Reviewed, UniProtKB/Swiss-Prot P53974 (ARK1_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in regulation of actin cytoskeleton organization and endocytosis. Ref.2 Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with ABP1, which is required for proper actin patch localization. Ref.4
Subcellular location	Cytoplasm › cytoskeleton › actin patch. Note: Cortical actin patches. Ref.2 Ref.5
Miscellaneous	Present with 1551 molecules/cell in log phase SD medium. Ref.6
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
Gene Ontology (GO)
Biological process	actin cortical patch assembly Traceable author statement. Source: SGD actin filament organization Ref.2 Inferred from genetic interaction. Source: SGD cytokinesis Traceable author statement. Source: SGD protein amino acid phosphorylation Ref.2 Inferred from direct assay. Source: SGD regulation of endocytosis Inferred from mutant phenotype. Source: SGD
Cellular component	actin cortical patch Ref.2 Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Ref.2 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABP1	P15891	2	EBI-9817,EBI-2036
ARC40	P38328	1	EBI-9817,EBI-2777
YAP1802	P53309	1	EBI-9817,EBI-23557

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	9	ATP By similarity
	Region	602 – 615	14	Interaction with SH3 domain of ABP1
Sites
	Active site	159	1	Proton acceptor By similarity
	Binding site	56	1	ATP By similarity
Amino acid modifications
	Modified residue	478	1	Phosphoserine Ref.7 Ref.9
	Modified residue	502	1	Phosphoserine Ref.9
	Modified residue	522	1	Phosphoserine Ref.9
	Modified residue	535	1	Phosphoserine Ref.9 Ref.8
	Modified residue	568	1	Phosphoserine Ref.9
	Modified residue	569	1	Phosphoserine Ref.9
Experimental info
	Mutagenesis	56	1	K → A: Abolishes protein kinase activity. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P53974-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 139CA4CA1B6A181F	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

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. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"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: 10087264] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-56.
[3]	"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: 11694597] [Abstract] Cited for: FUNCTION.
[4]	"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: 11668184] [Abstract] Cited for: INTERACTION WITH ABP1.
[5]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, MASS SPECTROMETRY.
[8]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, MASS SPECTROMETRY.
[9]	"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: 18407956] [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
EMBLGenBankDDBJ	Z71296 Genomic DNA. Translation: CAA95882.1.
PIR	S62932.
RefSeq	NP_014378.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4381N.
IntAct	P53974. 7 interactions.
Genome annotation databases
Ensembl	YNL020C. Saccharomyces cerevisiae. [Contig view]
GeneID	855711.
GenomeReviews	Gene locus YNL020C in contig Y13139_GR.
KEGG	sce:YNL020C.
NMPDR	fig|4932.3.peg.5456.
Organism-specific databases
CYGD	YNL020c.
SGD	S000004965. ARK1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P53974.
Enzyme and pathway databases
BRENDA	2.7.11.1. 250.
Gene expression databases
ArrayExpress	P53974.
GermOnline	YNL020C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	980061.

Entry information

Entry name

ARK1_YEAST

Accession

Primary (citable) accession number: P53974

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)