Wee1-like protein kinase - Rattus norvegicus (Rat)

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Q63802 (WEE1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. 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:
Wee1-like protein kinase
EC=2.7.10.2

Alternative name(s):
Wee1A kinase

Gene names

Name:

Wee1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	646 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation By similarity.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Enzyme regulation	Synthesis is increased during S and G2 phases, presumably by an increase in transcription; activity is decreased by phosphorylation during m phase. Protein levels fall in M phase as a result of decreased synthesis combined with degradation. Activity seems to be negatively regulated by phosphorylation upon entry into mitosis, although N-terminal phosphorylation might also regulate the protein stability via protection from proteolysis or might regulate the subcellular location By similarity.
Subunit structure	Binds to 14-3-3 protein zeta.
Subcellular location	Nucleus By similarity.
Post-translational modification	Phosphorylated during M and G1 phases. Also autophosphorylated. Phosphorylation at Ser-642 by BRSK1 and BRSK2 in post-mitotic neurons, leads to down-regulate WEE1 activity in polarized neurons. Phosphorylated at Ser-52 and Ser-123 by PLK1 and CDK1, respectively, generating an signal for degradation that can be recognized by the SCF(BTRC) complex, leading to its ubiquitination and degradation at the onset of G2/M phase By similarity. Dephosphorylated at Thr-239 by CTDP1 By similarity. Ubiquitinated and degraded at the onset of G2/M phase By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW establishment of cell polarity Inferred from electronic annotation. Source: Compara microtubule cytoskeleton organization Inferred from electronic annotation. Source: Compara mitosis Inferred from electronic annotation. Source: UniProtKB-KW neuron projection morphogenesis Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 646

646

Wee1-like protein kinase

PRO_0000086812

Regions

Domain

298 – 568

271

Protein kinase

Nucleotide binding

304 – 312

ATP By similarity

Compositional bias

34 – 42

Poly-Glu

Compositional bias

74 – 77

Poly-Arg

Compositional bias

97 – 101

Poly-Gly

Sites

Active site

425

Proton acceptor By similarity

Metal binding

430

Magnesium; via carbonyl oxygen By similarity

Metal binding

462

Magnesium; via carbonyl oxygen By similarity

Binding site

327

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine; by PLK1 By similarity

Modified residue

123

Phosphoserine; by CDK1 By similarity

Modified residue

127

Phosphoserine By similarity

Modified residue

139

Phosphoserine

Modified residue

150

Phosphoserine By similarity

Modified residue

190

Phosphothreonine By similarity

Modified residue

239

Phosphothreonine By similarity

Modified residue

311

Phosphoserine By similarity

Modified residue

642

Phosphoserine; by BRSK1 and BRSK2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q63802 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 740120F51C811DAF
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FASTA

646

71,496

        10         20         30         40         50         60 
MSFLSRQQPP PTRRAAAACS LRQKLIFSPG SDCEEEEEEE EEGSGHSTGE DSAFQEPDSP 

        70         80         90        100        110        120 
LPSARSPAEA EAERRRRSPG AEPSSPGELE EDLLLRGGGG GAQAAGGGAE GDSWEEEGFG 

       130        140        150        160        170        180 
SSSPVKSPTT AYFLGSSFSP VRCGGPGDAS PRGCGVPRAM DDPCSPQPDY PSTPPHKTFR 

       190        200        210        220        230        240 
KLRLFDTPHT PKSLLSKARV IDSSSVKLRG SSLFMDTEKS GKREFDTRQT PQVNINPFTP 

       250        260        270        280        290        300 
DPVMLHSSGQ CRGRKRAYFN DSSEDMEASD YEFEDETRPA KRITITESNM KSRYTTEFHE 

       310        320        330        340        350        360 
LEKIGSGEFG SVFKCVKRLD GCIYAIKRSK KPLAGSVDEQ NALREVYAHA VLGQHPHVVR 

       370        380        390        400        410        420 
YFSAWAEDDH MLIQNEYCNG GSLADAVSEN YRVMSYFTEA ELKDLLLQVG RGLRYIHSMS 

       430        440        450        460        470        480 
LVHMDIKPSN IFISRTSIPN AVSEEGDEDD WISNKVMFKI GDLGHVTRIS SPQVEEGDSR 

       490        500        510        520        530        540 
FLANEVLQEN YSHLPKADIF ALALTVVCAA GAEPLPRNGD QWHEIRQGRL PRIPQVLSQE 

       550        560        570        580        590        600 
LTELLKVMIH PDPERRPSAM VLVKHSVLLS ASRKSAEQLR IELNAEKFKN SLLQKELKKA 

       610        620        630        640 
QMAAKVAAEE RALLTDRMAT RSTTQSNRTS RLIGKKMNRS VSLTIY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Furunobu A. Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D31838 mRNA. Translation: BAA06624.1. BC090346 mRNA. Translation: AAH90346.1.
IPI	IPI00555159.
RefSeq	NP_001012760.1. NM_001012742.1.
UniGene	Rn.208255.
3D structure databases
ProteinModelPortal	Q63802.
SMR	Q63802. Positions 290-568.
ModBase	Search...
PTM databases
PhosphoSite	Q63802.
Proteomic databases
PaxDb	Q63802.
PRIDE	Q63802.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000013362; ENSRNOP00000013362; ENSRNOG00000010017.
GeneID	308937.
KEGG	rno:308937.
UCSC	RGD:1307895. rat.
Organism-specific databases
CTD	7465.
RGD	1307895. Wee1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00530000063230.
HOGENOM	HOG000004824.
HOVERGEN	HBG005050.
InParanoid	Q63802.
KO	K06632.
OMA	RTYWNDS.
OrthoDB	EOG44TP7J.
Enzyme and pathway databases
BRENDA	2.7.11.1. 5301.
Gene expression databases
Genevestigator	Q63802.
GermOnline	ENSRNOG00000010017. Rattus norvegicus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_AS. IPR017164. Wee1-like_protein_kinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PIRSF	PIRSF037281. Wee1-like_protein_kinase. 1 hit.
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	659827.

Entry information

Entry name

WEE1_RAT

Accession

Primary (citable) accession number: Q63802
Secondary accession number(s): Q5EAN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 104 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

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents