KIF11_MOUSE
ID KIF11_MOUSE Reviewed; 1052 AA.
AC Q6P9P6; Q9Z1J0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Kinesin-like protein KIF11;
DE AltName: Full=Kinesin-related motor protein Eg5;
GN Name=Kif11;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-1052.
RX PubMed=10659681; DOI=10.1023/a:1006949006728;
RA Ferhat L., Cook C., Kuriyama R., Baas P.W.;
RT "The nuclear/mitotic apparatus protein NuMA is a component of the
RT somatodendritic microtubule arrays of the neuron.";
RL J. Neurocytol. 27:887-899(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Motor protein required for establishing a bipolar spindle
CC during mitosis. Required in non-mitotic cells for transport of
CC secretory proteins from the Golgi complex to the cell surface.
CC {ECO:0000250|UniProtKB:P52732}.
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 with
CC RARRES1 and AGBL2 (By similarity). {ECO:0000250|UniProtKB:P52732}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52732}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P52732}.
CC -!- PTM: Phosphorylated exclusively on serine during S phase, but on both
CC serine and Thr-925 during mitosis, so controlling the association of
CC KIF11 with the spindle apparatus (probably during early prophase).
CC {ECO:0000250|UniProtKB:P52732}.
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; BC060670; AAH60670.1; -; mRNA.
DR EMBL; AJ223293; CAA11228.1; -; mRNA.
DR CCDS; CCDS29777.1; -.
DR RefSeq; NP_034745.1; NM_010615.1.
DR AlphaFoldDB; Q6P9P6; -.
DR SMR; Q6P9P6; -.
DR BioGRID; 200928; 9.
DR DIP; DIP-62086N; -.
DR IntAct; Q6P9P6; 2.
DR STRING; 10090.ENSMUSP00000012587; -.
DR iPTMnet; Q6P9P6; -.
DR PhosphoSitePlus; Q6P9P6; -.
DR EPD; Q6P9P6; -.
DR jPOST; Q6P9P6; -.
DR MaxQB; Q6P9P6; -.
DR PaxDb; Q6P9P6; -.
DR PeptideAtlas; Q6P9P6; -.
DR PRIDE; Q6P9P6; -.
DR ProteomicsDB; 263528; -.
DR Antibodypedia; 1871; 449 antibodies from 39 providers.
DR DNASU; 16551; -.
DR Ensembl; ENSMUST00000012587; ENSMUSP00000012587; ENSMUSG00000012443.
DR GeneID; 16551; -.
DR KEGG; mmu:16551; -.
DR UCSC; uc008hin.1; mouse.
DR CTD; 3832; -.
DR MGI; MGI:1098231; Kif11.
DR VEuPathDB; HostDB:ENSMUSG00000012443; -.
DR eggNOG; KOG0243; Eukaryota.
DR GeneTree; ENSGT00940000155921; -.
DR HOGENOM; CLU_001485_33_4_1; -.
DR InParanoid; Q6P9P6; -.
DR OMA; INLWAER; -.
DR OrthoDB; 179272at2759; -.
DR PhylomeDB; Q6P9P6; -.
DR TreeFam; TF105230; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16551; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Kif11; mouse.
DR PRO; PR:Q6P9P6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6P9P6; protein.
DR Bgee; ENSMUSG00000012443; Expressed in embryonic post-anal tail and 121 other tissues.
DR Genevisible; Q6P9P6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007100; P:mitotic centrosome separation; IMP:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0046602; P:regulation of mitotic centrosome separation; ISS:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:MGI.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR GO; GO:0007051; P:spindle organization; ISO:MGI.
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 Acetylation; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Isopeptide bond; Microtubule; Mitosis;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1052
FT /note="Kinesin-like protein KIF11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253343"
FT DOMAIN 17..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 950..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 364..478
FT /evidence="ECO:0000255"
FT COILED 963..988
FT /evidence="ECO:0000255"
FT COMPBIAS 985..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52732"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52732"
FT MOD_RES 925
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52732"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52732"
FT CONFLICT 152
FT /note="E -> D (in Ref. 2; CAA11228)"
FT /evidence="ECO:0000305"
FT CONFLICT 246..247
FT /note="ET -> Q (in Ref. 2; CAA11228)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="S -> C (in Ref. 2; CAA11228)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="L -> R (in Ref. 2; CAA11228)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="A -> R (in Ref. 2; CAA11228)"
FT /evidence="ECO:0000305"
FT CONFLICT 994
FT /note="H -> L (in Ref. 2; CAA11228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1052 AA; 118027 MW; 2AE184121D8DCE5B CRC64;
MASQPSSLKK KEEKGRNIQV VVRCRPFNLA ERKANAHSVV ECDHARKEVS VRTAGLTDKT
SKKTYTFDMV FGASTKQIDV YRSVVCPILD EVIMGYNCTI FAYGQTGTGK TFTMEGERSP
NEVYTWEEDP LAGIIPRTLH QIFEKLTDNG TEFSVKVSLL EIYNEELFDL LSPSSDVSER
LQMFDDPRNK RGVIIKGLEE ITVHNKDEVY QILEKGAAKR TTAATLMNAY SSRSHSVFSV
TIHMKETTID GEELVKIGKL NLVDLAGSEN IGRSGAVDKR AREAGNINQS LLTLGRVITA
LVERTPHIPY RESKLTRILQ DSLGGRTRTS IIATISPASF NLEETLSTLE YAHRAKNIMN
KPEVNQKLTK KALIKEYTEE IERLKRDLAA AREKNGVYIS EESFRAMNGK VTVQEEQIVE
LVEKIAVLEE ELSKATELFM DSKNELDQCK SDLQTKTQEL ETTQKHLQET KLQLVKEEYV
SSALERTEKT LHDTASKLLN TVKETTRAVS GLHSKLDRKR AIDEHNAEAQ ESFGKNLNSL
FNNMEELIKD GSAKQKAMLD VHKTLFGNLM SSSVSALDTI TTTALESLVS IPENVSARVS
QISDMILEEQ SLAAQSKSVL QGLIDELVTD LFTSLKTIVA PSVVSILNIN KQLQHIFRAS
STVAEKVEDQ KREIDSFLSI LCNNLHELRE NTVSSLVESQ KLCGDLTEDL KTIKETHSQE
LCQLSSSWAE RFCALEKKYE NIQKPLNSIQ ENTELRSTDI INKTTVHSKK ILAESDGLLQ
ELRHFNQEGT QLVEESVGHC SSLNSNLETV SQEITQKCGT LNTSTVHFSD QWASCLSKRK
EELENLMEFV NGCCKASSSE ITKKVREQSA AVANQHSSFV AQMTSDEESC KAGSLELDKT
IKTGLTKLNC FLKQDLKLDI PTGMTPERKK YLYPTTLVRT EPREQLLDQL QKKQPPMMLN
SSEASKETSQ DMDEEREALE QCTEELVSPE TTEHPSADCS SSRGLPFFQR KKPHGKDKEN
RGLNPVEKYK VEEASDLSIS KSRLPLHTSI NL
