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P07527 (WEE1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitosis inhibitor protein kinase wee1

EC=2.7.10.2
Alternative name(s):
P107 protein kinase homolog
Gene names
Name:wee1
ORF Names:SPCC18B5.03
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length877 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein kinase that acts both on serines and on tyrosines. It acts as a dosage-dependent negative regulator of entry into mitosis (G2 to M transition). Phosphorylates and inhibits cdc2. Ref.4

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Enzyme regulation

Negatively regulated by phosphorylation in the M-phase.

Subcellular location

Nucleus Ref.3.

Post-translational modification

Phosphorylated in the C-terminal by NIM1/CDR1.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentNucleus
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Traceable author statement PubMed 1549179. Source: PomBase

activation of bipolar cell growth

Inferred from mutant phenotype PubMed 20501954. Source: PomBase

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle checkpoint

Inferred from mutant phenotype PubMed 16049679. Source: PomBase

negative regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 22624651Ref.1. Source: PomBase

negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle

Inferred from direct assay PubMed 8428596. Source: PomBase

negative regulation of protein kinase activity by regulation of protein phosphorylation

Inferred from direct assay PubMed 1372994. Source: PomBase

peptidyl-serine autophosphorylation

Inferred from direct assay Ref.4. Source: PomBase

peptidyl-tyrosine autophosphorylation

Inferred from direct assay Ref.4. Source: PomBase

peptidyl-tyrosine phosphorylation

Inferred from genetic interaction PubMed 1372994. Source: PomBase

regulation of cell size

Non-traceable author statement. Source: PomBase

   Cellular_componentmedial cortical node

Inferred from direct assay PubMed 19474792. Source: PomBase

mitotic spindle pole body

Inferred from direct assay PubMed 16823372PubMed 19474789. Source: PomBase

nucleoplasm

Traceable author statement PubMed 9034337. Source: PomBase

nucleus

Inferred from direct assay PubMed 19474789PubMed 7813446. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 1372994. Source: PomBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from direct assay Ref.4. Source: PomBase

protein serine/threonine kinase activity

Inferred from direct assay Ref.4. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 877877Mitosis inhibitor protein kinase wee1
PRO_0000086815

Regions

Domain566 – 843278Protein kinase
Nucleotide binding572 – 5809ATP By similarity

Sites

Active site6931Proton acceptor By similarity
Metal binding6981Magnesium; via carbonyl oxygen By similarity
Metal binding7111Magnesium; via carbonyl oxygen By similarity
Binding site5961ATP By similarity

Experimental info

Mutagenesis5961K → L: Inactivates enzyme.

Sequences

Sequence LengthMass (Da)Tools
P07527 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: C8B5113D66C39D10

FASTA87796,261
        10         20         30         40         50         60 
MSSSSNTSSH RSYGLRRSQR SMNLNRATLL APPTPSSLYD ANNSTSSTSS QKPNTSFTSL 

        70         80         90        100        110        120 
FGPRKQTTSS PSFSHAAPLH PLSPPSFTHS QPQIQAQPVP RRPSLFDRPN LVSRSSSRLG 

       130        140        150        160        170        180 
DSPSLSPVAQ VANPIHHTAP SPSDVRAFPI HKNASTGVKR SFFSSSMSNG AMSPPSHSPS 

       190        200        210        220        230        240 
PFLQSSQHIP PSTPAQKLRK KNNFDSFRIS NSHISPFASG SFSPFATSSP NFLSTSTPAP 

       250        260        270        280        290        300 
PNSNNANPST LFSSIPSSRH TTSNHFPSNS AQSSLFSPTA RPLTARKLGF ASSQTKSAVS 

       310        320        330        340        350        360 
NNHSRNSSKD ASFMMKSFIP SNRSHPQTQQ NESSLFSDNS MVNSSSNSFS LFPNATLPNP 

       370        380        390        400        410        420 
PSSELLTTPF QQIKPPSQVF MSTGLLSKQH RPRKNINFTP LPPSTPSKPS TFVRPHSSST 

       430        440        450        460        470        480 
DSPPSPSTPS NTQTDSYFIQ RENTPTNHNS IPTIQLEKSS MDFLRFDPPP SAVKTSHNYG 

       490        500        510        520        530        540 
LPFLSNQRCP ATPTRNPFAF ENTVSIHMDG RQPSPIKSRN NNQMSFAMEE EADVSQPSSS 

       550        560        570        580        590        600 
SFTLSFPSAL TSSKVSSSTS HLLTRFRNVT LLGSGEFSEV FQVEDPVEKT LKYAVKKLKV 

       610        620        630        640        650        660 
KFSGPKERNR LLQEVSIQRA LKGHDHIVEL MDSWEHGGFL YMQVELCENG SLDRFLEEQG 

       670        680        690        700        710        720 
QLSRLDEFRV WKILVEVALG LQFIHHKNYV HLDLKPANVM ITFEGTLKIG DFGMASVWPV 

       730        740        750        760        770        780 
PRGMEREGDC EYIAPEVLAN HLYDKPADIF SLGITVFEAA ANIVLPDNGQ SWQKLRSGDL 

       790        800        810        820        830        840 
SDAPRLSSTD NGSSLTSSSR ETPANSIIGQ GGLDRVVEWM LSPEPRNRPT IDQILATDEV 

       850        860        870 
CWVEMRRKAG AIIYEGIHGS SSNPQGDQMM EDWQVNV 

« Hide

References

« Hide 'large scale' references
[1]"Negative regulation of mitosis by wee1+, a gene encoding a protein kinase homolog."
Russell P., Nurse P.
Cell 49:559-567(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 406-625, SUBCELLULAR LOCATION.
Strain: ATCC 38364 / 968.
[4]"Fission yeast p107wee1 mitotic inhibitor is a tyrosine/serine kinase."
Featherstone C., Russell P.
Nature 349:808-811(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16508 Genomic DNA. Translation: AAA35354.1.
CU329672 Genomic DNA. Translation: CAB52150.1.
AB027900 Genomic DNA. Translation: BAA87204.1.
PIRA25962.
RefSeqNP_587933.1. NM_001022924.2.

3D structure databases

ProteinModelPortalP07527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275695. 71 interactions.
DIPDIP-16N.
MINTMINT-4686928.
STRING4896.SPCC18B5.03-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC18B5.03.1; SPCC18B5.03.1:pep; SPCC18B5.03.
GeneID2539123.
KEGGspo:SPCC18B5.03.

Organism-specific databases

PomBaseSPCC18B5.03.

Phylogenomic databases

KOK03114.
OMAYELARCK.
OrthoDBEOG7380FJ.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800295.
PROP07527.

Entry information

Entry nameWEE1_SCHPO
AccessionPrimary (citable) accession number: P07527
Secondary accession number(s): Q9UU00
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names