KIF24_HUMAN
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 03-AUG-2022, entry version 159.
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=12; 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};
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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; 39.
DR IntAct; Q5T7B8; 23.
DR STRING; 9606.ENSP00000368464; -.
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; Q5T7B8; -.
DR PeptideAtlas; Q5T7B8; -.
DR PRIDE; Q5T7B8; -.
DR ProteomicsDB; 64650; -. [Q5T7B8-1]
DR ProteomicsDB; 64651; -. [Q5T7B8-2]
DR ProteomicsDB; 64652; -. [Q5T7B8-3]
DR ProteomicsDB; 64653; -. [Q5T7B8-4]
DR Antibodypedia; 11186; 113 antibodies from 18 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 CTD; 347240; -.
DR DisGeNET; 347240; -.
DR GeneCards; KIF24; -.
DR HGNC; HGNC:19916; KIF24.
DR HPA; ENSG00000186638; Tissue enhanced (testis).
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; NLFVWIS; -.
DR OrthoDB; 418348at2759; -.
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; 9 hits in 1085 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 ventricular zone and 101 other 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 Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
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 Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF52540; SSF52540; 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
