KI18A_MOUSE
ID KI18A_MOUSE Reviewed; 886 AA.
AC Q91WD7; Q3TP77; Q8BLL1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Kinesin-like protein KIF18A;
GN Name=Kif18a;
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=Embryo, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
CC -!- FUNCTION: Microtubule-depolymerizing kinesin which plays a role in
CC chromosome congression by reducing the amplitude of preanaphase
CC oscillations and slowing poleward movement during anaphase, thus
CC suppressing chromosome movements. May stabilize the CENPE-BUB1B complex
CC at the kinetochores during early mitosis and maintains CENPE levels at
CC kinetochores during chromosome congression (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CENPE and ESR1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AK044795; BAC32095.2; -; mRNA.
DR EMBL; AK164649; BAE37860.1; -; mRNA.
DR EMBL; BC016095; AAH16095.1; -; mRNA.
DR CCDS; CCDS16507.1; -.
DR RefSeq; NP_647464.1; NM_139303.1.
DR AlphaFoldDB; Q91WD7; -.
DR SMR; Q91WD7; -.
DR BioGRID; 230733; 11.
DR IntAct; Q91WD7; 8.
DR STRING; 10090.ENSMUSP00000028527; -.
DR iPTMnet; Q91WD7; -.
DR PhosphoSitePlus; Q91WD7; -.
DR EPD; Q91WD7; -.
DR MaxQB; Q91WD7; -.
DR PaxDb; Q91WD7; -.
DR PeptideAtlas; Q91WD7; -.
DR PRIDE; Q91WD7; -.
DR ProteomicsDB; 269215; -.
DR Antibodypedia; 25467; 149 antibodies from 26 providers.
DR DNASU; 228421; -.
DR Ensembl; ENSMUST00000028527; ENSMUSP00000028527; ENSMUSG00000027115.
DR GeneID; 228421; -.
DR KEGG; mmu:228421; -.
DR UCSC; uc008lmb.1; mouse.
DR CTD; 81930; -.
DR MGI; MGI:2446977; Kif18a.
DR VEuPathDB; HostDB:ENSMUSG00000027115; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000159058; -.
DR HOGENOM; CLU_001485_21_5_1; -.
DR InParanoid; Q91WD7; -.
DR OMA; TFIICED; -.
DR OrthoDB; 703086at2759; -.
DR PhylomeDB; Q91WD7; -.
DR TreeFam; TF105231; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 228421; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Kif18a; mouse.
DR PRO; PR:Q91WD7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91WD7; protein.
DR Bgee; ENSMUSG00000027115; Expressed in animal zygote and 170 other tissues.
DR Genevisible; Q91WD7; MM.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0005828; C:kinetochore microtubule; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0070463; F:tubulin-dependent ATPase activity; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:MGI.
DR GO; GO:0007019; P:microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 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 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Glycoprotein; Isopeptide bond; Microtubule; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..886
FT /note="Kinesin-like protein KIF18A"
FT /id="PRO_0000125459"
FT DOMAIN 11..355
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 774..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 370..404
FT /evidence="ECO:0000255"
FT COMPBIAS 776..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT CROSSLNK 683
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT CROSSLNK 782
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NI77"
FT CROSSLNK 862
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NI77"
SQ SEQUENCE 886 AA; 100935 MW; F611802A899AF0E1 CRC64;
MSGTEEDLCH RMKVVVRVRP ENTKEKAVQF CKVVHVVDKH ILSFDPKQEE ISFFHRKKTT
NFDITKRQNK DLKFVFDAVF DETSTQMEVF EHTTKPILHS FLNGYNCTVF AYGATGSGKT
HTMLGSAAEP GVMYLTMLDL FKCIDEIKEE KECSTAVSYL EVYNEQIRDL LTNSGPLAVR
EDSQKGVVVQ GLTLHQPKSS EEILQLLDNG NKNRTQHPTD VNAVSSRSHA VFQIYLRQQD
KTASINQNVR IAKMSLIDLA GSERASVSGA KGSRFVEGTN INKSLLALGN VINALANTKR
RNQHIPYRNS KLTRLLKDSL GGNCQTIMIA AVSPSSLFYD DTYNTLKYAN RAKEIKSSLK
SNVLNLNSHI SQYVKICNMQ KAEILMLKEK LKAYEEQKAL SDRNDCAKLV HSNPEDRETE
RFQEILNCLF QNREGIRQEY LKLEMLLKAN ALKSSYHQQC HKQIEMMCSE DKVEKATCKR
DHRLEKLKTN SCFLEKKKEE VSKQFDENTN WLHRVENEMR LLGQNGDIPE ALNKELHCHH
LHLQNKELKT QMAHMTALAC LQEQQHKQTE AVLNALLPVL RKQYWKLKET GLSNAAFDSD
FKDIEHLVER KKVVAWADQT NEHSNRNDLP GISLLMTFPQ LEPIQSISCC TSVSDPNVLK
LTPQRRTRRK IIPSPLKVQH TQKSALSEST QLNDSFSKEL QPIVYTPEDC KKAQDLFPSL
TRTSSQSANV MNDNSQKALC RIESPLSRTE CKQGLYSTST LCDSIRGLKN KWPEQEPLAS
SKSSVHRIES SSFSTKDSMP ESAGVPSYMA MTTAAKRKWK QMSSTSNASI KSDESCGFAK
RIRRDNSSVK PMQENRLKVG YKRNTNKTNS NMLRKFRRNT SKENVQ
