STK36_HUMAN
ID STK36_HUMAN Reviewed; 1315 AA.
AC Q9NRP7; B7WPM3; Q8TC32; Q9H9N9; Q9UF35; Q9ULE2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Serine/threonine-protein kinase 36;
DE EC=2.7.11.1;
DE AltName: Full=Fused homolog;
GN Name=STK36 {ECO:0000312|EMBL:AAH26158.1};
GN Synonyms=KIAA1278 {ECO:0000312|EMBL:BAA86592.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAF97028.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GLI1;
RP GLI2; GLI3 AND SUFU, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-33.
RX PubMed=10806483; DOI=10.1038/35010610;
RA Murone M., Luoh S.-L., Stone D., Li W., Gurney A., Armanini M., Grey C.,
RA Rosenthal A., de Sauvage F.J.;
RT "Gli regulation by the opposing activities of fused and suppressor of
RT fused.";
RL Nat. Cell Biol. 2:310-312(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA86592.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAA86592.1};
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH26158.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-463
RP AND THR-767.
RC TISSUE=Testis {ECO:0000312|EMBL:AAH26158.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 823-1315 (ISOFORM 1).
RC TISSUE=Testis;
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 [6] {ECO:0000305, ECO:0000312|EMBL:BAB14184.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 839-1315 (ISOFORM 1), AND VARIANT
RP ASP-1003.
RC TISSUE=Teratocarcinoma {ECO:0000312|EMBL:BAB14184.1};
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 [7]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-90; TRP-240; ARG-295; ASN-329; VAL-462;
RP SER-476; TRP-477; GLN-583; CYS-660; PRO-672; TYR-767; ALA-816; GLN-839;
RP VAL-840; ASP-1003; CYS-1111; GLN-1112; LYS-1138; SER-1185 AND PRO-1313.
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 INVOLVEMENT IN CILD46, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=28543983; DOI=10.1002/humu.23261;
RA Edelbusch C., Cindric S., Dougherty G.W., Loges N.T., Olbrich H.,
RA Rivlin J., Wallmeier J., Pennekamp P., Amirav I., Omran H.;
RT "Mutation of serine/threonine protein kinase 36 (STK36) causes primary
RT ciliary dyskinesia with a central pair defect.";
RL Hum. Mutat. 38:964-969(2017).
CC -!- FUNCTION: Serine/threonine protein kinase which plays an important role
CC in the sonic hedgehog (Shh) pathway by regulating the activity of GLI
CC transcription factors (PubMed:10806483). Controls the activity of the
CC transcriptional regulators GLI1, GLI2 and GLI3 by opposing the effect
CC of SUFU and promoting their nuclear localization (PubMed:10806483).
CC GLI2 requires an additional function of STK36 to become
CC transcriptionally active, but the enzyme does not need to possess an
CC active kinase catalytic site for this to occur (PubMed:10806483).
CC Required for postnatal development, possibly by regulating the
CC homeostasis of cerebral spinal fluid or ciliary function. Essential for
CC construction of the central pair apparatus of motile cilia.
CC {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:28543983}.
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 Evidence={ECO:0000250|UniProtKB:P23647};
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; Evidence={ECO:0000250|UniProtKB:P23647};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with GLI1, GLI2 and GLI3 (PubMed:10806483).
CC Interacts with SPAG16 and KIF27. {ECO:0000250|UniProtKB:Q69ZM6,
CC ECO:0000269|PubMed:10806483}.
CC -!- INTERACTION:
CC Q9NRP7; P54252: ATXN3; NbExp=3; IntAct=EBI-863797, EBI-946046;
CC Q9NRP7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-863797, EBI-10976677;
CC Q9NRP7; P14136: GFAP; NbExp=3; IntAct=EBI-863797, EBI-744302;
CC Q9NRP7; O14901: KLF11; NbExp=3; IntAct=EBI-863797, EBI-948266;
CC Q9NRP7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-863797, EBI-5235340;
CC Q9NRP7; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-863797, EBI-740595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10806483}. Nucleus
CC {ECO:0000269|PubMed:10806483}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:28543983}. Note=Low levels also present in the
CC nucleus. {ECO:0000269|PubMed:10806483}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:14702039,
CC ECO:0000269|PubMed:15489334};
CC IsoId=Q9NRP7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10574462};
CC IsoId=Q9NRP7-2; Sequence=VSP_051983;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in most fetal tissues,
CC adult ovaries and at high levels in adult testis, where it is localized
CC in germ cells (PubMed:10806483). Expressed in respiratory epithelial
CC cells of the lung (PubMed:28543983). {ECO:0000269|PubMed:10806483,
CC ECO:0000269|PubMed:28543983}.
CC -!- DISEASE: Ciliary dyskinesia, primary, 46 (CILD46) [MIM:619436]: 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. CILD46 is an autosomal recessive form. No
CC situs abnormalities have been observed. {ECO:0000269|PubMed:28543983}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86592.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14184.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF200815; AAF97028.1; -; mRNA.
DR EMBL; AB033104; BAA86592.1; ALT_INIT; mRNA.
DR EMBL; AC009974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026158; AAH26158.1; -; mRNA.
DR EMBL; AL133630; CAB63754.1; -; mRNA.
DR EMBL; AK022692; BAB14184.1; ALT_FRAME; mRNA.
DR CCDS; CCDS2421.1; -. [Q9NRP7-1]
DR CCDS; CCDS58750.1; -. [Q9NRP7-2]
DR PIR; T43465; T43465.
DR RefSeq; NP_001230242.1; NM_001243313.1. [Q9NRP7-2]
DR RefSeq; NP_056505.2; NM_015690.4. [Q9NRP7-1]
DR RefSeq; XP_005246521.1; XM_005246464.1.
DR RefSeq; XP_016859293.1; XM_017003804.1. [Q9NRP7-2]
DR AlphaFoldDB; Q9NRP7; -.
DR SMR; Q9NRP7; -.
DR BioGRID; 118032; 31.
DR IntAct; Q9NRP7; 26.
DR STRING; 9606.ENSP00000295709; -.
DR BindingDB; Q9NRP7; -.
DR ChEMBL; CHEMBL4312; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9NRP7; -.
DR iPTMnet; Q9NRP7; -.
DR PhosphoSitePlus; Q9NRP7; -.
DR BioMuta; STK36; -.
DR DMDM; 90101761; -.
DR EPD; Q9NRP7; -.
DR jPOST; Q9NRP7; -.
DR MassIVE; Q9NRP7; -.
DR MaxQB; Q9NRP7; -.
DR PaxDb; Q9NRP7; -.
DR PeptideAtlas; Q9NRP7; -.
DR PRIDE; Q9NRP7; -.
DR ProteomicsDB; 82401; -. [Q9NRP7-1]
DR ProteomicsDB; 82402; -. [Q9NRP7-2]
DR Antibodypedia; 34284; 186 antibodies from 29 providers.
DR DNASU; 27148; -.
DR Ensembl; ENST00000295709.8; ENSP00000295709.3; ENSG00000163482.12. [Q9NRP7-1]
DR Ensembl; ENST00000392105.7; ENSP00000375954.3; ENSG00000163482.12. [Q9NRP7-2]
DR Ensembl; ENST00000440309.5; ENSP00000394095.1; ENSG00000163482.12. [Q9NRP7-1]
DR GeneID; 27148; -.
DR KEGG; hsa:27148; -.
DR MANE-Select; ENST00000295709.8; ENSP00000295709.3; NM_015690.5; NP_056505.2.
DR UCSC; uc002viu.4; human. [Q9NRP7-1]
DR CTD; 27148; -.
DR DisGeNET; 27148; -.
DR GeneCards; STK36; -.
DR HGNC; HGNC:17209; STK36.
DR HPA; ENSG00000163482; Low tissue specificity.
DR MalaCards; STK36; -.
DR MIM; 607652; gene.
DR MIM; 619436; phenotype.
DR neXtProt; NX_Q9NRP7; -.
DR OpenTargets; ENSG00000163482; -.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR PharmGKB; PA38212; -.
DR VEuPathDB; HostDB:ENSG00000163482; -.
DR eggNOG; KOG0597; Eukaryota.
DR GeneTree; ENSGT00940000158375; -.
DR HOGENOM; CLU_002453_2_0_1; -.
DR InParanoid; Q9NRP7; -.
DR OMA; LCPSFLH; -.
DR PhylomeDB; Q9NRP7; -.
DR TreeFam; TF105340; -.
DR PathwayCommons; Q9NRP7; -.
DR SignaLink; Q9NRP7; -.
DR SIGNOR; Q9NRP7; -.
DR BioGRID-ORCS; 27148; 6 hits in 1109 CRISPR screens.
DR ChiTaRS; STK36; human.
DR GeneWiki; STK36; -.
DR GenomeRNAi; 27148; -.
DR Pharos; Q9NRP7; Tbio.
DR PRO; PR:Q9NRP7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NRP7; protein.
DR Bgee; ENSG00000163482; Expressed in right uterine tube and 144 other tissues.
DR ExpressionAtlas; Q9NRP7; baseline and differential.
DR Genevisible; Q9NRP7; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:FlyBase.
DR GO; GO:0001222; F:transcription corepressor binding; IDA:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IEA:Ensembl.
DR GO; GO:0007228; P:positive regulation of hh target transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:FlyBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045193; Fused-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22983; PTHR22983; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Ciliopathy;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Developmental protein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Primary ciliary dyskinesia;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1315
FT /note="Serine/threonine-protein kinase 36"
FT /id="PRO_0000229020"
FT DOMAIN 4..254
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 312..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P23647,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23647,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT VAR_SEQ 838..858
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574462"
FT /id="VSP_051983"
FT VARIANT 90
FT /note="I -> M (in dbSNP:rs55706732)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041177"
FT VARIANT 240
FT /note="R -> W (in dbSNP:rs35038757)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041178"
FT VARIANT 295
FT /note="K -> R (in dbSNP:rs1863703)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041179"
FT VARIANT 329
FT /note="D -> N (in dbSNP:rs34027859)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041180"
FT VARIANT 462
FT /note="L -> V (in dbSNP:rs45586733)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041181"
FT VARIANT 463
FT /note="K -> N (in dbSNP:rs17856747)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025727"
FT VARIANT 476
FT /note="F -> S (in dbSNP:rs34128793)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041182"
FT VARIANT 477
FT /note="R -> W (in dbSNP:rs16859180)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041183"
FT VARIANT 583
FT /note="R -> Q (in dbSNP:rs1344642)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041184"
FT VARIANT 638
FT /note="Q -> P (in dbSNP:rs6709303)"
FT /id="VAR_057112"
FT VARIANT 660
FT /note="S -> C (in a breast pleomorphic lobular carcinoma
FT sample; somatic mutation; dbSNP:rs1244829273)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041185"
FT VARIANT 672
FT /note="L -> P (in dbSNP:rs35448374)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041186"
FT VARIANT 767
FT /note="S -> T (in dbSNP:rs17856748)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025728"
FT VARIANT 767
FT /note="S -> Y (in an ovarian papillary serous
FT adenocarcinoma sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041187"
FT VARIANT 816
FT /note="T -> A (in dbSNP:rs34271431)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041188"
FT VARIANT 839
FT /note="R -> Q (in dbSNP:rs13023540)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041189"
FT VARIANT 840
FT /note="L -> V (in dbSNP:rs36099639)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041190"
FT VARIANT 1003
FT /note="G -> D (in dbSNP:rs1863704)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_025729"
FT VARIANT 1004
FT /note="V -> I (in dbSNP:rs55633575)"
FT /id="VAR_061747"
FT VARIANT 1111
FT /note="Y -> C (in dbSNP:rs56278660)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041191"
FT VARIANT 1112
FT /note="R -> Q (in dbSNP:rs12993599)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041192"
FT VARIANT 1138
FT /note="Q -> K (in an ovarian serous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041193"
FT VARIANT 1185
FT /note="P -> S (in an ovarian endometrioid sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041194"
FT VARIANT 1313
FT /note="H -> P"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041195"
FT MUTAGEN 33
FT /note="K->R: No effect on nuclear localization of GLI1 or
FT GLI2 or on GLI-mediated transcription."
FT /evidence="ECO:0000269|PubMed:10806483"
FT CONFLICT 229
FT /note="N -> D (in Ref. 4; AAH26158)"
FT /evidence="ECO:0000305"
FT CONFLICT 971..986
FT /note="Missing (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003
FT /note="G -> V (in Ref. 1; AAF97028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1315 AA; 143995 MW; 793F4638F1871C01 CRC64;
MEKYHVLEMI GEGSFGRVYK GRRKYSAQVV ALKFIPKLGR SEKELRNLQR EIEIMRGLRH
PNIVHMLDSF ETDKEVVVVT DYAEGELFQI LEDDGKLPED QVQAIAAQLV SALYYLHSHR
ILHRDMKPQN ILLAKGGGIK LCDFGFARAM STNTMVLTSI KGTPLYMSPE LVEERPYDHT
ADLWSVGCIL YELAVGTPPF YATSIFQLVS LILKDPVRWP STISPCFKNF LQGLLTKDPR
QRLSWPDLLY HPFIAGHVTI ITEPAGPDLG TPFTSRLPPE LQVLKDEQAH RLAPKGNQSR
ILTQAYKRMA EEAMQKKHQN TGPALEQEDK TSKVAPGTAP LPRLGATPQE SSLLAGILAS
ELKSSWAKSG TGEVPSAPRE NRTTPDCERA FPEERPEVLG QRSTDVVDLE NEEPDSDNEW
QHLLETTEPV PIQLKAPLTL LCNPDFCQRI QSQLHEAGGQ ILKGILEGAS HILPAFRVLS
SLLSSCSDSV ALYSFCREAG LPGLLLSLLR HSQESNSLQQ QSWYGTFLQD LMAVIQAYFA
CTFNLERSQT SDSLQVFQEA ANLFLDLLGK LLAQPDDSEQ TLRRDSLMCF TVLCEAMDGN
SRAISKAFYS SLLTTQQVVL DGLLHGLTVP QLPVHTPQGA PQVSQPLREQ SEDIPGAISS
ALAAICTAPV GLPDCWDAKE QVCWHLANQL TEDSSQLRPS LISGLQHPIL CLHLLKVLYS
CCLVSEGLCR LLGQEPLALE SLFMLIQGKV KVVDWEESTE VTLYFLSLLV FRLQNLPCGM
EKLGSDVATL FTHSHVVSLV SAAACLLGQL GQQGVTFDLQ PMEWMAAATH ALSAPAEVRL
TPPGSCGFYD GLLILLLQLL TEQGKASLIR DMSSSEMWTV LWHRFSMVLR LPEEASAQEG
ELSLSSPPSP EPDWTLISPQ GMAALLSLAM ATFTQEPQLC LSCLSQHGSI LMSILKHLLC
PSFLNQLRQA PHGSEFLPVV VLSVCQLLCF PFALDMDADL LIGVLADLRD SEVAAHLLQV
CCYHLPLMQV ELPISLLTRL ALMDPTSLNQ FVNTVSASPR TIVSFLSVAL LSDQPLLTSD
LLSLLAHTAR VLSPSHLSFI QELLAGSDES YRPLRSLLGH PENSVRAHTY RLLGHLLQHS
MALRGALQSQ SGLLSLLLLG LGDKDPVVRC SASFAVGNAA YQAGPLGPAL AAAVPSMTQL
LGDPQAGIRR NVASALGNLG PEGLGEELLQ CEVPQRLLEM ACGDPQPNVK EAALIALRSL
QQEPGIHQVL VSLGASEKLS LLSLGNQSLP HSSPRPASAK HCRKLIHLLR PAHSM
