{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q15058","secondaryAccessions":["Q14CI8","Q4G0A5","Q5T1W3"],"uniProtkbId":"KIF14_HUMAN","entryAudit":{"firstPublicDate":"2002-09-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":210,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Kinesin-like protein KIF14"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:19181"}],"value":"KIF14"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:19181"}],"value":"KIAA0042"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"L0N7N1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15843429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16431929"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16648480"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23209302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24784001"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24854087"}],"value":"Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (PubMed:16648480, PubMed:24784001). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis, regulates the cerebellar, cerebral cortex and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16431929"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16820410"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20309963"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23209302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24784001"}],"value":"Directly interacts with PRC1 within a complex also containing KIF4A, KIF20A and KIF23; targets to the central spindle. Directly interacts with CIT depending on the activation state of the kinase (stronger interaction with the kinase-dead form); targets to the midbody. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. Interacts with AKT1; the interaction is detected in the plasma membrane upon INS stimulation and promotes AKT1 phosphorylation. Interacts with SVIL; at midbody during cytokinesis. Interacts with RADIL (via PDZ domain); recruits RADIL to the microtubule network restricting RADIL from interaction with activated RAP1A (PubMed:23209302)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q15058","intActId":"EBI-1045252"},"interactantTwo":{"uniProtKBAccession":"O46385","geneName":"SVIL","intActId":"EBI-6995105"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16431929"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16648480"}],"value":"Nuclear localization observed during interphase (PubMed:16431929). Nuclear localization triggered by entry into mitosis (PubMed:16648480). Cytoplasmic in interphase (PubMed:16648480). Cytoplasmic in metaphase cells (PubMed:16431929). From prophase to metaphase, accumulates at the developing spindle poles and their associated microtubules. During anaphase, accumulates at the spindle midzone. Localization to the central spindle and midbody during anaphase is dependent upon PRC1 and CIT presence. In cells ready to undergo abscission, concentrates at the contractile ring"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16431929"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16648480"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16431929"}],"value":"Cytoplasm, cytoskeleton, spindle","id":"SL-0251"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16431929"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20309963"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28892560"}],"value":"Midbody","id":"SL-0469"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16648480"}],"value":"Up-regulated in cells progressing through G2/M phase"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"L0N7N1"}],"value":"The kinesin motor domain binds to microtubules with high affinity and has a robust ATPase activity but a very slow motility. The kinesin motor domain protects microtubules from cold depolymerization. Binds to each tubulin heterodimer resulting in a microtubule complexes. Binds at the tubulin intradimer interface, at the crest of the protofilament, and orients slightly toward the next protofilament"}],"commentType":"DOMAIN"},{"commentType":"DISEASE","disease":{"diseaseId":"Meckel syndrome 12","diseaseAccession":"DI-04349","acronym":"MKS12","description":"A form of Meckel syndrome, a disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly.","diseaseCrossReference":{"database":"MIM","id":"616258"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24128419"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Microcephaly 20, primary, autosomal recessive","diseaseAccession":"DI-05207","acronym":"MCPH20","description":"A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH20 features include mild to moderate intellectual disability, autistic features, poor speech. Disease severity is highly variable.","diseaseCrossReference":{"database":"MIM","id":"617914"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28892560"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29343805"}]},"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28892560"}],"value":"The disease is caused by variants affecting the gene represented in this entry. The disease-causing variant NM_014875.2:c.263T>A, which produces a premature truncation of the protein at Leu-88 (p.Leu88Ter), may also partly result in the deletion of 372 bp of exon 2 of KIF14 by activation of a cryptic splice site. This in-frame deletion predicts a protein that lacks 124 aa (p.Gly58-Leu181del). The disease-causing mutation NM_014875.2:c.3662G>T, resulting in the missence variant p.Gly1221Val, may also induce the skipping of exon 24, resulting in a protein that misses 76 aa (p.Gly1221_ Lys1296delinsVal)"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24784001"}],"value":"It is resistant to docetaxel anhydrous"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00283"}],"value":"Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAA05392.2","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/44138/KIF14","ftp":false}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1648,"modifier":"EXACT"}},"description":"Kinesin-like protein KIF14","featureId":"PRO_0000125449"},{"type":"Domain","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":701,"modifier":"EXACT"}},"description":"Kinesin 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