NEK10_HUMAN
ID NEK10_HUMAN Reviewed; 1172 AA.
AC Q6ZWH5; A8MWG1; B9ZVR0; Q45VJ4; Q6ZR11; Q7Z671; Q86XB1; Q96MB3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase Nek10 {ECO:0000305};
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis A-related kinase 10;
DE Short=NimA-related protein kinase 10;
GN Name=NEK10 {ECO:0000312|HGNC:HGNC:18592};
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] (ISOFORMS 3; 4 AND 5).
RC TISSUE=Testis, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Huang B., Lin L., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-1172 (ISOFORM 2), AND VARIANT
RP SER-513.
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-50; VAL-66; SER-67; LYS-379; SER-513;
RP SER-659 AND VAL-701.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [8]
RP FUNCTION, MUTAGENESIS OF LYS-548, AND INTERACTION WITH RAF1 AND MAP2K1.
RX PubMed=20956560; DOI=10.1128/mcb.00648-10;
RA Moniz L.S., Stambolic V.;
RT "Nek10 mediates G2/M cell cycle arrest and MEK autoactivation in response
RT to UV irradiation.";
RL Mol. Cell. Biol. 31:30-42(2011).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN CILD44, MUTAGENESIS OF LYS-548
RP AND SER-684, AND VARIANTS CILD44 LEU-748 AND CYS-773.
RX PubMed=31959991; DOI=10.1038/s41591-019-0730-x;
RA Chivukula R.R., Montoro D.T., Leung H.M., Yang J., Shamseldin H.E.,
RA Taylor M.S., Dougherty G.W., Zariwala M.A., Carson J., Daniels M.L.A.,
RA Sears P.R., Black K.E., Hariri L.P., Almogarri I., Frenkel E.M.,
RA Vinarsky V., Omran H., Knowles M.R., Tearney G.J., Alkuraya F.S.,
RA Sabatini D.M.;
RT "A human ciliopathy reveals essential functions for NEK10 in airway
RT mucociliary clearance.";
RL Nat. Med. 26:244-251(2020).
CC -!- FUNCTION: Plays a role in the cellular response to UV irradiation.
CC Mediates G2/M cell cycle arrest, MEK autoactivation and ERK1/2-
CC signaling pathway activation in response to UV irradiation. In ciliated
CC cells of airways, it is involved in the regulation of mucociliary
CC transport (PubMed:31959991). {ECO:0000269|PubMed:20956560,
CC ECO:0000269|PubMed:31959991}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with RAF1 and MAP2K1; the interaction is direct with
CC RAF1 and required for ERK1/2-signaling pathway activation in response
CC to UV irradiation. {ECO:0000269|PubMed:20956560}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q6ZWH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZWH5-2; Sequence=VSP_021536, VSP_035692;
CC Name=3;
CC IsoId=Q6ZWH5-3; Sequence=VSP_021534, VSP_021535;
CC Name=4;
CC IsoId=Q6ZWH5-4; Sequence=VSP_035690, VSP_035691;
CC Name=5;
CC IsoId=Q6ZWH5-5; Sequence=VSP_035688, VSP_035689;
CC Name=6;
CC IsoId=Q6ZWH5-6; Sequence=VSP_035688, VSP_035689, VSP_035694;
CC Name=7;
CC IsoId=Q6ZWH5-7; Sequence=VSP_035688, VSP_035689, VSP_035693;
CC -!- TISSUE SPECIFICITY: Expressed in the lung.
CC {ECO:0000269|PubMed:31959991}.
CC -!- DISEASE: Ciliary dyskinesia, primary, 44 (CILD44) [MIM:618781]: A form
CC of primary ciliary dyskinesia, a disorder characterized by
CC abnormalities of motile cilia. Respiratory infections leading to
CC chronic inflammation and bronchiectasis are recurrent, due to defects
CC in the respiratory cilia. CILD44 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:31959991}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; AK057247; BAB71395.1; -; mRNA.
DR EMBL; AK123061; BAC85527.1; -; mRNA.
DR EMBL; AK128585; BAC87513.1; -; mRNA.
DR EMBL; DQ104438; AAZ20184.1; -; mRNA.
DR EMBL; AC133142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64376.1; -; Genomic_DNA.
DR EMBL; BC045758; AAH45758.1; -; mRNA.
DR EMBL; BX537852; CAD97860.1; -; mRNA.
DR CCDS; CCDS46781.1; -. [Q6ZWH5-4]
DR CCDS; CCDS77713.1; -. [Q6ZWH5-5]
DR RefSeq; NP_001026911.1; NM_001031741.3. [Q6ZWH5-6]
DR RefSeq; NP_001291313.1; NM_001304384.1. [Q6ZWH5-5]
DR RefSeq; NP_689747.3; NM_152534.4. [Q6ZWH5-1]
DR RefSeq; NP_955379.2; NM_199347.3. [Q6ZWH5-4]
DR RefSeq; XP_016861250.1; XM_017005761.1. [Q6ZWH5-1]
DR RefSeq; XP_016861251.1; XM_017005762.1. [Q6ZWH5-1]
DR RefSeq; XP_016861252.1; XM_017005763.1. [Q6ZWH5-1]
DR RefSeq; XP_016861253.1; XM_017005764.1. [Q6ZWH5-1]
DR RefSeq; XP_016861254.1; XM_017005765.1. [Q6ZWH5-1]
DR AlphaFoldDB; Q6ZWH5; -.
DR SMR; Q6ZWH5; -.
DR BioGRID; 127428; 7.
DR IntAct; Q6ZWH5; 10.
DR STRING; 9606.ENSP00000343847; -.
DR BindingDB; Q6ZWH5; -.
DR ChEMBL; CHEMBL3108655; -.
DR GlyGen; Q6ZWH5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZWH5; -.
DR PhosphoSitePlus; Q6ZWH5; -.
DR BioMuta; NEK10; -.
DR DMDM; 380865464; -.
DR EPD; Q6ZWH5; -.
DR jPOST; Q6ZWH5; -.
DR MassIVE; Q6ZWH5; -.
DR PaxDb; Q6ZWH5; -.
DR PeptideAtlas; Q6ZWH5; -.
DR PRIDE; Q6ZWH5; -.
DR ProteomicsDB; 68479; -. [Q6ZWH5-1]
DR ProteomicsDB; 68480; -. [Q6ZWH5-2]
DR ProteomicsDB; 68482; -. [Q6ZWH5-4]
DR ProteomicsDB; 68483; -. [Q6ZWH5-5]
DR ProteomicsDB; 68484; -. [Q6ZWH5-6]
DR ProteomicsDB; 68485; -. [Q6ZWH5-7]
DR Antibodypedia; 27441; 77 antibodies from 24 providers.
DR DNASU; 152110; -.
DR Ensembl; ENST00000295720.10; ENSP00000295720.6; ENSG00000163491.17. [Q6ZWH5-5]
DR Ensembl; ENST00000341435.9; ENSP00000343847.5; ENSG00000163491.17. [Q6ZWH5-4]
DR Ensembl; ENST00000383771.8; ENSP00000373281.4; ENSG00000163491.17. [Q6ZWH5-6]
DR Ensembl; ENST00000429845.6; ENSP00000395849.2; ENSG00000163491.17. [Q6ZWH5-1]
DR GeneID; 152110; -.
DR KEGG; hsa:152110; -.
DR UCSC; uc003cdt.3; human. [Q6ZWH5-1]
DR CTD; 152110; -.
DR DisGeNET; 152110; -.
DR GeneCards; NEK10; -.
DR HGNC; HGNC:18592; NEK10.
DR HPA; ENSG00000163491; Tissue enhanced (testis, tongue).
DR MalaCards; NEK10; -.
DR MIM; 618726; gene.
DR MIM; 618781; phenotype.
DR neXtProt; NX_Q6ZWH5; -.
DR OpenTargets; ENSG00000163491; -.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR PharmGKB; PA38594; -.
DR VEuPathDB; HostDB:ENSG00000163491; -.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000161037; -.
DR HOGENOM; CLU_011739_0_0_1; -.
DR InParanoid; Q6ZWH5; -.
DR OMA; VCLQLIP; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; Q6ZWH5; -.
DR TreeFam; TF336430; -.
DR PathwayCommons; Q6ZWH5; -.
DR SignaLink; Q6ZWH5; -.
DR BioGRID-ORCS; 152110; 13 hits in 1105 CRISPR screens.
DR ChiTaRS; NEK10; human.
DR GenomeRNAi; 152110; -.
DR Pharos; Q6ZWH5; Tchem.
DR PRO; PR:Q6ZWH5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6ZWH5; protein.
DR Bgee; ENSG00000163491; Expressed in olfactory segment of nasal mucosa and 112 other tissues.
DR ExpressionAtlas; Q6ZWH5; baseline and differential.
DR Genevisible; Q6ZWH5; HS.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:1902911; C:protein kinase complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0120197; P:mucociliary clearance; IMP:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:UniProtKB.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IMP:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR CDD; cd08528; STKc_Nek10; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042666; Nek10_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Ciliopathy; Coiled coil;
KW Disease variant; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Primary ciliary dyskinesia; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1172
FT /note="Serine/threonine-protein kinase Nek10"
FT /id="PRO_0000259767"
FT REPEAT 209..251
FT /note="ARM"
FT DOMAIN 519..712
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 855..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 481..514
FT /evidence="ECO:0000255"
FT COMPBIAS 909..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 655
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 525..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..688
FT /note="Missing (in isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_035688"
FT VAR_SEQ 190..218
FT /note="YIFQKLAAVKDQREWVTTSGAHKTLVNLL -> CKCYCRDTAIFVDLLEKAV
FT WCLQQETRIL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021534"
FT VAR_SEQ 219..1172
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021535"
FT VAR_SEQ 672..725
FT /note="TDFGLAKQKQENSKLTSVVGTILYSCPEVLKSEPYGEKADVWAVGCILYQMA
FT TL -> SCLKCAAPLPSLSCSCSGHIKRAGSSFAFCYHWELPDASQEANAIMVPVQPAE
FT P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021536"
FT VAR_SEQ 689..697
FT /note="VVGTILYSC -> MVPVQPAEP (in isoform 5, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_035689"
FT VAR_SEQ 698..712
FT /note="PEVLKSEPYGEKADV -> VQHLYLRSPAPALAT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035690"
FT VAR_SEQ 713..1172
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035691"
FT VAR_SEQ 726..1172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_035692"
FT VAR_SEQ 957..1013
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_035693"
FT VAR_SEQ 1004..1013
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035694"
FT VARIANT 50
FT /note="F -> L (in dbSNP:rs56125830)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040928"
FT VARIANT 66
FT /note="A -> V (in an ovarian mucinous carcinoma sample;
FT somatic mutation; dbSNP:rs201821707)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040929"
FT VARIANT 67
FT /note="G -> S (in dbSNP:rs55958314)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040930"
FT VARIANT 379
FT /note="E -> K (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040931"
FT VARIANT 513
FT /note="L -> S (in dbSNP:rs10510592)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_040932"
FT VARIANT 659
FT /note="N -> S (in dbSNP:rs55833401)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040933"
FT VARIANT 701
FT /note="L -> V (in dbSNP:rs34313679)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040934"
FT VARIANT 748
FT /note="P -> L (in CILD44; unknown pathological
FT significance; dbSNP:rs1575215909)"
FT /evidence="ECO:0000269|PubMed:31959991"
FT /id="VAR_083827"
FT VARIANT 773
FT /note="R -> C (in CILD44; unknown pathological
FT significance; dbSNP:rs766982731)"
FT /evidence="ECO:0000269|PubMed:31959991"
FT /id="VAR_083828"
FT MUTAGEN 548
FT /note="K->R: Catalytically inactive. Impaired mucociliary
FT transport."
FT /evidence="ECO:0000269|PubMed:20956560,
FT ECO:0000269|PubMed:31959991"
FT MUTAGEN 684
FT /note="S->D: Increased mucociliary transport."
FT /evidence="ECO:0000269|PubMed:31959991"
FT CONFLICT 239
FT /note="S -> G (in Ref. 6; CAD97860)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="I -> F (in Ref. 2; AAZ20184)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="T -> A (in Ref. 2; AAZ20184)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="S -> P (in Ref. 2; AAZ20184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1172 AA; 133259 MW; 28D76407922020C8 CRC64;
MPDQDKKVKT TEKSTDKQQE ITIRDYSDLK RLRCLLNVQS SKQQLPAINF DSAQNSMTKS
EPAIRAGGHR ARGQWHESTE AVELENFSIN YKNERNFSKH PQRKLFQEIF TALVKNRLIS
REWVNRAPSI HFLRVLICLR LLMRDPCYQE ILHSLGGIEN LAQYMEIVAN EYLGYGEEQH
TVDKLVNMTY IFQKLAAVKD QREWVTTSGA HKTLVNLLGA RDTNVLLGSL LALASLAESQ
ECREKISELN IVENLLMILH EYDLLSKRLT AELLRLLCAE PQVKEQVKLY EGIPVLLSLL
HSDHLKLLWS IVWILVQVCE DPETSVEIRI WGGIKQLLHI LQGDRNFVSD HSSIGSLSSA
NAAGRIQQLH LSEDLSPREI QENTFSLQAA CCAALTELVL NDTNAHQVVQ ENGVYTIAKL
ILPNKQKNAA KSNLLQCYAF RALRFLFSME RNRPLFKRLF PTDLFEIFID IGHYVRDISA
YEELVSKLNL LVEDELKQIA ENIESINQNK APLKYIGNYA ILDHLGSGAF GCVYKVRKHS
GQNLLAMKEV NLHNPAFGKD KKDRDSSVRN IVSELTIIKE QLYHPNIVRY YKTFLENDRL
YIVMELIEGA PLGEHFSSLK EKHHHFTEER LWKIFIQLCL ALRYLHKEKR IVHRDLTPNN
IMLGDKDKVT VTDFGLAKQK QENSKLTSVV GTILYSCPEV LKSEPYGEKA DVWAVGCILY
QMATLSPPFY STNMLSLATK IVEAVYEPVP EGIYSEKVTD TISRCLTPDA EARPDIVEVS
SMISDVMMKY LDNLSTSQLS LEKKLERERR RTQRYFMEAN RNTVTCHHEL AVLSHETFEK
ASLSSSSSGA ASLKSELSES ADLPPEGFQA SYGKDEDRAC DEILSDDNFN LENAEKDTYS
EVDDELDISD NSSSSSSSPL KESTFNILKR SFSASGGERQ SQTRDFTGGT GSRPRPALLP
LDLLLKVPPH MLRAHIKEIE AELVTGWQSH SLPAVILRNL KDHGPQMGTF LWQASAGIAV
SQRKVRQISD PIQQILIQLH KIIYITQLPP ALHHNLKRRV IERFKKSLFS QQSNPCNLKS
EIKKLSQGSP EPIEPNFFTA DYHLLHRSSG GNSLSPNDPT GLPTSIELEE GITYEQMQTV
IEEVLEESGY YNFTSNRYHS YPWGTKNHPT KR
