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P40494 (PRK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcytoskeletonactin 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABP1P1589110EBI-9703,EBI-2036
PEX13P806672EBI-9703,EBI-13206

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 810810Actin-regulating kinase PRK1
PRO_0000086581

Regions

Domain22 – 298277Protein kinase
Nucleotide binding28 – 369ATP By similarity
Region743 – 75614Interaction with SH3 domain of ABP1

Sites

Active site1581Proton acceptor By similarity
Binding site561ATP By similarity

Amino acid modifications

Modified residue4021Phosphoserine Ref.11 Ref.12
Modified residue4281Phosphoserine Ref.12
Modified residue4841Phosphoserine Ref.11 Ref.12
Modified residue5531Phosphothreonine Ref.12
Modified residue5561Phosphoserine Ref.12

Experimental info

Mutagenesis561K → A: Abolishes protein kinase activity. Ref.4
Sequence conflict7861A → R in AAA86529. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40494 [UniParc].

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

FASTA81091,032
        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' 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. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[11]"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 SER-402 AND SER-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-428; SER-484; THR-553 AND SER-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS50889.
RefSeqNP_012171.1. NM_001179443.1.

3D structure databases

ProteinModelPortalP40494.
SMRP40494. Positions 25-300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34897. 139 interactions.
DIPDIP-6271N.
IntActP40494. 26 interactions.
MINTMINT-593513.
STRING4932.YIL095W.

Proteomic databases

PaxDbP40494.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL095W; YIL095W; YIL095W.
GeneID854713.
KEGGsce:YIL095W.

Organism-specific databases

CYGDYIL095w.
SGDS000001357. PRK1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00510000046552.
HOGENOMHOG000247884.
KOK08853.
OMANANIACL.
OrthoDBEOG74BK1F.

Enzyme and pathway databases

BioCycYEAST:G3O-31354-MONOMER.

Gene expression databases

GenevestigatorP40494.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977380.

Entry information

Entry namePRK1_YEAST
AccessionPrimary (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: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

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

SIMILARITY comments

Index of protein domains and families