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 27-MAR-2024, entry version 195. 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}; 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; 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. DR AlphaFoldDB; Q9NRP7; -. DR SMR; Q9NRP7; -. DR BioGRID; 118032; 43. DR IntAct; Q9NRP7; 24. 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; 9606-ENSP00000295709; -. DR PeptideAtlas; Q9NRP7; -. DR ProteomicsDB; 82401; -. [Q9NRP7-1] DR ProteomicsDB; 82402; -. [Q9NRP7-2] DR Antibodypedia; 34284; 229 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 AGR; HGNC:17209; -. 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 OrthoDB; 275383at2759; -. DR PhylomeDB; Q9NRP7; -. DR TreeFam; TF105340; -. DR PathwayCommons; Q9NRP7; -. DR SignaLink; Q9NRP7; -. DR SIGNOR; Q9NRP7; -. DR BioGRID-ORCS; 27148; 6 hits in 1185 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 146 other cell types or tissues. DR ExpressionAtlas; Q9NRP7; baseline and differential. 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 CDD; cd14002; STKc_STK36; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. 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; PROTEIN KINASE RELATED; 1. DR PANTHER; PTHR22983:SF6; SERINE_THREONINE-PROTEIN KINASE 36; 1. DR Pfam; PF13646; HEAT_2; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF48371; ARM repeat; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q9NRP7; HS. 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 //