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 27-MAR-2024, entry version 200. 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="https://atlasgeneticsoncology.org/gene/44138/KIF14"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 1831. DR IntAct; Q15058; 76. DR MINT; Q15058; -. DR STRING; 9606.ENSP00000356319; -. DR BindingDB; Q15058; -. DR ChEMBL; CHEMBL5576; -. DR GlyCosmos; Q15058; 2 sites, 1 glycan. DR GlyGen; Q15058; 4 sites, 1 O-linked glycan (4 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; 9606-ENSP00000356319; -. DR PeptideAtlas; Q15058; -. DR ProteomicsDB; 60413; -. DR Pumba; Q15058; -. DR Antibodypedia; 20633; 187 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 AGR; HGNC:19181; -. 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; RGEDVFC; -. DR OrthoDB; 126886at2759; -. 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; 425 hits in 1165 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 107 other cell types or tissues. 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 chromosome alignment; 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; cd22707; FHA_KIF14; 1. DR CDD; cd01365; KISc_KIF1A_KIF1B; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR InterPro; IPR000253; FHA_dom. 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; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1. DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR Genevisible; Q15058; HS. 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:29343805" FT /id="VAR_080624" FT VARIANT 827 FT /note="Missing (in MCPH20; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28892560" FT /id="VAR_080625" FT VARIANT 841 FT /note="S -> F (in MCPH20; uncertain significance; FT 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 //