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 10-OCT-2018, entry version 162. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF97028.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RP GLI1; GLI2; GLI3 AND SUFU, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, RP AND 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., RA Grey C., 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. RT The complete sequences of 100 new cDNA clones from brain which code RT for large 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 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 RP ASN-463 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 RT project: 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., 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 RP VARIANT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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; RP VAL-462; SER-476; TRP-477; GLN-583; CYS-660; PRO-672; TYR-767; RP ALA-816; GLN-839; VAL-840; ASP-1003; CYS-1111; GLN-1112; LYS-1138; RP SER-1185 AND PRO-1313. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Serine/threonine protein kinase which plays an important CC role in the sonic hedgehog (Shh) pathway by regulating the CC activity of GLI transcription factors (PubMed:10806483). Controls CC the activity of the transcriptional regulators GLI1, GLI2 and GLI3 CC by opposing the effect of SUFU and promoting their nuclear CC localization (PubMed:10806483). GLI2 requires an additional CC function of STK36 to become transcriptionally active, but the CC enzyme does not need to possess an active kinase catalytic site CC for this to occur (PubMed:10806483). Required for postnatal CC development, possibly by regulating the homeostasis of cerebral CC spinal fluid or ciliary function (By similarity). Essential for CC construction of the central pair apparatus of motile cilia. CC {ECO:0000250|UniProtKB:Q69ZM6, ECO:0000269|PubMed:10806483}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {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 P08151:GLI1; NbExp=2; IntAct=EBI-863797, EBI-308084; CC P10071:GLI3; NbExp=2; IntAct=EBI-863797, EBI-308055; CC Q9UMX1:SUFU; NbExp=3; IntAct=EBI-863797, EBI-740595; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10806483}. CC Nucleus {ECO:0000269|PubMed:10806483}. Note=Low levels also CC present in the 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 Note=No experimental confirmation available. {ECO:0000305}; CC -!- TISSUE SPECIFICITY: Expressed at low levels in most fetal tissues, CC adult ovaries and at high levels in adult testis, where it is CC localized in germ cells. {ECO:0000269|PubMed:10806483}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA86592.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB14184.1; Type=Frameshift; Positions=987; 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. [Q9NRP7-1] DR RefSeq; XP_016859293.1; XM_017003804.1. [Q9NRP7-2] DR UniGene; Hs.471404; -. DR UniGene; Hs.712986; -. DR ProteinModelPortal; Q9NRP7; -. DR SMR; Q9NRP7; -. DR BioGrid; 118032; 14. DR IntAct; Q9NRP7; 8. DR STRING; 9606.ENSP00000295709; -. DR BindingDB; Q9NRP7; -. DR ChEMBL; CHEMBL4312; -. DR iPTMnet; Q9NRP7; -. DR PhosphoSitePlus; Q9NRP7; -. DR BioMuta; STK36; -. DR DMDM; 90101761; -. DR EPD; Q9NRP7; -. DR MaxQB; Q9NRP7; -. DR PaxDb; Q9NRP7; -. DR PeptideAtlas; Q9NRP7; -. DR PRIDE; Q9NRP7; -. DR ProteomicsDB; 82401; -. DR ProteomicsDB; 82402; -. [Q9NRP7-2] DR DNASU; 27148; -. DR Ensembl; ENST00000295709; ENSP00000295709; ENSG00000163482. [Q9NRP7-1] DR Ensembl; ENST00000392105; ENSP00000375954; ENSG00000163482. [Q9NRP7-2] DR Ensembl; ENST00000440309; ENSP00000394095; ENSG00000163482. [Q9NRP7-1] DR GeneID; 27148; -. DR KEGG; hsa:27148; -. DR UCSC; uc002viu.4; human. [Q9NRP7-1] DR CTD; 27148; -. DR EuPathDB; HostDB:ENSG00000163482.11; -. DR GeneCards; STK36; -. DR H-InvDB; HIX0002836; -. DR HGNC; HGNC:17209; STK36. DR HPA; HPA027409; -. DR HPA; HPA027453; -. DR HPA; HPA030058; -. DR MIM; 607652; gene. DR neXtProt; NX_Q9NRP7; -. DR OpenTargets; ENSG00000163482; -. DR PharmGKB; PA38212; -. DR eggNOG; KOG0597; Eukaryota. DR eggNOG; ENOG410XRQ6; LUCA. DR GeneTree; ENSGT00910000144066; -. DR HOGENOM; HOG000015284; -. DR HOVERGEN; HBG094005; -. DR InParanoid; Q9NRP7; -. DR KO; K06228; -. DR OMA; MACGDPQ; -. DR OrthoDB; EOG091G04G9; -. DR PhylomeDB; Q9NRP7; -. DR TreeFam; TF105340; -. DR SignaLink; Q9NRP7; -. DR SIGNOR; Q9NRP7; -. DR ChiTaRS; STK36; human. DR GeneWiki; STK36; -. DR GenomeRNAi; 27148; -. DR PRO; PR:Q9NRP7; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000163482; Expressed in 163 organ(s), highest expression level in right uterine tube. DR CleanEx; HS_STK36; -. DR ExpressionAtlas; Q9NRP7; baseline and differential. DR Genevisible; Q9NRP7; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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:0004674; F:protein serine/threonine kinase activity; TAS:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB. DR GO; GO:0007420; P:brain development; IEA:Ensembl. DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB. DR GO; GO:0003351; P:epithelial cilium 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 Gene3D; 1.25.10.10; -; 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 Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF48371; SSF48371; 6. 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; Cilium biogenesis/degradation; KW Complete proteome; Cytoplasm; Developmental protein; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Polymorphism; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 1315 Serine/threonine-protein kinase 36. FT /FTId=PRO_0000229020. FT DOMAIN 4 254 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 10 18 ATP. {ECO:0000250|UniProtKB:P23647, FT ECO:0000255|PROSITE-ProRule:PRU00159}. FT ACT_SITE 125 125 Proton acceptor. FT {ECO:0000250|UniProtKB:P23647, FT ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027}. FT BINDING 33 33 ATP. FT VAR_SEQ 838 858 Missing (in isoform 2). FT {ECO:0000303|PubMed:10574462}. FT /FTId=VSP_051983. FT VARIANT 90 90 I -> M (in dbSNP:rs55706732). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041177. FT VARIANT 240 240 R -> W (in dbSNP:rs35038757). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041178. FT VARIANT 295 295 K -> R (in dbSNP:rs1863703). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041179. FT VARIANT 329 329 D -> N (in dbSNP:rs34027859). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041180. FT VARIANT 462 462 L -> V (in dbSNP:rs45586733). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041181. FT VARIANT 463 463 K -> N (in dbSNP:rs17856747). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_025727. FT VARIANT 476 476 F -> S (in dbSNP:rs34128793). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041182. FT VARIANT 477 477 R -> W (in dbSNP:rs16859180). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041183. FT VARIANT 583 583 R -> Q (in dbSNP:rs1344642). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041184. FT VARIANT 638 638 Q -> P (in dbSNP:rs6709303). FT /FTId=VAR_057112. FT VARIANT 660 660 S -> C (in a breast pleomorphic lobular FT carcinoma sample; somatic mutation; FT dbSNP:rs1244829273). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041185. FT VARIANT 672 672 L -> P (in dbSNP:rs35448374). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041186. FT VARIANT 767 767 S -> T (in dbSNP:rs17856748). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_025728. FT VARIANT 767 767 S -> Y (in an ovarian papillary serous FT adenocarcinoma sample; somatic mutation). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041187. FT VARIANT 816 816 T -> A (in dbSNP:rs34271431). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041188. FT VARIANT 839 839 R -> Q (in dbSNP:rs13023540). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041189. FT VARIANT 840 840 L -> V (in dbSNP:rs36099639). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041190. FT VARIANT 1003 1003 G -> D (in dbSNP:rs1863704). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17344846}. FT /FTId=VAR_025729. FT VARIANT 1004 1004 V -> I (in dbSNP:rs55633575). FT /FTId=VAR_061747. FT VARIANT 1111 1111 Y -> C (in dbSNP:rs56278660). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041191. FT VARIANT 1112 1112 R -> Q (in dbSNP:rs12993599). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041192. FT VARIANT 1138 1138 Q -> K (in an ovarian serous carcinoma FT sample; somatic mutation). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041193. FT VARIANT 1185 1185 P -> S (in an ovarian endometrioid FT sample; somatic mutation). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041194. FT VARIANT 1313 1313 H -> P. {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041195. FT MUTAGEN 33 33 K->R: No effect on nuclear localization FT of GLI1 or GLI2 or on GLI-mediated FT transcription. FT {ECO:0000269|PubMed:10806483}. FT CONFLICT 229 229 N -> D (in Ref. 4; AAH26158). FT {ECO:0000305}. FT CONFLICT 971 986 Missing (in Ref. 6). {ECO:0000305}. FT CONFLICT 1003 1003 G -> V (in Ref. 1; AAF97028). FT {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 //