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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
 
 
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