KIF11_HUMAN
ID KIF11_HUMAN Reviewed; 1056 AA.
AC P52732; A0AV49; B2RMV3; Q15716; Q5VWX0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Kinesin-like protein KIF11;
DE AltName: Full=Kinesin-like protein 1;
DE AltName: Full=Kinesin-like spindle protein HKSP;
DE AltName: Full=Kinesin-related motor protein Eg5;
DE AltName: Full=Thyroid receptor-interacting protein 5;
DE Short=TR-interacting protein 5;
DE Short=TRIP-5;
GN Name=KIF11; Synonyms=EG5, KNSL1, TRIP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-926, AND MUTAGENESIS.
RX PubMed=8548803; DOI=10.1016/0092-8674(95)90142-6;
RA Blangy A., Lane H.A., D'Herin P., Harper M., Kress M., Nigg E.A.;
RT "Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a
RT kinesin-related motor essential for bipolar spindle formation in vivo.";
RL Cell 83:1159-1169(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9701554; DOI=10.1242/jcs.111.17.2551;
RA Whitehead C.M., Rattner J.B.;
RT "Expanding the role of HsEg5 within the mitotic and post-mitotic phases of
RT the cell cycle.";
RL J. Cell Sci. 111:2551-2561(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 818-867.
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-458, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP FUNCTION, INTERACTION WITH NEK6, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-926 AND SER-1033, AND MUTAGENESIS OF THR-926 AND SER-1033.
RX PubMed=19001501; DOI=10.1242/jcs.035360;
RA Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C.,
RA Avruch J., Roig J.;
RT "The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site
RT necessary for mitotic spindle formation.";
RL J. Cell Sci. 121:3912-3921(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-926, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH RARRES1 AND AGBL2.
RX PubMed=21303978; DOI=10.1158/0008-5472.can-10-2294;
RA Sahab Z.J., Hall M.D., Me Sung Y., Dakshanamurthy S., Ji Y., Kumar D.,
RA Byers S.W.;
RT "Tumor suppressor RARRES1 interacts with cytoplasmic carboxypeptidase AGBL2
RT to regulate the alpha-tubulin tyrosination cycle.";
RL Cancer Res. 71:1219-1228(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-458; THR-925; THR-926 AND
RP SER-1033, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-477, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-368.
RX PubMed=11328809; DOI=10.1074/jbc.m100395200;
RA Turner J., Anderson R., Guo J., Beraud C., Fletterick R., Sakowicz R.;
RT "Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel
RT conformation of the neck-linker.";
RL J. Biol. Chem. 276:25496-25502(2001).
RN [19]
RP IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
RX PubMed=17707232; DOI=10.1016/j.molcel.2007.07.024;
RA Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H.,
RA Tempst P., Glass C.K., Rosenfeld M.G.;
RT "A histone H2A deubiquitinase complex coordinating histone acetylation and
RT H1 dissociation in transcriptional regulation.";
RL Mol. Cell 27:609-621(2007).
RN [20]
RP VARIANTS MCLMR LEU-144; CYS-234; CYS-235 AND CYS-944.
RX PubMed=22284827; DOI=10.1016/j.ajhg.2011.12.018;
RA Ostergaard P., Simpson M.A., Mendola A., Vasudevan P., Connell F.C.,
RA van Impel A., Moore A.T., Loeys B.L., Ghalamkarpour A., Onoufriadis A.,
RA Martinez-Corral I., Devery S., Leroy J.G., van Laer L., Singer A.,
RA Bialer M.G., McEntagart M., Quarrell O., Brice G., Trembath R.C.,
RA Schulte-Merker S., Makinen T., Vikkula M., Mortimer P.S., Mansour S.,
RA Jeffery S.;
RT "Mutations in KIF11 cause autosomal-dominant microcephaly variably
RT associated with congenital lymphedema and chorioretinopathy.";
RL Am. J. Hum. Genet. 90:356-362(2012).
CC -!- FUNCTION: Motor protein required for establishing a bipolar spindle
CC during mitosis (PubMed:19001501). Required in non-mitotic cells for
CC transport of secretory proteins from the Golgi complex to the cell
CC surface (PubMed:23857769). {ECO:0000269|PubMed:19001501,
CC ECO:0000269|PubMed:23857769}.
CC -!- SUBUNIT: Interacts with the thyroid hormone receptor in the presence of
CC thyroid hormone. Component of a large chromatin remodeling complex, at
CC least composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Interacts (via C-
CC terminus) with the kinase NEK6 in both interphase and mitosis.
CC Interacts with RARRES1 and AGBL2 (PubMed:21303978).
CC {ECO:0000269|PubMed:17707232, ECO:0000269|PubMed:19001501,
CC ECO:0000269|PubMed:21303978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19001501,
CC ECO:0000269|PubMed:23857769}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:19001501}.
CC -!- PTM: Phosphorylated exclusively on serine during S phase, but on both
CC serine and Thr-926 during mitosis, so controlling the association of
CC KIF11 with the spindle apparatus (probably during early prophase).
CC {ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:8548803}.
CC -!- PTM: A subset of this protein primarily localized at the spindle pole
CC is phosphorylated by NEK6 during mitosis; phosphorylation is required
CC for mitotic function. {ECO:0000269|PubMed:19001501}.
CC -!- DISEASE: Microcephaly with or without chorioretinopathy, lymphedema, or
CC intellectual disability (MCLMR) [MIM:152950]: An autosomal dominant
CC disorder that involves an overlapping but variable spectrum of central
CC nervous system and ocular developmental anomalies. Microcephaly ranges
CC from mild to severe and is often associated with mild to moderate
CC developmental delay and a characteristic facial phenotype with
CC upslanting palpebral fissures, broad nose with rounded tip, long
CC philtrum with thin upper lip, prominent chin, and prominent ears.
CC Chorioretinopathy is the most common eye abnormality, but retinal
CC folds, microphthalmia, and myopic and hypermetropic astigmatism have
CC also been reported, and some individuals have no overt ocular
CC phenotype. Congenital lymphedema, when present, is typically confined
CC to the dorsa of the feet, and lymphoscintigraphy reveals the absence of
CC radioactive isotope uptake from the webspaces between the toes.
CC {ECO:0000269|PubMed:22284827}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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; X85137; CAA59449.1; -; mRNA.
DR EMBL; U37426; AAA86132.1; -; mRNA.
DR EMBL; AL360222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126211; AAI26212.1; -; mRNA.
DR EMBL; BC136474; AAI36475.1; -; mRNA.
DR EMBL; L40372; AAC41739.1; -; mRNA.
DR CCDS; CCDS7422.1; -.
DR PIR; G02157; G02157.
DR RefSeq; NP_004514.2; NM_004523.3.
DR PDB; 1II6; X-ray; 2.10 A; A/B=1-368.
DR PDB; 1Q0B; X-ray; 1.90 A; A/B=2-368.
DR PDB; 1X88; X-ray; 1.80 A; A/B=10-368.
DR PDB; 1YRS; X-ray; 2.50 A; A/B=1-368.
DR PDB; 2FKY; X-ray; 2.30 A; A/B=2-368.
DR PDB; 2FL2; X-ray; 2.50 A; A/B=2-368.
DR PDB; 2FL6; X-ray; 2.50 A; A/B=2-368.
DR PDB; 2FME; X-ray; 2.10 A; A/B=1-368.
DR PDB; 2G1Q; X-ray; 2.51 A; A/B=1-368.
DR PDB; 2GM1; X-ray; 2.30 A; A/B/D/E=1-368.
DR PDB; 2IEH; X-ray; 2.70 A; A/B=2-368.
DR PDB; 2PG2; X-ray; 1.85 A; A/B=1-368.
DR PDB; 2Q2Y; X-ray; 2.50 A; A/B=2-368.
DR PDB; 2Q2Z; X-ray; 3.00 A; A/B=2-368.
DR PDB; 2UYI; X-ray; 2.10 A; A/B=1-368.
DR PDB; 2UYM; X-ray; 2.11 A; A/B=1-368.
DR PDB; 2WOG; X-ray; 2.00 A; A/B/C=1-368.
DR PDB; 2X2R; X-ray; 2.20 A; A/B/C=1-368.
DR PDB; 2X7C; X-ray; 1.90 A; A/B=1-368.
DR PDB; 2X7D; X-ray; 2.30 A; A/B=1-368.
DR PDB; 2X7E; X-ray; 2.40 A; A/B=1-368.
DR PDB; 2XAE; X-ray; 2.60 A; A/B/C=1-368.
DR PDB; 3CJO; X-ray; 2.28 A; A/B=2-368.
DR PDB; 3HQD; X-ray; 2.19 A; A/B=1-369.
DR PDB; 3K3B; X-ray; 2.40 A; A/B=1-368.
DR PDB; 3K5E; X-ray; 1.97 A; A/B=1-368.
DR PDB; 3KEN; X-ray; 2.50 A; A=1-369.
DR PDB; 3L9H; X-ray; 2.00 A; A/B=1-368.
DR PDB; 3WPN; X-ray; 2.80 A; A=1-369.
DR PDB; 3ZCW; X-ray; 1.69 A; A=16-363.
DR PDB; 4A1Z; X-ray; 2.80 A; A/B=1-368.
DR PDB; 4A28; X-ray; 2.55 A; A/B=1-368.
DR PDB; 4A50; X-ray; 2.75 A; A=1-368.
DR PDB; 4A51; X-ray; 2.75 A; A/B/C/D/E/F/G=1-368.
DR PDB; 4A5Y; X-ray; 2.45 A; A/B/C=1-368.
DR PDB; 4AP0; X-ray; 2.59 A; A/B/C/D=1-368.
DR PDB; 4AQV; EM; 9.70 A; C=1-367.
DR PDB; 4AQW; EM; 9.50 A; C=1-367.
DR PDB; 4AS7; X-ray; 2.40 A; A=1-368.
DR PDB; 4B7B; X-ray; 2.50 A; A=1-368.
DR PDB; 4BBG; X-ray; 2.75 A; A=1-368.
DR PDB; 4BXN; X-ray; 2.79 A; A/B=1-368.
DR PDB; 4CK5; EM; 10.00 A; C=1-367.
DR PDB; 4CK6; EM; 9.20 A; C=1-367.
DR PDB; 4CK7; EM; 9.20 A; C=1-367.
DR PDB; 4ZCA; X-ray; 2.30 A; A/B=1-369.
DR PDB; 4ZHI; X-ray; 2.30 A; A/B=1-369.
DR PDB; 5JV3; X-ray; 2.01 A; A/B/C/D=366-391.
DR PDB; 5ZO7; X-ray; 2.60 A; A/B=17-369.
DR PDB; 5ZO8; X-ray; 2.20 A; A/B=17-369.
DR PDB; 5ZO9; X-ray; 2.70 A; A/B=17-369.
DR PDB; 6G6Y; X-ray; 1.80 A; A=1-368.
DR PDB; 6G6Z; X-ray; 2.80 A; A=1-368.
DR PDB; 6HKX; X-ray; 2.80 A; A/B=1-368.
DR PDB; 6HKY; X-ray; 2.75 A; A/B/C=1-368.
DR PDB; 6TA3; EM; 3.80 A; K=1-369.
DR PDB; 6TA4; EM; 6.10 A; K=1-369.
DR PDB; 6TIW; EM; 1.09 A; K=1-369.
DR PDB; 6TLE; X-ray; 1.75 A; A/B=2-368.
DR PDB; 6TRL; X-ray; 2.20 A; A/B=2-368.
DR PDB; 6Y1I; X-ray; 3.00 A; A/B/C=1-368.
DR PDBsum; 1II6; -.
DR PDBsum; 1Q0B; -.
DR PDBsum; 1X88; -.
DR PDBsum; 1YRS; -.
DR PDBsum; 2FKY; -.
DR PDBsum; 2FL2; -.
DR PDBsum; 2FL6; -.
DR PDBsum; 2FME; -.
DR PDBsum; 2G1Q; -.
DR PDBsum; 2GM1; -.
DR PDBsum; 2IEH; -.
DR PDBsum; 2PG2; -.
DR PDBsum; 2Q2Y; -.
DR PDBsum; 2Q2Z; -.
DR PDBsum; 2UYI; -.
DR PDBsum; 2UYM; -.
DR PDBsum; 2WOG; -.
DR PDBsum; 2X2R; -.
DR PDBsum; 2X7C; -.
DR PDBsum; 2X7D; -.
DR PDBsum; 2X7E; -.
DR PDBsum; 2XAE; -.
DR PDBsum; 3CJO; -.
DR PDBsum; 3HQD; -.
DR PDBsum; 3K3B; -.
DR PDBsum; 3K5E; -.
DR PDBsum; 3KEN; -.
DR PDBsum; 3L9H; -.
DR PDBsum; 3WPN; -.
DR PDBsum; 3ZCW; -.
DR PDBsum; 4A1Z; -.
DR PDBsum; 4A28; -.
DR PDBsum; 4A50; -.
DR PDBsum; 4A51; -.
DR PDBsum; 4A5Y; -.
DR PDBsum; 4AP0; -.
DR PDBsum; 4AQV; -.
DR PDBsum; 4AQW; -.
DR PDBsum; 4AS7; -.
DR PDBsum; 4B7B; -.
DR PDBsum; 4BBG; -.
DR PDBsum; 4BXN; -.
DR PDBsum; 4CK5; -.
DR PDBsum; 4CK6; -.
DR PDBsum; 4CK7; -.
DR PDBsum; 4ZCA; -.
DR PDBsum; 4ZHI; -.
DR PDBsum; 5JV3; -.
DR PDBsum; 5ZO7; -.
DR PDBsum; 5ZO8; -.
DR PDBsum; 5ZO9; -.
DR PDBsum; 6G6Y; -.
DR PDBsum; 6G6Z; -.
DR PDBsum; 6HKX; -.
DR PDBsum; 6HKY; -.
DR PDBsum; 6TA3; -.
DR PDBsum; 6TA4; -.
DR PDBsum; 6TIW; -.
DR PDBsum; 6TLE; -.
DR PDBsum; 6TRL; -.
DR PDBsum; 6Y1I; -.
DR AlphaFoldDB; P52732; -.
DR SMR; P52732; -.
DR BioGRID; 110030; 222.
DR CORUM; P52732; -.
DR DIP; DIP-53686N; -.
DR IntAct; P52732; 105.
DR MINT; P52732; -.
DR STRING; 9606.ENSP00000260731; -.
DR BindingDB; P52732; -.
DR ChEMBL; CHEMBL4581; -.
DR DrugBank; DB08244; (1S)-1-CYCLOPROPYL-2-[(2S)-4-(2,5-DIFLUOROPHENYL)-2-PHENYL-2,5-DIHYDRO-1H-PYRROL-1-YL]-2-OXOETHANAMINE.
DR DrugBank; DB08246; (2S)-4-(2,5-DIFLUOROPHENYL)-N,N-DIMETHYL-2-PHENYL-2,5-DIHYDRO-1H-PYRROLE-1-CARBOXAMIDE.
DR DrugBank; DB08239; (2S)-4-(2,5-DIFLUOROPHENYL)-N-METHYL-2-PHENYL-N-PIPERIDIN-4-YL-2,5-DIHYDRO-1H-PYRROLE-1-CARBOXAMIDE.
DR DrugBank; DB07064; (4R)-4-(3-HYDROXYPHENYL)-N,N,7,8-TETRAMETHYL-3,4-DIHYDROISOQUINOLINE-2(1H)-CARBOXAMIDE.
DR DrugBank; DB08033; (5R)-N,N-DIETHYL-5-METHYL-2-[(THIOPHEN-2-YLCARBONYL)AMINO]-4,5,6,7-TETRAHYDRO-1-BENZOTHIOPHENE-3-CARBOXAMIDE.
DR DrugBank; DB08250; (5S)-5-(3-AMINOPROPYL)-3-(2,5-DIFLUOROPHENYL)-N-ETHYL-5-PHENYL-4,5-DIHYDRO-1H-PYRAZOLE-1-CARBOXAMIDE.
DR DrugBank; DB03996; 3-[(5s)-1-Acetyl-3-(2-Chlorophenyl)-4,5-Dihydro-1h-Pyrazol-5-Yl]Phenol.
DR DrugBank; DB08198; [(4R)-4-(3-HYDROXYPHENYL)-1,6-DIMETHYL-2-THIOXO-1,2,3,4-TETRAHYDROPYRIMIDIN-5-YL](PHENYL)METHANONE.
DR DrugBank; DB06040; Filanesib.
DR DrugBank; DB08037; MK-0731.
DR DrugBank; DB04331; Monastrol.
DR DrugBank; DB08032; N,N-DIETHYL-2-[(2-THIENYLCARBONYL)AMINO]-4,5,6,7-TETRAHYDRO-1-BENZOTHIOPHENE-3-CARBOXAMIDE.
DR DrugCentral; P52732; -.
DR GuidetoPHARMACOLOGY; 2788; -.
DR GlyGen; P52732; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P52732; -.
DR MetOSite; P52732; -.
DR PhosphoSitePlus; P52732; -.
DR SwissPalm; P52732; -.
DR BioMuta; KIF11; -.
DR DMDM; 116242604; -.
DR EPD; P52732; -.
DR jPOST; P52732; -.
DR MassIVE; P52732; -.
DR MaxQB; P52732; -.
DR PaxDb; P52732; -.
DR PeptideAtlas; P52732; -.
DR PRIDE; P52732; -.
DR ProteomicsDB; 56504; -.
DR Antibodypedia; 1871; 449 antibodies from 39 providers.
DR DNASU; 3832; -.
DR Ensembl; ENST00000260731.5; ENSP00000260731.3; ENSG00000138160.7.
DR GeneID; 3832; -.
DR KEGG; hsa:3832; -.
DR MANE-Select; ENST00000260731.5; ENSP00000260731.3; NM_004523.4; NP_004514.2.
DR UCSC; uc001kic.4; human.
DR CTD; 3832; -.
DR DisGeNET; 3832; -.
DR GeneCards; KIF11; -.
DR HGNC; HGNC:6388; KIF11.
DR HPA; ENSG00000138160; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; KIF11; -.
DR MIM; 148760; gene.
DR MIM; 152950; phenotype.
DR neXtProt; NX_P52732; -.
DR OpenTargets; ENSG00000138160; -.
DR Orphanet; 2526; Microcephaly-lymphedema-chorioretinopathy syndrome.
DR PharmGKB; PA30177; -.
DR VEuPathDB; HostDB:ENSG00000138160; -.
DR eggNOG; KOG0243; Eukaryota.
DR GeneTree; ENSGT00940000155921; -.
DR HOGENOM; CLU_001485_33_4_1; -.
DR InParanoid; P52732; -.
DR OMA; INLWAER; -.
DR OrthoDB; 179272at2759; -.
DR PhylomeDB; P52732; -.
DR TreeFam; TF105230; -.
DR BRENDA; 5.6.1.3; 2681.
DR PathwayCommons; P52732; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; P52732; -.
DR SIGNOR; P52732; -.
DR BioGRID-ORCS; 3832; 793 hits in 1094 CRISPR screens.
DR ChiTaRS; KIF11; human.
DR EvolutionaryTrace; P52732; -.
DR GeneWiki; Kinesin_family_member_11; -.
DR GenomeRNAi; 3832; -.
DR Pharos; P52732; Tchem.
DR PRO; PR:P52732; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P52732; protein.
DR Bgee; ENSG00000138160; Expressed in ventricular zone and 131 other tissues.
DR Genevisible; P52732; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005871; C:kinesin complex; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; TAS:ProtInc.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0007100; P:mitotic centrosome separation; IEA:Ensembl.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IDA:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; TAS:ProtInc.
DR GO; GO:0046602; P:regulation of mitotic centrosome separation; IMP:UniProtKB.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
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; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Isopeptide bond;
KW Microtubule; Mitosis; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1056
FT /note="Kinesin-like protein KIF11"
FT /id="PRO_0000125372"
FT DOMAIN 18..359
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 364..480
FT /evidence="ECO:0000255"
FT COILED 736..763
FT /evidence="ECO:0000255"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 925
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 926
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:19001501,
FT ECO:0000269|PubMed:8548803, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1033
FT /note="Phosphoserine; by NEK6"
FT /evidence="ECO:0000269|PubMed:19001501,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 144
FT /note="F -> L (in MCLMR)"
FT /evidence="ECO:0000269|PubMed:22284827"
FT /id="VAR_067829"
FT VARIANT 234
FT /note="R -> C (in MCLMR)"
FT /evidence="ECO:0000269|PubMed:22284827"
FT /id="VAR_067830"
FT VARIANT 235
FT /note="S -> C (in MCLMR; dbSNP:rs387906643)"
FT /evidence="ECO:0000269|PubMed:22284827"
FT /id="VAR_067831"
FT VARIANT 944
FT /note="R -> C (in MCLMR; dbSNP:rs387906642)"
FT /evidence="ECO:0000269|PubMed:22284827"
FT /id="VAR_067832"
FT VARIANT 1042
FT /note="L -> F (in dbSNP:rs34417963)"
FT /id="VAR_049682"
FT MUTAGEN 926
FT /note="T->A: No mitotic phosphorylation. No binding to
FT spindle apparatus."
FT /evidence="ECO:0000269|PubMed:19001501"
FT MUTAGEN 1033
FT /note="S->A: Still binds to the mitotic spindle but mitotic
FT progression is impaired."
FT /evidence="ECO:0000269|PubMed:19001501"
FT MUTAGEN 1033
FT /note="S->D: Still binds to the mitotic spindle but mitotic
FT progression is impaired."
FT /evidence="ECO:0000269|PubMed:19001501"
FT CONFLICT 674..675
FT /note="EL -> RNS (in Ref. 1; CAA59449)"
FT /evidence="ECO:0000305"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5ZO7"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3ZCW"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3ZCW"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6TLE"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3ZCW"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4ZHI"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:3ZCW"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3CJO"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3L9H"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2PG2"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6TLE"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 235..248
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:2WOG"
FT STRAND 254..265
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2FME"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3HQD"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4BXN"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:6TRL"
FT HELIX 290..304
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:3ZCW"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:3ZCW"
FT HELIX 372..391
FT /evidence="ECO:0007829|PDB:5JV3"
SQ SEQUENCE 1056 AA; 119159 MW; C7F2606FE68DA8EA CRC64;
MASQPNSSAK KKEEKGKNIQ VVVRCRPFNL AERKASAHSI VECDPVRKEV SVRTGGLADK
SSRKTYTFDM VFGASTKQID VYRSVVCPIL DEVIMGYNCT IFAYGQTGTG KTFTMEGERS
PNEEYTWEED PLAGIIPRTL HQIFEKLTDN GTEFSVKVSL LEIYNEELFD LLNPSSDVSE
RLQMFDDPRN KRGVIIKGLE EITVHNKDEV YQILEKGAAK RTTAATLMNA YSSRSHSVFS
VTIHMKETTI DGEELVKIGK LNLVDLAGSE NIGRSGAVDK RAREAGNINQ SLLTLGRVIT
ALVERTPHVP YRESKLTRIL QDSLGGRTRT SIIATISPAS LNLEETLSTL EYAHRAKNIL
NKPEVNQKLT KKALIKEYTE EIERLKRDLA AAREKNGVYI SEENFRVMSG KLTVQEEQIV
ELIEKIGAVE EELNRVTELF MDNKNELDQC KSDLQNKTQE LETTQKHLQE TKLQLVKEEY
ITSALESTEE KLHDAASKLL NTVEETTKDV SGLHSKLDRK KAVDQHNAEA QDIFGKNLNS
LFNNMEELIK DGSSKQKAML EVHKTLFGNL LSSSVSALDT ITTVALGSLT SIPENVSTHV
SQIFNMILKE QSLAAESKTV LQELINVLKT DLLSSLEMIL SPTVVSILKI NSQLKHIFKT
SLTVADKIED QKKELDGFLS ILCNNLHELQ ENTICSLVES QKQCGNLTED LKTIKQTHSQ
ELCKLMNLWT ERFCALEEKC ENIQKPLSSV QENIQQKSKD IVNKMTFHSQ KFCADSDGFS
QELRNFNQEG TKLVEESVKH SDKLNGNLEK ISQETEQRCE SLNTRTVYFS EQWVSSLNER
EQELHNLLEV VSQCCEASSS DITEKSDGRK AAHEKQHNIF LDQMTIDEDK LIAQNLELNE
TIKIGLTKLN CFLEQDLKLD IPTGTTPQRK SYLYPSTLVR TEPREHLLDQ LKRKQPELLM
MLNCSENNKE ETIPDVDVEE AVLGQYTEEP LSQEPSVDAG VDCSSIGGVP FFQHKKSHGK
DKENRGINTL ERSKVEETTE HLVTKSRLPL RAQINL
