Actin-regulating kinase PRK1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40494 (PRK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Actin-regulating kinase PRK1
EC=2.7.11.1

Alternative name(s):
p53-regulating kinase 1

Gene names

Name:	PRK1
Synonyms:	PAK1
Ordered Locus Names:	YIL095W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	810 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in regulation of actin cytoskeleton organization and endocytosis. Ref.4 Ref.5 Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with ABP1, which is required for proper actin patch localization. Ref.7
Subcellular location	Cytoplasm › cytoskeleton › actin patch. Note: Cortical actin patches. Ref.4 Ref.8
Miscellaneous	Present with 1323 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. 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	actin cortical patch assembly Traceable author statement PubMed 10652251. Source: SGD actin filament organization Inferred from mutant phenotype PubMed 9885245. Source: SGD cytokinesis Traceable author statement PubMed 10652251. Source: SGD regulation of endocytosis Inferred from mutant phenotype PubMed 12956961. Source: SGD
Cellular_component	actin cortical patch Inferred from direct assay Ref.4 PubMed 9885245. Source: SGD mating projection tip Inferred from direct assay PubMed 19053807. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay PubMed 17978096 PubMed 9885245. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABP1	P15891	6	EBI-9703,EBI-2036

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 810

810

Actin-regulating kinase PRK1

PRO_0000086581

Regions

Domain

22 – 298

277

Protein kinase

Nucleotide binding

28 – 36

ATP By similarity

Region

743 – 756

Interaction with SH3 domain of ABP1

Sites

Active site

158

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

400

Phosphothreonine Ref.11 Ref.12

Modified residue

402

Phosphoserine Ref.12

Modified residue

428

Phosphoserine Ref.12

Modified residue

431

Phosphoserine Ref.12

Modified residue

484

Phosphoserine Ref.12

Modified residue

486

Phosphothreonine Ref.12

Modified residue

522

Phosphothreonine Ref.11

Modified residue

525

Phosphoserine Ref.11

Modified residue

540

Phosphoserine Ref.10

Modified residue

553

Phosphothreonine Ref.11

Modified residue

556

Phosphoserine Ref.11

Experimental info

Mutagenesis

K → A: Abolishes protein kinase activity. Ref.4

Sequence conflict

786

A → R in AAA86529. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P40494 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: AF710F930B39BC7E
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FASTA

810

91,032

        10         20         30         40         50         60 
MNTPQISLYE PGTILTVGSH HAKIIKYLTS GGFAQVYTAE ISPPDPYSNA NIACLKRVIV 

        70         80         90        100        110        120 
PHKQGLNTLR AEVDAMKLLR NNKHVVSYID SHAARSVNGI AYEVFVLMEF CERGGLIDFM 

       130        140        150        160        170        180 
NTRLQNRLQE SEILEIMSQT VQGITAMHAL QPPLIHRDIK IENVLISHDG LYKVCDFGSV 

       190        200        210        220        230        240 
SGVIRPPRNT QEFNYVQHDI LTNTTAQYRS PEMIDLYRGL PIDEKSDIWA LGVFLYKICY 

       250        260        270        280        290        300 
YTTPFEKSGE AGILHARYQY PSFPQYSDRL KNLIRLMLME APSQRPNICQ VLEEVSRLQN 

       310        320        330        340        350        360 
KPCPIRNFYL LRAMNQNANT QLAGEPSSTT YVPTQKFIPV QSLQSINQPP NMMPVTHVST 

       370        380        390        400        410        420 
TPNLGTFPIS INDNNKTEVT AHAGLQVGSH SNLTSPLMKT KSVPLSDEFA SLYYKELHPF 

       430        440        450        460        470        480 
QKSQTFKSVE SFQSPQRKSM PPLSLTPVNN DIFDRVSAIN RPNNYVDSET QTIDNMAVPN 

       490        500        510        520        530        540 
LKLSPTITSK SLSSTKEIAA PDNINGSKIV RSLSSKLKKV ITGESRGNSP IKSRQNTGDS 

       550        560        570        580        590        600 
IRSAFGKLRH GFTGNSVNNS RSASFDNNNV NGNGNNTNRR LVSSSTSSFP KFNSDTKRKE 

       610        620        630        640        650        660 
ESDKNQRLEK RRSMPPSILS DFDQHERNNS RTGSRDYYRS HSPVKKTQAS AKTTSKPTLI 

       670        680        690        700        710        720 
PDNGNVNINQ EKKESIQRRV HNLLKSSDDP VTYKSASGYG KYTDIGTETS NRHSSVRITP 

       730        740        750        760        770        780 
ITEEKFKKTL KDGVLDIKTK SNGKDKSRPP RPPPKPLHLR TEIQKIRNFS RLQSKKLPIE 

       790        800        810 
RISSEATETI VDVNVDDLEA DFRKRFPSKV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PAK1, a gene that can regulate p53 activity in yeast." Thiagalingam S., Kinzler K.W., Vogelstein B. Proc. Natl. Acad. Sci. U.S.A. 92:6062-6066(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast." Cope M.J.T.V., Yang S., Shang C., Drubin D.G. J. Cell Biol. 144:1203-1218(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-56.
[5]	"In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation." Watson H.A., Cope M.J.T.V., Groen A.C., Drubin D.G., Wendland B. Mol. Biol. Cell 12:3668-3679(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Regulation of yeast actin cytoskeleton-regulatory complex Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p." Zeng G., Yu X., Cai M. Mol. Biol. Cell 12:3759-3772(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis." Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K., Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L. J. Biol. Chem. 277:5290-5298(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ABP1.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, MASS SPECTROMETRY.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-400; THR-522; SER-525; THR-553 AND SER-556, MASS SPECTROMETRY.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-400; SER-402; SER-428; SER-431; SER-484 AND THR-486, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U24167 mRNA. Translation: AAA86529.1. Z46728 Genomic DNA. Translation: CAA86699.2. BK006942 Genomic DNA. Translation: DAA08458.1.
PIR	S50889.
RefSeq	NP_012171.1. NM_001179443.1.
3D structure databases
ProteinModelPortal	P40494.
SMR	P40494. Positions 25-300.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6271N.
IntAct	P40494. 24 interactions.
MINT	MINT-593513.
STRING	4932.YIL095W.
Proteomic databases
PaxDb	P40494.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL095W; YIL095W; YIL095W.
GeneID	854713.
KEGG	sce:YIL095W.
Organism-specific databases
CYGD	YIL095w.
SGD	S000001357. PRK1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00510000046552.
HOGENOM	HOG000247884.
KO	K08853.
OMA	NANIACL.
OrthoDB	EOG4NCQNG.
Gene expression databases
Genevestigator	P40494.
GermOnline	YIL095W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977380.

Entry information

Entry name

PRK1_YEAST

Accession

Primary (citable) accession number: P40494
Secondary accession number(s): D6VVJ2, Q02553

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents