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UniProtKB/Swiss-Prot entry P53974


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARK1_YEAST
Primary accession number P53974
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 71)
Name and origin of the protein
Protein name Actin-regulating kinase 1
Synonym EC 2.7.11.1
Gene name
Name: ARK1
OrderedLocusNames: YNL020C
ORFNames: N2823
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[2]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-56.
DOI=10.1083/jcb.144.6.1203; PubMed=10087264 [NCBI, ExPASy, EBI, Israel, Japan]
Cope M.J.T.V., Yang S., Shang C., Drubin D.G.;
"Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast.";
J. Cell Biol. 144:1203-1218(1999).
[3]
FUNCTION.
PubMed=11694597 [NCBI, ExPASy, EBI, Israel, Japan]
Watson H.A., Cope M.J.T.V., Groen A.C., Drubin D.G., Wendland B.;
"In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation.";
Mol. Biol. Cell 12:3668-3679(2001).
[4]
INTERACTION WITH ABP1.
DOI=10.1074/jbc.M109848200; PubMed=11668184 [NCBI, ExPASy, EBI, Israel, Japan]
Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K., Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L.;
"Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis.";
J. Biol. Chem. 277:5290-5298(2002).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-502; SER-522; SER-535; SER-568 AND SER-569, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z71296; CAA95882.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S62932; S62932.
RefSeq NP_014378.1; -.
3D structure databases
ModBase P53974.
Protein-protein interaction databases
DIP DIP:4381N; -.
IntAct P53974; -.
Organism-specific databases
CYGD YNL020c; -.
SGD S000004965; ARK1.
Yeast-GFP YNL020C.
Gene expression databases
ArrayExpress P53974; -.
GermOnline YNL020C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0030479; Cellular component: actin cortical patch (traceable author statement from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from mutant phenotype from SGD).
GO:0000147; Biological process: actin cortical patch assembly (traceable author statement from SGD).
GO:0007015; Biological process: actin filament organization (inferred from genetic interaction from SGD).
GO:0000910; Biological process: cytokinesis (traceable author statement from SGD).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from mutant phenotype from SGD).
GO:0030100; Biological process: regulation of endocytosis (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P53974.
ProtoNet P53974.
Genome annotation databases
Ensembl YNL020C; Saccharomyces cerevisiae. [Contig view]
GeneID 855711; -.
GenomeReviews Y13139_GR; YNL020C.
KEGG sce:YNL020C; -.
NMPDR fig|4932.3.peg.5456; -.
Phylogenomic databases
HOGENOM P53974; -.
Other
LinkHub P53974; -.
NextBio 980061; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   638  638     Actin-regulating kinase 1. PRO_0000085635
DOMAIN   22   298  277     Protein kinase. 
NP_BIND   28    36  9     ATP (By similarity). 
REGION   602   615  14     Interaction with SH3 domain of ABP1. 
ACT_SITE   159   159        Proton acceptor (By similarity). 
BINDING   56    56        ATP (By similarity). 
MOD_RES   478   478        Phosphoserine. 
MOD_RES   502   502        Phosphoserine. 
MOD_RES   522   522        Phosphoserine. 
MOD_RES   535   535        Phosphoserine. 
MOD_RES   568   568        Phosphoserine. 
MOD_RES   569   569        Phosphoserine. 
MUTAGEN   56    56        K->A: Abolishes protein kinase activity. 
Sequence information
Length: 638 AA [This is the length of the unprocessed precursor] Molecular weight: 71373 Da [This is the MW of the unprocessed precursor] CRC64: 139CA4CA1B6A181F [This is a checksum on the sequence]
        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 

P53974 in FASTA format

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View entry in raw text format (no links)
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