ID KIF24_HUMAN Reviewed; 1368 AA. AC Q5T7B8; Q2TB93; Q5T7B5; Q5T7B7; Q6ZU97; Q6ZUZ2; Q86XZ0; Q9NV43; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 2. DT 27-MAR-2024, entry version 168. DE RecName: Full=Kinesin-like protein KIF24; GN Name=KIF24; Synonyms=C9orf48; 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 GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 503-1368 (ISOFORM 1), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 32-1368 (ISOFORM 3), AND VARIANT PHE-837. RC TISSUE=Fetal brain, Ovarian carcinoma, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 509-1368 (ISOFORM 1), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 956-1368 (ISOFORM 4), AND VARIANT PHE-837. RC TISSUE=Duodenum; 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-102; SER-478 AND SER-1012, RP AND IDENTIFICATION BY MASS 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-478 AND SER-646, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH RP CCP110 AND CEP97, AND MUTAGENESIS OF 263-VAL-ASP-264 AND 483-LYS--CYS-485. RX PubMed=21620453; DOI=10.1016/j.cell.2011.04.028; RA Kobayashi T., Tsang W.Y., Li J., Lane W., Dynlacht B.D.; RT "Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and RT regulate ciliogenesis."; RL Cell 145:914-925(2011). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478 AND SER-646, AND RP IDENTIFICATION BY MASS 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 [8] RP INTERACTION WITH TALPID3. RX PubMed=24421332; DOI=10.1083/jcb.201304153; RA Kobayashi T., Kim S., Lin Y.C., Inoue T., Dynlacht B.D.; RT "The CP110-interacting proteins Talpid3 and Cep290 play overlapping and RT distinct roles in cilia assembly."; RL J. Cell Biol. 204:215-229(2014). RN [9] RP FUNCTION, PHOSPHORYLATION AT THR-621 AND SER-622, AND MUTAGENESIS OF RP 621-THR-SER-622. RX PubMed=26290419; DOI=10.1038/ncomms9087; RA Kim S., Lee K., Choi J.H., Ringstad N., Dynlacht B.D.; RT "Nek2 activation of Kif24 ensures cilium disassembly during the cell RT cycle."; RL Nat. Commun. 6:8087-8087(2015). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MPHOSPH9. RX PubMed=30375385; DOI=10.1038/s41467-018-06990-9; RA Huang N., Zhang D., Li F., Chai P., Wang S., Teng J., Chen J.; RT "M-Phase Phosphoprotein 9 regulates ciliogenesis by modulating CP110-CEP97 RT complex localization at the mother centriole."; RL Nat. Commun. 9:4511-4511(2018). CC -!- FUNCTION: Microtubule-dependent motor protein that acts as a negative CC regulator of ciliogenesis by mediating recruitment of CCP110 to mother CC centriole in cycling cells, leading to restrict nucleation of cilia at CC centrioles. Mediates depolymerization of microtubules of centriolar CC origin, possibly to suppress aberrant cilia formation CC (PubMed:21620453). Following activation by NEK2 involved in disassembly CC of primary cilium during G2/M phase but does not disassemble fully CC formed ciliary axonemes. As cilium assembly and disassembly is proposed CC to coexist in a dynamic equilibrium may suppress nascent cilium CC assembly and, potentially, ciliar re-assembly in cells that have CC already disassembled their cilia ensuring the completion of cilium CC removal in the later stages of the cell cycle (PubMed:26290419). Plays CC an important role in recruiting MPHOSPH9, a negative regulator of cilia CC formation to the distal end of mother centriole (PubMed:30375385). CC {ECO:0000269|PubMed:21620453, ECO:0000269|PubMed:26290419, CC ECO:0000269|PubMed:30375385}. CC -!- SUBUNIT: Interacts with CCP110, CEP97, TALPID3 (PubMed:21620453, CC PubMed:24421332). Interacts with MPHOSPH9 (PubMed:30375385). CC {ECO:0000269|PubMed:21620453, ECO:0000269|PubMed:24421332, CC ECO:0000269|PubMed:30375385}. CC -!- INTERACTION: CC Q5T7B8; O43303: CCP110; NbExp=14; IntAct=EBI-2556811, EBI-1566217; CC Q5T7B8; Q8IW35: CEP97; NbExp=13; IntAct=EBI-2556811, EBI-1566210; CC Q5T7B8; Q5T7B8: KIF24; NbExp=2; IntAct=EBI-2556811, EBI-2556811; CC Q5T7B8; P51955: NEK2; NbExp=7; IntAct=EBI-2556811, EBI-633182; CC Q5T7B8-2; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-10213781, EBI-541426; CC Q5T7B8-2; P68400: CSNK2A1; NbExp=3; IntAct=EBI-10213781, EBI-347804; CC Q5T7B8-2; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-10213781, EBI-5453285; CC Q5T7B8-2; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-10213781, EBI-14103818; CC Q5T7B8-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-10213781, EBI-7116203; CC Q5T7B8-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10213781, EBI-739832; CC Q5T7B8-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-10213781, EBI-1383852; CC Q5T7B8-2; Q86VV4: RANBP3L; NbExp=3; IntAct=EBI-10213781, EBI-12028066; CC Q5T7B8-2; O76064: RNF8; NbExp=3; IntAct=EBI-10213781, EBI-373337; CC Q5T7B8-2; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-10213781, EBI-10246152; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome, centriole {ECO:0000269|PubMed:21620453, CC ECO:0000269|PubMed:30375385}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:30375385}. CC Note=Primarily localizes to the mother centriole/basal body and is CC either absent at daughter centriole. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q5T7B8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5T7B8-2; Sequence=VSP_023210; CC Name=3; CC IsoId=Q5T7B8-3; Sequence=VSP_023211; CC Name=4; CC IsoId=Q5T7B8-4; Sequence=VSP_023212, VSP_023213; CC -!- DEVELOPMENTAL STAGE: Increases as cells progress through G1, peaks CC during S and G2 phases and decreases as cells enter mitosis during G2/M CC (at protein level). {ECO:0000269|PubMed:21620453}. CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI10504.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC86074.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC86329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AL353662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK001795; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK125180; BAC86074.1; ALT_INIT; mRNA. DR EMBL; AK125872; BAC86329.1; ALT_INIT; mRNA. DR EMBL; BC048311; AAH48311.1; -; mRNA. DR EMBL; BC110502; AAI10503.2; -; mRNA. DR EMBL; BC110503; AAI10504.1; ALT_INIT; mRNA. DR CCDS; CCDS6551.2; -. [Q5T7B8-1] DR RefSeq; NP_919289.2; NM_194313.2. [Q5T7B8-1] DR RefSeq; XP_011516165.1; XM_011517863.2. [Q5T7B8-1] DR RefSeq; XP_016870186.1; XM_017014697.1. [Q5T7B8-1] DR AlphaFoldDB; Q5T7B8; -. DR SMR; Q5T7B8; -. DR BioGRID; 131415; 40. DR IntAct; Q5T7B8; 23. DR STRING; 9606.ENSP00000384433; -. DR ChEMBL; CHEMBL3879840; -. DR iPTMnet; Q5T7B8; -. DR PhosphoSitePlus; Q5T7B8; -. DR BioMuta; KIF24; -. DR DMDM; 126215732; -. DR EPD; Q5T7B8; -. DR jPOST; Q5T7B8; -. DR MassIVE; Q5T7B8; -. DR MaxQB; Q5T7B8; -. DR PaxDb; 9606-ENSP00000368464; -. DR PeptideAtlas; Q5T7B8; -. DR ProteomicsDB; 64650; -. [Q5T7B8-1] DR ProteomicsDB; 64651; -. [Q5T7B8-2] DR ProteomicsDB; 64652; -. [Q5T7B8-3] DR ProteomicsDB; 64653; -. [Q5T7B8-4] DR Antibodypedia; 11186; 128 antibodies from 19 providers. DR DNASU; 347240; -. DR Ensembl; ENST00000379174.7; ENSP00000368472.3; ENSG00000186638.17. [Q5T7B8-2] DR Ensembl; ENST00000402558.7; ENSP00000384433.1; ENSG00000186638.17. [Q5T7B8-1] DR GeneID; 347240; -. DR KEGG; hsa:347240; -. DR MANE-Select; ENST00000402558.7; ENSP00000384433.1; NM_194313.4; NP_919289.2. DR UCSC; uc003zua.5; human. [Q5T7B8-1] DR AGR; HGNC:19916; -. DR CTD; 347240; -. DR DisGeNET; 347240; -. DR GeneCards; KIF24; -. DR HGNC; HGNC:19916; KIF24. DR HPA; ENSG00000186638; Tissue enhanced (testis). DR MalaCards; KIF24; -. DR MIM; 613747; gene. DR neXtProt; NX_Q5T7B8; -. DR OpenTargets; ENSG00000186638; -. DR PharmGKB; PA142671589; -. DR VEuPathDB; HostDB:ENSG00000186638; -. DR eggNOG; KOG0246; Eukaryota. DR GeneTree; ENSGT00940000154046; -. DR HOGENOM; CLU_007560_0_0_1; -. DR InParanoid; Q5T7B8; -. DR OMA; WGNTFAK; -. DR OrthoDB; 239968at2759; -. DR PhylomeDB; Q5T7B8; -. DR TreeFam; TF336001; -. DR PathwayCommons; Q5T7B8; -. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR SignaLink; Q5T7B8; -. DR BioGRID-ORCS; 347240; 10 hits in 1165 CRISPR screens. DR ChiTaRS; KIF24; human. DR GeneWiki; KIF24; -. DR GenomeRNAi; 347240; -. DR Pharos; Q5T7B8; Tbio. DR PRO; PR:Q5T7B8; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q5T7B8; Protein. DR Bgee; ENSG00000186638; Expressed in primordial germ cell in gonad and 102 other cell types or tissues. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008017; F:microtubule binding; IEA:InterPro. DR GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0007019; P:microtubule depolymerization; IDA:UniProtKB. DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro. DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB. DR CDD; cd01367; KISc_KIF2_like; 1. DR CDD; cd09541; SAM_KIF24-like; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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 InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR PANTHER; PTHR47971:SF8; KINESIN-LIKE PROTEIN KIF24; 1. DR PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 1. DR Pfam; PF00225; Kinesin; 1. DR Pfam; PF00536; SAM_1; 1. DR PRINTS; PR00380; KINESINHEAVY. DR SMART; SM00129; KISc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1. DR PROSITE; PS50067; KINESIN_MOTOR_2; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cilium biogenesis/degradation; KW Cytoplasm; Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1..1368 FT /note="Kinesin-like protein KIF24" FT /id="PRO_0000278248" FT DOMAIN 1..64 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT DOMAIN 223..546 FT /note="Kinesin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT REGION 89..112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 478..709 FT /note="Interaction with MPHOSPH9" FT /evidence="ECO:0000269|PubMed:30375385" FT REGION 557..584 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 602..639 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 651..670 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 729..753 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 792..849 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 864..938 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 952..984 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1054..1073 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1083..1148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 557..579 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 795..809 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 832..849 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 866..882 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 883..908 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 916..932 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 960..974 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 313..320 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 112 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 478 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163" FT MOD_RES 584 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6NWW5" FT MOD_RES 621 FT /note="Phosphothreonine; by NEK2" FT /evidence="ECO:0000269|PubMed:26290419" FT MOD_RES 622 FT /note="Phosphoserine; by NEK2" FT /evidence="ECO:0000269|PubMed:26290419" FT MOD_RES 646 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:23186163" FT MOD_RES 826 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6NWW5" FT MOD_RES 829 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6NWW5" FT MOD_RES 1012 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT VAR_SEQ 209..1368 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023211" FT VAR_SEQ 272..405 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_023210" FT VAR_SEQ 1131..1158 FT /note="SPSPIRQHPADKLPSREADLGEACQSRE -> GPGEKTSYKAWLAGVWFVHR FT PHQVALQQ (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023212" FT VAR_SEQ 1159..1368 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023213" FT VARIANT 50 FT /note="D -> E (in dbSNP:rs16935508)" FT /id="VAR_030720" FT VARIANT 109 FT /note="R -> G (in dbSNP:rs41274845)" FT /id="VAR_061284" FT VARIANT 140 FT /note="M -> V (in dbSNP:rs10972048)" FT /id="VAR_030721" FT VARIANT 218 FT /note="W -> L (in dbSNP:rs17350674)" FT /id="VAR_049706" FT VARIANT 837 FT /note="S -> F (in dbSNP:rs41274041)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_061285" FT VARIANT 1077 FT /note="T -> K (in dbSNP:rs34101674)" FT /id="VAR_049707" FT MUTAGEN 263..264 FT /note="VD->AA: Impairs ability to suppress cilia FT formation." FT /evidence="ECO:0000269|PubMed:21620453" FT MUTAGEN 483..485 FT /note="KEC->AAA: Impairs ability to suppress cilia FT formation." FT /evidence="ECO:0000269|PubMed:21620453" FT MUTAGEN 621..622 FT /note="TS->AA: Reduces phosphorylation by NEK2 and FT abolishes ability to suppress cilia formation." FT /evidence="ECO:0000269|PubMed:26290419" SQ SEQUENCE 1368 AA; 151903 MW; AE88C9E3A4C9FBFF CRC64; MASWLYECLC EAELAQYYSH FTALGLQKID ELAKITMKDY SKLGVHDMND RKRLFQLIKI IKIMQEEDKA VSIPERHLQT SSLRIKSQEL RSGPRRQLNF DSPADNKDRN ASNDGFEMCS LSDFSANEQK STYLKVLEHM LPDDSQYHTK TGILNATAGD SYVQTEISTS LFSPNYLSAI LGDCDIPIIQ RISHVSGYNY GIPHSCIRQN TSEKQNPWTE MEKIRVCVRK RPLGMREVRR GEINIITVED KETLLVHEKK EAVDLTQYIL QHVFYFDEVF GEACTNQDVY MKTTHPLIQH IFNGGNATCF AYGQTGAGKT YTMIGTHENP GLYALAAKDI FRQLEVSQPR KHLFVWISFY EIYCGQLYDL LNRRKRLFAR EDSKHMVQIV GLQELQVDSV ELLLEVILKG SKERSTGATG VNADSSRSHA VIQIQIKDSA KRTFGRISFI DLAGSERAAD ARDSDRQTKM EGAEINQSLL ALKECIRALD QEHTHTPFRQ SKLTQVLKDS FIGNAKTCMI ANISPSHVAT EHTLNTLRYA DRVKELKKGI KCCTSVTSRN RTSGNSSPKR IQSSPGALSE DKCSPKKVKL GFQQSLTVAA PGSTRGKVHP LTSHPPNIPF TSAPKVSGKR GGSRGSPSQE WVIHASPVKG TVRSGHVAKK KPEESAPLCS EKNRMGNKTV LGWESRASGP GEGLVRGKLS TKCKKVQTVQ PVQKQLVSRV ELSFGNAHHR AEYSQDSQRG TPARPASEAW TNIPPHQKER EEHLRFYHQQ FQQPPLLQQK LKYQPLKRSL RQYRPPEGQL TNETPPLFHS YSENHDGAQV EELDDSDFSE DSFSHISSQR ATKQRNTLEN SEDSFFLHQT WGQGPEKQVA ERQQSLFSSP RTGDKKDLTK SWVDSRDPIN HRRAALDHSC SPSKGPVDWS RENSTSSGPS PRDSLAEKPY CSQVDFIYRQ ERGGGSSFDL RKDASQSEVS GENEGNLPSP EEDGFTISLS HVAVPGSPDQ RDTVTTPLRE VSADGPIQVT STVKNGHAVP GEDPRGQLGT HAEYASGLMS PLTMSLLENP DNEGSPPSEQ LVQDGATHSL VAESTGGPVV SHTVPSGDQE AALPVSSATR HLWLSSSPPD NKPGGDLPAL SPSPIRQHPA DKLPSREADL GEACQSRETV LFSHEHMGSE QYDADAEETG LDGSWGFPGK PFTTIHMGVP HSGPTLTPRT GSSDVADQLW AQERKHPTRL GWQEFGLSTD PIKLPCNSEN VTWLKPRPIS RCLARPSSPL VPSCSPKTAG TLRQPTLEQA QQVVIRAHQE QLDEMAELGF KEETLMSQLA SNDFEDFVTQ LDEIMVLKSK CIQSLRSQLQ LYLTCHGPTA APEGTVPS //