Glycogen synthase kinase-3 beta - Xenopus laevis (African clawed frog)

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Q91757 (GSK3B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. History...

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

Documents (1) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Glycogen synthase kinase-3 beta
Short name=GSK-3 beta
EC=2.7.11.26

Alternative name(s):
Xgsk-3 protein

Gene names

Name:	gsk3b
Synonyms:	Xgsk-3

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in the organization of the formation of the main body axis of developing embryo. Acts as an inhibitor of differentiation of primary neurons. Inhibits the ability of ectopically expressed NEUROD1 and other bHLH factors to promote early retinal cell differentiation. May participate in the Wnt signaling pathway. Ref.1 Ref.2 Ref.4 Ref.5
Catalytic activity	ATP + [tau protein] = ADP + [tau protein] phosphate.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity.
Developmental stage	Expressed in the unfertilized egg and throughout the early embryonic stages. Expressed in the neural plate at stage 13. Expressed throughout the eye primordia and cranial ganglia at stage 25. Highly expressed in the differentiated retinal ganglion cell layer at stage 40. Ref.1 Ref.2 Ref.4
Post-translational modification	Phosphorylated. Activated by phosphorylation at Tyr-216.
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	Differentiation Neurogenesis Wnt signaling pathway
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	canonical Wnt receptor signaling pathway Inferred from direct assay PubMed 18215320. Source: BHF-UCL cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 18215320. Source: BHF-UCL nervous system development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB tau-protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 420

420

Glycogen synthase kinase-3 beta

PRO_0000412070

Regions

Domain

56 – 340

285

Protein kinase

Nucleotide binding

62 – 70

ATP By similarity

Sites

Active site

181

Proton acceptor By similarity

Binding site

ATP By similarity

Experimental info

Mutagenesis

K → R: Inhibits enzymatic activity. Induces duplication of the anterior dorsal axis. Ref.1 Ref.2

Sequence conflict

T → S in AAA84444. Ref.2

Sequence conflict

L → P in AAA84444. Ref.2

Sequence conflict

336

A → V in AAA84444. Ref.2

Sequence conflict

399

D → N in AAA84444. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q91757 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C02280BB8A35785D
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FASTA

420

46,903

        10         20         30         40         50         60 
MSGRPRTTSF AESCKPVQQP SSFGSMKVSR DKDGSKVTTV VATPGQGPDR QQEVTYTDTK 

        70         80         90        100        110        120 
VIGNGSFGVV YQAKLCDTGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG 

       130        140        150        160        170        180 
EKKDEVYLNL VLDYVPETVY RVARHYSRAK QALPIIYVKL YMYQLFRSLA YIHSFGICHR 

       190        200        210        220        230        240 
DIKPQNLLLD PETAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV 

       250        260        270        280        290        300 
WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP 

       310        320        330        340        350        360 
WTKVFRARTP PEAIALCSRL LEYTPTSRLT PLDACAHSFF DELRDPNLKL PNGREFPALF 

       370        380        390        400        410        420 
NFTTQELSSN PSLSSILIPA HARNQAAVST TSNTTSTSDS NTGERGSTNN AASASASNSS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of Spemann organizer formation by the intracellular kinase Xgsk-3." Pierce S.B., Kimelman D. Development 121:755-765(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF LYS-85, DEVELOPMENTAL STAGE.
[2]	"Role of glycogen synthase kinase 3 beta as a negative regulator of dorsoventral axis formation in Xenopus embryos." Dominguez I., Itoh K., Sokol S.Y. Proc. Natl. Acad. Sci. U.S.A. 92:8498-8502(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF LYS-85, DEVELOPMENTAL STAGE.
[3]	NIH - Xenopus Gene Collection (XGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo.
[4]	"The role of GSK3beta in regulating neuronal differentiation in Xenopus laevis." Marcus E.A., Kintner C., Harris W. Mol. Cell. Neurosci. 12:269-280(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[5]	"Posttranslational mechanisms control the timing of bHLH function and regulate retinal cell fate." Moore K.B., Schneider M.L., Vetter M.L. Neuron 34:183-195(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L38492 mRNA. Translation: AAC42224.1. U31862 mRNA. Translation: AAA84444.1. BC108581 mRNA. Translation: AAI08582.1.
PIR	I51425. I51692.
RefSeq	NP_001083752.1. NM_001090283.1.
UniGene	Xl.324.
3D structure databases
HSSP	HSSP built from PDB template 1I09 based on UniProtKB P49841.
ProteinModelPortal	Q91757.
SMR	Q91757. Positions 28-383.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	399097.
KEGG	xla:399097.
Organism-specific databases
CTD	2932.
Xenbase	XB-GENE-865674. gsk3b.
Phylogenomic databases
HOVERGEN	HBG014652.
KO	K03083.
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...

Entry information

Entry name

GSK3B_XENLA

Accession

Primary (citable) accession number: Q91757
Secondary accession number(s): Q91627

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents