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P07527

- WEE1_SCHPO

UniProt

P07527 - WEE1_SCHPO

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Protein

Mitosis inhibitor protein kinase wee1

Gene
wee1, SPCC18B5.03
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 cdc2.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 magnesium ions per subunit By similarity.

Enzyme regulationi

Negatively regulated by phosphorylation in the M-phase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei596 – 5961ATP By similarity
Active sitei693 – 6931Proton acceptor By similarity
Metal bindingi698 – 6981Magnesium; via carbonyl oxygen By similarity
Metal bindingi711 – 7111Magnesium; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi572 – 5809ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: PomBase
  3. metal ion binding Source: UniProtKB-KW
  4. non-membrane spanning protein tyrosine kinase activity Source: PomBase
  5. protein binding Source: PomBase
  6. protein serine/threonine kinase activity Source: PomBase

GO - Biological processi

  1. activation of bipolar cell growth Source: PomBase
  2. mitotic cell cycle checkpoint Source: PomBase
  3. mitotic DNA damage checkpoint Source: PomBase
  4. mitotic nuclear division Source: UniProtKB-KW
  5. negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle Source: PomBase
  6. negative regulation of G2/M transition of mitotic cell cycle Source: PomBase
  7. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: PomBase
  8. peptidyl-serine autophosphorylation Source: PomBase
  9. peptidyl-tyrosine autophosphorylation Source: PomBase
  10. peptidyl-tyrosine phosphorylation Source: PomBase
  11. regulation of cell size Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_217024. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitosis inhibitor protein kinase wee1 (EC:2.7.10.2)
Alternative name(s):
P107 protein kinase homolog
Gene namesi
Name:wee1
ORF Names:SPCC18B5.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome III

Organism-specific databases

PomBaseiSPCC18B5.03.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. medial cortical node Source: PomBase
  2. mitotic spindle pole body Source: PomBase
  3. nucleoplasm Source: PomBase
  4. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi596 – 5961K → L: Inactivates enzyme.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 877877Mitosis inhibitor protein kinase wee1PRO_0000086815Add
BLAST

Post-translational modificationi

Phosphorylated in the C-terminal by NIM1/CDR1.

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

BioGridi275695. 70 interactions.
DIPiDIP-16N.
MINTiMINT-4686928.
STRINGi4896.SPCC18B5.03-1.

Structurei

3D structure databases

ProteinModelPortaliP07527.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini566 – 843278Protein kinaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

KOiK03114.
OMAiYELARCK.
OrthoDBiEOG7380FJ.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 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.

P07527-1 [UniParc]FASTAAdd to Basket

« Hide

MSSSSNTSSH RSYGLRRSQR SMNLNRATLL APPTPSSLYD ANNSTSSTSS    50
QKPNTSFTSL FGPRKQTTSS PSFSHAAPLH PLSPPSFTHS QPQIQAQPVP 100
RRPSLFDRPN LVSRSSSRLG DSPSLSPVAQ VANPIHHTAP SPSDVRAFPI 150
HKNASTGVKR SFFSSSMSNG AMSPPSHSPS PFLQSSQHIP PSTPAQKLRK 200
KNNFDSFRIS NSHISPFASG SFSPFATSSP NFLSTSTPAP PNSNNANPST 250
LFSSIPSSRH TTSNHFPSNS AQSSLFSPTA RPLTARKLGF ASSQTKSAVS 300
NNHSRNSSKD ASFMMKSFIP SNRSHPQTQQ NESSLFSDNS MVNSSSNSFS 350
LFPNATLPNP PSSELLTTPF QQIKPPSQVF MSTGLLSKQH RPRKNINFTP 400
LPPSTPSKPS TFVRPHSSST DSPPSPSTPS NTQTDSYFIQ RENTPTNHNS 450
IPTIQLEKSS MDFLRFDPPP SAVKTSHNYG LPFLSNQRCP ATPTRNPFAF 500
ENTVSIHMDG RQPSPIKSRN NNQMSFAMEE EADVSQPSSS SFTLSFPSAL 550
TSSKVSSSTS HLLTRFRNVT LLGSGEFSEV FQVEDPVEKT LKYAVKKLKV 600
KFSGPKERNR LLQEVSIQRA LKGHDHIVEL MDSWEHGGFL YMQVELCENG 650
SLDRFLEEQG QLSRLDEFRV WKILVEVALG LQFIHHKNYV HLDLKPANVM 700
ITFEGTLKIG DFGMASVWPV PRGMEREGDC EYIAPEVLAN HLYDKPADIF 750
SLGITVFEAA ANIVLPDNGQ SWQKLRSGDL SDAPRLSSTD NGSSLTSSSR 800
ETPANSIIGQ GGLDRVVEWM LSPEPRNRPT IDQILATDEV CWVEMRRKAG 850
AIIYEGIHGS SSNPQGDQMM EDWQVNV 877
Length:877
Mass (Da):96,261
Last modified:April 1, 1988 - v1
Checksum:iC8B5113D66C39D10
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16508 Genomic DNA. Translation: AAA35354.1.
CU329672 Genomic DNA. Translation: CAB52150.1.
AB027900 Genomic DNA. Translation: BAA87204.1.
PIRiA25962.
RefSeqiNP_587933.1. NM_001022924.2.

Genome annotation databases

EnsemblFungiiSPCC18B5.03.1; SPCC18B5.03.1:pep; SPCC18B5.03.
GeneIDi2539123.
KEGGispo:SPCC18B5.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16508 Genomic DNA. Translation: AAA35354.1 .
CU329672 Genomic DNA. Translation: CAB52150.1 .
AB027900 Genomic DNA. Translation: BAA87204.1 .
PIRi A25962.
RefSeqi NP_587933.1. NM_001022924.2.

3D structure databases

ProteinModelPortali P07527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 275695. 70 interactions.
DIPi DIP-16N.
MINTi MINT-4686928.
STRINGi 4896.SPCC18B5.03-1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPCC18B5.03.1 ; SPCC18B5.03.1:pep ; SPCC18B5.03 .
GeneIDi 2539123.
KEGGi spo:SPCC18B5.03.

Organism-specific databases

PomBasei SPCC18B5.03.

Phylogenomic databases

KOi K03114.
OMAi YELARCK.
OrthoDBi EOG7380FJ.

Enzyme and pathway databases

Reactomei REACT_217024. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Miscellaneous databases

NextBioi 20800295.
PROi P07527.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiWEE1_SCHPO
AccessioniPrimary (citable) accession number: P07527
Secondary accession number(s): Q9UU00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: September 3, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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