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P50527 (STE20_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 132. 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:
Serine/threonine-protein kinase shk1/pak1

EC=2.7.11.1
Gene names
Name:shk1
Synonyms:orb2, pak1, ste20
ORF Names:SPBC1604.14c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

MAP4K component of the MAPK pathway required for the mating pheromone response. Phosphorylates histone H2B to form H2BS10ph By similarity. Phosphorylates tea1. Required for skb1-dependent mitotic inhibitory function. Regulates microtubule dynamics and cell polarity. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.10 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Forms an activated complex with GTP-bound ras-like cdc42. Interacts with skb1 and the SH3 domain of skb5 via its amino-terminal regulatory domain. Skb1, cdc42 and shk1 are able to form a ternary complex in vivo. Interacts with rga8 and may interact with byr2. Ref.1 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.12

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonspindle. Note: Localizes at cell ends, septum forming regions and at the mitotic spindle. Ref.10

Post-translational modification

Autophosphorylated on serine residues. Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 CRIB domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCdc42 protein signal transduction

Inferred from genetic interaction Ref.4. Source: PomBase

actin filament organization

Inferred from electronic annotation. Source: InterPro

cellular protein localization

Inferred from mutant phenotype Ref.12. Source: PomBase

establishment or maintenance of actin cytoskeleton polarity

Traceable author statement PubMed 15731009. Source: PomBase

establishment or maintenance of bipolar cell polarity regulating cell shape

Inferred from mutant phenotype PubMed 19646873. Source: PomBase

positive regulation of establishment of bipolar cell polarity regulating cell shape

Inferred from genetic interaction PubMed 12529446PubMed 9636183. Source: PomBase

regulation of cytokinesis

Inferred from mutant phenotype PubMed 12764131. Source: PomBase

regulation of microtubule cytoskeleton organization

Inferred from genetic interaction Ref.10. Source: PomBase

   Cellular_componentCdc42 GTPase complex

Traceable author statement Ref.9. Source: PomBase

cell division site

Inferred from direct assay Ref.10PubMed 16823372. Source: PomBase

cell tip

Inferred from direct assay Ref.10PubMed 16823372. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay PubMed 12764131Ref.12PubMed 9858584. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 658658Serine/threonine-protein kinase shk1/pak1
PRO_0000086651

Regions

Domain147 – 16014CRIB
Domain386 – 637252Protein kinase
Nucleotide binding392 – 4009ATP By similarity
Compositional bias85 – 884Poly-Ser
Compositional bias234 – 2374Poly-Ser
Compositional bias246 – 2494Poly-Ser
Compositional bias263 – 2675Poly-Ser

Sites

Active site5051Proton acceptor By similarity
Binding site4151ATP By similarity

Amino acid modifications

Modified residue3011Phosphoserine Ref.13
Modified residue3031Phosphoserine Ref.13

Experimental info

Sequence conflict492 – 4954GLQH → LYSD in AAC49125. Ref.1
Sequence conflict5371R → P in AAC49125. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50527 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 69D72E5C925021E5

FASTA65872,358
        10         20         30         40         50         60 
MERGTLQPRK KAPNGYGITP IVAHKTGEPV RYEVEDDLRK LKPSRTAPKP PAINTNLAED 

        70         80         90        100        110        120 
TFSGFPLSQS RTTVSRVSLG SRQHSSSSIR KLQTNVSDVR SYDERNQKKS AFENFVSSMS 

       130        140        150        160        170        180 
SFLTGGGSSP TSSYGSGSAS PRKSTVISSP FDPKHVTHVG FNYDTGEFTG MPTEWQALLK 

       190        200        210        220        230        240 
VSGITKSEQV QHPQAVLDAM AFYSQSKKYL EEGAKPPFPR ESTEKPLLSV SALSSSSHLQ 

       250        260        270        280        290        300 
PTSATSSSSR LYPSRPAPTP PASSSSSPLL SSQTVKTTTS NASRQPSPLV SSKSTDNIIR 

       310        320        330        340        350        360 
SHSPVLLTPQ TLSTSETKHI RPNNSTPYQR RAETSTKPKA VATPQKVEAP SAPRLQKRAP 

       370        380        390        400        410        420 
RQQSNDSAVL AKLQSICNPK NPTLLYRNFV KIGQGASGDV YSARQVGTNL SVAIKKMNIN 

       430        440        450        460        470        480 
QQPKKEFIVN EILVMKSHHH KNIVNFIDTF FYKSELWMVM EYMRGGSLTE VVTNNTLSEG 

       490        500        510        520        530        540 
QIAAICKETL EGLQHLHENG IVHRDIKSDN ILLSLQGDIK LTDFGFCAQI DSNMTKRTTM 

       550        560        570        580        590        600 
VGTPYWMAPE VVTRKEYGFK VDVWSLGIMA IEMVEGEPPY LNENPLRALY LIATIGTPKI 

       610        620        630        640        650 
SRPELLSSVF HDFLSKSLTV NPKQRPSSGE LLRHPFLKQA VPVSSLIPLI KSIHHSGK 

« Hide

References

« Hide 'large scale' references
[1]"Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating."
Ottilie S., Miller P.J., Johnson D.I., Creasy C.L., Sells M.A., Bagrodia S., Forsburg S.L., Chernoff J.
EMBO J. 14:5908-5919(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CDC42, FUNCTION.
[2]Marcus S.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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.
[4]"Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signaling module in the fission yeast Schizosaccharomyces pombe."
Marcus S., Polverino A., Chang E., Robbins D., Cobb M.H., Wigler M.
Proc. Natl. Acad. Sci. U.S.A. 92:6180-6184(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 119-658, INTERACTION WITH CDC42, FUNCTION.
[5]"The highly conserved skb1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog."
Gilbreth M., Yang P., Wang D., Frost J., Polverino A., Cobb M.H., Marcus S.
Proc. Natl. Acad. Sci. U.S.A. 93:13802-13807(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SKB1.
[6]"Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs."
Gilbreth M., Yang P., Bartholomeusz G., Pimental R.A., Kansra S., Gadiraju R., Marcus S.
Proc. Natl. Acad. Sci. U.S.A. 95:14781-14786(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC42.
[7]"Mis-specification of cortical identity in a fission yeast PAK mutant."
Sawin K.E., Hajibagheri M.A.N., Nurse P.
Curr. Biol. 9:1335-1338(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Direct activation of the fission yeast PAK Shk1 by the novel SH3 domain protein, Skb5."
Yang P., Pimental R.A., Lai H., Marcus S.
J. Biol. Chem. 274:36052-36057(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SKB5.
[9]"Direct binding and In vivo regulation of the fission yeast p21-activated kinase shk1 by the SH3 domain protein scd2."
Chang E., Bartholomeusz G., Pimental R.A., Chen J., Lai H., Wang L.L., Yang P., Marcus S.
Mol. Cell. Biol. 19:8066-8074(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCD2, AUTOPHOSPHORYLATION.
[10]"The p21-activated kinase, Shk1, is required for proper regulation of microtubule dynamics in the fission yeast, Schizosaccharomyces pombe."
Qyang Y., Yang P., Du H., Lai H., Kim H., Marcus S.
Mol. Microbiol. 44:325-334(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"The kelch repeat protein, Tea1, is a potential substrate target of the p21-activated kinase, Shk1, in the fission yeast, Schizosaccharomyces pombe."
Kim H., Yang P., Catanuto P., Verde F., Lai H., Du H., Chang F., Marcus S.
J. Biol. Chem. 278:30074-30082(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TEA1.
[12]"The novel Rho GTPase-activating protein family protein, Rga8, provides a potential link between Cdc42/p21-activated kinase and Rho signaling pathways in the fission yeast, Schizosaccharomyces pombe."
Yang P., Qyang Y., Bartholomeusz G., Zhou X., Marcus S.
J. Biol. Chem. 278:48821-48830(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RGA8.
[13]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-303, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22371 mRNA. Translation: AAC49125.1.
L41552 Genomic DNA. Translation: AAB52609.1.
CU329671 Genomic DNA. Translation: CAA22347.1.
PIRS60170.
T39500.
RefSeqNP_596626.1. NM_001022547.2.

3D structure databases

ProteinModelPortalP50527.
SMRP50527. Positions 146-189, 365-652.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276541. 22 interactions.
DIPDIP-949N.
IntActP50527. 1 interaction.
MINTMINT-111182.
STRING4896.SPBC1604.14c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1604.14c.1; SPBC1604.14c.1:pep; SPBC1604.14c.
GeneID2539997.
KEGGspo:SPBC1604.14c.

Organism-specific databases

PomBaseSPBC1604.14c.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234202.
KOK04409.
OMAVQARGPK.
OrthoDBEOG708W7W.

Enzyme and pathway databases

BRENDA2.7.11.1. 5615.

Family and domain databases

Gene3D3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR011026. WASP_C.
[Graphical view]
PfamPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF47912. SSF47912. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801140.

Entry information

Entry nameSTE20_SCHPO
AccessionPrimary (citable) accession number: P50527
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: February 19, 2014
This is version 132 of the entry and version 2 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