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Protein kinase shaggy (EC 2.7.11.1) (Protein zeste-white 3)

 SGG_DROME               Reviewed;         514 AA.
P18431; O76881; P23646; Q27603; Q27604; Q27605; Q8MRF7; Q9NF42;
Q9U094; Q9W4X3;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
05-SEP-2012, sequence version 3.
12-SEP-2018, entry version 211.
RecName: Full=Protein kinase shaggy;
EC=2.7.11.1;
AltName: Full=Protein zeste-white 3;
Name=sgg; Synonyms=gsk3, zw3; ORFNames=CG2621;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZYGOTIC), FUNCTION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=DP CN BW; TISSUE=Embryo;
PubMed=2118107;
Bourouis M., Moore P., Ruel L., Grau Y., Heitzler P., Simpson P.;
"An early embryonic product of the gene shaggy encodes a
serine/threonine protein kinase related to the CDC28/cdc2+
subfamily.";
EMBO J. 9:2877-2884(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SGG39; SGG46 AND ZYGOTIC),
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Embryo;
PubMed=8467811;
Ruel L., Pantesco V., Lutz Y., Simpson P., Bourouis M.;
"Functional significance of a family of protein kinases encoded at the
shaggy locus in Drosophila.";
EMBO J. 12:1657-1669(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R;
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS G AND ZYGOTIC).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-289 (ISOFORM ZYGOTIC/SGG39),
NUCLEOTIDE SEQUENCE [MRNA] OF 30-514 (ISOFORM SGG46), AND FUNCTION.
TISSUE=Embryo, and Ovary;
PubMed=2113617; DOI=10.1038/345825a0;
Siegfried E., Perkins L.A., Capaci T.M., Perrimon N.;
"Putative protein kinase product of the Drosophila segment-polarity
gene zeste-white3.";
Nature 345:825-829(1990).
[8]
PHOSPHORYLATION AT TYR-214.
PubMed=8382613;
Hughes K., Nikolakaki E., Plyte S.E., Totty N.F., Woodgett J.R.;
"Modulation of the glycogen synthase kinase-3 family by tyrosine
phosphorylation.";
EMBO J. 12:803-808(1993).
[9]
FUNCTION IN PHOSPHORYLATION OF ARM.
PubMed=7529201; DOI=10.1006/dbio.1994.1336;
Peifer M., Pai L.-M., Casey M.;
"Phosphorylation of the Drosophila adherens junction protein
Armadillo: roles for wingless signal and zeste-white 3 kinase.";
Dev. Biol. 166:543-556(1994).
[10]
INTERACTION WITH WG AND EN.
TISSUE=Embryo;
PubMed=1335365; DOI=10.1016/S0092-8674(05)80065-0;
Siegfried E., Chou T.B., Perrimon N.;
"wingless signaling acts through zeste-white 3, the Drosophila homolog
of glycogen synthase kinase-3, to regulate engrailed and establish
cell fate.";
Cell 71:1167-1179(1992).
[11]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF ALA-81.
PubMed=15269269; DOI=10.1523/JNEUROSCI.1580-04.2004;
Franco B., Bogdanik L., Bobinnec Y., Debec A., Bockaert J.,
Parmentier M.L., Grau Y.;
"Shaggy, the homolog of glycogen synthase kinase 3, controls
neuromuscular junction growth in Drosophila.";
J. Neurosci. 24:6573-6577(2004).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH COS.
PubMed=15691767; DOI=10.1016/j.devcel.2005.01.001;
Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.;
"Hedgehog-regulated Costal2-kinase complexes control phosphorylation
and proteolytic processing of Cubitus interruptus.";
Dev. Cell 8:267-278(2005).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16570248; DOI=10.1002/cm.20128;
Bobinnec Y., Morin X., Debec A.;
"Shaggy/GSK-3beta kinase localizes to the centrosome and to
specialized cytoskeletal structures in Drosophila.";
Cell Motil. Cytoskeleton 63:313-320(2006).
[14]
FUNCTION IN PHOSPHORYLATION OF FUTSCH.
PubMed=16949836; DOI=10.1016/j.mcn.2006.07.004;
Gogel S., Wakefield S., Tear G., Klambt C., Gordon-Weeks P.R.;
"The Drosophila microtubule associated protein Futsch is
phosphorylated by Shaggy/Zeste-white 3 at an homologous GSK3beta
phosphorylation site in MAP1B.";
Mol. Cell. Neurosci. 33:188-199(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; TYR-214 AND
SER-217, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[16]
FUNCTION IN PHOSPHORYLATION OF SRA, AND TISSUE SPECIFICITY.
PubMed=22421435; DOI=10.1073/pnas.1120367109;
Takeo S., Swanson S.K., Nandanan K., Nakai Y., Aigaki T.,
Washburn M.P., Florens L., Hawley R.S.;
"Shaggy/glycogen synthase kinase 3beta and phosphorylation of
Sarah/regulator of calcineurin are essential for completion of
Drosophila female meiosis.";
Proc. Natl. Acad. Sci. U.S.A. 109:6382-6389(2012).
-!- FUNCTION: Required for several developmental events such as
syncytial blastoderm formation and embryonic segmentation. Is
involved in transcriptional regulation. Required for arm
phosphorylation. Wg signaling operates by inactivating the sgg
repression of en autoactivation. Negatively controls the
neuromuscular junction (NMJ) growth in presynaptic motoneurons.
Plays a role in the regulation of microtubule dynamics and actin
cytoskeleton during embryogenesis. Required for phosphorylation of
sra in activated eggs. Essential for completion of meiosis,
possibly by triggering calcineurin activation via sra
phosphorylation. Phosphorylates microtubule-associated protein
futsch in axons. {ECO:0000269|PubMed:15269269,
ECO:0000269|PubMed:16570248, ECO:0000269|PubMed:16949836,
ECO:0000269|PubMed:2113617, ECO:0000269|PubMed:2118107,
ECO:0000269|PubMed:22421435, ECO:0000269|PubMed:7529201,
ECO:0000269|PubMed:8467811}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with cos. {ECO:0000269|PubMed:1335365,
ECO:0000269|PubMed:15691767}.
-!- INTERACTION:
O77059:cry; NbExp=2; IntAct=EBI-242141, EBI-94117;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Cytoplasm, cell cortex.
Cell junction, synapse. Cell projection, axon. Note=In syncytial
embryos, detected at the centrosomes throughout the cell cycle,
and in the mitotic spindle and pseudocleavage furrows invaginating
from the cell cortex during mitosis. Concentrated at the growing
end of membranes during the cellularization process. After
cellularization, localized to the centrosomes during mitosis and
to the nucleus at the end of telophase. Enriched in the
presynaptic side of the neuromuscular junction, with some signal
detected also in axonal branches.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=Zygotic; Synonyms=B, C;
IsoId=P18431-2; Sequence=Displayed;
Note=Major isoform.;
Name=SGG46; Synonyms=Maternal, D;
IsoId=P18431-1; Sequence=VSP_044105;
Note=Ref.3 (AAF45801) and Ref.5 (CAA19676/CAB65860) sequences
are in conflict in position: 9:R->A. Ref.7 (CAA37952) sequence
is in conflict in positions: 256:EEEE->E. Ref.7 (CAA37952)
sequence is in conflict in positions: 539:AD->RI. Ref.5
(CAA19676/CAB65860) sequences are in conflict in positions:
258:EE->E. {ECO:0000305};
Name=SGG39; Synonyms=A, J;
IsoId=P18431-3; Sequence=VSP_044106;
Name=G;
IsoId=P18431-4; Sequence=VSP_044104;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in ovaries and activated eggs (at
protein level). Expression is over all the embryo at all stages,
no local accumulation is observed. {ECO:0000269|PubMed:2118107,
ECO:0000269|PubMed:22421435, ECO:0000269|PubMed:8467811}.
-!- DEVELOPMENTAL STAGE: Isoform SGG46 is expressed at low levels in
12-24 hours embryos. Isoform Zygotic and isoform SGG39 are
expressed in 12-24 hours embryos and present throughout the
larval, pupal and adult stages (at protein level). Isoform Zygotic
is expressed maternally and zygotically but reduced throughout
later embryonic development. Expression persists throughout larval
stages. {ECO:0000269|PubMed:2118107, ECO:0000269|PubMed:8467811}.
-!- DISRUPTION PHENOTYPE: Mutants display an overdeveloped
neuromuscular junction (NMJ), with the number of boutons greatly
increased. {ECO:0000269|PubMed:15269269}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA37952.1; Type=Frameshift; Positions=473; Evidence={ECO:0000305};
Sequence=CAA50216.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; X70862; CAA50212.1; -; mRNA.
EMBL; X70863; CAA50213.1; -; mRNA.
EMBL; X70864; CAA50214.1; -; mRNA.
EMBL; X70865; CAA50215.1; -; mRNA.
EMBL; X70866; CAA50216.1; ALT_SEQ; mRNA.
EMBL; X53332; CAA37419.1; -; mRNA.
EMBL; AE014298; AAF45801.2; -; Genomic_DNA.
EMBL; AE014298; AAN09082.1; -; Genomic_DNA.
EMBL; AE014298; AAN09083.1; -; Genomic_DNA.
EMBL; AE014298; AAS65255.1; -; Genomic_DNA.
EMBL; AL024485; CAA19676.1; -; Genomic_DNA.
EMBL; AL034544; CAA19676.1; JOINED; Genomic_DNA.
EMBL; AL121804; CAB65860.1; -; Genomic_DNA.
EMBL; AL024485; CAB65860.1; JOINED; Genomic_DNA.
EMBL; AL121804; CAB72296.1; -; Genomic_DNA.
EMBL; AL024485; CAB72296.1; JOINED; Genomic_DNA.
EMBL; AY122193; AAM52705.1; -; mRNA.
EMBL; AY119664; AAM50318.1; -; mRNA.
EMBL; X54005; CAA37951.1; -; mRNA.
EMBL; X54006; CAA37952.1; ALT_FRAME; mRNA.
PIR; S35325; S35325.
PIR; S35327; S35327.
PIR; S35328; S35423.
RefSeq; NP_476714.1; NM_057366.5. [P18431-3]
RefSeq; NP_476715.1; NM_057367.5. [P18431-2]
RefSeq; NP_476716.2; NM_057368.5.
RefSeq; NP_599105.1; NM_134278.3. [P18431-2]
RefSeq; NP_726822.1; NM_166947.3. [P18431-2]
RefSeq; NP_726823.1; NM_166948.4. [P18431-2]
RefSeq; NP_996335.1; NM_206612.3. [P18431-4]
RefSeq; NP_996336.1; NM_206613.3. [P18431-3]
RefSeq; NP_996337.1; NM_206614.3. [P18431-2]
RefSeq; NP_996338.1; NM_206615.2. [P18431-2]
UniGene; Dm.7795; -.
ProteinModelPortal; P18431; -.
SMR; P18431; -.
BioGrid; 57779; 178.
DIP; DIP-39170N; -.
IntAct; P18431; 698.
STRING; 7227.FBpp0304140; -.
iPTMnet; P18431; -.
PaxDb; P18431; -.
PRIDE; P18431; -.
EnsemblMetazoa; FBtr0070466; FBpp0070449; FBgn0003371. [P18431-2]
EnsemblMetazoa; FBtr0070467; FBpp0070450; FBgn0003371. [P18431-3]
EnsemblMetazoa; FBtr0070468; FBpp0070451; FBgn0003371. [P18431-2]
EnsemblMetazoa; FBtr0070469; FBpp0070452; FBgn0003371. [P18431-2]
EnsemblMetazoa; FBtr0070470; FBpp0070453; FBgn0003371. [P18431-2]
EnsemblMetazoa; FBtr0070472; FBpp0089162; FBgn0003371. [P18431-2]
EnsemblMetazoa; FBtr0070473; FBpp0089158; FBgn0003371. [P18431-2]
EnsemblMetazoa; FBtr0070474; FBpp0089159; FBgn0003371. [P18431-3]
EnsemblMetazoa; FBtr0070475; FBpp0089160; FBgn0003371. [P18431-4]
GeneID; 31248; -.
KEGG; dme:Dmel_CG2621; -.
CTD; 31248; -.
FlyBase; FBgn0003371; sgg.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00520000055635; -.
InParanoid; P18431; -.
KO; K03083; -.
OMA; HRIIPEQ; -.
OrthoDB; EOG091G099S; -.
BRENDA; 2.7.11.26; 1994.
Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-DME-196299; Beta-catenin phosphorylation cascade.
Reactome; R-DME-209155; Phosphorylation of AXN and APC.
Reactome; R-DME-209159; Assembly of the CI containing complexes.
Reactome; R-DME-209190; Phosphorylation of CI.
Reactome; R-DME-209214; Phosphorylation of SMO.
Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
Reactome; R-DME-209387; Phosphorylation of ARR.
Reactome; R-DME-209396; Phosphorylation of ARM.
Reactome; R-DME-209413; Assembly of the 'destruction complex'.
Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
Reactome; R-DME-432553; Phosphorylation of PER and TIM.
Reactome; R-DME-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
SignaLink; P18431; -.
ChiTaRS; sgg; fly.
GenomeRNAi; 31248; -.
PRO; PR:P18431; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0003371; Expressed in 27 organ(s), highest expression level in head.
ExpressionAtlas; P18431; baseline and differential.
Genevisible; P18431; DM.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; HDA:FlyBase.
GO; GO:0035324; C:female germline ring canal; IDA:UniProtKB.
GO; GO:0045169; C:fusome; IDA:FlyBase.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
GO; GO:0022416; P:chaeta development; IMP:FlyBase.
GO; GO:0008407; P:chaeta morphogenesis; NAS:FlyBase.
GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
GO; GO:0009649; P:entrainment of circadian clock; IMP:FlyBase.
GO; GO:0003382; P:epithelial cell morphogenesis; IMP:FlyBase.
GO; GO:0090163; P:establishment of epithelial cell planar polarity; IMP:FlyBase.
GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
GO; GO:0046959; P:habituation; IMP:FlyBase.
GO; GO:0007507; P:heart development; TAS:FlyBase.
GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
GO; GO:0045475; P:locomotor rhythm; NAS:FlyBase.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:FlyBase.
GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:FlyBase.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:FlyBase.
GO; GO:0045886; P:negative regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:FlyBase.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
GO; GO:1903052; P:positive regulation of proteolysis involved in cellular protein catabolic process; IDA:FlyBase.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:FlyBase.
GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; NAS:UniProtKB.
GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
GO; GO:0045610; P:regulation of hemocyte differentiation; IMP:FlyBase.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
GO; GO:0042306; P:regulation of protein import into nucleus; TAS:FlyBase.
GO; GO:0030162; P:regulation of proteolysis; IDA:FlyBase.
GO; GO:0072347; P:response to anesthetic; IMP:FlyBase.
GO; GO:0007622; P:rhythmic behavior; TAS:FlyBase.
GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
GO; GO:0007051; P:spindle organization; IMP:FlyBase.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0035309; P:wing and notum subfield formation; IMP:FlyBase.
CDD; cd14137; STKc_GSK3; 1.
InterPro; IPR033573; GSK3B.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR039192; STKc_GSK3.
PANTHER; PTHR24057:SF8; PTHR24057:SF8; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell junction; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Kinase; Meiosis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Segmentation polarity protein;
Serine/threonine-protein kinase; Synapse; Transferase.
CHAIN 1 514 Protein kinase shaggy.
/FTId=PRO_0000086641.
DOMAIN 54 338 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 60 68 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 386 509 Ala/Gly-rich.
ACT_SITE 179 179 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 83 83 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 214 214 Phosphotyrosine.
{ECO:0000269|PubMed:18327897,
ECO:0000269|PubMed:8382613}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 1 29 MSGRPRTSSFAEGNKQSPSLVLGGVKTCS -> MLINRGSL
LEG (in isoform G).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_044104.
VAR_SEQ 1 29 MSGRPRTSSFAEGNKQSPSLVLGGVKTCS -> MATTTTTQ
RAGAAPALNLLPASNNNINNTLINNNNNNNNTSNSNNNNNN
VISQPIKIPLTERFSSQTSTGSADSGVIVSSASQQQLQLPP
PRSSSGSLSLPQAPPGGKWRQKQQRQQLLLSQDSGIENGVT
TRPSKAKDNQGAGKASHNATSSKESGAQSNSSSESLGSNCS
EAQEQQRVRASSALELSSVDTPVIVGGVVSGGNSILRSRIK
YKSTNSTGTQGFDVEDRIDEVDICDDDDVDCDDRGSEIEEE
EEEEEDDGVNVDDDVEEADNQSDNQSGIIINLKSQTEQEEE
VDEVDAKPKNRLLPPDQAELTVAAAMARRRDAKSLATDGHI
YFPLLKISEDPHIDSKLINRKDGLQDTMYYLDEFGSPKLRE
KFARKQKQLLAKQQKQLMKRERRSEEQRKKRNTTVASNLAA
SGAVVDDTKDDYKQQPHCDTSSRSKNNSVPNPPSSHLHQNH
NHLVVDVQEDVDDVNVVATSDVDSGVVKMRRHSHDNHYDRI
PRSNAATITTRPQIDQQSSHHQNTEDVEQGAEPQIDGEADL
DADADADSDGSGENVKTAKLARTQSCVSWTKVVQKFKNILG
(in isoform SGG46).
{ECO:0000303|PubMed:2113617,
ECO:0000303|PubMed:8467811}.
/FTId=VSP_044105.
VAR_SEQ 513 514 DS -> GSQSNSALNSSGSGGSGNGEAAGSGSGSGSGSGGG
NGGDNDAGDSGAIASGGGAAETEAAASG (in isoform
SGG39). {ECO:0000303|PubMed:8467811}.
/FTId=VSP_044106.
MUTAGEN 81 81 A->T: Increases the amount of synaptic
boutons and microtubule loops when
expressed presynaptically.
{ECO:0000269|PubMed:15269269}.
CONFLICT 244 244 V -> I (in Ref. 2; CAA37419).
{ECO:0000305}.
CONFLICT 397 397 A -> R (in Ref. 7; CAA37952).
{ECO:0000305}.
CONFLICT 406 406 T -> A (in Ref. 2; CAA37419 and 7;
AAM50318). {ECO:0000305}.
CONFLICT 446 446 A -> R (in Ref. 7; CAA37952).
{ECO:0000305}.
CONFLICT 462 462 A -> R (in Ref. 7; CAA37952).
{ECO:0000305}.
CONFLICT 473 473 Missing (in Ref. 7; CAA37952).
{ECO:0000305}.
CONFLICT 513 514 DS -> GE (in Ref. 5; CAA19676/CAB65860).
{ECO:0000305}.
SEQUENCE 514 AA; 53872 MW; 193EE2A1294BE494 CRC64;
MSGRPRTSSF AEGNKQSPSL VLGGVKTCSR DGSKITTVVA TPGQGTDRVQ EVSYTDTKVI
GNGSFGVVFQ AKLCDTGELV AIKKVLQDRR FKNRELQIMR KLEHCNIVKL LYFFYSSGEK
RDEVFLNLVL EYIPETVYKV ARQYAKTKQT IPINFIRLYM YQLFRSLAYI HSLGICHRDI
KPQNLLLDPE TAVLKLCDFG SAKQLLHGEP NVSYICSRYY RAPELIFGAI NYTTKIDVWS
AGCVLAELLL GQPIFPGDSG VDQLVEVIKV LGTPTREQIR EMNPNYTEFK FPQIKSHPWQ
KVFRIRTPTE AINLVSLLLE YTPSARITPL KACAHPFFDE LRMEGNHTLP NGRDMPPLFN
FTEHELSIQP SLVPQLLPKH LQNASGPGGN RPSAGGAASI AASGSTSVSS TGSGASVEGS
AQPQSQGTAA AAGSGSGGAT AGTGGASAGG PGSGNNSSSG GASGAPSAVA AGGANAAVAG
GAGGGGGAGA ATAAATATGA IGATNAGGAN VTDS


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