KI18B_MOUSE
ID KI18B_MOUSE Reviewed; 834 AA.
AC Q6PFD6; Q3U0T0; Q80V20;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Kinesin-like protein KIF18B;
GN Name=Kif18b;
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=NOD; TISSUE=Spleen;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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: In complex with KIF2C, constitutes the major microtubule
CC plus-end depolymerizing activity in mitotic cells. Its major role may
CC be to transport KIF2C and/or MAPRE1 along microtubules (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAPRE1; this interaction is required for
CC efficient accumulation at microtubule plus ends. Interacts with KIF2C
CC at microtubule tips; this interaction increases the affinity of both
CC partners for microtubule plus ends and is required for robust
CC microtubule depolymerization. KIF2C phosphorylation by AURKA or AURKB
CC strongly reduces KIF18B-binding. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000305}. Note=Present predominantly in
CC the nucleus and to a lesser extent in the cytoplasm of interphase
CC cells. During mitosis, found to be closely associated with astral
CC microtubule plus ends emanating from the spindle pole during
CC prometaphase and metaphase (By similarity). {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; AK156592; BAE33771.1; -; mRNA.
DR EMBL; AL731670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049272; AAH49272.1; -; mRNA.
DR EMBL; BC057614; AAH57614.1; -; mRNA.
DR CCDS; CCDS25508.1; -.
DR RefSeq; NP_932063.2; NM_197959.2.
DR RefSeq; XP_011247545.1; XM_011249243.1.
DR AlphaFoldDB; Q6PFD6; -.
DR SMR; Q6PFD6; -.
DR BioGRID; 213921; 9.
DR IntAct; Q6PFD6; 7.
DR STRING; 10090.ENSMUSP00000021311; -.
DR iPTMnet; Q6PFD6; -.
DR PhosphoSitePlus; Q6PFD6; -.
DR SwissPalm; Q6PFD6; -.
DR EPD; Q6PFD6; -.
DR jPOST; Q6PFD6; -.
DR MaxQB; Q6PFD6; -.
DR PaxDb; Q6PFD6; -.
DR PeptideAtlas; Q6PFD6; -.
DR PRIDE; Q6PFD6; -.
DR ProteomicsDB; 269216; -.
DR Antibodypedia; 8290; 25 antibodies from 10 providers.
DR DNASU; 70218; -.
DR Ensembl; ENSMUST00000021311; ENSMUSP00000021311; ENSMUSG00000051378.
DR GeneID; 70218; -.
DR KEGG; mmu:70218; -.
DR UCSC; uc007lsy.2; mouse.
DR CTD; 146909; -.
DR MGI; MGI:2446979; Kif18b.
DR VEuPathDB; HostDB:ENSMUSG00000051378; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000161200; -.
DR HOGENOM; CLU_001485_21_5_1; -.
DR InParanoid; Q6PFD6; -.
DR OMA; HQEEKRF; -.
DR OrthoDB; 703086at2759; -.
DR PhylomeDB; Q6PFD6; -.
DR TreeFam; TF105231; -.
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; 70218; 23 hits in 73 CRISPR screens.
DR ChiTaRS; Kif18b; mouse.
DR PRO; PR:Q6PFD6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PFD6; protein.
DR Bgee; ENSMUSG00000051378; Expressed in cleaving embryo and 127 other tissues.
DR Genevisible; Q6PFD6; MM.
DR GO; GO:0000235; C:astral microtubule; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:1990752; C:microtubule end; ISO:MGI.
DR GO; GO:0035371; C:microtubule plus-end; ISO:MGI.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; 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:0003774; F:cytoskeletal motor activity; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007019; P:microtubule depolymerization; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
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 cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..834
FT /note="Kinesin-like protein KIF18B"
FT /id="PRO_0000318970"
FT DOMAIN 9..353
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 400..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..404
FT /evidence="ECO:0000255"
FT MOTIF 619..627
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 400..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 669
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y91"
FT CONFLICT 211
FT /note="S -> I (in Ref. 3; AAH57614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 91936 MW; 3043F4339E0B82AD CRC64;
MVMAVEDSVV RVVVRVRPPT PKELESQRRP VIQVVDERML VFDPEECDGG FPGLKWSGSH
NGPKKKGKDL TFVFDRVFGE MATQEDVFQH TTHNILDSFL QGYNCSVFAY GATGAGKTHT
MLGREGEPGI MYLTTMELYR RLEARQEEKQ FEVLISYLEV YNEQIHDLLE PKGPLTIRED
PDKGVVVPGL SFHQPASAEQ LLEMLTRGNC SRTQHPTDAN ATSSRSHAIF QIFVKQQDRV
PGLTQALRVA KMSLIDLAGS ERASSTHAKG ERLREGANIN RSLLALINVL NALADAKGRK
SHVPYRDSKL TRLLKDSIGG NCRTVMIAAI SPSSLTYEDT YNTLKYADRA KEIRLTLKSN
VISVDHHISQ YATICQQLQA EVAFLREKLQ MYEAGAQALQ QQCSPQPPTL SIPQSLSSSS
LQPGPSSQSS TLECHAKNET LQEESLGSDA QGQEIVEESA SEQEQCPQDK QCPTQKPEPN
LPGSPSPSVQ AKPGTGQHSP QKQDADHSKQ LALQVLRLAQ RQYSLLQAAN LLTPDMISEF
ETLQQLVLEE SVDHRAESPR SPALARGDPL AQALCSESKS SGYCGPVTRT MAKQLNGLTH
TLGAPLAPDC TSDKTFQKPT KEKKRKLTPE EPGSLPAPNL EMKRQRQSFL PCLRRGSLPK
AQPCSEPRTP KRERASSPSP SSRVCPATVI KSRVPLGPSA LQNCSTPLAL PTRDLNTTFN
VSEESPSKPS FQEFVDWEKV SPELNSTDQP FLPSAPVFIF TKGRKPSLPA VTASKKRRTM
RPSVSRGRSC IARLHSSTLK KPNRPFTVPE PPLSPHCLDD QRTPKGLTGV TESY
