KL61_DROME
ID KL61_DROME Reviewed; 1066 AA.
AC P46863; Q8T0A6; Q9W0I8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Kinesin-like protein Klp61F {ECO:0000303|PubMed:8227131};
DE AltName: Full=Bipolar kinesin KRP-130 {ECO:0000303|PubMed:8918872};
GN Name=Klp61F {ECO:0000312|FlyBase:FBgn0004378}; Synonyms=KLP2;
GN ORFNames=CG9191 {ECO:0000312|FlyBase:FBgn0004378};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8227131; DOI=10.1083/jcb.123.3.665;
RA Heck M.M.S., Pereira A., Pesavento P.A., Yannoni Y., Spradling A.C.,
RA Goldstein L.S.B.;
RT "The kinesin-like protein KLP61F is essential for mitosis in Drosophila.";
RL J. Cell Biol. 123:665-679(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-357.
RC STRAIN=DP CN BW;
RX PubMed=1924306; DOI=10.1073/pnas.88.19.8470;
RA Stewart R.J., Pesavento P.A., Woerpel D.N., Goldstein L.S.B.;
RT "Identification and partial characterization of six members of the kinesin
RT superfamily in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8470-8474(1991).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION AS KRP-130, AND FUNCTION.
RX PubMed=8918872; DOI=10.1038/384225a0;
RA Kashina A.S., Scholey J.M., Leszyk J.D., Saxton W.M.;
RT "An essential bipolar mitotic motor.";
RL Nature 384:225-225(1996).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8589456; DOI=10.1091/mbc.6.11.1563;
RA Barton N.R., Pereira A.J., Goldstein L.S.;
RT "Motor activity and mitotic spindle localization of the Drosophila kinesin-
RT like protein KLP61F.";
RL Mol. Biol. Cell 6:1563-1574(1995).
RN [8]
RP SUBUNIT.
RX PubMed=8538794; DOI=10.1038/379270a0;
RA Kashina A.S., Baskin R.J., Cole D.G., Wedaman K.P., Saxton W.M.,
RA Scholey J.M.;
RT "A bipolar kinesin.";
RL Nature 379:270-272(1996).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10469596; DOI=10.1016/s0960-9822(99)80400-x;
RA Wilson P.G.;
RT "BimC motor protein KLP61F cycles between mitotic spindles and fusomes in
RT Drosophila germ cells.";
RL Curr. Biol. 9:923-926(1999).
RN [10]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=9885249; DOI=10.1083/jcb.144.1.125;
RA Sharp D.J., McDonald K.L., Brown H.M., Matthies H.J., Walczak C.,
RA Vale R.D., Mitchison T.J., Scholey J.M.;
RT "The bipolar kinesin, KLP61F, cross-links microtubules within interpolar
RT microtubule bundles of Drosophila embryonic mitotic spindles.";
RL J. Cell Biol. 144:125-138(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-520 AND SER-949, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [12]
RP FUNCTION.
RX PubMed=19062285; DOI=10.1016/j.cub.2008.10.026;
RA van den Wildenberg S.M., Tao L., Kapitein L.C., Schmidt C.F., Scholey J.M.,
RA Peterman E.J.;
RT "The homotetrameric kinesin-5 KLP61F preferentially crosslinks microtubules
RT into antiparallel orientations.";
RL Curr. Biol. 18:1860-1864(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-933; SER-949; SER-1043;
RP THR-1045; SER-1050 AND SER-1054, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [14]
RP SUBCELLULAR LOCATION, INTERACTION WITH WEE1, PHOSPHORYLATION, AND
RP MUTAGENESIS OF TYR-23; TYR-152 AND TYR-207.
RX PubMed=19800237; DOI=10.1016/j.cub.2009.08.013;
RA Garcia K., Stumpff J., Duncan T., Su T.T.;
RT "Tyrosines in the kinesin-5 head domain are necessary for phosphorylation
RT by Wee1 and for mitotic spindle integrity.";
RL Curr. Biol. 19:1670-1676(2009).
RN [15]
RP FUNCTION.
RX PubMed=19158379; DOI=10.1091/mbc.e08-10-1033;
RA Brust-Mascher I., Sommi P., Cheerambathur D.K., Scholey J.M.;
RT "Kinesin-5-dependent poleward flux and spindle length control in Drosophila
RT embryo mitosis.";
RL Mol. Biol. Cell 20:1749-1762(2009).
RN [16]
RP FUNCTION.
RX PubMed=23857769; DOI=10.1083/jcb.201303163;
RA Wakana Y., Villeneuve J., van Galen J., Cruz-Garcia D., Tagaya M.,
RA Malhotra V.;
RT "Kinesin-5/Eg5 is important for transport of CARTS from the trans-Golgi
RT network to the cell surface.";
RL J. Cell Biol. 202:241-250(2013).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.4 ANGSTROMS) OF 1-368, AND INTERACTION
RP WITH MICROTUBULES.
RX PubMed=19285086; DOI=10.1016/j.jmb.2009.03.008;
RA Bodey A.J., Kikkawa M., Moores C.A.;
RT "9-Angstrom structure of a microtubule-bound mitotic motor.";
RL J. Mol. Biol. 388:218-224(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 634-837, SUBUNIT, AND MUTAGENESIS
RP OF PHE-669; LEU-726; 729-MET-MET-730; ARG-740; ARG-761 AND TYR-775.
RX PubMed=24714498; DOI=10.7554/elife.02217;
RA Scholey J.E., Nithianantham S., Scholey J.M., Al-Bassam J.;
RT "Structural basis for the assembly of the mitotic motor Kinesin-5 into
RT bipolar tetramers.";
RL Elife 3:E02217-E02217(2014).
CC -!- FUNCTION: Important role in mitotic dividing cells (PubMed:8227131).
CC Microtubule motor required for spindle body separation
CC (PubMed:8918872). Slow plus-end directed microtubule motor capable of
CC cross-linking and sliding apart antiparallel microtubules, thereby
CC pushing apart the associated spindle poles during spindle assembly and
CC function (PubMed:8918872, PubMed:8589456, PubMed:19062285). Forms
CC cross-links between microtubules within interpolar microtubule bundles
CC (PubMed:9885249, PubMed:19158379). Contributes to the length of the
CC metaphase spindle, maintains the prometaphase spindle by antagonizing
CC Ncd, drives anaphase B, and also contributes to normal chromosome
CC congression, kinetochore spacing, and anaphase A rates
CC (PubMed:19158379). Displays microtubule-stimulated ATPase activity
CC (PubMed:8589456). Required for normal fusome organization
CC (PubMed:10469596). Required in non-mitotic cells for transport of
CC secretory proteins from the Golgi complex to the cell surface
CC (PubMed:23857769). {ECO:0000269|PubMed:10469596,
CC ECO:0000269|PubMed:19062285, ECO:0000269|PubMed:19158379,
CC ECO:0000269|PubMed:23857769, ECO:0000269|PubMed:8227131,
CC ECO:0000269|PubMed:8589456, ECO:0000269|PubMed:8918872,
CC ECO:0000269|PubMed:9885249}.
CC -!- SUBUNIT: Homotetramer (PubMed:8538794, PubMed:9885249,
CC PubMed:24714498). Consists of two pairs of polypeptides associated by
CC coiled-coil interactions to form two homodimers (PubMed:8538794). The
CC homodimers are linked by lateral interactions between their coiled-coil
CC regions to form a bipolar homotetramer consisting of a central rod with
CC two motor domains projecting from either end (PubMed:8538794). Parallel
CC coiled coils extend from each pair of motor heads, switch to two
CC antiparallel coiled coils in the central region and then back to
CC parallel coiled coils (PubMed:24714498). Interacts with Wee1
CC (PubMed:19800237). {ECO:0000269|PubMed:19800237,
CC ECO:0000269|PubMed:24714498, ECO:0000269|PubMed:8538794,
CC ECO:0000269|PubMed:9885249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:10469596, ECO:0000269|PubMed:19800237,
CC ECO:0000269|PubMed:8589456, ECO:0000269|PubMed:9885249}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:8589456}. Cytoplasm
CC {ECO:0000269|PubMed:10469596, ECO:0000269|PubMed:9885249}. Note=In
CC somatic cells, cytoplasmic during interphase, localized to centrosomal
CC asters at the onset of mitosis in prophase and associated with spindle
CC structures during the remainder of mitosis (PubMed:10469596). In male
CC and female germ cells, associates with fusomes during interphase, then
CC localizes to centrosomal asters during prophase and to spindles in
CC metaphase (PubMed:10469596). Coincident with spindle microtubules from
CC prophase to metaphase and, as mitosis proceeds, found both at the
CC spindle poles and along the spindle fibers (PubMed:8589456).
CC {ECO:0000269|PubMed:10469596, ECO:0000269|PubMed:8589456}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in proliferating tissues
CC during embryonic and larval development. {ECO:0000269|PubMed:8227131}.
CC -!- PTM: Phosphorylation is required for localization to mitotic spindles
CC (PubMed:9885249). Phosphorylation of Thr-933 during mitosis controls
CC association with the spindle apparatus (By similarity). Phosphorylated
CC in vitro by Wee1 (PubMed:19800237). {ECO:0000250|UniProtKB:P52732,
CC ECO:0000269|PubMed:19800237, ECO:0000269|PubMed:9885249}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; U01842; AAA03718.1; -; mRNA.
DR EMBL; AE014296; AAF47458.2; -; Genomic_DNA.
DR EMBL; AY069442; AAL39587.1; -; mRNA.
DR EMBL; M74428; AAA28655.1; -; Genomic_DNA.
DR PIR; A48669; A48669.
DR RefSeq; NP_476818.1; NM_057470.5.
DR PDB; 2WBE; EM; 9.40 A; C=1-368.
DR PDB; 4PXT; X-ray; 2.90 A; A/B=634-837.
DR PDB; 4PXU; X-ray; 2.60 A; A/B=634-837.
DR PDB; 6VPO; EM; 4.40 A; C=1-369.
DR PDB; 6VPP; EM; 4.40 A; C=1-369.
DR PDBsum; 2WBE; -.
DR PDBsum; 4PXT; -.
DR PDBsum; 4PXU; -.
DR PDBsum; 6VPO; -.
DR PDBsum; 6VPP; -.
DR AlphaFoldDB; P46863; -.
DR SMR; P46863; -.
DR BioGRID; 63681; 15.
DR DIP; DIP-22047N; -.
DR IntAct; P46863; 9.
DR MINT; P46863; -.
DR STRING; 7227.FBpp0072616; -.
DR ChEMBL; CHEMBL1795160; -.
DR iPTMnet; P46863; -.
DR PaxDb; P46863; -.
DR PRIDE; P46863; -.
DR DNASU; 38135; -.
DR EnsemblMetazoa; FBtr0072733; FBpp0072616; FBgn0004378.
DR GeneID; 38135; -.
DR KEGG; dme:Dmel_CG9191; -.
DR CTD; 38135; -.
DR FlyBase; FBgn0004378; Klp61F.
DR VEuPathDB; VectorBase:FBgn0004378; -.
DR eggNOG; KOG0243; Eukaryota.
DR GeneTree; ENSGT00940000155921; -.
DR HOGENOM; CLU_001485_33_4_1; -.
DR InParanoid; P46863; -.
DR OMA; PGHKDIE; -.
DR OrthoDB; 179272at2759; -.
DR PhylomeDB; P46863; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR SignaLink; P46863; -.
DR BioGRID-ORCS; 38135; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; P46863; -.
DR GenomeRNAi; 38135; -.
DR PRO; PR:P46863; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004378; Expressed in eye disc (Drosophila) and 37 other tissues.
DR ExpressionAtlas; P46863; baseline and differential.
DR Genevisible; P46863; DM.
DR GO; GO:0005818; C:aster; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0045169; C:fusome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0005871; C:kinesin complex; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IDA:FlyBase.
DR GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:FlyBase.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IDA:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051299; P:centrosome separation; IMP:FlyBase.
DR GO; GO:0045478; P:fusome organization; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0007100; P:mitotic centrosome separation; IMP:FlyBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0031535; P:plus-end directed microtubule sliding; IDA:FlyBase.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IMP:FlyBase.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR025901; Kinesin-assoc_MT-bd_dom.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF13931; Microtub_bind; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Microtubule; Mitosis;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1066
FT /note="Kinesin-like protein Klp61F"
FT /id="PRO_0000125371"
FT DOMAIN 19..356
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 990..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..462
FT /evidence="ECO:0000255"
FT COILED 540..569
FT /evidence="ECO:0000255"
FT COILED 639..738
FT /evidence="ECO:0000255"
FT COILED 808..875
FT /evidence="ECO:0000255"
FT COILED 889..918
FT /evidence="ECO:0000255"
FT COMPBIAS 1016..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 933
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1045
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 23
FT /note="Y->F: Spindle defects and greatly reduced
FT phosphorylation by Wee1 in vitro; when associated with F-
FT 152 and F-207."
FT /evidence="ECO:0000269|PubMed:19800237"
FT MUTAGEN 152
FT /note="Y->F: Spindle defects and greatly reduced
FT phosphorylation by Wee1 in vitro; when associated with F-23
FT and F-207."
FT /evidence="ECO:0000269|PubMed:19800237"
FT MUTAGEN 207
FT /note="Y->F: Spindle defects and greatly reduced
FT phosphorylation by Wee1 in vitro; when associated with F-23
FT and F-152."
FT /evidence="ECO:0000269|PubMed:19800237"
FT MUTAGEN 669
FT /note="F->E: Remains tetrameric."
FT /evidence="ECO:0000269|PubMed:24714498"
FT MUTAGEN 726
FT /note="L->D: Mainly tetrameric. Mainly dimeric; when
FT associated with R-775."
FT /evidence="ECO:0000269|PubMed:24714498"
FT MUTAGEN 726
FT /note="L->K: Mainly tetrameric."
FT /evidence="ECO:0000269|PubMed:24714498"
FT MUTAGEN 729..730
FT /note="MM->EE: Mainly monomeric."
FT /evidence="ECO:0000269|PubMed:24714498"
FT MUTAGEN 740
FT /note="R->A: Formation of tetramers, dimers and monomers."
FT /evidence="ECO:0000269|PubMed:24714498"
FT MUTAGEN 761
FT /note="R->A: Formation of tetramers and dimers."
FT /evidence="ECO:0000269|PubMed:24714498"
FT MUTAGEN 775
FT /note="Y->R: Mainly tetrameric with formation of some
FT monomers. Mainly dimeric; when associated with D-726."
FT /evidence="ECO:0000269|PubMed:24714498"
FT CONFLICT 962
FT /note="L -> Q (in Ref. 1; AAA03718)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="V -> D (in Ref. 1; AAA03718)"
FT /evidence="ECO:0000305"
FT HELIX 641..695
FT /evidence="ECO:0007829|PDB:4PXU"
FT HELIX 698..790
FT /evidence="ECO:0007829|PDB:4PXU"
FT HELIX 792..794
FT /evidence="ECO:0007829|PDB:4PXU"
SQ SEQUENCE 1066 AA; 121163 MW; 363647366EE0721F CRC64;
MDISGGNTSR QPQKKSNQNI QVYVRVRPLN SRERCIRSAE VVDVVGPREV VTRHTLDSKL
TKKFTFDRSF GPESKQCDVY SVVVSPLIEE VLNGYNCTVF AYGQTGTGKT HTMVGNETAE
LKSSWEDDSD IGIIPRALSH LFDELRMMEV EYTMRISYLE LYNEELCDLL STDDTTKIRI
FDDSTKKGSV IIQGLEEIPV HSKDDVYKLL EKGKERRKTA TTLMNAQSSR SHTVFSIVVH
IRENGIEGED MLKIGKLNLV DLAGSENVSK AGNEKGIRVR ETVNINQSLL TLGRVITALV
DRAPHVPYRE SKLTRLLQES LGGRTKTSII ATISPGHKDI EETLSTLEYA HRAKNIQNKP
EVNQKLTKKT VLKEYTEEID KLKRDLMAAR DKNGIYLAEE TYGEITLKLE SQNRELNEKM
LLLKALKDEL QNKEKIFSEV SMSLVEKTQE LKKTEENLLN TKGTLLLTKK VLTKTKRRYK
EKKELVASHM KTEQVLTTQA QEILAAADLA TDDTHQLHGT IERRRELDEK IRRSCDQFKD
RMQDNLEMIG GSLNLYQDQQ AALKEQLSQE MVNSSYVSQR LALNSSKSIE MLKEMCAQSL
QDQTNLHNKL IGEVMKISDQ HSQAFVAKLM EQMQQQQLLM SKEIQTNLQV IEENNQRHKA
MLDSMQEKFA TIIDSSLQSV EEHAKQMHKK LEQLGAMSLP DAEELQNLQE ELANERALAQ
QEDALLESMM MQMEQIKNLR SKNSISMSVH LNKMEESRLT RNHRIDDIKS GIQDYQKLGI
EASQSAQAEL TSQMEAGMLC LDQGVANCSM LQVHMKNLNQ KYEKETNENV GSVRVHHNQV
EIICQESKQQ LEAVQEKTEV NLEQMVDARQ QLITEDRQRF IGHATVATDL VQESNRQFSE
HAEHQRQQLQ ICEQELVRFQ QSELKTYAPT GTTPSKRDFV YPRTLVATSP HQEIVRRYRQ
ELDWSDLDTT ATIDECSEGE HDVSMHSVQE LSETETIMNS TPIEPVDGVT VKRGCGTTRN
SNSNALKPPV ATGGKRSSSL SRSLTPSKTS PRGSPAFVRH NKENVA
