ID   ARK1_YEAST              Reviewed;         638 AA.
AC   P53974;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-DEC-2008, entry version 73.
DE   RecName: Full=Actin-regulating kinase 1;
DE            EC=2.7.11.1;
GN   Name=ARK1; OrderedLocusNames=YNL020C; ORFNames=N2823;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313269; PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
RA   Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA   Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA   Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA   Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA   Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA   Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA   Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA   Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA   Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA   Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA   Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA   Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA   Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT   and its evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-56.
RX   MEDLINE=99189262; PubMed=10087264; DOI=10.1083/jcb.144.6.1203;
RA   Cope M.J.T.V., Yang S., Shang C., Drubin D.G.;
RT   "Novel protein kinases Ark1p and Prk1p associate with and regulate the
RT   cortical actin cytoskeleton in budding yeast.";
RL   J. Cell Biol. 144:1203-1218(1999).
RN   [3]
RP   FUNCTION.
RX   PubMed=11694597;
RA   Watson H.A., Cope M.J.T.V., Groen A.C., Drubin D.G., Wendland B.;
RT   "In vivo role for actin-regulating kinases in endocytosis and yeast
RT   epsin phosphorylation.";
RL   Mol. Biol. Cell 12:3668-3679(2001).
RN   [4]
RP   INTERACTION WITH ABP1.
RX   PubMed=11668184; DOI=10.1074/jbc.M109848200;
RA   Fazi B., Cope M.J.T.V., Douangamath A., Ferracuti S., Schirwitz K.,
RA   Zucconi A., Drubin D.G., Wilmanns M., Cesareni G., Castagnoli L.;
RT   "Unusual binding properties of the SH3 domain of the yeast actin-
RT   binding protein Abp1: structural and functional analysis.";
RL   J. Biol. Chem. 277:5290-5298(2002).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA   Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT   "Proteome-wide identification of in vivo targets of DNA damage
RT   checkpoint kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-502; SER-522;
RP   SER-535; SER-568 AND SER-569, AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Involved in regulation of actin cytoskeleton
CC       organization and endocytosis.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with ABP1, which is required for proper actin
CC       patch localization.
CC   -!- INTERACTION:
CC       P15891:ABP1; NbExp=2; IntAct=EBI-9817, EBI-2036;
CC       P53309:YAP1802; NbExp=1; IntAct=EBI-9817, EBI-23557;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch.
CC       Note=Cortical actin patches.
CC   -!- MISCELLANEOUS: Present with 1551 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; Z71296; CAA95882.1; -; Genomic_DNA.
DR   PIR; S62932; S62932.
DR   RefSeq; NP_014378.1; -.
DR   DIP; DIP:4381N; -.
DR   IntAct; P53974; 5.
DR   Ensembl; YNL020C; Saccharomyces cerevisiae.
DR   GeneID; 855711; -.
DR   GenomeReviews; Y13139_GR; YNL020C.
DR   KEGG; sce:YNL020C; -.
DR   NMPDR; fig|4932.3.peg.5456; -.
DR   CYGD; YNL020c; -.
DR   SGD; S000004965; ARK1.
DR   HOGENOM; P53974; -.
DR   LinkHub; P53974; -.
DR   NextBio; 980061; -.
DR   ArrayExpress; P53974; -.
DR   GermOnline; YNL020C; Saccharomyces cerevisiae.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0000147; P:actin cortical patch assembly; TAS:SGD.
DR   GO; GO:0007015; P:actin filament organization; IGI:SGD.
DR   GO; GO:0000910; P:cytokinesis; TAS:SGD.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   GO; GO:0030100; P:regulation of endocytosis; IMP:SGD.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_bd_CS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    638       Actin-regulating kinase 1.
FT                                /FTId=PRO_0000085635.
FT   DOMAIN       22    298       Protein kinase.
FT   NP_BIND      28     36       ATP (By similarity).
FT   REGION      602    615       Interaction with SH3 domain of ABP1.
FT   ACT_SITE    159    159       Proton acceptor (By similarity).
FT   BINDING      56     56       ATP (By similarity).
FT   MOD_RES     478    478       Phosphoserine.
FT   MOD_RES     502    502       Phosphoserine.
FT   MOD_RES     522    522       Phosphoserine.
FT   MOD_RES     535    535       Phosphoserine.
FT   MOD_RES     568    568       Phosphoserine.
FT   MOD_RES     569    569       Phosphoserine.
FT   MUTAGEN      56     56       K->A: Abolishes protein kinase activity.
SQ   SEQUENCE   638 AA;  71373 MW;  139CA4CA1B6A181F CRC64;
     MNQPQIGTYN VGTQLTVGSH QVEIIKYLTS GGFAQVYSAL INPPDPHSNS SVACLKRVIV
     PDKPSLNTLR AEVDAMRLLK NNRYVVSYID SHAAKAMLHN GSYEVFVLME YCERGGLIDF
     MNTRLQNRLH EFEILQIMSQ VTQGVAAMHA LQPPLIHRDI KIENVLISAN NEYKLCDFGS
     VCGIIRPPRN SQELSYVQQD ILKNTTAQYR SPEMIDTFRG LPIDEKSDIW ALGIFLYKLC
     YYTTPFEKGG DLAILSGKFE FPLYPNYSEQ LKGLIRDILV QDPRHRPNVY QLLKRISIMQ
     NVPCPINDIQ VVQAPSSHLN LTELHQLSAT QNILSLNSPT TMENTMPNAT FQISMADNTT
     TAQMHPNRKP SQIAYDASFS NSAKGSQPLF DKSQNMYHAL DPPLVEPLAS SVSNNDNELK
     ANSATKLKQA IVSEAHTFRQ NNSIDFPLQN IIPQYEDSSS SSDESYSGDV DELKKTRSLG
     SYSTRGNIKK NQSVKESLTS SSLPGTSFTP TSTKVNLKHE NSPFKSTFVN TIDNSKDDLN
     KPSYEDLDVS KQNLKNSIQQ RMIDKLNSSE ESFNARKMSK VKLHEKGEID KPTMLKSSGP
     ISKDKKTKPT PPPKPSHLKP KPPPKPLLLA GRKLSLDK
//