Glycogen synthase kinase-3 - Caenorhabditis elegans

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Q9U2Q9 (GSK3_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glycogen synthase kinase-3
EC=2.7.11.26

Gene names

Name:	gsk-3
Synonyms:	sgg-1
ORF Names:	Y18D10A.5

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphorylates oma-1, a regulator of the oocyte-to-embryo transition, enabling its degradation. Phosphorylates skn-1, preventing it from accumulating in nuclei and thus inhibiting phase II gene expression in the oxidative stress defense. Involved in mesendoderm specification and mitotic spindle orientation in EMS blastomeres. Thought to be a branch point in these processes as proteins downstream are not required. Negatively regulates Wnt signaling in vulval precursor cells and acts as a Wnt-independent repressor of med-1 and med-2 in the C lineage inhibiting mesoderm development. Required for normal lifespan and LiCl-induced lifespan extension. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10
Catalytic activity	ATP + [tau protein] = ADP + [tau protein] phosphate. Ref.10
Subunit structure	Monomer By similarity. Interacts with axl-1. Ref.8 Ref.9
Disruption phenotype	Worms exhibit defects in endoderm specification and mitotic spindle alignment. Mutants show reduced degradation of oma-1 and have shortened lifespan. Ref.1
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Stress response Wnt signaling pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway, regulating spindle positioning Inferred from mutant phenotype Ref.1. Source: WormBase engulfment of apoptotic cell Inferred from mutant phenotype PubMed 20126385. Source: WormBase germ cell development Inferred from genetic interaction PubMed 19264959. Source: WormBase multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of Wnt receptor signaling pathway Inferred from mutant phenotype Ref.8. Source: UniProtKB response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from sequence or structural similarity Ref.1. Source: WormBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.5. Source: WormBase tau-protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
axl-1	Q3LRZ3	4	EBI-330089,EBI-327368
mac-1	Q9NAG4	3	EBI-330089,EBI-2005767
pry-1	O62090	3	EBI-330089,EBI-2917690

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 362

362

Glycogen synthase kinase-3

PRO_0000349136

Regions

Domain

36 – 320

285

Protein kinase

Nucleotide binding

42 – 50

ATP By similarity

Sites

Active site

161

Proton acceptor By similarity

Binding site

ATP By similarity

Experimental info

Sequence conflict

350

V → I in AAD45354. Ref.1

Sequence conflict

352

T → P in AAD45354. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9U2Q9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: ABDD2F49CC475BF5
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FASTA

362

40,882

        10         20         30         40         50         60 
MNKQLLSCSL KSGKQVTMVV ASVATDGVDQ QVEISYYDQK VIGNGSFGVV FLAKLSTTNE 

        70         80         90        100        110        120 
MVAIKKVLQD KRFKNRELQI MRKLNHPNIV KLKYFFYSSG EKKDELYLNL ILEYVPETVY 

       130        140        150        160        170        180 
RVARHYSKQR QQIPMIYVKL YMYQLLRSLA YIHSIGICHR DIKPQNLLID PESGVLKLCD 

       190        200        210        220        230        240 
FGSAKYLVRN EPNVSYICSR YYRAPELIFG ATNYTNSIDV WSAGTVMAEL LLGQPIFPGD 

       250        260        270        280        290        300 
SGVDQLVEII KVLGTPTREQ IQSMNPNYKE FKFPQIKAHP WNKVFRVHTP AEAIDLISKI 

       310        320        330        340        350        360 
IEYTPTSRPT PQAACQHAFF DELRNPDARL PSGRPLPTLE MDGPMGTGEV STTSGDVAGP 


SA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Wnt pathway components orient a mitotic spindle in the early Caenorhabditis elegans embryo without requiring gene transcription in the responding cell." Schlesinger A., Shelton C.A., Maloof J.N., Meneghini M.D., Bowerman B. Genes Dev. 13:2028-2038(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Restriction of mesendoderm to a single blastomere by the combined action of SKN-1 and a GSK-3beta homolog is mediated by MED-1 and -2 in C. elegans." Maduro M.F., Meneghini M.D., Bowerman B., Broitman-Maduro G., Rothman J.H. Mol. Cell 7:475-485(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"Multiple Wnt signaling pathways converge to orient the mitotic spindle in early C. elegans embryos." Walston T., Tuskey C., Edgar L., Hawkins N., Ellis G., Bowerman B., Wood W., Hardin J. Dev. Cell 7:831-841(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"DYRK2 and GSK-3 phosphorylate and promote the timely degradation of OMA-1, a key regulator of the oocyte-to-embryo transition in C. elegans." Nishi Y., Lin R. Dev. Biol. 288:139-149(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Regulation of the Caenorhabditis elegans oxidative stress defense protein SKN-1 by glycogen synthase kinase-3." An J.H., Vranas K., Lucke M., Inoue H., Hisamoto N., Matsumoto K., Blackwell T.K. Proc. Natl. Acad. Sci. U.S.A. 102:16275-16280(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"The conserved kinases CDK-1, GSK-3, KIN-19, and MBK-2 promote OMA-1 destruction to regulate the oocyte-to-embryo transition in C. elegans." Shirayama M., Soto M.C., Ishidate T., Kim S., Nakamura K., Bei Y., van den Heuvel S., Mello C.C. Curr. Biol. 16:47-55(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Multiple redundant Wnt signaling components function in two processes during C. elegans vulval development." Gleason J.E., Szyleyko E.A., Eisenmann D.M. Dev. Biol. 298:442-457(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Two functionally distinct axin-like proteins regulate canonical Wnt signaling in C. elegans." Oosterveen T., Coudreuse D.Y.M., Yang P.-T., Fraser E., Bergsma J., Dale T.C., Korswagen H.C. Dev. Biol. 308:438-448(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AXL-1.
[10]	"Pharmacogenetic analysis of lithium-induced delayed aging in Caenorhabditis elegans." McColl G., Killilea D.W., Hubbard A.E., Vantipalli M.C., Melov S., Lithgow G.J. J. Biol. Chem. 283:350-357(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF159950 mRNA. Translation: AAD45354.1. AL034393 Genomic DNA. Translation: CAA22311.1.
PIR	T26520.
RefSeq	NP_493243.1. NM_060842.5.
3D structure databases
HSSP	HSSP built from PDB template 1Q5K based on UniProtKB P49841.
ProteinModelPortal	Q9U2Q9.
SMR	Q9U2Q9. Positions 15-339.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-25216N.
IntAct	Q9U2Q9. 11 interactions.
MINT	MINT-1073589.
STRING	6239.Y18D10A.5.
Proteomic databases
PaxDb	Q9U2Q9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	Y18D10A.5.1; Y18D10A.5.1; Y18D10A.5. Y18D10A.5.2; Y18D10A.5.2; Y18D10A.5.
GeneID	173149.
KEGG	cel:CELE_Y18D10A.5.
UCSC	Y18D10A.5. c. elegans.
Organism-specific databases
CTD	173149.
WormBase	Y18D10A.5; CE21401; WBGene00001746; gsk-3.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00520000055635.
HOGENOM	HOG000233017.
InParanoid	Q9U2Q9.
KO	K03083.
OMA	MKTTMPI.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	878473.

Entry information

Entry name

GSK3_CAEEL

Accession

Primary (citable) accession number: Q9U2Q9
Secondary accession number(s): Q9Y0C2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents