KI20B_MOUSE
ID KI20B_MOUSE Reviewed; 1774 AA.
AC Q80WE4; E9QPW5; Q3V347; Q80VC0; Q8BLI2; Q99PT5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Kinesin-like protein KIF20B {ECO:0000305};
DE AltName: Full=Kinesin family member 20B {ECO:0000312|MGI:MGI:2444576};
DE AltName: Full=Kinesin-related motor interacting with PIN1 {ECO:0000250|UniProtKB:Q96Q89};
DE AltName: Full=M-phase phosphoprotein 1 {ECO:0000250|UniProtKB:Q96Q89};
DE Short=MPP1 {ECO:0000250|UniProtKB:Q96Q89};
GN Name=Kif20b {ECO:0000312|MGI:MGI:2444576};
GN Synonyms=Mphosph1 {ECO:0000250|UniProtKB:Q96Q89};
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 [MRNA] (ISOFORM 2).
RA Shan Y.X., Yu L.;
RT "Cloning and characterization of a novel mouse M-phase phosphoprotein
RT gene.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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] OF 1-781 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-732 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-384 (ISOFORM 4).
RX PubMed=11416179; DOI=10.1073/pnas.111145398;
RA Miki H., Setou M., Kaneshiro K.;
RT "All kinesin superfamily protein, KIF, genes in mouse and human.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7004-7011(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1232-1774.
RC STRAIN=FVB/N-3; 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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-950, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1694, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=24173802; DOI=10.1242/dev.093286;
RA Janisch K.M., Vock V.M., Fleming M.S., Shrestha A., Grimsley-Myers C.M.,
RA Rasoul B.A., Neale S.A., Cupp T.D., Kinchen J.M., Liem K.F. Jr.,
RA Dwyer N.D.;
RT "The vertebrate-specific Kinesin-6, Kif20b, is required for normal
RT cytokinesis of polarized cortical stem cells and cerebral cortex size.";
RL Development 140:4672-4682(2013).
RN [10]
RP FUNCTION, INTERACTION WITH SHTN1, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF TYR-1047 AND ARG-1048.
RX PubMed=23864681; DOI=10.1523/jneurosci.5425-12.2013;
RA Sapir T., Levy T., Sakakibara A., Rabinkov A., Miyata T., Reiner O.;
RT "Shootin1 acts in concert with KIF20B to promote polarization of migrating
RT neurons.";
RL J. Neurosci. 33:11932-11948(2013).
CC -!- FUNCTION: Plus-end-directed motor enzyme that is required for
CC completion of cytokinesis (By similarity). Required for proper midbody
CC organization and abscission in polarized cortical stem cells
CC (PubMed:24173802). Plays a role in the regulation of neuronal
CC polarization by mediating the transport of specific cargos.
CC Participates in the mobilization of SHTN1 and in the accumulation of
CC PIP3 in the growth cone of primary hippocampal neurons in a tubulin and
CC actin-dependent manner (PubMed:23864681). In the developing
CC telencephalon, cooperates with SHTN1 to promote both the transition
CC from the multipolar to the bipolar stage and the radial migration of
CC cortical neurons from the ventricular zone toward the superficial layer
CC of the neocortex (PubMed:23864681). Involved in cerebral cortex growth
CC (PubMed:24173802). Acts as an oncogene for promoting bladder cancer
CC cells proliferation, apoptosis inhibition and carcinogenic progression
CC (By similarity). {ECO:0000250|UniProtKB:Q96Q89,
CC ECO:0000269|PubMed:23864681, ECO:0000269|PubMed:24173802}.
CC -!- SUBUNIT: Oligomerizes (via kinesin motor domain). Associates with
CC microtubules. Interacts (via C-terminal globular tail region) with PIN1
CC (via WW domain). Interacts with PRC1 (By similarity). Interacts with
CC SHTN1 (via N-terminus); the interaction is direct and promotes the
CC association of SHTN1 to microtubules in primary neurons
CC (PubMed:23864681). Associates with microtubules (PubMed:23864681).
CC {ECO:0000250|UniProtKB:Q96Q89, ECO:0000269|PubMed:23864681}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24173802}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:23864681}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q96Q89}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q96Q89}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q96Q89}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:24173802}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q96Q89}. Midbody {ECO:0000269|PubMed:23864681,
CC ECO:0000269|PubMed:24173802}. Cell projection, axon
CC {ECO:0000269|PubMed:23864681}. Cell projection, growth cone
CC {ECO:0000269|PubMed:23864681}. Note=Localizes mainly in the nucleus
CC during interphase although it is also detected in the cytoplasm without
CC clear association with microtubules (By similarity). Localized to the
CC central spindle during cytokinetic furrowing and with the midbody
CC during abscission (PubMed:24173802). A 2-3 fold expression increase is
CC seen as cells progress from G1 to G2/M phase. During prophase and
CC metaphase it is found throughout the cytoplasm and at anaphase
CC accumulates at the midplan of the cell and forms a distinct band
CC extending across the spindle midzone. At anaphase it is concentrated in
CC the midbody (By similarity). Colocalized partially along microtubules
CC in primary neurons (PubMed:23864681). Colocalized with SHTN1 along
CC microtubules to the tip of the growing cone in primary hippocampal
CC neurons (PubMed:23864681). Localized in midbodies between dividing
CC radial progenitors in the ventricular zone (PubMed:23864681).
CC Colocalized with PRC1 in the nucleus of bladder carcinoma cells at the
CC interphase. Colocalized with PRC1 in bladder carcinoma cells at
CC prophase, metaphase, early anaphase, at the midzone in late anaphase
CC and at the contractile ring in telophase (By similarity).
CC {ECO:0000250|UniProtKB:Q96Q89, ECO:0000269|PubMed:23864681,
CC ECO:0000269|PubMed:24173802}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80WE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WE4-2; Sequence=VSP_022623, VSP_022626;
CC Name=3;
CC IsoId=Q80WE4-3; Sequence=VSP_022626;
CC Name=4;
CC IsoId=Q80WE4-4; Sequence=VSP_022624, VSP_022625;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:24173802). {ECO:0000269|PubMed:24173802}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing brain
CC (PubMed:23864681). Expressed in the apical aspect of the ventricular
CC zone, in the marginal zone, in a narrow stripe between the intermediate
CC zone and the cortical plate at 14.5 dpc (PubMed:23864681). Expressed in
CC multipolar cells at 14 dpc (at protein level) (PubMed:23864681).
CC Expressed in neuronal stem/progenitor cells at 14.5 dpc
CC (PubMed:24173802). {ECO:0000269|PubMed:23864681,
CC ECO:0000269|PubMed:24173802}.
CC -!- PTM: Phosphorylated during mitosis by CDK1.
CC {ECO:0000250|UniProtKB:Q96Q89}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48954.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP14646.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY259532; AAP14646.1; ALT_FRAME; mRNA.
DR EMBL; AC113244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK045067; BAC32207.1; -; mRNA.
DR EMBL; AK049225; BAE43340.1; -; mRNA.
DR EMBL; AB054030; BAB32494.1; -; Genomic_DNA.
DR EMBL; BC048954; AAH48954.1; ALT_FRAME; mRNA.
DR CCDS; CCDS37967.1; -. [Q80WE4-1]
DR CCDS; CCDS89382.1; -. [Q80WE4-3]
DR RefSeq; NP_898867.1; NM_183046.1. [Q80WE4-1]
DR RefSeq; XP_006527143.1; XM_006527080.2. [Q80WE4-1]
DR RefSeq; XP_006527144.1; XM_006527081.2. [Q80WE4-1]
DR RefSeq; XP_006527149.1; XM_006527086.2. [Q80WE4-2]
DR AlphaFoldDB; Q80WE4; -.
DR SMR; Q80WE4; -.
DR BioGRID; 232217; 30.
DR IntAct; Q80WE4; 14.
DR STRING; 10090.ENSMUSP00000084599; -.
DR iPTMnet; Q80WE4; -.
DR PhosphoSitePlus; Q80WE4; -.
DR EPD; Q80WE4; -.
DR jPOST; Q80WE4; -.
DR MaxQB; Q80WE4; -.
DR PaxDb; Q80WE4; -.
DR PeptideAtlas; Q80WE4; -.
DR PRIDE; Q80WE4; -.
DR ProteomicsDB; 263438; -. [Q80WE4-1]
DR ProteomicsDB; 263439; -. [Q80WE4-2]
DR ProteomicsDB; 263440; -. [Q80WE4-3]
DR ProteomicsDB; 263441; -. [Q80WE4-4]
DR Antibodypedia; 30294; 98 antibodies from 20 providers.
DR DNASU; 240641; -.
DR Ensembl; ENSMUST00000087341; ENSMUSP00000084599; ENSMUSG00000024795. [Q80WE4-1]
DR Ensembl; ENSMUST00000223907; ENSMUSP00000153034; ENSMUSG00000024795. [Q80WE4-3]
DR GeneID; 240641; -.
DR KEGG; mmu:240641; -.
DR UCSC; uc008hgz.1; mouse. [Q80WE4-1]
DR UCSC; uc008hha.1; mouse. [Q80WE4-2]
DR CTD; 9585; -.
DR MGI; MGI:2444576; Kif20b.
DR VEuPathDB; HostDB:ENSMUSG00000024795; -.
DR eggNOG; KOG0247; Eukaryota.
DR GeneTree; ENSGT00940000155989; -.
DR HOGENOM; CLU_002380_0_0_1; -.
DR InParanoid; Q80WE4; -.
DR OMA; DQHHNRL; -.
DR OrthoDB; 314538at2759; -.
DR PhylomeDB; Q80WE4; -.
DR TreeFam; TF105232; -.
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; 240641; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Kif20b; mouse.
DR PRO; PR:Q80WE4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q80WE4; protein.
DR Bgee; ENSMUSG00000024795; Expressed in undifferentiated genital tubercle and 148 other tissues.
DR ExpressionAtlas; Q80WE4; baseline and differential.
DR Genevisible; Q80WE4; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0070938; C:contractile ring; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0050699; F:WW domain binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; IMP:UniProtKB.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0035372; P:protein localization to microtubule; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IDA:MGI.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:InterPro.
DR GO; GO:2001222; P:regulation of neuron migration; IGI:MGI.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR028828; KIF20B.
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 PANTHER; PTHR24115:SF534; PTHR24115:SF534; 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 Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Mitosis; Motor protein; Nucleotide-binding; Nucleus; Oncogene;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1774
FT /note="Kinesin-like protein KIF20B"
FT /id="PRO_0000274054"
FT DOMAIN 58..477
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 538..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1059
FT /note="Necessary and sufficient for interaction with SHTN1"
FT /evidence="ECO:0000269|PubMed:23864681"
FT REGION 1514..1774
FT /note="Interaction with PIN1"
FT /evidence="ECO:0000250|UniProtKB:Q96Q89"
FT REGION 1625..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 525..601
FT /evidence="ECO:0000255"
FT COILED 705..747
FT /evidence="ECO:0000255"
FT COILED 824..946
FT /evidence="ECO:0000255"
FT COILED 1021..1507
FT /evidence="ECO:0000255"
FT COMPBIAS 740..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q89"
FT MOD_RES 950
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q89"
FT MOD_RES 1598
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q96Q89"
FT MOD_RES 1612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q89"
FT MOD_RES 1669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q89"
FT MOD_RES 1694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..386
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022623"
FT VAR_SEQ 227..237
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_022624"
FT VAR_SEQ 375
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_022625"
FT VAR_SEQ 666..705
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_022626"
FT MUTAGEN 1047
FT /note="Y->F: Reduces interaction with SHTN1; when
FT associated with A-1048."
FT /evidence="ECO:0000269|PubMed:23864681"
FT MUTAGEN 1048
FT /note="R->A: Reduces interaction with SHTN1; when
FT associated with F-1047."
FT /evidence="ECO:0000269|PubMed:23864681"
FT CONFLICT 675
FT /note="D -> E (in Ref. 3; BAE43340)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="S -> P (in Ref. 3; BAE43340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1774 AA; 203514 MW; 3EBB3D6553E79DA1 CRC64;
MESHLNPDGV PRPSYVFSAD PIARPLEINF DGVKLDLSHE FSLVASNPAA NSLGSKNYLQ
VCLRIRPFTQ SEKEHEAEGC VQVLDSQSVL LKDPQSILGH LSEKSSGQVA QKFSFSKVFG
PETSQKEFFL GCIMQPVKDL LEGHSRLIFT YGLTNSGKTY TFQGTEENIG ILPRTLNVLF
DSLQERLYTK MSFKPHRCRE YLKLSSDQEK EESANKNTLL RQIKEVTIHN DSYDVLCGHL
TNSLTIPEFE ESVNSCDQSS LNVDNIKYSV WVSFFEIYNE SIYDLFVPVS SKFQKRKMLR
LSQDIKGYSF IKDLQWVQVS DSKEAYRLLK LGVKHQSVAF TKLNNASSRS HSIFTIRILQ
IEDSEIPRVT RVSELSLCDL AGSERSMKTQ NEGERLREAG NINTSLLTLG KCINVLKNSE
KSKVQHVPFR ESKLTHYFQS FFTGKGKICM IINISQSCSA YDETLNVLKF STTAQRVYVP
DTLSSSQEKS FASNKSLQDV SLDSNLDNKI LNVKRKTVSW ENSLEDVLEN EDLVEDLEEN
EETQNMETEL TDEDSDKSLE ECRVSTCHKK NKELLDLIEK LNKRLINENK EKLTLELKIR
EEVTQEFTQY WSQREADFKE TLLHEREILE ENAERRLAIF KDLVGKCDSQ DEPTNRICDI
ELETEEAHNY VGVEDIFHSL QDDVTDIKKQ AELAHLYITS LVDPQEAIAC LQLKFNQVKA
ELAETKEELI KAQEELKNRE SNSLVQALKT SSKVDTSLTS NKSTCNETSE MPKNSRAQTH
SERKRLNEDG LQLGEPPAKK GLILVSPPIT EEQNKMGEMQ QSVSEVVEGN RVLKEKNEEL
KRLLTIGENE LRNEKEEKAE LNKQVVSLQQ QLRFFEEKNS SLRADVEQIQ ASYNSAVAEL
QTQKAVNQEQ RDRILKLSQE METAARSIES NVSQIKQMQT KIDELRSLDS PSHISKIDLL
NLQDLSSGAK GDNCLNTSQQ LPGGDFSSTW VKEYHTQEIS RENSFHASIE AIWEECKEIV
KASSKKSHQI QGLEEQIEKL QVEVKGYREE NSDLRAQESQ GKNRDHQLKE KESLIQQLRE
ELQEKSVSLR VQVQLVAERE QALSELSQDV TCYKAKIKDL EVIVETQKDE CKRLVELEQS
ILEKESAILK LEANLKECEA KHQDHIRTND LSAKEVKFRE EVTRLANNLH DTKQLLQSKE
EENEISRQET EKLKEELAAN SILTQNLKAD LQKKEEDCAE LKEKFIDAKK QIEQVQREVS
VMRDEEKLLR IKINELEKKK NQYSQDLDMK QRTIQQLKEQ LSNQKMEEAV QQYEKVCKDL
SVKEKLVEDM RLTLVEQEQT QAEQDRVLEA KSEEADWLAT ELDKWKEKFK DLETRSNQRL
NTGTMDDLDV LTRKFSKLQD ELQESEEKYK ADRKKWLEEK AVLTTQAKEA ENVRNREMRK
YADDRERCLK LQNEVETLTA QLAEKNSELQ KWREERDQLV TAVETQMKAL LSSCKHKDEE
IQELRKAAAK STGTENQTMN PKPEYNDSVD LGGVETEPQS TSLEISRNTA EDGSVVLDSC
EVSTENVQST RFPKPELEIQ FTPLQPNKMA VKHPGCPTPV TIKIPKARKR KSGEVEEDLV
KCENKKNSTP RSNVKFPVSE HRNSPVKKEQ KVSVGPSSKK TYSLRSQAST VSANIASKKR
EGTLQKFGDF LQHSPTILQS KAKKIIETMS SPKLSTVEVS KENVSQPKKA KRKLYRNEIS
SPINISGQVI LMEQKVKETD HQILKRRLRT RTAK
