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Reviewed, UniProtKB/Swiss-Prot P33886 (WIS1_SCHPO)

Last modified November 3, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein kinase wis1
    EC=2.7.12.2
Alternative name(s):
    Protein kinase sty2
Gene names
Name: wis1
Synonyms: spc2, sty2
ORF Names: SPBC409.07c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Dosage-dependent regulator of mitosis with serine/ threonine protein kinase activity. May play a role in the integration of nutritional sensing with the control over entry into mitosis. It may interact with cdc25, wee1 and win1. May activate sty1.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Post-translational modification

Dephosphorylated by pyp1 and pyp2. Ref.3

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

protein amino acid phosphorylation

Inferred from genetic interaction. Source: GeneDB_SPombe

regulation of mitotic cell cycle Ref.1

Inferred from mutant phenotype. Source: GeneDB_SPombe

regulation of translation in response to stress

Inferred from mutant phenotype. Source: GeneDB_SPombe

response to arsenic

Inferred from mutant phenotype. Source: GeneDB_SPombe

response to hydrogen peroxide

Inferred from mutant phenotype. Source: GeneDB_SPombe

response to osmotic stress

Traceable author statement. Source: GeneDB_SPombe

stress-activated MAPK cascade

Traceable author statement. Source: GeneDB_SPombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase activity

Inferred from genetic interaction. Source: GeneDB_SPombe

protein binding

Inferred from physical interaction. Source: GeneDB_SPombe

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Protein kinase wis1
PRO_0000086817

Regions

Domain320 – 579260Protein kinase
Nucleotide binding326 – 3349ATP By similarity

Sites

Active site4411Proton acceptor By similarity
Binding site3491ATP By similarity

Amino acid modifications

Modified residue1681Phosphoserine Ref.3
Modified residue2531Phosphoserine Ref.3
Modified residue4691Phosphoserine By similarity
Modified residue4731Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P33886-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 3EB97AF74190AD93

FASTA60564,762
        10         20         30         40         50         60 
MSSPNNQPLS CSLRQLSISP TAPPGDVGTP GSLLSLSSSS SSNTDSSGSS LGSLSLNSNS 

        70         80         90        100        110        120 
SGSDNDSKVS SPSREIPSDP PLPRAVPTVR LGRSTSSRSR NSLNLDMKDP SEKPRRSLPT 

       130        140        150        160        170        180 
AAGQNNIGSP PTPPGPFPGG LSTDIQEKLK AFHASRSKSM PEVVNKISSP TTPIVGMGQR 

       190        200        210        220        230        240 
GSYPLPNSQL AGRLSNSPVK SPNMPESGLA KSLAAARNPL LNRPTSFNRQ TRIRRAPPGK 

       250        260        270        280        290        300 
LDLSNSNPTS PVSPSSMASR RGLNIPPTLK QAVSETPFST FSDILDAKSG TLNFKNKAVL 

       310        320        330        340        350        360 
NSEGVNFSSG SSFRINMSEI IKLEELGKGN YGVVYKALHQ PTGVTMALKE IRLSLEEATF 

       370        380        390        400        410        420 
NQIIMELDIL HKAVSPYIVD FYGAFFVEGS VFICMEYMDA GSMDKLYAGG IKDEGVLART 

       430        440        450        460        470        480 
AYAVVQGLKT LKEEHNIIHR DVKPTNVLVN SNGQVKLCDF GVSGNLVASI SKTNIGCQSY 

       490        500        510        520        530        540 
MAPERIRVGG PTNGVLTYTV QADVWSLGLT ILEMALGAYP YPPESYTSIF AQLSAICDGD 

       550        560        570        580        590        600 
PPSLPDSFSP EARDFVNKCL NKNPSLRPDY HELANHPWLL KYQNADVDMA SWAKGALKEK 


GEKRS 

« Hide

References

« Hide 'large scale' references
[1]"The wis1 protein kinase is a dosage-dependent regulator of mitosis in Schizosaccharomyces pombe."
Warbrick E., Fantes P.A.
EMBO J. 10:4291-4299(1991) [PubMed: 1756736] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 38366 / 972.
[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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-253, MASS SPECTROMETRY.

Cross-references

Sequence databases

X62631 Genomic DNA. Translation: CAA44499.1.
CU329671 Genomic DNA. Translation: CAB52609.1.
PIRS18648.
RefSeqNP_595457.1.

3D structure databases

HSSPHSSP built from PDB template 1VR2 based on UniProtKB P35968.
ModBaseSearch...

Protein-protein interaction databases

STRINGP33886.

Genome annotation databases

GeneID2541055.
GenomeReviewsGene locus wis1 in contig CU329671_GR.
KEGGspo:SPBC409.07c.
NMPDRfig|4896.1.peg.1323.

Organism-specific databases

GeneDB_SpombeSPBC409.07c.

Phylogenomic databases

OMADYHELAN.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-003522-MON.
BRENDA2.7.12.2. 653.

Gene expression databases

ArrayExpressP33886.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameWIS1_SCHPO
AccessionPrimary (citable) accession number: P33886
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 3, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents