KIF14_HUMAN
ID KIF14_HUMAN Reviewed; 1648 AA.
AC Q15058; Q14CI8; Q4G0A5; Q5T1W3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Kinesin-like protein KIF14 {ECO:0000305};
GN Name=KIF14 {ECO:0000312|HGNC:HGNC:19181};
GN Synonyms=KIAA0042 {ECO:0000312|HGNC:HGNC:19181};
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-1633.
RC TISSUE=Uterus;
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 [5]
RP FUNCTION.
RX PubMed=15843429; DOI=10.1091/mbc.e05-02-0167;
RA Zhu C., Zhao J., Bibikova M., Leverson J.D., Bossy-Wetzel E., Fan J.-B.,
RA Abraham R.T., Jiang W.;
RT "Functional analysis of human microtubule-based motor proteins, the
RT kinesins and dyneins, in mitosis/cytokinesis using RNA interference.";
RL Mol. Biol. Cell 16:3187-3199(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1292, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRC1 AND CIT.
RX PubMed=16431929; DOI=10.1083/jcb.200511061;
RA Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B., Nigg E.A.,
RA Barr F.A.;
RT "KIF14 and citron kinase act together to promote efficient cytokinesis.";
RL J. Cell Biol. 172:363-372(2006).
RN [8]
RP INTERACTION WITH ARRB2.
RX PubMed=16820410; DOI=10.1242/jcs.03046;
RA Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.;
RT "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa.";
RL J. Cell Sci. 119:3047-3056(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16648480; DOI=10.1128/mcb.26.10.3853-3863.2006;
RA Carleton M., Mao M., Biery M., Warrener P., Kim S., Buser C.,
RA Marshall C.G., Fernandes C., Annis J., Linsley P.S.;
RT "RNA interference-mediated silencing of mitotic kinesin KIF14 disrupts cell
RT cycle progression and induces cytokinesis failure.";
RL Mol. Cell. Biol. 26:3853-3863(2006).
RN [10]
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 [11]
RP INTERACTION WITH SVIL, AND SUBCELLULAR LOCATION.
RX PubMed=20309963; DOI=10.1002/cm.20449;
RA Smith T.C., Fang Z., Luna E.J.;
RT "Novel interactors and a role for supervillin in early cytokinesis.";
RL Cytoskeleton 67:346-364(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RADIL.
RX PubMed=23209302; DOI=10.1083/jcb.201206051;
RA Ahmed S.M., Theriault B.L., Uppalapati M., Chiu C.W., Gallie B.L.,
RA Sidhu S.S., Angers S.;
RT "KIF14 negatively regulates Rap1a-Radil signaling during breast cancer
RT progression.";
RL J. Cell Biol. 199:951-967(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-272; THR-277;
RP SER-346; THR-915; SER-937 AND SER-1292, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
RN [16]
RP FUNCTION.
RX PubMed=24854087; DOI=10.1038/emm.2014.23;
RA Xu H., Choe C., Shin S.H., Park S.W., Kim H.S., Jung S.H., Yim S.H.,
RA Kim T.M., Chung Y.J.;
RT "Silencing of KIF14 interferes with cell cycle progression and cytokinesis
RT by blocking the p27(Kip1) ubiquitination pathway in hepatocellular
RT carcinoma.";
RL Exp. Mol. Med. 46:E97-E97(2014).
RN [17]
RP FUNCTION, AND INTERACTION WITH AKT1.
RX PubMed=24784001; DOI=10.1016/j.neo.2014.03.008;
RA Singel S.M., Cornelius C., Zaganjor E., Batten K., Sarode V.R.,
RA Buckley D.L., Peng Y., John G.B., Li H.C., Sadeghi N., Wright W.E., Lum L.,
RA Corson T.W., Shay J.W.;
RT "KIF14 promotes AKT phosphorylation and contributes to chemoresistance in
RT triple-negative breast cancer.";
RL Neoplasia 16:247-256(2014).
RN [18]
RP INVOLVEMENT IN MKS12.
RX PubMed=24128419; DOI=10.1111/cge.12301;
RA Filges I., Nosova E., Bruder E., Tercanli S., Townsend K., Gibson W.T.,
RA Roethlisberger B., Heinimann K., Hall J.G., Gregory-Evans C.Y.,
RA Wasserman W.W., Miny P., Friedman J.M.;
RT "Exome sequencing identifies mutations in KIF14 as a novel cause of an
RT autosomal recessive lethal fetal ciliopathy phenotype.";
RL Clin. Genet. 86:220-228(2014).
RN [19]
RP INVOLVEMENT IN MCPH20, VARIANTS MCPH20 88-LEU--VAL-1648 DEL; VAL-827 DEL;
RP ASP-849 AND VAL-1221, AND SUBCELLULAR LOCATION.
RX PubMed=28892560; DOI=10.1002/ana.25044;
RA Moawia A., Shaheen R., Rasool S., Waseem S.S., Ewida N., Budde B.,
RA Kawalia A., Motameny S., Khan K., Fatima A., Jameel M., Ullah F., Akram T.,
RA Ali Z., Abdullah U., Irshad S., Hoehne W., Noegel A.A., Al-Owain M.,
RA Hoertnagel K., Stoebe P., Baig S.M., Nuernberg P., Alkuraya F.S., Hahn A.,
RA Hussain M.S.;
RT "Mutations of KIF14 cause primary microcephaly by impairing cytokinesis.";
RL Ann. Neurol. 82:562-577(2017).
RN [20]
RP INVOLVEMENT IN MCPH20, AND VARIANTS MCPH20 ARG-459 AND PHE-841.
RX PubMed=29343805; DOI=10.1038/s41431-017-0088-9;
RA Makrythanasis P., Maroofian R., Stray-Pedersen A., Musaev D., Zaki M.S.,
RA Mahmoud I.G., Selim L., Elbadawy A., Jhangiani S.N., Coban Akdemir Z.H.,
RA Gambin T., Sorte H.S., Heiberg A., McEvoy-Venneri J., James K.N.,
RA Stanley V., Belandres D., Guipponi M., Santoni F.A., Ahangari N., Tara F.,
RA Doosti M., Iwaszkiewicz J., Zoete V., Backe P.H., Hamamy H., Gleeson J.G.,
RA Lupski J.R., Karimiani E.G., Antonarakis S.E.;
RT "Biallelic variants in KIF14 cause intellectual disability with
RT microcephaly.";
RL Eur. J. Hum. Genet. 26:330-339(2018).
CC -!- FUNCTION: Microtubule motor protein that binds to microtubules with
CC high affinity through each tubulin heterodimer and has an ATPase
CC activity (By similarity). Plays a role in many processes like cell
CC division, cytokinesis and also in cell proliferation and apoptosis
CC (PubMed:24784001, PubMed:16648480). During cytokinesis, targets to
CC central spindle and midbody through its interaction with PRC1 and CIT
CC respectively (PubMed:16431929). Regulates cell growth through
CC regulation of cell cycle progression and cytokinesis (PubMed:24854087).
CC During cell cycle progression acts through SCF-dependent proteasomal
CC ubiquitin-dependent protein catabolic process which controls CDKN1B
CC degradation, resulting in positive regulation of cyclins, including
CC CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis,
CC regulates the cerebellar, cerebral cortex and olfactory bulb
CC development through regulation of apoptosis, cell proliferation and
CC cell division (By similarity). Also is required for chromosome
CC congression and alignment during mitotic cell cycle process
CC (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics,
CC and cell migration through its interaction with RADIL resulting in
CC regulation of RAP1A-mediated inside-out integrin activation by
CC tethering RADIL on microtubules (PubMed:23209302).
CC {ECO:0000250|UniProtKB:L0N7N1, ECO:0000269|PubMed:15843429,
CC ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:16648480,
CC ECO:0000269|PubMed:23209302, ECO:0000269|PubMed:24784001,
CC ECO:0000269|PubMed:24854087}.
CC -!- SUBUNIT: Directly interacts with PRC1 within a complex also containing
CC KIF4A, KIF20A and KIF23; targets to the central spindle. Directly
CC interacts with CIT depending on the activation state of the kinase
CC (stronger interaction with the kinase-dead form); targets to the
CC midbody. Interacts with ARRB2; the interaction is detected in the
CC nucleus upon OR1D2 stimulation. Interacts with AKT1; the interaction is
CC detected in the plasma membrane upon INS stimulation and promotes AKT1
CC phosphorylation. Interacts with SVIL; at midbody during cytokinesis.
CC Interacts with RADIL (via PDZ domain); recruits RADIL to the
CC microtubule network restricting RADIL from interaction with activated
CC RAP1A (PubMed:23209302). {ECO:0000269|PubMed:16431929,
CC ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:20309963,
CC ECO:0000269|PubMed:23209302, ECO:0000269|PubMed:24784001}.
CC -!- INTERACTION:
CC Q15058; O46385: SVIL; Xeno; NbExp=3; IntAct=EBI-1045252, EBI-6995105;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16431929}. Cytoplasm
CC {ECO:0000269|PubMed:16648480}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:16431929}. Midbody {ECO:0000269|PubMed:16431929,
CC ECO:0000269|PubMed:20309963, ECO:0000269|PubMed:28892560}. Note=Nuclear
CC localization observed during interphase (PubMed:16431929). Nuclear
CC localization triggered by entry into mitosis (PubMed:16648480).
CC Cytoplasmic in interphase (PubMed:16648480). Cytoplasmic in metaphase
CC cells (PubMed:16431929). From prophase to metaphase, accumulates at the
CC developing spindle poles and their associated microtubules. During
CC anaphase, accumulates at the spindle midzone. Localization to the
CC central spindle and midbody during anaphase is dependent upon PRC1 and
CC CIT presence. In cells ready to undergo abscission, concentrates at the
CC contractile ring. {ECO:0000269|PubMed:16431929,
CC ECO:0000269|PubMed:16648480}.
CC -!- INDUCTION: Up-regulated in cells progressing through G2/M phase.
CC {ECO:0000269|PubMed:16648480}.
CC -!- DOMAIN: The kinesin motor domain binds to microtubules with high
CC affinity and has a robust ATPase activity but a very slow motility. The
CC kinesin motor domain protects microtubules from cold depolymerization.
CC Binds to each tubulin heterodimer resulting in a microtubule complexes.
CC Binds at the tubulin intradimer interface, at the crest of the
CC protofilament, and orients slightly toward the next protofilament.
CC {ECO:0000250|UniProtKB:L0N7N1}.
CC -!- DISEASE: Meckel syndrome 12 (MKS12) [MIM:616258]: A form of Meckel
CC syndrome, a disorder characterized by a combination of renal cysts and
CC variably associated features including developmental anomalies of the
CC central nervous system (typically encephalocele), hepatic ductal
CC dysplasia and cysts, and polydactyly. {ECO:0000269|PubMed:24128419}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Microcephaly 20, primary, autosomal recessive (MCPH20)
CC [MIM:617914]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age, sex and
CC ethnically matched mean. Brain weight is markedly reduced and the
CC cerebral cortex is disproportionately small. MCPH20 features include
CC mild to moderate intellectual disability, autistic features, poor
CC speech. Disease severity is highly variable.
CC {ECO:0000269|PubMed:28892560, ECO:0000269|PubMed:29343805}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. The disease-causing variant NM_014875.2:c.263T>A, which produces
CC a premature truncation of the protein at Leu-88 (p.Leu88Ter), may also
CC partly result in the deletion of 372 bp of exon 2 of KIF14 by
CC activation of a cryptic splice site. This in-frame deletion predicts a
CC protein that lacks 124 aa (p.Gly58-Leu181del). The disease-causing
CC mutation NM_014875.2:c.3662G>T, resulting in the missence variant
CC p.Gly1221Val, may also induce the skipping of exon 24, resulting in a
CC protein that misses 76 aa (p.Gly1221_ Lys1296delinsVal).
CC {ECO:0000269|PubMed:28892560}.
CC -!- MISCELLANEOUS: It is resistant to docetaxel anhydrous.
CC {ECO:0000269|PubMed:24784001}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05392.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KIF14ID44138ch1q32.html";
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DR EMBL; D26361; BAA05392.2; ALT_INIT; mRNA.
DR EMBL; AL445483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91316.1; -; Genomic_DNA.
DR EMBL; BC098582; AAH98582.1; -; mRNA.
DR EMBL; BC113742; AAI13743.1; -; mRNA.
DR CCDS; CCDS30963.1; -.
DR RefSeq; NP_001292721.1; NM_001305792.1.
DR RefSeq; NP_055690.1; NM_014875.2.
DR RefSeq; XP_011508533.1; XM_011510231.2.
DR RefSeq; XP_011508534.1; XM_011510232.2.
DR RefSeq; XP_016858494.1; XM_017003005.1.
DR AlphaFoldDB; Q15058; -.
DR SMR; Q15058; -.
DR BioGRID; 115256; 1809.
DR IntAct; Q15058; 64.
DR MINT; Q15058; -.
DR STRING; 9606.ENSP00000356319; -.
DR BindingDB; Q15058; -.
DR ChEMBL; CHEMBL5576; -.
DR GlyGen; Q15058; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q15058; -.
DR MetOSite; Q15058; -.
DR PhosphoSitePlus; Q15058; -.
DR SwissPalm; Q15058; -.
DR BioMuta; KIF14; -.
DR DMDM; 23396633; -.
DR EPD; Q15058; -.
DR jPOST; Q15058; -.
DR MassIVE; Q15058; -.
DR MaxQB; Q15058; -.
DR PaxDb; Q15058; -.
DR PeptideAtlas; Q15058; -.
DR PRIDE; Q15058; -.
DR ProteomicsDB; 60413; -.
DR Antibodypedia; 20633; 158 antibodies from 21 providers.
DR DNASU; 9928; -.
DR Ensembl; ENST00000367350.5; ENSP00000356319.4; ENSG00000118193.12.
DR Ensembl; ENST00000614960.4; ENSP00000483069.1; ENSG00000118193.12.
DR GeneID; 9928; -.
DR KEGG; hsa:9928; -.
DR MANE-Select; ENST00000367350.5; ENSP00000356319.4; NM_014875.3; NP_055690.1.
DR UCSC; uc010ppk.2; human.
DR CTD; 9928; -.
DR DisGeNET; 9928; -.
DR GeneCards; KIF14; -.
DR HGNC; HGNC:19181; KIF14.
DR HPA; ENSG00000118193; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; KIF14; -.
DR MIM; 611279; gene.
DR MIM; 616258; phenotype.
DR MIM; 617914; phenotype.
DR neXtProt; NX_Q15058; -.
DR OpenTargets; ENSG00000118193; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR Orphanet; 439897; Lethal fetal cerebrorenogenitourinary agenesis/hypoplasia syndrome.
DR PharmGKB; PA38820; -.
DR VEuPathDB; HostDB:ENSG00000118193; -.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000156834; -.
DR HOGENOM; CLU_003253_0_0_1; -.
DR InParanoid; Q15058; -.
DR OMA; VVLIKHW; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; Q15058; -.
DR TreeFam; TF105221; -.
DR PathwayCommons; Q15058; -.
DR Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q15058; -.
DR SIGNOR; Q15058; -.
DR BioGRID-ORCS; 9928; 402 hits in 1087 CRISPR screens.
DR ChiTaRS; KIF14; human.
DR GeneWiki; KIF14; -.
DR GenomeRNAi; 9928; -.
DR Pharos; Q15058; Tbio.
DR PRO; PR:Q15058; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15058; protein.
DR Bgee; ENSG00000118193; Expressed in secondary oocyte and 106 other tissues.
DR Genevisible; Q15058; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0090543; C:Flemming body; IDA:HPA.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:MGI.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
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:0030165; F:PDZ domain binding; IDA:MGI.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:Ensembl.
DR GO; GO:0021846; P:cell proliferation in forebrain; ISS:UniProtKB.
DR GO; GO:0021695; P:cerebellar cortex development; ISS:UniProtKB.
DR GO; GO:0021685; P:cerebellar granular layer structural organization; ISS:UniProtKB.
DR GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; IDA:MGI.
DR GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0033624; P:negative regulation of integrin activation; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:1903429; P:regulation of cell maturation; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0032487; P:regulation of Rap protein signal transduction; IMP:MGI.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF49879; SSF49879; 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; Ciliopathy; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Meckel syndrome; Microtubule; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Primary microcephaly;
KW Reference proteome.
FT CHAIN 1..1648
FT /note="Kinesin-like protein KIF14"
FT /id="PRO_0000125449"
FT DOMAIN 358..701
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 825..891
FT /note="FHA"
FT REGION 1..356
FT /note="Required for PRC1-binding"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..737
FT /note="Required for microtubule-binding with high affinity"
FT /evidence="ECO:0000250|UniProtKB:L0N7N1"
FT REGION 901..1648
FT /note="Required for CIT-binding"
FT REGION 1600..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 705..791
FT /evidence="ECO:0000255"
FT COILED 922..1079
FT /evidence="ECO:0000255"
FT COILED 1332..1348
FT /evidence="ECO:0000255"
FT COILED 1468..1500
FT /evidence="ECO:0000255"
FT COMPBIAS 1600..1615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 915
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 88..1648
FT /note="Missing (in MCPH20; drastically decreased expression
FT at the mRNA level; loss of localization at the midbody
FT during cytokinesis and consequently loss of CIT/CRIK
FT recruitment to the midbody)"
FT /evidence="ECO:0000269|PubMed:28892560"
FT /id="VAR_080623"
FT VARIANT 459
FT /note="G -> R (in MCPH20; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29343805"
FT /id="VAR_080624"
FT VARIANT 827
FT /note="Missing (in MCPH20; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28892560"
FT /id="VAR_080625"
FT VARIANT 841
FT /note="S -> F (in MCPH20; unknown pathological
FT significance; dbSNP:rs139385693)"
FT /evidence="ECO:0000269|PubMed:29343805"
FT /id="VAR_080626"
FT VARIANT 849
FT /note="H -> D (in MCPH20; Decreased expression at the mRNA
FT level and loss of localization at the midbody during
FT cytokinesis and consequently loss of CIT/CRIK recruitment
FT to the midbody, when analyzed in primary fibroblasts from a
FT patient who is a compound heterozygous with variant V-1221;
FT dbSNP:rs1553259528)"
FT /evidence="ECO:0000269|PubMed:28892560"
FT /id="VAR_080627"
FT VARIANT 1221
FT /note="G -> V (in MCPH20; Decreased expression at the mRNA
FT level and loss of localization at the midbody during
FT cytokinesis and consequently loss of CIT/CRIK recruitment
FT to the midbody, when analyzed in primary fibroblasts from a
FT patient who is a compound heterozygous with variant D-849)"
FT /evidence="ECO:0000269|PubMed:28892560"
FT /id="VAR_080628"
FT VARIANT 1633
FT /note="P -> A (in dbSNP:rs12120084)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037777"
FT CONFLICT 660
FT /note="W -> C (in Ref. 4; AAH98582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1648 AA; 186492 MW; FB1423668A7B79D7 CRC64;
MSLHSTHNRN NSGDILDIPS SQNSSSLNAL THSSRLKLHL KSDMSECEND DPLLRSAGKV
RDINRTYVIS ASRKTADMPL TPNPVGRLAL QRRTTRNKES SLLVSELEDT TEKTAETRLT
LQRRAKTDSA EKWKTAEIDS VKMTLNVGGE TENNGVSKES RTNVRIVNNA KNSFVASSVP
LDEDPQVIEM MADKKYKETF SAPSRANENV ALKYSSNRPP IASLSQTEVV RSGHLTTKPT
QSKLDIKVLG TGNLYHRSIG KEIAKTSNKF GSLEKRTPTK CTTEHKLTTK CSLPQLKSPA
PSILKNRMSN LQVKQRPKSS FLANKQERSA ENTILPEEET VVQNTSAGKD PLKVENSQVT
VAVRVRPFTK REKIEKASQV VFMSGKEITV EHPDTKQVYN FIYDVSFWSF DECHPHYASQ
TTVYEKLAAP LLERAFEGFN TCLFAYGQTG SGKSYTMMGF SEEPGIIPRF CEDLFSQVAR
KQTQEVSYHI EMSFFEVYNE KIHDLLVCKD ENGQRKQPLR VREHPVYGPY VEALSMNIVS
SYADIQSWLE LGNKQRATAA TGMNDKSSRS HSVFTLVMTQ TKTEFVEGEE HDHRITSRIN
LIDLAGSERC STAHTNGDRL KEGVSINKSL LTLGKVISAL SEQANQRSVF IPYRESVLTW
LLKESLGGNS KTAMIATISP AASNIEETLS TLRYANQARL IVNIAKVNED MNAKLIRELK
AEIAKLKAAQ RNSRNIDPER YRLCRQEITS LRMKLHQQER DMAEMQRVWK EKFEQAEKRK
LQETKELQKA GIMFQMDNHL PNLVNLNEDP QLSEMLLYMI KEGTTTVGKY KPNSSHDIQL
SGVLIADDHC TIKNFGGTVS IIPVGEAKTY VNGKHILEIT VLRHGDRVIL GGDHYFRFNH
PVEVQKGKRP SGRDTPISEG PKDFEFAKNE LLMAQRSQLE AEIKEAQLKA KEEMMQGIQI
AKEMAQQELS SQKAAYESKI KALEAELREE SQRKKMQEIN NQKANHKIEE LEKAKQHLEQ
EIYVNKKRLE METLATKQAL EDHSIRHARI LEALETEKQK IAKEVQILQQ NRNNRDKTFT
VQTTWSSMKL SMMIQEANAI SSKLKTYYVF GRHDISDKSS SDTSIRVRNL KLGISTFWSL
EKFESKLAAM KELYESNGSN RGEDAFCDPE DEWEPDITDA PVSSLSRRRS RSLMKNRRIS
GCLHDIQVHP IKNLHSSHSS GLMDKSSTIY SNSAESFLPG ICKELIGSSL DFFGQSYDEE
RTIADSLINS FLKIYNGLFA ISKAHEEQDE ESQDNLFSSD RAIQSLTIQT ACAFEQLVVL
MKHWLSDLLP CTNIARLEDE LRQEVKKLGG YLQLFLQGCC LDISSMIKEA QKNAIQIVQQ
AVKYVGQLAV LKGSKLHFLE NGNNKAASVQ EEFMDAVCDG VGLGMKILLD SGLEKAKELQ
HELFRQCTKN EVTKEMKTNA MGLIRSLENI FAESKIKSFR RQVQEENFEY QDFKRMVNRA
PEFLKLKHCL EKAIEIIISA LKGCHSDINL LQTCVESIRN LASDFYSDFS VPSTSVGSYE
SRVTHIVHQE LESLAKSLLF CFESEESPDL LKPWETYNQN TKEEHQQSKS SGIDGSKNKG
VPKRVYELHG SSPAVSSEEC TPSRIQWV
