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Protein

Protein kinase shaggy

Gene

sgg

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei83 – 831ATPPROSITE-ProRule annotation
Active sitei179 – 1791Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi60 – 689ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: FlyBase
  • protein kinase activity Source: FlyBase
  • protein serine/threonine kinase activity Source: FlyBase

GO - Biological processi

  • blastoderm segmentation Source: FlyBase
  • chaeta morphogenesis Source: FlyBase
  • chitin-based larval cuticle pattern formation Source: FlyBase
  • circadian rhythm Source: FlyBase
  • entrainment of circadian clock Source: FlyBase
  • epithelial cell morphogenesis Source: FlyBase
  • establishment of epithelial cell planar polarity Source: FlyBase
  • female meiotic division Source: FlyBase
  • habituation Source: FlyBase
  • heart development Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • locomotor rhythm Source: FlyBase
  • negative regulation of JUN kinase activity Source: FlyBase
  • negative regulation of smoothened signaling pathway Source: FlyBase
  • negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • negative regulation of Wnt signaling pathway Source: FlyBase
  • Notch signaling pathway Source: FlyBase
  • olfactory learning Source: FlyBase
  • oogenesis Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • positive regulation of mitotic metaphase/anaphase transition Source: FlyBase
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: FlyBase
  • positive regulation of protein catabolic process Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • pseudocleavage involved in syncytial blastoderm formation Source: UniProtKB
  • regulation of calcineurin-NFAT signaling cascade Source: UniProtKB
  • regulation of circadian rhythm Source: FlyBase
  • regulation of hemocyte differentiation Source: FlyBase
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
  • regulation of protein import into nucleus Source: FlyBase
  • regulation of proteolysis Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • response to anesthetic Source: FlyBase
  • rhythmic behavior Source: FlyBase
  • segment polarity determination Source: FlyBase
  • sensory organ development Source: FlyBase
  • somatic stem cell population maintenance Source: FlyBase
  • spindle organization Source: FlyBase
  • synaptic growth at neuromuscular junction Source: FlyBase
  • wing and notum subfield formation Source: FlyBase
  • Wnt signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Segmentation polarity protein, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Meiosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.26. 1994.
ReactomeiR-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-196299. Beta-catenin phosphorylation cascade.
R-DME-3371453. Regulation of HSF1-mediated heat shock response.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
SignaLinkiP18431.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase shaggy (EC:2.7.11.1)
Alternative name(s):
Protein zeste-white 3
Gene namesi
Name:sgg
Synonyms:gsk3, zw3
ORF Names:CG2621
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003371. sgg.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • cell cortex Source: UniProtKB-SubCell
  • cell junction Source: UniProtKB-KW
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: FlyBase
  • female germline ring canal Source: UniProtKB
  • fusome Source: FlyBase
  • mitotic spindle Source: UniProtKB
  • neuromuscular junction Source: UniProtKB
  • nucleoplasm Source: FlyBase
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Nucleus, Synapse

Pathology & Biotechi

Disruption phenotypei

Mutants display an overdeveloped neuromuscular junction (NMJ), with the number of boutons greatly increased.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811A → T: Increases the amount of synaptic boutons and microtubule loops when expressed presynaptically. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 514514Protein kinase shaggyPRO_0000086641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei213 – 2131Phosphoserine1 Publication
Modified residuei214 – 2141Phosphotyrosine2 Publications
Modified residuei217 – 2171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18431.
PRIDEiP18431.

PTM databases

iPTMnetiP18431.

Expressioni

Tissue specificityi

Expressed in ovaries and activated eggs (at protein level). Expression is over all the embryo at all stages, no local accumulation is observed.3 Publications

Developmental stagei

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.2 Publications

Gene expression databases

BgeeiP18431.
ExpressionAtlasiP18431. differential.
GenevisibleiP18431. DM.

Interactioni

Subunit structurei

Interacts with cos.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cryO770592EBI-242141,EBI-94117

Protein-protein interaction databases

BioGridi57779. 146 interactions.
DIPiDIP-39170N.
IntActiP18431. 697 interactions.
STRINGi7227.FBpp0304140.

Structurei

3D structure databases

ProteinModelPortaliP18431.
SMRiP18431. Positions 33-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 338285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi386 – 509124Ala/Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0658. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00520000055635.
InParanoidiP18431.
KOiK03083.
OrthoDBiEOG7TF78V.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform Zygotic (identifier: P18431-2) [UniParc]FASTAAdd to basket

Also known as: B, C

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGRPRTSSF AEGNKQSPSL VLGGVKTCSR DGSKITTVVA TPGQGTDRVQ
60 70 80 90 100
EVSYTDTKVI GNGSFGVVFQ AKLCDTGELV AIKKVLQDRR FKNRELQIMR
110 120 130 140 150
KLEHCNIVKL LYFFYSSGEK RDEVFLNLVL EYIPETVYKV ARQYAKTKQT
160 170 180 190 200
IPINFIRLYM YQLFRSLAYI HSLGICHRDI KPQNLLLDPE TAVLKLCDFG
210 220 230 240 250
SAKQLLHGEP NVSYICSRYY RAPELIFGAI NYTTKIDVWS AGCVLAELLL
260 270 280 290 300
GQPIFPGDSG VDQLVEVIKV LGTPTREQIR EMNPNYTEFK FPQIKSHPWQ
310 320 330 340 350
KVFRIRTPTE AINLVSLLLE YTPSARITPL KACAHPFFDE LRMEGNHTLP
360 370 380 390 400
NGRDMPPLFN FTEHELSIQP SLVPQLLPKH LQNASGPGGN RPSAGGAASI
410 420 430 440 450
AASGSTSVSS TGSGASVEGS AQPQSQGTAA AAGSGSGGAT AGTGGASAGG
460 470 480 490 500
PGSGNNSSSG GASGAPSAVA AGGANAAVAG GAGGGGGAGA ATAAATATGA
510
IGATNAGGAN VTDS
Note: Major isoform.
Length:514
Mass (Da):53,872
Last modified:September 5, 2012 - v3
Checksum:i193EE2A1294BE494
GO
Isoform SGG46 (identifier: P18431-1) [UniParc]FASTAAdd to basket

Also known as: Maternal, D

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MSGRPRTSSFAEGNKQSPSLVLGGVKTCS → MATTTTTQRA...VVQKFKNILG

Show »
Length:1,067
Mass (Da):114,440
Checksum:iB4E98AFBF4807979
GO
Isoform SGG39 (identifier: P18431-3) [UniParc]FASTAAdd to basket

Also known as: A, J

The sequence of this isoform differs from the canonical sequence as follows:
     513-514: DS → GSQSNSALNSSGSGGSGNGEAAGSGSGSGSGSGGGNGGDNDAGDSGAIASGGGAAETEAAASG

Show »
Length:575
Mass (Da):58,772
Checksum:i477B3E036464E4D5
GO
Isoform G (identifier: P18431-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MSGRPRTSSFAEGNKQSPSLVLGGVKTCS → MLINRGSLLEG

Note: No experimental confirmation available.
Show »
Length:496
Mass (Da):52,092
Checksum:i8059B6236E7B268D
GO

Sequence cautioni

The sequence CAA37952.1 differs from that shown. Reason: Frameshift at position 473. Curated
The sequence CAA50216.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441V → I in CAA37419 (PubMed:8467811).Curated
Sequence conflicti397 – 3971A → R in CAA37952 (PubMed:2113617).Curated
Sequence conflicti406 – 4061T → A in CAA37419 (PubMed:8467811).Curated
Sequence conflicti406 – 4061T → A in AAM50318 (PubMed:2113617).Curated
Sequence conflicti446 – 4461A → R in CAA37952 (PubMed:2113617).Curated
Sequence conflicti462 – 4621A → R in CAA37952 (PubMed:2113617).Curated
Sequence conflicti473 – 4731Missing in CAA37952 (PubMed:2113617).Curated
Sequence conflicti513 – 5142DS → GE in CAA19676 (PubMed:10731137).Curated
Sequence conflicti513 – 5142DS → GE in CAB65860 (PubMed:10731137).Curated
Isoform SGG46 (identifier: P18431-1)
Sequence conflicti9 – 91R → A in AAF45801 (PubMed:10731132).Curated
Sequence conflicti9 – 91R → A in CAA19676 (PubMed:10731137).Curated
Sequence conflicti9 – 91R → A in CAB65860 (PubMed:10731137).Curated
Sequence conflicti256 – 2594EEEE → E in CAA37952 (PubMed:2113617).Curated
Sequence conflicti258 – 2592EE → E in CAA19676 (PubMed:10731137).Curated
Sequence conflicti258 – 2592EE → E in CAB65860 (PubMed:10731137).Curated
Sequence conflicti539 – 5402AD → RI in CAA37952 (PubMed:2113617).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929MSGRP…VKTCS → MLINRGSLLEG in isoform G. 1 PublicationVSP_044104Add
BLAST
Alternative sequencei1 – 2929MSGRP…VKTCS → MATTTTTQRAGAAPALNLLP ASNNNINNTLINNNNNNNNT SNSNNNNNNVISQPIKIPLT ERFSSQTSTGSADSGVIVSS ASQQQLQLPPPRSSSGSLSL PQAPPGGKWRQKQQRQQLLL SQDSGIENGVTTRPSKAKDN QGAGKASHNATSSKESGAQS NSSSESLGSNCSEAQEQQRV RASSALELSSVDTPVIVGGV VSGGNSILRSRIKYKSTNST GTQGFDVEDRIDEVDICDDD DVDCDDRGSEIEEEEEEEED DGVNVDDDVEEADNQSDNQS GIIINLKSQTEQEEEVDEVD AKPKNRLLPPDQAELTVAAA MARRRDAKSLATDGHIYFPL LKISEDPHIDSKLINRKDGL QDTMYYLDEFGSPKLREKFA RKQKQLLAKQQKQLMKRERR SEEQRKKRNTTVASNLAASG AVVDDTKDDYKQQPHCDTSS RSKNNSVPNPPSSHLHQNHN HLVVDVQEDVDDVNVVATSD VDSGVVKMRRHSHDNHYDRI PRSNAATITTRPQIDQQSSH HQNTEDVEQGAEPQIDGEAD LDADADADSDGSGENVKTAK LARTQSCVSWTKVVQKFKNI LG in isoform SGG46. 2 PublicationsVSP_044105Add
BLAST
Alternative sequencei513 – 5142DS → GSQSNSALNSSGSGGSGNGE AAGSGSGSGSGSGGGNGGDN DAGDSGAIASGGGAAETEAA ASG in isoform SGG39. 1 PublicationVSP_044106

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70862 mRNA. Translation: CAA50212.1.
X70863 mRNA. Translation: CAA50213.1.
X70864 mRNA. Translation: CAA50214.1.
X70865 mRNA. Translation: CAA50215.1.
X70866 mRNA. Translation: CAA50216.1. Sequence problems.
X53332 mRNA. Translation: CAA37419.1.
AE014298 Genomic DNA. Translation: AAF45801.2.
AE014298 Genomic DNA. Translation: AAN09082.1.
AE014298 Genomic DNA. Translation: AAN09083.1.
AE014298 Genomic DNA. Translation: AAS65255.1.
AL024485, AL034544 Genomic DNA. Translation: CAA19676.1.
AL121804, AL024485 Genomic DNA. Translation: CAB65860.1.
AL121804, AL024485 Genomic DNA. Translation: CAB72296.1.
AY122193 mRNA. Translation: AAM52705.1.
AY119664 mRNA. Translation: AAM50318.1.
X54005 mRNA. Translation: CAA37951.1.
X54006 mRNA. Translation: CAA37952.1. Frameshift.
PIRiS35325.
S35327.
S35328. S35423.
RefSeqiNP_476714.1. NM_057366.5. [P18431-3]
NP_476715.1. NM_057367.5. [P18431-2]
NP_476716.2. NM_057368.5.
NP_599105.1. NM_134278.3. [P18431-2]
NP_726822.1. NM_166947.3. [P18431-2]
NP_726823.1. NM_166948.4. [P18431-2]
NP_996335.1. NM_206612.3. [P18431-4]
NP_996336.1. NM_206613.3. [P18431-3]
NP_996337.1. NM_206614.3. [P18431-2]
NP_996338.1. NM_206615.2. [P18431-2]
UniGeneiDm.7795.

Genome annotation databases

EnsemblMetazoaiFBtr0070466; FBpp0070449; FBgn0003371. [P18431-2]
FBtr0070468; FBpp0070451; FBgn0003371. [P18431-2]
FBtr0070469; FBpp0070452; FBgn0003371. [P18431-2]
FBtr0070470; FBpp0070453; FBgn0003371. [P18431-2]
FBtr0070472; FBpp0089162; FBgn0003371. [P18431-2]
FBtr0070473; FBpp0089158; FBgn0003371. [P18431-2]
GeneIDi31248.
KEGGidme:Dmel_CG2621.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70862 mRNA. Translation: CAA50212.1.
X70863 mRNA. Translation: CAA50213.1.
X70864 mRNA. Translation: CAA50214.1.
X70865 mRNA. Translation: CAA50215.1.
X70866 mRNA. Translation: CAA50216.1. Sequence problems.
X53332 mRNA. Translation: CAA37419.1.
AE014298 Genomic DNA. Translation: AAF45801.2.
AE014298 Genomic DNA. Translation: AAN09082.1.
AE014298 Genomic DNA. Translation: AAN09083.1.
AE014298 Genomic DNA. Translation: AAS65255.1.
AL024485, AL034544 Genomic DNA. Translation: CAA19676.1.
AL121804, AL024485 Genomic DNA. Translation: CAB65860.1.
AL121804, AL024485 Genomic DNA. Translation: CAB72296.1.
AY122193 mRNA. Translation: AAM52705.1.
AY119664 mRNA. Translation: AAM50318.1.
X54005 mRNA. Translation: CAA37951.1.
X54006 mRNA. Translation: CAA37952.1. Frameshift.
PIRiS35325.
S35327.
S35328. S35423.
RefSeqiNP_476714.1. NM_057366.5. [P18431-3]
NP_476715.1. NM_057367.5. [P18431-2]
NP_476716.2. NM_057368.5.
NP_599105.1. NM_134278.3. [P18431-2]
NP_726822.1. NM_166947.3. [P18431-2]
NP_726823.1. NM_166948.4. [P18431-2]
NP_996335.1. NM_206612.3. [P18431-4]
NP_996336.1. NM_206613.3. [P18431-3]
NP_996337.1. NM_206614.3. [P18431-2]
NP_996338.1. NM_206615.2. [P18431-2]
UniGeneiDm.7795.

3D structure databases

ProteinModelPortaliP18431.
SMRiP18431. Positions 33-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57779. 146 interactions.
DIPiDIP-39170N.
IntActiP18431. 697 interactions.
STRINGi7227.FBpp0304140.

PTM databases

iPTMnetiP18431.

Proteomic databases

PaxDbiP18431.
PRIDEiP18431.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070466; FBpp0070449; FBgn0003371. [P18431-2]
FBtr0070468; FBpp0070451; FBgn0003371. [P18431-2]
FBtr0070469; FBpp0070452; FBgn0003371. [P18431-2]
FBtr0070470; FBpp0070453; FBgn0003371. [P18431-2]
FBtr0070472; FBpp0089162; FBgn0003371. [P18431-2]
FBtr0070473; FBpp0089158; FBgn0003371. [P18431-2]
GeneIDi31248.
KEGGidme:Dmel_CG2621.

Organism-specific databases

CTDi31248.
FlyBaseiFBgn0003371. sgg.

Phylogenomic databases

eggNOGiKOG0658. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00520000055635.
InParanoidiP18431.
KOiK03083.
OrthoDBiEOG7TF78V.

Enzyme and pathway databases

BRENDAi2.7.11.26. 1994.
ReactomeiR-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-196299. Beta-catenin phosphorylation cascade.
R-DME-3371453. Regulation of HSF1-mediated heat shock response.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
SignaLinkiP18431.

Miscellaneous databases

ChiTaRSisgg. fly.
GenomeRNAii31248.
PROiP18431.

Gene expression databases

BgeeiP18431.
ExpressionAtlasiP18431. differential.
GenevisibleiP18431. DM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An early embryonic product of the gene shaggy encodes a serine/threonine protein kinase related to the CDC28/cdc2+ subfamily."
    Bourouis M., Moore P., Ruel L., Grau Y., Heitzler P., Simpson P.
    EMBO J. 9:2877-2884(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZYGOTIC), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: DP CN BW.
    Tissue: Embryo.
  2. "Functional significance of a family of protein kinases encoded at the shaggy locus in Drosophila."
    Ruel L., Pantesco V., Lutz Y., Simpson P., Bourouis M.
    EMBO J. 12:1657-1669(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SGG39; SGG46 AND ZYGOTIC), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  3. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  6. "A Drosophila full-length cDNA resource."
    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.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS G AND ZYGOTIC).
    Strain: Berkeley.
    Tissue: Embryo.
  7. "Putative protein kinase product of the Drosophila segment-polarity gene zeste-white3."
    Siegfried E., Perkins L.A., Capaci T.M., Perrimon N.
    Nature 345:825-829(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-289 (ISOFORM ZYGOTIC/SGG39), NUCLEOTIDE SEQUENCE [MRNA] OF 30-514 (ISOFORM SGG46), FUNCTION.
    Tissue: Embryo and Ovary.
  8. "Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation."
    Hughes K., Nikolakaki E., Plyte S.E., Totty N.F., Woodgett J.R.
    EMBO J. 12:803-808(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-214.
  9. "Phosphorylation of the Drosophila adherens junction protein Armadillo: roles for wingless signal and zeste-white 3 kinase."
    Peifer M., Pai L.-M., Casey M.
    Dev. Biol. 166:543-556(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ARM.
  10. "wingless signaling acts through zeste-white 3, the Drosophila homolog of glycogen synthase kinase-3, to regulate engrailed and establish cell fate."
    Siegfried E., Chou T.B., Perrimon N.
    Cell 71:1167-1179(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WG AND EN.
    Tissue: Embryo.
  11. "Shaggy, the homolog of glycogen synthase kinase 3, controls neuromuscular junction growth in Drosophila."
    Franco B., Bogdanik L., Bobinnec Y., Debec A., Bockaert J., Parmentier M.L., Grau Y.
    J. Neurosci. 24:6573-6577(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-81.
  12. "Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus."
    Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.
    Dev. Cell 8:267-278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH COS.
  13. "Shaggy/GSK-3beta kinase localizes to the centrosome and to specialized cytoskeletal structures in Drosophila."
    Bobinnec Y., Morin X., Debec A.
    Cell Motil. Cytoskeleton 63:313-320(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "The Drosophila microtubule associated protein Futsch is phosphorylated by Shaggy/Zeste-white 3 at an homologous GSK3beta phosphorylation site in MAP1B."
    Gogel S., Wakefield S., Tear G., Klambt C., Gordon-Weeks P.R.
    Mol. Cell. Neurosci. 33:188-199(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF FUTSCH.
  15. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; TYR-214 AND SER-217, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  16. "Shaggy/glycogen synthase kinase 3beta and phosphorylation of Sarah/regulator of calcineurin are essential for completion of Drosophila female meiosis."
    Takeo S., Swanson S.K., Nandanan K., Nakai Y., Aigaki T., Washburn M.P., Florens L., Hawley R.S.
    Proc. Natl. Acad. Sci. U.S.A. 109:6382-6389(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SRA, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSGG_DROME
AccessioniPrimary (citable) accession number: P18431
Secondary accession number(s): O76881
, P23646, Q27603, Q27604, Q27605, Q8MRF7, Q9NF42, Q9U094, Q9W4X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: September 5, 2012
Last modified: June 8, 2016
This is version 186 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.