Actin-regulating kinase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53974 (ARK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 112. History...

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

Documents (4) |

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 1
EC=2.7.11.1

Gene names

Name:	ARK1
Ordered Locus Names:	YNL020C
ORF Names:	N2823

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	638 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in regulation of actin cytoskeleton organization and endocytosis. Ref.3 Ref.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with ABP1, which is required for proper actin patch localization. Ref.5
Subcellular location	Cytoplasm › cytoskeleton › actin patch. Note: Cortical actin patches. Ref.3 Ref.6
Miscellaneous	Present with 1551 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	3D-structure 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 Ref.3. 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.3. 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. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABP1	P15891	4	EBI-9817,EBI-2036

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 638

638

Actin-regulating kinase 1

PRO_0000085635

Regions

Domain

22 – 298

277

Protein kinase

Nucleotide binding

28 – 36

ATP By similarity

Region

602 – 615

Interaction with SH3 domain of ABP1

Sites

Active site

159

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

478

Phosphoserine Ref.8 Ref.10

Modified residue

502

Phosphoserine Ref.10

Modified residue

522

Phosphoserine Ref.10

Modified residue

535

Phosphoserine Ref.9 Ref.10

Modified residue

568

Phosphoserine Ref.10

Modified residue

569

Phosphoserine Ref.10

Experimental info

Mutagenesis

K → A: Abolishes protein kinase activity. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P53974 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 139CA4CA1B6A181F
Show »

FASTA

638

71,373

        10         20         30         40         50         60 
MNQPQIGTYN VGTQLTVGSH QVEIIKYLTS GGFAQVYSAL INPPDPHSNS SVACLKRVIV 

        70         80         90        100        110        120 
PDKPSLNTLR AEVDAMRLLK NNRYVVSYID SHAAKAMLHN GSYEVFVLME YCERGGLIDF 

       130        140        150        160        170        180 
MNTRLQNRLH EFEILQIMSQ VTQGVAAMHA LQPPLIHRDI KIENVLISAN NEYKLCDFGS 

       190        200        210        220        230        240 
VCGIIRPPRN SQELSYVQQD ILKNTTAQYR SPEMIDTFRG LPIDEKSDIW ALGIFLYKLC 

       250        260        270        280        290        300 
YYTTPFEKGG DLAILSGKFE FPLYPNYSEQ LKGLIRDILV QDPRHRPNVY QLLKRISIMQ 

       310        320        330        340        350        360 
NVPCPINDIQ VVQAPSSHLN LTELHQLSAT QNILSLNSPT TMENTMPNAT FQISMADNTT 

       370        380        390        400        410        420 
TAQMHPNRKP SQIAYDASFS NSAKGSQPLF DKSQNMYHAL DPPLVEPLAS SVSNNDNELK 

       430        440        450        460        470        480 
ANSATKLKQA IVSEAHTFRQ NNSIDFPLQN IIPQYEDSSS SSDESYSGDV DELKKTRSLG 

       490        500        510        520        530        540 
SYSTRGNIKK NQSVKESLTS SSLPGTSFTP TSTKVNLKHE NSPFKSTFVN TIDNSKDDLN 

       550        560        570        580        590        600 
KPSYEDLDVS KQNLKNSIQQ RMIDKLNSSE ESFNARKMSK VKLHEKGEID KPTMLKSSGP 

       610        620        630 
ISKDKKTKPT PPPKPSHLKP KPPPKPLLLA GRKLSLDK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"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].
[7]	"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].
[8]	"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-478, MASS SPECTROMETRY.
[9]	"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 SER-535, MASS SPECTROMETRY.
[10]	"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-478; SER-502; SER-522; SER-535; SER-568 AND SER-569, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z71296 Genomic DNA. Translation: CAA95882.1.
BK006947 Genomic DNA. Translation: DAA10525.1.

PIR

S62932.

RefSeq

NP_014378.1. NM_001182859.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RPN	NMR	-	B	605-621	[»]

ProteinModelPortal

P53974.

SMR

P53974. Positions 11-333.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4381N.

IntAct

P53974. 17 interactions.

MINT

MINT-511765.

STRING

4932.YNL020C.

Proteomic databases

PaxDb

P53974.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL020C; YNL020C; YNL020C.

GeneID

855711.

KEGG

sce:YNL020C.

Organism-specific databases

CYGD

YNL020c.

SGD

S000004965. ARK1.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00510000046552.

HOGENOM

HOG000247884.

K08853.

OMA

KHINSEA.

OrthoDB

EOG4NCQNG.

Enzyme and pathway databases

BioCyc

YEAST:G3O-33058-MONOMER.

Gene expression databases

Genevestigator

P53974.

GermOnline

YNL020C. 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

EvolutionaryTrace

P53974.

NextBio

980061.

Entry information

Entry name

ARK1_YEAST

Accession

Primary (citable) accession number: P53974
Secondary accession number(s): D6W1F9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 112 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 XIV

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents