STK36_MOUSE
ID STK36_MOUSE Reviewed; 1316 AA.
AC Q69ZM6; Q6PDI0; Q80XQ6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Serine/threonine-protein kinase 36;
DE EC=2.7.11.1;
DE AltName: Full=Fused homolog;
GN Name=Stk36 {ECO:0000312|MGI:MGI:1920831}; Synonyms=Kiaa1278;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18600476; DOI=10.1007/s12079-007-0014-y;
RA Maloveryan A., Finta C., Osterlund T., Kogerman P.;
RT "A possible role of mouse Fused (STK36) in Hedgehog signaling and Gli
RT transcription factor regulation.";
RL J. Cell Commun. Signal. 1:165-173(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD32420.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD32420.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH58698.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH58698.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH58698.1};
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] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
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 [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16055717; DOI=10.1128/mcb.25.16.7054-7068.2005;
RA Merchant M., Evangelista M., Luoh S.-M., Frantz G.D., Chalasani S.,
RA Carano R.A., van Hoy M., Ramirez J., Ogasawara A.K., McFarland L.M.,
RA Filvaroff E.H., French D.M., de Sauvage F.J.;
RT "Loss of the serine/threonine kinase fused results in postnatal growth
RT defects and lethality due to progressive hydrocephalus.";
RL Mol. Cell. Biol. 25:7054-7068(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPAG16 AND KIF27.
RX PubMed=19305393; DOI=10.1038/nature07883;
RA Wilson C.W., Nguyen C.T., Chen M.H., Yang J.H., Gacayan R., Huang J.,
RA Chen J.N., Chuang P.T.;
RT "Fused has evolved divergent roles in vertebrate Hedgehog signalling and
RT motile ciliogenesis.";
RL Nature 459:98-102(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Controls the activity of the transcriptional
CC regulators GLI1, GLI2 and GLI3 by opposing the effect of SUFU and
CC promoting their nuclear localization. GLI2 requires an additional
CC function of STK36 to become transcriptionally active, but the enzyme
CC does not need to possess an active kinase catalytic site for this to
CC occur. 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:16055717, ECO:0000269|PubMed:18600476,
CC ECO:0000269|PubMed:19305393}.
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 SPAG16 and KIF27.
CC {ECO:0000269|PubMed:19305393}.
CC -!- INTERACTION:
CC Q69ZM6; Q7M6Z4: Kif27; NbExp=2; IntAct=EBI-15765145, EBI-15765182;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19305393}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NRP7}. Cytoplasm, cytoskeleton, cilium
CC axoneme. Note=Low levels also present in the nucleus.
CC {ECO:0000250|UniProtKB:Q9NRP7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15368895};
CC IsoId=Q69ZM6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q69ZM6-2; Sequence=VSP_040760, VSP_040762, VSP_040763;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q69ZM6-3; Sequence=VSP_040761;
CC -!- TISSUE SPECIFICITY: Weakly expressed in the heart and thymus, present
CC at moderate to high levels in the lungs, pancreas, and kidneys and at
CC higher levels in the brain and cerebellum. Very highly expressed in the
CC testis. {ECO:0000269|PubMed:16055717, ECO:0000269|PubMed:18600476}.
CC -!- DEVELOPMENTAL STAGE: At 13.5 dpc is widely distributed in the
CC forebrain, midbrain, hindbrain, spinal cord, somites, developing limb
CC buds and skin. {ECO:0000269|PubMed:10806483}.
CC -!- DISRUPTION PHENOTYPE: Mice display profound growth retardation with a
CC communicating form of hydrocephalus, nasal inflammation and early
CC mortality. {ECO:0000269|PubMed:16055717}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43103.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAD32420.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK173142; BAD32420.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AC117610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043103; AAH43103.1; ALT_SEQ; mRNA.
DR EMBL; BC058698; AAH58698.1; -; mRNA.
DR CCDS; CCDS35619.1; -. [Q69ZM6-1]
DR RefSeq; NP_778196.2; NM_175031.3. [Q69ZM6-1]
DR AlphaFoldDB; Q69ZM6; -.
DR SMR; Q69ZM6; -.
DR BioGRID; 234622; 3.
DR DIP; DIP-59751N; -.
DR IntAct; Q69ZM6; 2.
DR STRING; 10090.ENSMUSP00000084430; -.
DR iPTMnet; Q69ZM6; -.
DR PhosphoSitePlus; Q69ZM6; -.
DR MaxQB; Q69ZM6; -.
DR PaxDb; Q69ZM6; -.
DR PRIDE; Q69ZM6; -.
DR ProteomicsDB; 258758; -. [Q69ZM6-1]
DR ProteomicsDB; 258759; -. [Q69ZM6-2]
DR ProteomicsDB; 258760; -. [Q69ZM6-3]
DR Antibodypedia; 34284; 186 antibodies from 29 providers.
DR DNASU; 269209; -.
DR Ensembl; ENSMUST00000087183; ENSMUSP00000084430; ENSMUSG00000033276. [Q69ZM6-1]
DR Ensembl; ENSMUST00000087186; ENSMUSP00000084433; ENSMUSG00000033276. [Q69ZM6-3]
DR GeneID; 269209; -.
DR KEGG; mmu:269209; -.
DR UCSC; uc007bmu.1; mouse. [Q69ZM6-1]
DR UCSC; uc011wnc.1; mouse. [Q69ZM6-3]
DR CTD; 27148; -.
DR MGI; MGI:1920831; Stk36.
DR VEuPathDB; HostDB:ENSMUSG00000033276; -.
DR eggNOG; KOG0597; Eukaryota.
DR GeneTree; ENSGT00940000158375; -.
DR HOGENOM; CLU_002453_2_0_1; -.
DR InParanoid; Q69ZM6; -.
DR OrthoDB; 979202at2759; -.
DR PhylomeDB; Q69ZM6; -.
DR TreeFam; TF105340; -.
DR BioGRID-ORCS; 269209; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q69ZM6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q69ZM6; protein.
DR Bgee; ENSMUSG00000033276; Expressed in gastrula and 118 other tissues.
DR ExpressionAtlas; Q69ZM6; baseline and differential.
DR Genevisible; Q69ZM6; MM.
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; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISS:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IDA:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0007228; P:positive regulation of hh target transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; ISO:MGI.
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;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Developmental protein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1316
FT /note="Serine/threonine-protein kinase 36"
FT /id="PRO_0000229021"
FT DOMAIN 4..254
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 389..418
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 /evidence="ECO:0000250|UniProtKB:P23647,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 225..260
FT /note="SCFKNFLQGLLTKDPRQRLSWPDLLHHPFIAGRVTI -> V (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_040760"
FT VAR_SEQ 461..588
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040761"
FT VAR_SEQ 862..864
FT /note="QVQ -> Q (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_040762"
FT VAR_SEQ 1021..1032
FT /note="VCCHHLSLLQAE -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_040763"
FT CONFLICT 330
FT /note="G -> R (in Ref. 2; BAD32420)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="H -> Y (in Ref. 2; BAD32420)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="Y -> C (in Ref. 2; BAD32420)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="V -> A (in Ref. 2; BAD32420)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="I -> T (in Ref. 2; BAD32420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1316 AA; 144180 MW; 30ED81B0E9694270 CRC64;
MEKYHVLEMI GEGSFGRVYK GRKKYSAQVV ALKFIPKLGR SEKELRNLQR EIEIMRGLWH
PNIVHMLDSF ETDKEVVVVT DYAEGELFQI LEDDGKLPED QVQAIAAQLV SALYYLHSHR
ILHRDMKPQN ILLAKGGGIK LCDFGFARAM STNTMVLTSI KGTPLYMSPE LVEERPYDHT
ADLWSVGCIL YELAVGTPPF YTTSIFQLVS LILKDPVRWP STISSCFKNF LQGLLTKDPR
QRLSWPDLLH HPFIAGRVTI ITEPAGSDLG TPFTSRLPPE LQVLKDEQAH RLAPKGNQSR
ILRQACKLMA EEAKQKEDQN AGSALEQEDG LCKVTPSTAP VPGLKATPQE SSLLAGILAS
EMKNNWEDWG AGEAPRTSRE NHINLECEQG FPEPRPEAMG RQSTDVVDPE NEEPDSDDEW
QRLLETSEPG PVQLKSPLTL LCNPDFCQRI QSQLRGTGEQ ILKGVLDGVS HLLPVLRILS
SLLSSCNDSV LLYSFCQEAG LPELPLSLLR YSQESSSIQQ QPWYGALLRD LVAVVQAYFS
CTFNLERSQT GDSLQVFQEA ASLFLDLLGK LLAQSDDSEQ TFRRDSLMCF AVLCEAVDGN
SWAVSKAFYS SLLTTQRAVL DGLLHGLTVP QLPFHTPPGA PQVSQPLREQ SEDVPGAISS
ALAAMCTAPV GLPSCWDAKE QVSWHLANQL TEDSSQLRPS LISGLRHHVL CLHLLKVLYA
CCYISERLCH ILGQEPLALE SLLMLVQGKV KVADWEESTE VALYLLSLLV FRLQDLPSGM
EKLGSEVATL FTHSHVVSLV NAAACLLGQL GQQGVTFDLQ PREWIAAAAH ALSAPAEVRL
TPPYSCGFYD GLLILLLQLL MQVQGKPGLI RDVVGSEVWT ILWHRFSMAL RLPEEVSAQE
DDLLLSSPSS LEPDWTLISP QGMAALLSLA MAIFTQESQL CLSHLSQHGS VLMLTLKHLL
SPSFLHHLSQ APQGPEFLPV VVLSVCKLLC FPFALDVDAD LLVGVLADLR ASEVVVCLLQ
VCCHHLSLLQ AELPIGLLTR LALTDSASLK QFVNTVATSS RAIISFLSVV LLSDQPLMIS
DLLSLLTHTA RILSPSHLSF IQELLSGSDE SYRPLRSLLG HSENTVRVRA YGLLGHLLQH
SMALRGALQS QSGLLNLLLL GLGDKDPAVR RSASFAVGNA AYQAGPLGPA LAAAVPSMTQ
LLGDAQDGIR RNAASALGNL GPEGLGKELL KCQVPQRLLE MACGDPQPTV KEAALIALRS
LQQESCIHQV LVSLGASEKL ALLSLGNQLL PNSSNRPASV RHCRKLIQLL RPTHST
