P50527 (STE20_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase shk1/pak1
EC=2.7.11.1

Gene names

Name:	shk1
Synonyms:	orb2, pak1, ste20
ORF Names:	SPBC1604.14c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	658 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › spindle. 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 component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Cdc42 protein signal transduction Inferred from genetic interaction Ref.4. Source: PomBase 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 cell cycle cytokinesis Inferred from mutant phenotype PubMed 12764131. Source: PomBase regulation of microtubule cytoskeleton organization Inferred from genetic interaction Ref.10. Source: PomBase
Cellular_component	Cdc42 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_function	ATP 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
scd2	P40996	3	EBI-767318,EBI-767302

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 658	658	Serine/threonine-protein kinase shk1/pak1		PRO_0000086651
Regions
	Domain	147 – 160	14	CRIB
	Domain	386 – 637	252	Protein kinase
	Nucleotide binding	392 – 400	9	ATP By similarity
	Compositional bias	85 – 88	4	Poly-Ser
	Compositional bias	234 – 237	4	Poly-Ser
	Compositional bias	246 – 249	4	Poly-Ser
	Compositional bias	263 – 267	5	Poly-Ser
Sites
	Active site	505	1	Proton acceptor By similarity
	Binding site	415	1	ATP By similarity
Amino acid modifications
	Modified residue	301	1	Phosphoserine Ref.13
	Modified residue	303	1	Phosphoserine Ref.13
Experimental info
	Sequence conflict	492 – 495	4	GLQH → LYSD in AAC49125. Ref.1
	Sequence conflict	537	1	R → P in AAC49125. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P50527 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 69D72E5C925021E5	FASTA	658	72,358
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	S60170. T39500.
RefSeq	NP_596626.1. NM_001022547.2.
3D structure databases
ProteinModelPortal	P50527.
SMR	P50527. Positions 146-189, 365-652.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-949N.
IntAct	P50527. 3 interactions.
MINT	MINT-111182.
STRING	4896.SPBC1604.14c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC1604.14c.1; SPBC1604.14c.1:pep; SPBC1604.14c.
GeneID	2539997.
KEGG	spo:SPBC1604.14c.
Organism-specific databases
PomBase	SPBC1604.14c.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000234202.
KO	K04409.
OMA	FPRESTE.
OrthoDB	EOG4G7G6X.
Enzyme and pathway databases
BRENDA	2.7.11.1. 5615.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000095. PAK_box_Rho-bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00786. PBD. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00285. PBD. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50108. CRIB. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801140.

Entry information

Entry name

STE20_SCHPO

Accession

Primary (citable) accession number: P50527

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program