KIF2B_MOUSE
ID KIF2B_MOUSE Reviewed; 668 AA.
AC Q8C0N1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Kinesin-like protein KIF2B;
GN Name=Kif2b;
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=Testis;
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 TISSUE=Testis;
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 [4]
RP PROTEIN SEQUENCE OF 21-39, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Plus end-directed microtubule-dependent motor required for
CC spindle assembly and chromosome movement during mitosis. Has
CC microtubule depolymerization activity. Plays a role in chromosome
CC congression. {ECO:0000250|UniProtKB:Q8N4N8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q8N4N8}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8N4N8}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q8N4N8}.
CC Note=Association with kinetochore is transient.
CC {ECO:0000250|UniProtKB:Q8N4N8}.
CC -!- PTM: Phosphorylation at Thr-125 by PLK1 is required for activity in the
CC correction of kinetochore-microtubules attachment errors, while
CC phosphorylation at Ser-204 also by PLK1 is required for the kinetochore
CC localization and activity in prometaphase.
CC {ECO:0000250|UniProtKB:Q8N4N8}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AK030188; BAC26831.1; -; mRNA.
DR EMBL; AL662779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100484; AAI00485.1; -; mRNA.
DR CCDS; CCDS36281.1; -.
DR RefSeq; NP_082823.1; NM_028547.2.
DR AlphaFoldDB; Q8C0N1; -.
DR SMR; Q8C0N1; -.
DR STRING; 10090.ENSMUSP00000058084; -.
DR iPTMnet; Q8C0N1; -.
DR PhosphoSitePlus; Q8C0N1; -.
DR jPOST; Q8C0N1; -.
DR MaxQB; Q8C0N1; -.
DR PaxDb; Q8C0N1; -.
DR PRIDE; Q8C0N1; -.
DR ProteomicsDB; 269304; -.
DR Antibodypedia; 30815; 164 antibodies from 25 providers.
DR DNASU; 73470; -.
DR Ensembl; ENSMUST00000061019; ENSMUSP00000058084; ENSMUSG00000046755.
DR GeneID; 73470; -.
DR KEGG; mmu:73470; -.
DR UCSC; uc007kxf.1; mouse.
DR CTD; 84643; -.
DR MGI; MGI:1920720; Kif2b.
DR VEuPathDB; HostDB:ENSMUSG00000046755; -.
DR eggNOG; KOG0246; Eukaryota.
DR GeneTree; ENSGT00940000163180; -.
DR HOGENOM; CLU_001485_19_1_1; -.
DR InParanoid; Q8C0N1; -.
DR OMA; EMSLQRD; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q8C0N1; -.
DR TreeFam; TF105222; -.
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; 73470; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q8C0N1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C0N1; protein.
DR Bgee; ENSMUSG00000046755; Expressed in seminiferous tubule of testis and 19 other tissues.
DR ExpressionAtlas; Q8C0N1; baseline and differential.
DR Genevisible; Q8C0N1; MM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0051983; P:regulation of chromosome segregation; 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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Kinetochore; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..668
FT /note="Kinesin-like protein KIF2B"
FT /id="PRO_0000253717"
FT DOMAIN 213..543
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 585..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..177
FT /evidence="ECO:0000255"
FT COILED 646..667
FT /evidence="ECO:0000255"
FT COMPBIAS 585..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 303..310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 125
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8N4N8"
FT MOD_RES 204
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8N4N8"
SQ SEQUENCE 668 AA; 75469 MW; 30743B57668E94D4 CRC64;
MASQFCLPLA PRLSPLKPLK SHFTDFQVGI CVAIQRSDKR IHLAVVTEIN RENSWVTVEW
VEKGVKKGKK IELETVLLLN PALASLEHQR SRRPLRPVSV VPSTAIGDQR TATKWIAMIP
HRNETPSGDS QTLMIPSNPC LMKRKKSPCL REIEKLQKQR EKRRRLQLEI RARRALDINT
GNPNFETMRM IEEYRRRLDS SKMSSLEPPE DHRICVCVRK RPLNQRETTM KDLDIITIPS
HNVVMVHESK QKVDLTRYLE NQTFCFDHAF DDKASNELVY QFTARPLVES IFRKGMATCF
AYGQTGSGKT HTMGGAFLGK AQDCSKGIYA LVAQDVFLLL KTPAYEKLEL KVYGTFFEIY
GGKVYDLLNW KKKLQVLEDG NQQVQVVGLQ EQEVSCVEEV LNLVELGNSC RTSGQTSVNA
HSSRSHAVFQ LILKAGGKLH GKFSLVDLAG NERGADTAKA TRKRQLEGAE INKSLLALKE
CIRALGKNKS HTPFRASKLT QVLRDSFIGQ NSYTCMIATI SPGMTSCENT LNTLRYANRV
KELALEARPY HHCVSPPGHE VPLMIENDNT NSGKSLQRDE VIQIPTVEKE EEKESDELTS
KKEPAASWSR SNQWWEAIQE TAEGVNGDVD FCIAQSLSVL EQKIGVLTDI QKKLQSLRED
LQKKSQVE
