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Protein

Putative glycogen synthase kinase-3 homolog

Gene

gskt

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + [tau protein] = ADP + [tau protein] phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621ATPPROSITE-ProRule annotation
Active sitei158 – 1581Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 479ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • male gamete generation Source: FlyBase
  • protein phosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_283069. Degradation of GLI2 by the proteasome.
REACT_289889. GLI3 is processed to GLI3R by the proteasome.
REACT_291749. Regulation of HSF1-mediated heat shock response.
REACT_334074. AKT phosphorylates targets in the cytosol.
REACT_343579. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_351382. Beta-catenin phosphorylation cascade.
REACT_354443. Degradation of beta-catenin by the destruction complex.
SignaLinkiP83101.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative glycogen synthase kinase-3 homolog (EC:2.7.11.26)
Short name:
GSK-3
Alternative name(s):
Protein gasket
Gene namesi
Name:gskt
ORF Names:CG31003
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0046332. gskt.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Putative glycogen synthase kinase-3 homologPRO_0000085984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylation on Tyr-193 is necessary for the activity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP83101.

Expressioni

Gene expression databases

BgeeiP83101.
GenevisibleiP83101. DM.

Interactioni

Protein-protein interaction databases

IntActiP83101. 2 interactions.
STRINGi7227.FBpp0085145.

Structurei

3D structure databases

ProteinModelPortaliP83101.
SMRiP83101. Positions 12-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 317285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi452 – 49948Asp-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00520000055635.
InParanoidiP83101.
KOiK03083.
OMAiWSKVFRI.
OrthoDBiEOG7TF78V.
PhylomeDBiP83101.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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]

Sequencei

Sequence statusi: Complete.

P83101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQSKNSGL TNKVTTVVAT NAFGADVMSE ISYTDAKVVG NGSFGVVFQA
60 70 80 90 100
KMVPSNEMVA IKKVLQDRRF KNRELQIMRK LRHDNIITLK WFFFSSGEKR
110 120 130 140 150
DEVYLNLVME FLPETLYKVE RQYARAKQTL PVNFVRLYMY QLLRSMGYLH
160 170 180 190 200
SLGFCHRDIK PQNMLLDSET GVLKLCDFGS AKQLISGEPN VSYICSRYYR
210 220 230 240 250
APELIFGSTD YTTKIDMWSA GCVMSELLLG QLIFPGDSGV DQIVEIVKVM
260 270 280 290 300
GTPTSEQLHD MNPHYKQFKL PELKPHPWSK VFRIRTPAEA IDLVSKMLIY
310 320 330 340 350
SPNARVSPLM GCAHPFFDEL RQDPHQQLPN GRSLPPLFNF TDYEKTIEPD
360 370 380 390 400
TMPLLLPRAQ GSSTTKEPSA AHRNRNTAGE ESPRKTEDSQ KPATAALSKS
410 420 430 440 450
PGPSGKALES PPGFLQHDLG NGDHVAVGTM PMEPLTLEQN HFAAESYAVG
460 470 480 490 500
EDAEDNLEED VGDENDYDYD DGGQCNSTYI SDDMDEASES DDDDFEEEDE

N
Length:501
Mass (Da):56,237
Last modified:October 1, 2001 - v1
Checksum:i949DBCADBD72A2C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAN14270.1.
BT001338 mRNA. Translation: AAN71093.1.
RefSeqiNP_733426.1. NM_170547.3.
UniGeneiDm.14965.

Genome annotation databases

EnsemblMetazoaiFBtr0085784; FBpp0085145; FBgn0046332.
GeneIDi318552.
KEGGidme:Dmel_CG31003.
UCSCiCG31003-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAN14270.1.
BT001338 mRNA. Translation: AAN71093.1.
RefSeqiNP_733426.1. NM_170547.3.
UniGeneiDm.14965.

3D structure databases

ProteinModelPortaliP83101.
SMRiP83101. Positions 12-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP83101. 2 interactions.
STRINGi7227.FBpp0085145.

Proteomic databases

PRIDEiP83101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085784; FBpp0085145; FBgn0046332.
GeneIDi318552.
KEGGidme:Dmel_CG31003.
UCSCiCG31003-RA. d. melanogaster.

Organism-specific databases

CTDi318552.
FlyBaseiFBgn0046332. gskt.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00520000055635.
InParanoidiP83101.
KOiK03083.
OMAiWSKVFRI.
OrthoDBiEOG7TF78V.
PhylomeDBiP83101.

Enzyme and pathway databases

ReactomeiREACT_283069. Degradation of GLI2 by the proteasome.
REACT_289889. GLI3 is processed to GLI3R by the proteasome.
REACT_291749. Regulation of HSF1-mediated heat shock response.
REACT_334074. AKT phosphorylates targets in the cytosol.
REACT_343579. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_351382. Beta-catenin phosphorylation cascade.
REACT_354443. Degradation of beta-catenin by the destruction complex.
SignaLinkiP83101.

Miscellaneous databases

GenomeRNAii318552.
NextBioi845394.
PROiP83101.

Gene expression databases

BgeeiP83101.
GenevisibleiP83101. DM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Testis.

Entry informationi

Entry nameiGSK3H_DROME
AccessioniPrimary (citable) accession number: P83101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: October 1, 2001
Last modified: June 24, 2015
This is version 107 of the entry and version 1 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

External Data

Dasty 3

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 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.