KI18B_HUMAN
ID KI18B_HUMAN Reviewed; 852 AA.
AC Q86Y91; A0A0C4DGP2; A0A0C4DGP5; A6NJI2; B7ZM49; B9EGM8; D5L6I1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Kinesin-like protein KIF18B;
GN Name=KIF18B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20600703; DOI=10.1016/j.gene.2010.06.007;
RA Lee Y.M., Kim E., Park M., Moon E., Ahn S.M., Kim W., Hwang K.B., Kim Y.K.,
RA Choi W., Kim W.;
RT "Cell cycle-regulated expression and subcellular localization of a kinesin-
RT 8 member human KIF18B.";
RL Gene 466:16-25(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; THR-417; SER-452;
RP SER-480; SER-633; SER-639; SER-662 AND SER-822, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND SER-662, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP FUNCTION, INTERACTION WITH MAPRE1 AND KIF2C, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=21820309; DOI=10.1016/j.cub.2011.07.017;
RA Tanenbaum M.E., Macurek L., van der Vaart B., Galli M., Akhmanova A.,
RA Medema R.H.;
RT "A complex of Kif18b and MCAK promotes microtubule depolymerization and is
RT negatively regulated by Aurora kinases.";
RL Curr. Biol. 21:1356-1365(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-558; SER-633;
RP SER-662 AND THR-674, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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.
CC {ECO:0000269|PubMed:20600703, ECO:0000269|PubMed:21820309}.
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:0000269|PubMed:21820309}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton.
CC Note=Present predominantly in the nucleus and to a lesser extent in the
CC cytoplasm of interphase cells. During mitosis, found to be closely
CC associated with astral microtubule plus ends emanating from the spindle
CC pole during prometaphase and metaphase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86Y91-5; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86Y91-6; Sequence=VSP_060111, VSP_060112, VSP_060113;
CC -!- TISSUE SPECIFICITY: Shows a prominent expression in the amygdala.
CC {ECO:0000269|PubMed:20600703}.
CC -!- DEVELOPMENTAL STAGE: Regulated in a cell cycle-dependent manner. Not
CC expressed in the G1 phase. In G2, sequestered in the nucleus. Maximal
CC levels seen at late G2/M phase and early prometaphase. Degraded at the
CC metaphase-anaphase transition (at protein level).
CC {ECO:0000269|PubMed:20600703, ECO:0000269|PubMed:21820309}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADE43428.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; GU808359; ADE43428.1; ALT_SEQ; mRNA.
DR EMBL; AC015936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044933; AAH44933.1; -; mRNA.
DR EMBL; BC136590; AAI36591.1; -; mRNA.
DR EMBL; BC144271; AAI44272.1; -; mRNA.
DR CCDS; CCDS45709.2; -. [Q86Y91-5]
DR CCDS; CCDS58555.1; -. [Q86Y91-6]
DR RefSeq; NP_001251503.1; NM_001264573.1. [Q86Y91-6]
DR RefSeq; NP_001252506.1; NM_001265577.1. [Q86Y91-5]
DR AlphaFoldDB; Q86Y91; -.
DR SMR; Q86Y91; -.
DR BioGRID; 127024; 57.
DR IntAct; Q86Y91; 19.
DR MINT; Q86Y91; -.
DR STRING; 9606.ENSP00000465992; -.
DR GlyGen; Q86Y91; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86Y91; -.
DR PhosphoSitePlus; Q86Y91; -.
DR BioMuta; KIF18B; -.
DR DMDM; 325511395; -.
DR EPD; Q86Y91; -.
DR jPOST; Q86Y91; -.
DR MassIVE; Q86Y91; -.
DR MaxQB; Q86Y91; -.
DR PaxDb; Q86Y91; -.
DR PeptideAtlas; Q86Y91; -.
DR PRIDE; Q86Y91; -.
DR Antibodypedia; 8290; 25 antibodies from 10 providers.
DR DNASU; 146909; -.
DR Ensembl; ENST00000587309.5; ENSP00000465377.1; ENSG00000186185.14. [Q86Y91-6]
DR Ensembl; ENST00000593135.6; ENSP00000465992.1; ENSG00000186185.14. [Q86Y91-5]
DR GeneID; 146909; -.
DR KEGG; hsa:146909; -.
DR MANE-Select; ENST00000593135.6; ENSP00000465992.1; NM_001265577.2; NP_001252506.1.
DR UCSC; uc010wjh.4; human. [Q86Y91-5]
DR CTD; 146909; -.
DR DisGeNET; 146909; -.
DR GeneCards; KIF18B; -.
DR HGNC; HGNC:27102; KIF18B.
DR HPA; ENSG00000186185; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 614570; gene.
DR neXtProt; NX_Q86Y91; -.
DR OpenTargets; ENSG00000186185; -.
DR VEuPathDB; HostDB:ENSG00000186185; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000161200; -.
DR HOGENOM; CLU_001485_21_5_1; -.
DR InParanoid; Q86Y91; -.
DR OMA; HQEEKRF; -.
DR OrthoDB; 703086at2759; -.
DR PhylomeDB; Q86Y91; -.
DR PathwayCommons; Q86Y91; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q86Y91; -.
DR BioGRID-ORCS; 146909; 183 hits in 1084 CRISPR screens.
DR ChiTaRS; KIF18B; human.
DR GenomeRNAi; 146909; -.
DR Pharos; Q86Y91; Tbio.
DR PRO; PR:Q86Y91; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q86Y91; protein.
DR Bgee; ENSG00000186185; Expressed in trabecular bone tissue and 128 other tissues.
DR ExpressionAtlas; Q86Y91; baseline and differential.
DR GO; GO:0000235; C:astral microtubule; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; IDA:HPA.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
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; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0051302; P:regulation of cell division; IDA: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 Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..852
FT /note="Kinesin-like protein KIF18B"
FT /id="PRO_0000318969"
FT DOMAIN 7..351
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 390..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..736
FT /note="KIF2C-binding"
FT REGION 767..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 366..393
FT /evidence="ECO:0000255"
FT MOTIF 624..632
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT MOTIF 653..656
FT /note="MAPRE1-binding"
FT MOTIF 774..777
FT /note="MAPRE1-binding"
FT MOTIF 800..803
FT /note="MAPRE1-binding"
FT COMPBIAS 398..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 674
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 413
FT /note="H -> HLPSSPLPPHPPS (in isoform 2)"
FT /id="VSP_060111"
FT VAR_SEQ 818..821
FT /note="ELPL -> GDWH (in isoform 2)"
FT /id="VSP_060112"
FT VAR_SEQ 822..852
FT /note="Missing (in isoform 2)"
FT /id="VSP_060113"
FT VARIANT 506
FT /note="Q -> R (in dbSNP:rs17546822)"
FT /id="VAR_038925"
SQ SEQUENCE 852 AA; 93011 MW; 82E15D4D75EA1F52 CRC64;
MAVEDSTLQV VVRVRPPTPR ELDSQRRPVV QVVDERVLVF NPEEPDGGFP GLKWGGTHDG
PKKKGKDLTF VFDRVFGEAA TQQDVFQHTT HSVLDSFLQG YNCSVFAYGA TGAGKTHTML
GREGDPGIMY LTTVELYRRL EARQQEKHFE VLISYQEVYN EQIHDLLEPK GPLAIREDPD
KGVVVQGLSF HQPASAEQLL EILTRGNRNR TQHPTDANAT SSRSHAIFQI FVKQQDRVPG
LTQAVQVAKM SLIDLAGSER ASSTHAKGER LREGANINRS LLALINVLNA LADAKGRKTH
VPYRDSKLTR LLKDSLGGNC RTVMIAAISP SSLTYEDTYN TLKYADRAKE IRLSLKSNVT
SLDCHISQYA TICQQLQAEV AALRKKLQVY EGGGQPPPQD LPGSPKSGPP PEHQPCTPEL
PAGPRALQEE SLGMEAQVER AMEGNSSDQE QSPEDEDEGP AEEVPTQMPE QNPTHALPES
PRLTLQPKPV VGHFSARELD GDRSKQLALK VLCVAQRQYS LLQAANLLTP DMITEFETLQ
QLVQEEKIEP GAEALRTSGL ARGAPLAQEL CSESIPVPSP LCPEPPGYTG PVTRTMARRL
SGPLHTLGIP PGPNCTPAQG SRWPMEKKRR RPSALEADSP MAPKRGTKRQ RQSFLPCLRR
GSLPDTQPSQ GPSTPKGERA SSPCHSPRVC PATVIKSRVP LGPSAMQNCS TPLALPTRDL
NATFDLSEEP PSKPSFHECI GWDKIPQELS RLDQPFIPRA PVPLFTMKGP KPTSSLPGTS
ACKKKRVASS SVSHGRSRIA RLPSSTLKRP AGPLVLPELP LSPLCPSNRR NGKDLIRVGR
ALSAGNGVTK VS
