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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.
13-FEB-2019, entry version 215.
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:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- 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; 184.
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; -.
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-3371453; Regulation of HSF1-mediated heat shock response.
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.
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: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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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1493: Carbon assimilation C4 pathway
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[ASK7 BIN2 DWF12 SK21 UCU1 At4g18710 F28A21.120] Shaggy-related protein kinase eta (EC 2.7.11.1) (ASK-eta) (Protein BRASSINOSTEROID INSENSITIVE 2) (Protein ULTRACURVATA 1) (Shaggy-related protein kinase 21) (AtSK21)
[ASK3 SK12 At3g05840 F10A16.14] Shaggy-related protein kinase gamma (EC 2.7.11.1) (ASK-gamma) (Shaggy-related protein kinase 12) (AtSK12)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[UL97] Serine/threonine protein kinase UL97 (EC 2.7.1.-) (Ganciclovir kinase) (HSRF3 protein)
[Pik3cg Pi3kg1] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (PI3-kinase subunit gamma) (PI3K-gamma) (PI3Kgamma) (PtdIns-3-kinase subunit gamma) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma) (PtdIns-3-kinase subunit p110-gamma) (p110gamma) (Phosphoinositide-3-kinase catalytic gamma polypeptide) (Serine/threonine protein kinase PIK3CG) (EC 2.7.11.1) (p120-PI3K)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[PHKG1 PHKG] Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-1) (Serine/threonine-protein kinase PHKG1) (EC 2.7.11.1) (EC 2.7.11.26)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[stk-1 bur1 B20D17.070 NCU01435] Serine/threonine-protein kinase bur1 (EC 2.7.11.22) (EC 2.7.11.23) (Serine-threonine kinase 1)
[ERECTA ER QRP1 QRS1 TE1 At2g26330 T1D16.3] LRR receptor-like serine/threonine-protein kinase ERECTA (EC 2.7.11.1) (Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1) (Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1) (Protein TRANSPIRATION EFFICIENCY 1)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[Gsk3b] Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[PRKAA1 AMPK1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Prkaa1 Ampk1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[PIK3CA] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)
[PIK3CG] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (PI3-kinase subunit gamma) (PI3K-gamma) (PI3Kgamma) (PtdIns-3-kinase subunit gamma) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma) (PtdIns-3-kinase subunit p110-gamma) (p110gamma) (Phosphoinositide-3-kinase catalytic gamma polypeptide) (Serine/threonine protein kinase PIK3CG) (EC 2.7.11.1) (p120-PI3K)
[Prkaa1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[PRKAA2 AMPK AMPK2] 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[TK UL23] Thymidine kinase (EC 2.7.1.21)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[RPS6KA3 ISPK1 MAPKAPK1B RSK2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (Insulin-stimulated protein kinase 1) (ISPK-1) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)

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