: 1051: 1045: 1042: 1041: 1033: 1032: 1026: 1020: 1019: 1014: 1009: 1005: 1004: 994: 993: 990: 989: 978: 977: 975: 974: 969: 964: 959: 954: 949: 944: 939: 934: 929: 924: 919: 914: 908: 906: 902: 901: 899: 898: 893: 888: 883: 878: 873: 868: 863: 858: 853: 848: 843: 837: 835: 831: 830: 828: 827: 822: 817: 812: 807: 802: 797: 792: 786: 784: 780: 779: 769: 768: 765: 764: 761: 760: 757: 756: 749: 743: 742: 739: 738: 730: 729: 726: 725: 723: 722: 718: 714: 710: 709:primary oocyte 706: 702: 698: 694: 690: 686: 685:tail of embryo 682: 679: 678: 667: 664: 663: 661: 660: 656: 652: 648: 644: 640: 636: 632: 628: 624: 620: 617: 616: 604: 603: 595: 584: 578: 577: 574:RNA expression 566: 565: 562: 561: 553: 549: 548: 540: 537: 532: 526: 525: 516: 509: 503: 499: 498: 493: 487: 486: 478: 477: 465: 464: 461: 460: 452: 448: 447: 439: 436: 431: 425: 424: 415: 408: 402: 398: 397: 390: 384: 383: 375: 374: 362: 361: 318: 314: 313: 305: 297: 296: 292: 291: 288: 287: 284: 283: 89: 88: 80: 79: 68: 62: 61: 53: 52: 44: 43: 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 6462: 6451: 6448: 6446: 6443: 6441: 6438: 6437: 6435: 6418:on 2014-11-07 6417: 6413: 6409: 6404: 6401: 6398: 6394: 6390: 6387:Wadsworth P. 6385: 6382: 6379: 6376: 6366:on 2013-05-16 6365: 6361: 6360:Mitchison Lab 6357: 6354:Mitchison T. 6352: 6349: 6347:Kim, Sunyoung 6346: 6344:Kapoor, Tarun 6343: 6340: 6338:Block, Steven 6337: 6333: 6329: 6324: 6323: 6319: 6312: 6308: 6304: 6300: 6296: 6292: 6288: 6284: 6279: 6275: 6271: 6266: 6261: 6256: 6251: 6247: 6243: 6242:J. Biol. Chem 6239: 6234: 6230: 6226: 6221: 6216: 6211: 6206: 6202: 6198: 6197:J. Biol. Chem 6194: 6189: 6185: 6181: 6177: 6173: 6170:(4): 1371–2. 6169: 6165: 6160: 6156: 6152: 6148: 6144: 6139: 6134: 6131:(4): 334–42. 6130: 6126: 6122: 6117: 6113: 6109: 6104: 6099: 6095: 6091: 6087: 6083: 6079: 6074: 6070: 6066: 6061: 6056: 6053:(3): 723–34. 6052: 6048: 6044: 6039: 6035: 6031: 6027: 6023: 6018: 6013: 6010:(5): 363–71. 6009: 6005: 6001: 5996: 5992: 5988: 5983: 5978: 5973: 5968: 5964: 5960: 5956: 5952: 5948: 5943: 5942: 5937: 5929: 5925: 5920: 5915: 5910: 5905: 5901: 5897: 5893: 5885: 5882: 5879: 5875: 5870: 5867: 5862: 5858: 5854: 5850: 5847:(6): 864–72. 5846: 5842: 5835: 5828: 5825: 5820: 5816: 5811: 5806: 5801: 5796: 5792: 5788: 5784: 5777: 5774: 5769: 5765: 5760: 5755: 5751: 5747: 5743: 5739: 5735: 5731: 5727: 5720: 5717: 5712: 5708: 5703: 5698: 5694: 5690: 5686: 5682: 5678: 5671: 5668: 5663: 5659: 5654: 5649: 5645: 5641: 5638:(2): 566–76. 5637: 5633: 5629: 5622: 5619: 5614: 5610: 5606: 5602: 5598: 5594: 5590: 5586: 5579: 5576: 5571: 5567: 5563: 5559: 5556:(8): 2041–5. 5555: 5551: 5543: 5540: 5535: 5531: 5526: 5521: 5517: 5513: 5509: 5505: 5501: 5494: 5491: 5486: 5479: 5476: 5471: 5467: 5462: 5457: 5453: 5449: 5445: 5441: 5437: 5430: 5427: 5422: 5418: 5413: 5408: 5404: 5400: 5396: 5389: 5386: 5381: 5377: 5373: 5369: 5364: 5359: 5355: 5351: 5347: 5343: 5339: 5332: 5329: 5324: 5320: 5316: 5312: 5308: 5304: 5300: 5296: 5295:Nat Chem Biol 5289: 5286: 5281: 5277: 5272: 5267: 5263: 5259: 5255: 5251: 5247: 5240: 5237: 5232: 5228: 5224: 5220: 5216: 5212: 5211:J Am Chem Soc 5205: 5202: 5197: 5193: 5188: 5183: 5179: 5175: 5171: 5167: 5163: 5156: 5153: 5148: 5144: 5140: 5136: 5131: 5126: 5123:(2): 547–54. 5122: 5118: 5111: 5108: 5103: 5099: 5094: 5089: 5085: 5081: 5080:J. Biol. Chem 5077: 5070: 5067: 5062: 5058: 5053: 5048: 5044: 5040: 5036: 5029: 5026: 5021: 5017: 5013: 5009: 5005: 5001: 4994: 4991: 4986: 4982: 4978: 4974: 4970: 4966: 4962: 4958: 4951: 4948: 4943: 4939: 4935: 4931: 4927: 4923: 4919: 4915: 4908: 4905: 4893: 4889: 4885: 4881: 4876: 4871: 4867: 4863: 4859: 4852: 4849: 4844: 4840: 4836: 4832: 4828: 4824: 4817: 4814: 4809: 4805: 4800: 4795: 4791: 4787: 4783: 4779: 4778:Nat Cell Biol 4775: 4768: 4765: 4760: 4756: 4751: 4746: 4742: 4738: 4734: 4730: 4727:(6): 1671–7. 4726: 4722: 4718: 4711: 4708: 4703: 4699: 4694: 4689: 4685: 4681: 4677: 4673: 4669: 4665: 4661: 4654: 4651: 4646: 4642: 4637: 4632: 4628: 4624: 4621:(4): 1783–8. 4620: 4616: 4612: 4605: 4602: 4597: 4593: 4588: 4583: 4579: 4575: 4571: 4567: 4563: 4556: 4553: 4548: 4544: 4540: 4536: 4531: 4526: 4522: 4518: 4511: 4508: 4503: 4499: 4495: 4491: 4487: 4483: 4476: 4473: 4468: 4464: 4460: 4456: 4452: 4448: 4441: 4438: 4433: 4429: 4424: 4419: 4414: 4409: 4405: 4401: 4397: 4390: 4387: 4382: 4378: 4373: 4368: 4363: 4358: 4354: 4350: 4346: 4339: 4336: 4331: 4327: 4322: 4317: 4313: 4309: 4305: 4298: 4295: 4290: 4286: 4281: 4276: 4272: 4268: 4264: 4260: 4256: 4249: 4246: 4241: 4237: 4232: 4227: 4223: 4219: 4215: 4211: 4207: 4200: 4197: 4192: 4188: 4183: 4178: 4175:(9): 989–96. 4174: 4170: 4166: 4159: 4156: 4151: 4147: 4143: 4139: 4134: 4129: 4125: 4121: 4118:(8): 743–54. 4117: 4113: 4109: 4102: 4099: 4094: 4090: 4086: 4082: 4078: 4074: 4070: 4066: 4065:Nat Cell Biol 4059: 4056: 4051: 4047: 4042: 4037: 4033: 4029: 4025: 4021: 4014: 4011: 4006: 4002: 3997: 3992: 3988: 3984: 3980: 3973: 3970: 3965: 3961: 3956: 3951: 3947: 3943: 3939: 3935: 3931: 3924: 3921: 3916: 3912: 3907: 3902: 3898: 3894: 3890: 3886: 3883:(7): 519–25. 3882: 3878: 3874: 3867: 3864: 3859: 3855: 3850: 3845: 3841: 3837: 3833: 3829: 3825: 3821: 3817: 3810: 3807: 3802: 3798: 3793: 3788: 3784: 3780: 3776: 3769: 3766: 3761: 3757: 3752: 3747: 3743: 3739: 3735: 3731: 3727: 3720: 3717: 3712: 3708: 3703: 3698: 3693: 3688: 3684: 3680: 3676: 3672: 3668: 3661: 3658: 3653: 3649: 3645: 3641: 3637: 3633: 3626: 3624: 3620: 3615: 3611: 3607: 3603: 3599: 3595: 3592:(8): 527–39. 3591: 3587: 3580: 3577: 3572: 3568: 3563: 3558: 3554: 3550: 3547:(3): 269–86. 3546: 3542: 3538: 3531: 3528: 3523: 3519: 3515: 3511: 3508:(4): 181–90. 3507: 3503: 3495: 3492: 3487: 3483: 3478: 3473: 3469: 3465: 3461: 3457: 3453: 3446: 3443: 3438: 3434: 3429: 3424: 3420: 3416: 3412: 3408: 3404: 3397: 3394: 3389: 3385: 3380: 3375: 3371: 3367: 3363: 3359: 3355: 3348: 3345: 3340: 3336: 3331: 3326: 3322: 3318: 3314: 3310: 3306: 3302: 3298: 3291: 3288: 3283: 3279: 3274: 3269: 3265: 3261: 3257: 3253: 3249: 3242: 3239: 3234: 3230: 3226: 3222: 3217: 3212: 3208: 3204: 3196: 3193: 3188: 3184: 3179: 3174: 3171:(5): 408–16. 3170: 3166: 3162: 3155: 3152: 3147: 3143: 3139: 3135: 3131: 3127: 3123: 3119: 3115: 3111: 3104: 3101: 3096: 3092: 3087: 3082: 3078: 3074: 3070: 3066: 3062: 3058: 3052: 3049: 3044: 3040: 3035: 3030: 3025: 3020: 3016: 3012: 3008: 3001: 2999: 2995: 2990: 2986: 2982: 2978: 2973: 2968: 2964: 2960: 2953: 2950: 2945: 2941: 2936: 2931: 2926: 2921: 2917: 2913: 2909: 2902: 2900: 2898: 2896: 2892: 2887: 2883: 2878: 2873: 2869: 2865: 2861: 2857: 2853: 2849: 2845: 2838: 2835: 2830: 2826: 2822: 2818: 2814: 2810: 2803: 2801: 2797: 2792: 2788: 2783: 2778: 2774: 2770: 2767:(5): 975–88. 2766: 2762: 2758: 2751: 2749: 2747: 2743: 2738: 2734: 2730: 2726: 2721: 2716: 2712: 2708: 2704: 2697: 2695: 2691: 2686: 2682: 2677: 2672: 2668: 2664: 2661:(2): 742–56. 2660: 2656: 2655:Mol Biol Cell 2652: 2645: 2642: 2637: 2633: 2629: 2625: 2621: 2617: 2613: 2606: 2604: 2602: 2600: 2598: 2596: 2592: 2587: 2583: 2579: 2575: 2571: 2567: 2560: 2558: 2554: 2549: 2545: 2541: 2537: 2533: 2529: 2525: 2521: 2517: 2513: 2506: 2503: 2498: 2494: 2490: 2486: 2482: 2478: 2474: 2470: 2463: 2460: 2455: 2451: 2446: 2441: 2437: 2433: 2429: 2422: 2419: 2414: 2410: 2405: 2400: 2396: 2392: 2389:(3): 665–79. 2388: 2384: 2380: 2373: 2370: 2365: 2361: 2356: 2351: 2347: 2343: 2339: 2335: 2331: 2327: 2323: 2316: 2313: 2308: 2304: 2299: 2294: 2290: 2286: 2282: 2278: 2277:Mol Biol Cell 2274: 2267: 2265: 2261: 2256: 2252: 2247: 2242: 2238: 2234: 2230: 2226: 2222: 2215: 2212: 2207: 2203: 2199: 2195: 2191: 2187: 2183: 2179: 2175: 2171: 2164: 2162: 2158: 2153: 2149: 2144: 2139: 2134: 2129: 2125: 2121: 2117: 2110: 2107: 2102: 2098: 2094: 2090: 2086: 2082: 2078: 2074: 2067: 2064: 2059: 2055: 2050: 2045: 2041: 2037: 2034:(1): 125–38. 2033: 2029: 2025: 2018: 2015: 2010: 2006: 2001: 1996: 1992: 1988: 1984: 1980: 1976: 1972: 1968: 1961: 1959: 1957: 1953: 1948: 1944: 1939: 1934: 1930: 1926: 1922: 1915: 1913: 1911: 1907: 1902: 1896: 1894: 1890: 1885: 1881: 1876: 1871: 1867: 1863: 1860:(2): 133–49. 1859: 1855: 1851: 1844: 1841: 1829: 1825: 1819: 1816: 1811: 1807: 1801: 1798: 1793: 1789: 1783: 1780: 1776: 1772: 1767: 1765: 1763: 1759: 1755: 1751: 1746: 1744: 1742: 1738: 1732: 1723: 1719: 1715: 1711: 1706: 1701: 1697: 1693: 1689: 1685: 1682:(2): 133–49. 1681: 1677: 1676: 1671: 1664: 1663: 1658: 1653: 1649: 1644: 1643: 1640: 1635: 1633: 1631: 1627: 1623: 1616: 1614: 1608: 1606: 1602: 1598: 1596: 1592: 1588: 1584: 1580: 1576: 1570: 1563: 1560: 1557: 1554: 1551: 1550: 1549: 1546: 1537: 1535: 1533: 1529: 1519: 1515: 1513: 1512:crowd surfing 1508: 1502: 1500: 1495: 1494: 1490: 1486: 1485: 1478: 1476: 1473: 1469: 1464: 1461: 1453: 1451: 1448: 1444: 1440: 1436: 1432: 1423: 1421: 1417: 1413: 1411: 1410: 1403: 1396: 1394: 1392: 1387: 1383: 1379: 1371: 1369: 1367: 1363: 1359: 1354: 1352: 1348: 1344: 1340: 1336: 1332: 1328: 1324: 1321: 1317: 1305: 1300: 1296: 1292: 1289: 1285: 1278: 1276: 1273: 1269: 1265: 1261: 1258: 1254: 1250: 1243: 1241: 1235: 1231: 1228: 1222: 1220: 1214: 1210: 1207: 1203: 1196: 1194: 1188: 1184: 1181: 1175: 1173: 1167: 1163: 1160: 1158:RefSeq (mRNA) 1156: 1149: 1148: 1143: 1139: 1136: 1130: 1129: 1124: 1120: 1117: 1115: 1111: 1104: 1103: 1098: 1094: 1091: 1085: 1084: 1079: 1075: 1072: 1070: 1066: 1059: 1058: 1053: 1049: 1046: 1040: 1039: 1034: 1030: 1027: 1025: 1021: 1018: 1015: 1013: 1010: 1006: 1003: 999: 995: 988: 984: 979: 973: 970: 968: 965: 963: 960: 958: 955: 953: 950: 948: 945: 943: 940: 938: 935: 933: 932:cell division 930: 928: 925: 923: 920: 918: 915: 913: 910: 909: 907: 904: 903: 897: 894: 892: 889: 887: 884: 882: 879: 877: 874: 872: 869: 867: 864: 862: 859: 857: 854: 852: 849: 847: 844: 842: 839: 838: 836: 833: 832: 826: 823: 821: 818: 816: 813: 811: 808: 806: 803: 801: 798: 796: 793: 791: 788: 787: 785: 782: 781: 778: 777:Gene ontology 774: 770: 758: 753: 750: 748: 744: 736: 731: 720: 716: 712: 708: 704: 700: 696: 692: 688: 684: 683: 680: 676: 671: 668: 658: 654: 650: 646: 642: 638: 634: 630: 626: 622: 621: 618: 614: 609: 606: 605: 602: 600: 596: 594: 593: 589: 588: 585: 583: 579: 575: 571: 567: 559: 554: 550: 546: 541: 535:19|19 C2 531: 527: 520: 513: 507: 500: 492: 488: 484: 479: 475: 470: 466: 458: 453: 449: 445: 440: 430: 426: 419: 412: 406: 399: 395: 389: 385: 381: 376: 372: 367: 363: 359: 355: 351: 347: 343: 339: 335: 331: 327: 323: 315: 310: 303: 298: 293: 282: 280: 276: 272: 268: 264: 260: 256: 252: 248: 244: 240: 236: 232: 228: 224: 220: 216: 212: 208: 204: 200: 196: 192: 188: 184: 180: 176: 172: 168: 164: 160: 156: 152: 148: 144: 140: 136: 132: 128: 124: 120: 116: 112: 108: 104: 100: 96: 90: 85: 82: 81: 77: 74: 67: 63: 58: 54: 50: 45: 40: 35: 30: 19: 6420:. Retrieved 6416:the original 6412:Research Lab 6411: 6393:Research Lab 6392: 6368:. Retrieved 6364:the original 6359: 6331: 6289:(1): 69–71. 6286: 6282: 6245: 6241: 6200: 6196: 6167: 6163: 6128: 6124: 6085: 6081: 6050: 6046: 6007: 6003: 5954: 5950: 5899: 5895: 5884: 5869: 5844: 5840: 5827: 5790: 5786: 5776: 5733: 5730:J Theor Biol 5729: 5719: 5684: 5680: 5670: 5635: 5631: 5621: 5591:(1): 88–94. 5588: 5584: 5578: 5553: 5549: 5542: 5510:(1): 28–32. 5507: 5503: 5493: 5484: 5478: 5443: 5439: 5429: 5402: 5398: 5388: 5345: 5341: 5331: 5301:(9): 480–5. 5298: 5294: 5288: 5253: 5250:Biochemistry 5249: 5239: 5214: 5210: 5204: 5169: 5166:Biochemistry 5165: 5155: 5120: 5116: 5110: 5083: 5079: 5069: 5042: 5038: 5028: 5003: 4999: 4993: 4960: 4956: 4950: 4917: 4913: 4907: 4895:. 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Cell Biol 3251: 3241: 3206: 3202: 3195: 3168: 3164: 3154: 3113: 3109: 3103: 3068: 3064: 3051: 3014: 3010: 2962: 2959:Biochemistry 2958: 2952: 2915: 2911: 2851: 2847: 2837: 2812: 2809:Biochemistry 2808: 2764: 2760: 2710: 2706: 2658: 2654: 2644: 2619: 2615: 2569: 2565: 2515: 2511: 2505: 2472: 2468: 2462: 2435: 2431: 2421: 2386: 2382: 2372: 2329: 2325: 2315: 2280: 2276: 2228: 2224: 2214: 2173: 2169: 2123: 2119: 2109: 2085:10.1038/9025 2076: 2072: 2066: 2031: 2028:J. Cell Biol 2027: 2017: 1974: 1970: 1928: 1924: 1857: 1853: 1843: 1831:. 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Neurosci 2120:J Biol Chem 2079:(1): 51–4. 1528:fluorophore 1391:growth cone 866:microtubule 815:ATP binding 705:bone marrow 639:bone marrow 556:37,410,307 543:37,364,851 455:92,655,395 442:92,574,105 295:Identifiers 6434:Categories 6422:2012-12-31 6370:2012-12-31 6125:Hum. Mutat 6004:Hum. Mutat 5902:(52): 52. 5736:: 107–15. 5117:J Mol Biol 5039:Cancer Res 4447:J Mol Biol 4308:J Cell Sci 3730:J Cell Sci 3638:: 614–31. 3301:Curr. Biol 3065:J Cell Sci 3057:Mogilner A 2566:J Cell Sci 2432:J Cell Sci 2326:Nat Commun 1777:, May 2017 1756:, May 2017 1733:References 1595:litronesib 1564:CK0106023. 1409:C. elegans 1362:centrosome 962:cell cycle 601:(ortholog) 338:HomoloGene 6406:Sharp D. 6047:Mol. Cell 5342:Curr Biol 5125:CiteSeerX 4892:205008902 4721:Biophys J 4664:Curr Biol 4615:Curr Biol 4525:CiteSeerX 4169:Chem Biol 4112:Curr Biol 4020:Biochem J 3877:Curr Biol 3820:Curr Biol 3211:CiteSeerX 2967:CiteSeerX 2848:Biophys J 1722:Q21710690 1696:0378-1119 1591:filanesib 1583:SB-743921 1579:ispinesib 1553:monastrol 1548:include: 1545:monastrol 1339:Kinesin-5 1240:NP_034745 1219:NP_004514 1193:NM_010615 1172:NM_004523 1002:Orthologs 876:cytoplasm 346:GeneCards 6326:Baas P. 6311:20486238 6303:15858821 6274:15665380 6229:15247293 6164:Genomics 6155:24885305 6147:15024728 6112:14718566 6069:14527417 6034:24508630 6026:14517947 5991:11416179 5928:25934493 5876:(OMIM): 5861:19896928 5819:21148480 5768:21872609 5711:22139909 5662:20068098 5613:34867346 5605:17186004 5570:15808464 5534:20031160 5470:18974392 5421:16627469 5380:15690493 5372:15182685 5323:27535804 5315:16892050 5280:16342954 5231:23305346 5196:19236100 5147:14672662 5102:11328809 5061:15126370 5020:12783501 4985:27786369 4977:10577242 4942:25682969 4934:19156502 4884:11014160 4843:18690830 4808:16604065 4759:19751672 4702:21236672 4645:15458652 4596:18678707 4502:15049682 4467:23500491 4432:20154092 4381:20018897 4330:11801720 4240:17014086 4191:12323373 4142:16631581 4085:11231570 4050:23368718 3964:21969468 3915:18372177 3858:19800237 3801:18845538 3760:19001501 3652:23434636 3614:20577157 3606:22825217 3571:21166743 3522:15751098 3486:23035110 3437:21048148 3388:22539840 3339:19084405 3282:17846176 3233:14983520 3187:22832270 3165:Cell Rep 3146:32846903 3138:11641489 3095:20930139 3043:21127071 2989:15287721 2944:20299460 2886:20513406 2829:15476401 2791:10973989 2737:15725001 2729:15367702 2685:15548597 2636:10542155 2497:27420513 2454:17652157 2364:23299893 2307:21411631 2093:10559864 1884:23954229 1833:10 April 1773:– 1752:– 1718:Wikidata 1714:23954229 1472:dynactin 1372:Function 1341:, or as 1288:Wikidata 981:Sources: 846:membrane 701:epiblast 643:testicle 434:10q23.33 6265:1356610 6220:1356567 6184:1505978 5959:Bibcode 5919:4464120 5810:3037637 5759:3191284 5738:Bibcode 5702:4984525 5653:2844774 5525:3379885 5461:2597169 5350:Bibcode 5271:2270472 5187:3244877 4957:Science 4799:1523314 4750:2749793 4729:Bibcode 4693:3049310 4672:Bibcode 4623:Bibcode 4587:2500128 4547:8611530 4423:2856982 4372:2820811 4289:8896589 4280:2121043 4231:2288585 4150:7466868 4120:Bibcode 4093:9536723 4005:9235942 3955:3187703 3906:2408861 3885:Bibcode 3849:2762001 3828:Bibcode 3751:4066659 3711:7753799 3679:Bibcode 3562:3037443 3541:Traffic 3477:3482493 3428:3064264 3379:3347042 3330:2617768 3309:Bibcode 3273:2064629 3118:Bibcode 3110:Science 3086:2951465 3034:3057856 2935:2881790 2877:2877332 2856:Bibcode 2782:2175262 2616:Science 2586:1629247 2548:4234302 2540:2145514 2520:Bibcode 2489:2138511 2413:8227131 2404:2200134 2355:3562449 2334:Bibcode 2298:3084678 2255:9742151 2246:6793023 2206:4358461 2198:1406972 2178:Bibcode 2152:8083185 2143:3201834 2101:6229447 2058:9885249 2049:2148119 2009:8538794 2000:3203953 1979:Bibcode 1947:8548803 1875:3801170 1775:Ensembl 1754:Ensembl 1705:3801170 1587:MK-0731 1380:in the 1358:spindle 1327:mitosis 1323:protein 1114:UniProt 1069:Ensembl 1008:Species 987:QuickGO 886:nucleus 881:cytosol 856:spindle 576:pattern 334:1098231 302:Aliases 6309:  6301:  6272:  6262:  6227:  6217:  6182:  6153:  6145:  6110:  6103:379257 6100:  6067:  6032:  6024:  5989:  5979:  5926:  5916:  5859:  5817:  5807:  5766:  5756:  5709:  5699:  5681:Cancer 5660:  5650:  5611:  5603:  5568:  5548:KSP". 5532:  5522:  5468:  5458:  5419:  5378:  5370:  5321:  5313:  5278:  5268:  5229:  5194:  5184:  5145:  5127:  5100:  5059:  5018:  4983:  4975:  4940:  4932:  4890:  4882:  4841:  4806:  4796:  4757:  4747:  4700:  4690:  4643:  4594:  4584:  4545:  4527:  4500:  4465:  4430:  4420:  4379:  4369:  4328:  4287:  4277:  4238:  4228:  4189:  4148:  4140:  4091:  4083:  4048:  4003:  3962:  3952:  3913:  3903:  3856:  3846:  3799:  3758:  3748:  3709:  3699:  3650:  3612:  3604:  3569:  3559:  3520:  3484:  3474:  3435:  3425:  3386:  3376:  3337:  3327:  3280:  3270:  3231:  3213:  3185:  3144:  3136:  3093:  3083:  3041:  3031:  2987:  2969:  2942:  2932:  2884:  2874:  2827:  2789:  2779:  2735:  2727:  2683:  2676:545908 2673:  2634:  2584:  2546:  2538:  2512:Nature 2495:  2487:  2452:  2411:  2401:  2362:  2352:  2305:  2295:  2253:  2243:  2204:  2196:  2170:Nature 2150:  2140:  2099:  2091:  2056:  2046:  2007:  1997:  1971:Nature 1945:  1882:  1872:  1720:  1712:  1702:  1694:  1443:dynein 1366:cancer 1274:search 1272:PubMed 1147:Q6P9P6 1128:P52732 1024:Entrez 747:BioGPS 713:zygote 697:thymus 326:148760 6307:S2CID 6151:S2CID 6030:S2CID 5982:34614 5837:(PDF) 5609:S2CID 5376:S2CID 5319:S2CID 4981:S2CID 4938:S2CID 4888:S2CID 4146:S2CID 4089:S2CID 3702:41929 3610:S2CID 3142:S2CID 2733:S2CID 2544:S2CID 2493:S2CID 2202:S2CID 2097:S2CID 1662:Gene 1636:Notes 1630:MCLMR 1499:KIF5B 1447:siRNA 1439:KIF23 1435:KIF15 1331:KIF11 1318:is a 1057:16551 1017:Mouse 1012:Human 983:Amigo 635:gonad 599:Mouse 592:Human 539:Start 474:Mouse 438:Start 371:Human 350:KIF11 309:KIF11 42:KIF11 18:KIF11 6299:PMID 6287:136B 6270:PMID 6225:PMID 6180:PMID 6143:PMID 6108:PMID 6065:PMID 6022:PMID 5987:PMID 5924:PMID 5857:PMID 5815:PMID 5764:PMID 5707:PMID 5658:PMID 5601:PMID 5566:PMID 5530:PMID 5466:PMID 5417:PMID 5368:PMID 5311:PMID 5276:PMID 5227:PMID 5192:PMID 5143:PMID 5098:PMID 5057:PMID 5016:PMID 4973:PMID 4930:PMID 4899:2012 4880:PMID 4839:PMID 4804:PMID 4755:PMID 4698:PMID 4641:PMID 4592:PMID 4543:PMID 4498:PMID 4463:PMID 4428:PMID 4377:PMID 4326:PMID 4285:PMID 4236:PMID 4187:PMID 4138:PMID 4081:PMID 4046:PMID 4001:PMID 3960:PMID 3911:PMID 3854:PMID 3797:PMID 3756:PMID 3707:PMID 3648:PMID 3602:PMID 3567:PMID 3518:PMID 3482:PMID 3433:PMID 3384:PMID 3335:PMID 3278:PMID 3229:PMID 3183:PMID 3134:PMID 3091:PMID 3039:PMID 2985:PMID 2940:PMID 2882:PMID 2825:PMID 2787:PMID 2725:PMID 2681:PMID 2632:PMID 2582:PMID 2536:PMID 2485:PMID 2469:Cell 2450:PMID 2409:PMID 2360:PMID 2303:PMID 2251:PMID 2194:PMID 2148:PMID 2089:PMID 2054:PMID 2005:PMID 1943:PMID 1925:Cell 1880:PMID 1854:Gene 1835:2022 1710:PMID 1692:ISSN 1675:Gene 1468:TPX2 1437:and 1343:BimC 1038:3832 582:Bgee 530:Band 491:Chr. 429:Band 388:Chr. 342:3322 322:OMIM 279:4ZHI 275:4ZCA 271:4CK7 267:4CK6 263:4CK5 259:4BXN 255:4BBG 251:4B7B 247:4AS7 243:4AQW 239:4AQV 235:4AP0 231:4A5Y 227:4A51 223:4A50 219:4A28 215:4A1Z 211:3ZCW 207:3WPN 203:3L9H 199:3KEN 195:3K5E 191:3K3B 187:3HQD 183:3CJO 179:2XAE 175:2X7E 171:2X7D 167:2X7C 163:2X2R 159:2WOG 155:2UYM 151:2UYI 147:2Q2Z 143:2Q2Y 139:2PG2 135:2IEH 131:2GM1 127:2G1Q 123:2FME 119:2FL6 115:2FL2 111:2FKY 107:1YRS 103:1X88 99:1Q0B 95:1II6 76:RCSB 73:PDBe 6291:doi 6260:PMC 6250:doi 6246:280 6215:PMC 6205:doi 6201:279 6172:doi 6133:doi 6098:PMC 6090:doi 6055:doi 6012:doi 5977:PMC 5967:doi 5914:PMC 5904:doi 5849:doi 5805:PMC 5795:doi 5791:286 5754:PMC 5746:doi 5734:289 5697:PMC 5689:doi 5685:118 5648:PMC 5640:doi 5593:doi 5558:doi 5520:PMC 5512:doi 5508:161 5456:PMC 5448:doi 5407:doi 5403:281 5358:doi 5303:doi 5266:PMC 5258:doi 5219:doi 5215:135 5182:PMC 5174:doi 5135:doi 5121:335 5088:doi 5084:276 5047:doi 5008:doi 4965:doi 4961:286 4922:doi 4870:doi 4866:407 4831:doi 4794:PMC 4786:doi 4745:PMC 4737:doi 4688:PMC 4680:doi 4631:doi 4582:PMC 4574:doi 4570:182 4535:doi 4490:doi 4455:doi 4451:425 4418:PMC 4408:doi 4404:285 4367:PMC 4357:doi 4353:285 4316:doi 4312:115 4275:PMC 4267:doi 4263:135 4226:PMC 4218:doi 4177:doi 4128:doi 4073:doi 4036:hdl 4028:doi 4024:451 3991:doi 3987:272 3950:PMC 3942:doi 3938:195 3901:PMC 3893:doi 3844:PMC 3836:doi 3787:doi 3783:283 3746:PMC 3738:doi 3734:121 3697:PMC 3687:doi 3640:doi 3594:doi 3557:PMC 3549:doi 3510:doi 3472:PMC 3464:doi 3423:PMC 3415:doi 3374:PMC 3366:doi 3325:PMC 3317:doi 3268:PMC 3260:doi 3256:178 3221:doi 3173:doi 3126:doi 3114:294 3081:PMC 3073:doi 3069:123 3029:PMC 3019:doi 3015:286 2977:doi 2930:PMC 2920:doi 2916:285 2872:PMC 2864:doi 2817:doi 2777:PMC 2769:doi 2765:150 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