ATG1_YEAST
ID ATG1_YEAST Reviewed; 897 AA.
AC P53104; D6VTX3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Serine/threonine-protein kinase ATG1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:24440502, ECO:0000269|PubMed:24905091, ECO:0000269|PubMed:28821724};
DE AltName: Full=Autophagy protein 3 {ECO:0000303|PubMed:9190802};
DE AltName: Full=Autophagy-related protein 1 {ECO:0000303|PubMed:14536056};
DE AltName: Full=Cytoplasm to vacuole targeting protein 10 {ECO:0000303|PubMed:8663607};
GN Name=ATG1 {ECO:0000303|PubMed:14536056};
GN Synonyms=APG1 {ECO:0000303|PubMed:9169869},
GN AUT3 {ECO:0000303|PubMed:9190802}, CVT10 {ECO:0000303|PubMed:8663607};
GN OrderedLocusNames=YGL180W {ECO:0000312|SGD:S000003148}; ORFNames=G1615;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046087;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT from Saccharomyces cerevisiae.";
RL Yeast 13:55-64(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, AND
RP MUTAGENESIS OF ASP-211 AND GLU-237.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=9224897; DOI=10.1016/s0378-1119(97)00084-x;
RA Matsuura A., Tsukada M., Wada Y., Ohsumi Y.;
RT "Apg1p, a novel protein kinase required for the autophagic process in
RT Saccharomyces cerevisiae.";
RL Gene 192:245-250(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=8224160; DOI=10.1016/0014-5793(93)80398-e;
RA Tsukada M., Ohsumi Y.;
RT "Isolation and characterization of autophagy-defective mutants of
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 333:169-174(1993).
RN [6]
RP FUNCTION.
RX PubMed=8663607; DOI=10.1074/jbc.271.30.17621;
RA Harding T.M., Hefner-Gravink A., Thumm M., Klionsky D.J.;
RT "Genetic and phenotypic overlap between autophagy and the cytoplasm to
RT vacuole protein targeting pathway.";
RL J. Biol. Chem. 271:17621-17624(1996).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9190802; DOI=10.1128/jb.179.12.3875-3883.1997;
RA Straub M., Bredschneider M., Thumm M.;
RT "AUT3, a serine/threonine kinase gene, is essential for autophagocytosis in
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 179:3875-3883(1997).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=10837477; DOI=10.1074/jbc.m002813200;
RA Scott S.V., Nice D.C. III, Nau J.J., Weisman L.S., Kamada Y.,
RA Keizer-Gunnink I., Funakoshi T., Veenhuis M., Ohsumi Y., Klionsky D.J.;
RT "Apg13p and Vac8p are part of a complex of phosphoproteins that are
RT required for cytoplasm to vacuole targeting.";
RL J. Biol. Chem. 275:25840-25849(2000).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF LYS-54, AND INTERACTION WITH
RP ATG11; ATG13 AND ATG17.
RX PubMed=10995454; DOI=10.1083/jcb.150.6.1507;
RA Kamada Y., Funakoshi T., Shintani T., Nagano K., Ohsumi M., Ohsumi Y.;
RT "Tor-mediated induction of autophagy via an Apg1 protein kinase complex.";
RL J. Cell Biol. 150:1507-1513(2000).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11689437; DOI=10.1093/emboj/20.21.5971;
RA Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.;
RT "The pre-autophagosomal structure organized by concerted functions of APG
RT genes is essential for autophagosome formation.";
RL EMBO J. 20:5971-5981(2001).
RN [11]
RP INTERACTION WITH ATG11.
RX PubMed=11309418; DOI=10.1083/jcb.153.2.381;
RA Kim J., Kamada Y., Stromhaug P.E., Guan J., Hefner-Gravink A., Baba M.,
RA Scott S.V., Ohsumi Y., Dunn W.A. Jr., Klionsky D.J.;
RT "Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for
RT the vacuole.";
RL J. Cell Biol. 153:381-396(2001).
RN [12]
RP FUNCTION.
RX PubMed=11486014; DOI=10.1128/mcb.21.17.5742-5752.2001;
RA Wang Z., Wilson W.A., Fujino M.A., Roach P.J.;
RT "Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the
RT yeast homolog of AMP-activated protein kinase, and the cyclin-dependent
RT kinase Pho85p.";
RL Mol. Cell. Biol. 21:5742-5752(2001).
RN [13]
RP FUNCTION.
RX PubMed=11904149; DOI=10.1016/s0014-5793(02)02297-4;
RA Krampe S., Boles E.;
RT "Starvation-induced degradation of yeast hexose transporter Hxt7p is
RT dependent on endocytosis, autophagy and the terminal sequences of the
RT permease.";
RL FEBS Lett. 513:193-196(2002).
RN [14]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF LYS-54; MET-102; ASN-884 AND LEU-886.
RX PubMed=12589048; DOI=10.1091/mbc.e02-07-0413;
RA Abeliovich H., Zhang C., Dunn W.A. Jr., Shokat K.M., Klionsky D.J.;
RT "Chemical genetic analysis of Apg1 reveals a non-kinase role in the
RT induction of autophagy.";
RL Mol. Biol. Cell 14:477-490(2003).
RN [16]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX 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 [17]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [18]
RP FUNCTION.
RX PubMed=14723849; DOI=10.1016/s1534-5807(03)00402-7;
RA Reggiori F., Tucker K.A., Stromhaug P.E., Klionsky D.J.;
RT "The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from
RT the pre-autophagosomal structure.";
RL Dev. Cell 6:79-90(2004).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [20]
RP FUNCTION.
RX PubMed=17700056; DOI=10.4161/auto.4784;
RA Ma J., Jin R., Dobry C.J., Lawson S.K., Kumar A.;
RT "Overexpression of autophagy-related genes inhibits yeast filamentous
RT growth.";
RL Autophagy 3:604-609(2007).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17295840; DOI=10.1111/j.1365-2443.2007.01050.x;
RA Suzuki K., Kubota Y., Sekito T., Ohsumi Y.;
RT "Hierarchy of Atg proteins in pre-autophagosomal structure organization.";
RL Genes Cells 12:209-218(2007).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [23]
RP PHOSPHORYLATION AT SER-508 AND SER-515 BY PKA, MUTAGENESIS OF SER-508 AND
RP SER-515, AND FUNCTION.
RX PubMed=17699586; DOI=10.1091/mbc.e07-05-0485;
RA Yorimitsu T., Zaman S., Broach J.R., Klionsky D.J.;
RT "Protein kinase A and Sch9 cooperatively regulate induction of autophagy in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 18:4180-4189(2007).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=18497569; DOI=10.4161/auto.6308;
RA Ma J., Bharucha N., Dobry C.J., Frisch R.L., Lawson S., Kumar A.;
RT "Localization of autophagy-related proteins in yeast using a versatile
RT plasmid-based resource of fluorescent protein fusions.";
RL Autophagy 4:792-800(2008).
RN [25]
RP FUNCTION.
RX PubMed=18818209; DOI=10.1074/jbc.m802403200;
RA Kanki T., Klionsky D.J.;
RT "Mitophagy in yeast occurs through a selective mechanism.";
RL J. Biol. Chem. 283:32386-32393(2008).
RN [26]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18725539; DOI=10.1083/jcb.200801035;
RA Cao Y., Cheong H., Song H., Klionsky D.J.;
RT "In vivo reconstitution of autophagy in Saccharomyces cerevisiae.";
RL J. Cell Biol. 182:703-713(2008).
RN [27]
RP FUNCTION, AND INTERACTION WITH ATG13 AND ATG17.
RX PubMed=18077553; DOI=10.1091/mbc.e07-08-0826;
RA Cheong H., Nair U., Geng J., Klionsky D.J.;
RT "The Atg1 kinase complex is involved in the regulation of protein
RT recruitment to initiate sequestering vesicle formation for nonspecific
RT autophagy in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 19:668-681(2008).
RN [28]
RP FUNCTION.
RX PubMed=18701704; DOI=10.1091/mbc.e08-04-0363;
RA Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L.,
RA Millen J., Goldfarb D.S., Thumm M.;
RT "Piecemeal microautophagy of the nucleus requires the core macroautophagy
RT genes.";
RL Mol. Biol. Cell 19:4492-4505(2008).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-638 AND SER-647, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [31]
RP PHOSPHORYLATION AT THR-226 BY AUTOCATALYSIS, MUTAGENESIS OF THR-226,
RP ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=20439775; DOI=10.1534/genetics.110.116566;
RA Yeh Y.Y., Wrasman K., Herman P.K.;
RT "Autophosphorylation within the Atg1 activation loop is required for both
RT kinase activity and the induction of autophagy in Saccharomyces
RT cerevisiae.";
RL Genetics 185:871-882(2010).
RN [32]
RP FUNCTION.
RX PubMed=20855505; DOI=10.1083/jcb.200912089;
RA Mari M., Griffith J., Rieter E., Krishnappa L., Klionsky D.J., Reggiori F.;
RT "An Atg9-containing compartment that functions in the early steps of
RT autophagosome biogenesis.";
RL J. Cell Biol. 190:1005-1022(2010).
RN [33]
RP PHOSPHORYLATION AT SER-34; THR-129; SER-304; SER-365; SER-390; SER-515;
RP SER-533; SER-551; SER-552; THR-590; SER-621; SER-677; SER-680; SER-683;
RP SER-769 AND SER-783, MUTAGENESIS OF SER-34; SER-551; SER-552; SER-621;
RP SER-677; SER-680; SER-683; SER-769 AND SER-783, AND FUNCTION.
RX PubMed=21460632; DOI=10.4161/auto.7.7.15155;
RA Yeh Y.Y., Shah K.H., Chou C.C., Hsiao H.H., Wrasman K.M., Stephan J.S.,
RA Stamatakos D., Khoo K.H., Herman P.K.;
RT "The identification and analysis of phosphorylation sites on the Atg1
RT protein kinase.";
RL Autophagy 7:716-726(2011).
RN [34]
RP FUNCTION.
RX PubMed=21490424; DOI=10.4161/auto.7.8.15696;
RA Shin C.S., Huh W.K.;
RT "Bidirectional regulation between TORC1 and autophagy in Saccharomyces
RT cerevisiae.";
RL Autophagy 7:854-862(2011).
RN [35]
RP FUNCTION.
RX PubMed=21228276; DOI=10.1074/jbc.m110.177618;
RA Kario E., Amar N., Elazar Z., Navon A.;
RT "A new autophagy-related checkpoint in the degradation of an ERAD-M
RT target.";
RL J. Biol. Chem. 286:11479-11491(2011).
RN [36]
RP SUBUNIT, INTERACTION WITH ATG13, AND FUNCTION.
RX PubMed=21712380; DOI=10.1074/jbc.m111.250324;
RA Yeh Y.Y., Shah K.H., Herman P.K.;
RT "An Atg13 protein-mediated self-association of the Atg1 protein kinase is
RT important for the induction of autophagy.";
RL J. Biol. Chem. 286:28931-28939(2011).
RN [37]
RP FUNCTION.
RX PubMed=21576396; DOI=10.1083/jcb.201102092;
RA Mao K., Wang K., Zhao M., Xu T., Klionsky D.J.;
RT "Two MAPK-signaling pathways are required for mitophagy in Saccharomyces
RT cerevisiae.";
RL J. Cell Biol. 193:755-767(2011).
RN [38]
RP FUNCTION.
RX PubMed=22785534; DOI=10.1038/cddis.2012.90;
RA Clapp C., Portt L., Khoury C., Sheibani S., Norman G., Ebner P., Eid R.,
RA Vali H., Mandato C.A., Madeo F., Greenwood M.T.;
RT "14-3-3 protects against stress-induced apoptosis.";
RL Cell Death Dis. 3:E348-E348(2012).
RN [39]
RP INTERACTION WITH ATG13 AND ATG8, DOMAIN, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22885598; DOI=10.1038/emboj.2012.225;
RA Kraft C., Kijanska M., Kalie E., Siergiejuk E., Lee S.S., Semplicio G.,
RA Stoffel I., Brezovich A., Verma M., Hansmann I., Ammerer G., Hofmann K.,
RA Tooze S., Peter M.;
RT "Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8
RT regulates autophagy.";
RL EMBO J. 31:3691-3703(2012).
RN [40]
RP FUNCTION.
RX PubMed=22722939; DOI=10.1074/jbc.m112.361865;
RA Petroi D., Popova B., Taheri-Talesh N., Irniger S., Shahpasandzadeh H.,
RA Zweckstetter M., Outeiro T.F., Braus G.H.;
RT "Aggregate clearance of alpha-synuclein in Saccharomyces cerevisiae depends
RT more on autophagosome and vacuole function than on the proteasome.";
RL J. Biol. Chem. 287:27567-27579(2012).
RN [41]
RP INTERACTION WITH ATG8, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP TYR-429 AND VAL-432.
RX PubMed=22778255; DOI=10.1074/jbc.c112.387514;
RA Nakatogawa H., Ohbayashi S., Sakoh-Nakatogawa M., Kakuta S., Suzuki S.W.,
RA Kirisako H., Kondo-Kakuta C., Noda N.N., Yamamoto H., Ohsumi Y.;
RT "The autophagy-related protein kinase Atg1 interacts with the ubiquitin-
RT like protein Atg8 via the Atg8 family interacting motif to facilitate
RT autophagosome formation.";
RL J. Biol. Chem. 287:28503-28507(2012).
RN [42]
RP FUNCTION.
RX PubMed=22977244; DOI=10.1074/jbc.m112.371591;
RA Wang K., Yang Z., Liu X., Mao K., Nair U., Klionsky D.J.;
RT "Phosphatidylinositol 4-kinases are required for autophagic membrane
RT trafficking.";
RL J. Biol. Chem. 287:37964-37972(2012).
RN [43]
RP FUNCTION.
RX PubMed=22768199; DOI=10.1371/journal.pone.0040013;
RA Mijaljica D., Prescott M., Devenish R.J.;
RT "A late form of nucleophagy in Saccharomyces cerevisiae.";
RL PLoS ONE 7:E40013-E40013(2012).
RN [44]
RP FUNCTION.
RX PubMed=23230142; DOI=10.1242/jcs.103713;
RA Deffieu M., Bhatia-Kissova I., Salin B., Klionsky D.J., Pinson B.,
RA Manon S., Camougrand N.;
RT "Increased levels of reduced cytochrome b and mitophagy components are
RT required to trigger nonspecific autophagy following induced mitochondrial
RT dysfunction.";
RL J. Cell Sci. 126:415-426(2013).
RN [45]
RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF LYS-54 AND ASP-211.
RX PubMed=23549786; DOI=10.1242/jcs.122960;
RA Suzuki K., Akioka M., Kondo-Kakuta C., Yamamoto H., Ohsumi Y.;
RT "Fine mapping of autophagy-related proteins during autophagosome formation
RT in Saccharomyces cerevisiae.";
RL J. Cell Sci. 126:2534-2544(2013).
RN [46]
RP FUNCTION.
RX PubMed=23382696; DOI=10.1371/journal.pgen.1003245;
RA Matsui A., Kamada Y., Matsuura A.;
RT "The role of autophagy in genome stability through suppression of abnormal
RT mitosis under starvation.";
RL PLoS Genet. 9:E1003245-E1003245(2013).
RN [47]
RP FUNCTION IN PHOSPHORYLATION OF ATG9, AND CATALYTIC ACTIVITY.
RX PubMed=24905091; DOI=10.4161/auto.28971;
RA Papinski D., Kraft C.;
RT "Atg1 kinase organizes autophagosome formation by phosphorylating Atg9.";
RL Autophagy 10:1338-1340(2014).
RN [48]
RP PHOSPHORYLATION AT SER-356; SER-390 AND SER-517, FUNCTION, CATALYTIC
RP ACTIVITY, AND MUTAGENESIS OF ASP-211.
RX PubMed=24440502; DOI=10.1016/j.molcel.2013.12.011;
RA Papinski D., Schuschnig M., Reiter W., Wilhelm L., Barnes C.A.,
RA Maiolica A., Hansmann I., Pfaffenwimmer T., Kijanska M., Stoffel I.,
RA Lee S.S., Brezovich A., Lou J.H., Turk B.E., Aebersold R., Ammerer G.,
RA Peter M., Kraft C.;
RT "Early steps in autophagy depend on direct phosphorylation of Atg9 by the
RT Atg1 kinase.";
RL Mol. Cell 53:471-483(2014).
RN [49]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-211.
RX PubMed=28821724; DOI=10.1038/s41467-017-00302-3;
RA Sanchez-Wandelmer J., Kriegenburg F., Rohringer S., Schuschnig M.,
RA Gomez-Sanchez R., Zens B., Abreu S., Hardenberg R., Hollenstein D., Gao J.,
RA Ungermann C., Martens S., Kraft C., Reggiori F.;
RT "Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation.";
RL Nat. Commun. 8:295-295(2017).
CC -!- FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to
CC vacuole transport (Cvt) and found to be essential in autophagy, where
CC it is required for the formation of autophagosomes. Involved in the
CC clearance of protein aggregates which cannot be efficiently cleared by
CC the proteasome. Required for selective autophagic degradation of the
CC nucleus (nucleophagy) as well as for mitophagy which contributes to
CC regulate mitochondrial quantity and quality by eliminating the
CC mitochondria to a basal level to fulfill cellular energy requirements
CC and preventing excess ROS production (PubMed:18818209, PubMed:21576396,
CC PubMed:22768199, PubMed:23230142). Also involved in endoplasmic
CC reticulum-specific autophagic process, in selective removal of ER-
CC associated degradation (ERAD) substrates (PubMed:21228276). Plays a key
CC role in ATG9 and ATG23 cycling through the pre-autophagosomal structure
CC and is necessary to promote ATG18 binding to ATG9 through
CC phosphorylation of ATG9 (PubMed:14723849, PubMed:20855505,
CC PubMed:24905091, PubMed:24440502). Catalyzes phosphorylation of ATG4,
CC decreasing the interaction between ATG4 and ATG8 and impairing
CC deconjugation of PE-conjugated forms of ATG8 (PubMed:28821724).
CC Finally, ATG1 is also required for the maintenance of cell viability
CC under starvation and for glycogen storage during stationary phase.
CC Plays a role in genome stability through suppression of abnormal
CC mitosis under starvation, and in regulation of filamentous growth.
CC {ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:11486014,
CC ECO:0000269|PubMed:11689437, ECO:0000269|PubMed:11904149,
CC ECO:0000269|PubMed:12589048, ECO:0000269|PubMed:14723849,
CC ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:17699586,
CC ECO:0000269|PubMed:17700056, ECO:0000269|PubMed:18077553,
CC ECO:0000269|PubMed:18701704, ECO:0000269|PubMed:18725539,
CC ECO:0000269|PubMed:18818209, ECO:0000269|PubMed:20439775,
CC ECO:0000269|PubMed:20855505, ECO:0000269|PubMed:21228276,
CC ECO:0000269|PubMed:21460632, ECO:0000269|PubMed:21490424,
CC ECO:0000269|PubMed:21576396, ECO:0000269|PubMed:21712380,
CC ECO:0000269|PubMed:22722939, ECO:0000269|PubMed:22768199,
CC ECO:0000269|PubMed:22785534, ECO:0000269|PubMed:22885598,
CC ECO:0000269|PubMed:22977244, ECO:0000269|PubMed:23230142,
CC ECO:0000269|PubMed:23382696, ECO:0000269|PubMed:23549786,
CC ECO:0000269|PubMed:24440502, ECO:0000269|PubMed:24905091,
CC ECO:0000269|PubMed:28821724, ECO:0000269|PubMed:8224160,
CC ECO:0000269|PubMed:8663607, ECO:0000269|PubMed:9190802,
CC ECO:0000269|PubMed:9224897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:24440502, ECO:0000269|PubMed:24905091,
CC ECO:0000269|PubMed:28821724};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:24440502,
CC ECO:0000269|PubMed:24905091};
CC -!- ACTIVITY REGULATION: Activated by hypophosphorylated form of ATG13
CC (present in nitrogen starvation conditions). Also activated by
CC autophopsphorylation of Thr-226 and inhibited by phosphorylation of
CC Ser-34. {ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:20439775}.
CC -!- SUBUNIT: Homodimer. Dimerization requires the presence of ATG13. Forms
CC a ternary complex with ATG13 and ATG17. Interacts also with ATG11.
CC {ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:11309418,
CC ECO:0000269|PubMed:18077553, ECO:0000269|PubMed:21712380,
CC ECO:0000269|PubMed:22778255, ECO:0000269|PubMed:22885598}.
CC -!- INTERACTION:
CC P53104; Q12527: ATG11; NbExp=3; IntAct=EBI-2657, EBI-31977;
CC P53104; Q06628: ATG13; NbExp=18; IntAct=EBI-2657, EBI-36188;
CC P53104; P35193: ATG19; NbExp=2; IntAct=EBI-2657, EBI-29291;
CC P53104; P38182: ATG8; NbExp=3; IntAct=EBI-2657, EBI-2684;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Preautophagosomal structure membrane;
CC Peripheral membrane protein. Note=Formes punctate structures in
CC starvation conditions only when ATG13 and ATG17 were both present.
CC Localizes to both the isolation membrane (IM) and the vacuole-isolation
CC membrane contact site (VICS) during IM expansion. The IM is a membrane
CC sac generated from the pre-autophagosomal structure that ultimately
CC expands to become a mature autophagosome.
CC -!- DOMAIN: The LIR motif is required for the interaction with ATG8 and for
CC the association of ATG1 with autophagosomes.
CC {ECO:0000269|PubMed:22778255, ECO:0000269|PubMed:22885598}.
CC -!- PTM: Autophosphorylated at Thr-226 and Ser-390. The phosphorylation
CC state may play a role in the induction of protein degradation upon
CC starvation. Phosphorylation at Thr-226 within the activation loop is
CC required for protein kinase activity whereas phosphorylation at Ser-34
CC leads to inhibition of kinase activity. Phosphorylation of Ser-508 and
CC Ser-515 by PKA is required to induce autophagy but not for kinase
CC activity. {ECO:0000269|PubMed:17699586, ECO:0000269|PubMed:20439775,
CC ECO:0000269|PubMed:21460632, ECO:0000269|PubMed:24440502,
CC ECO:0000269|PubMed:9224897}.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X91489; CAA62794.1; -; Genomic_DNA.
DR EMBL; D29991; BAA21481.1; -; Genomic_DNA.
DR EMBL; Z72702; CAA96892.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07934.1; -; Genomic_DNA.
DR PIR; S61137; S61137.
DR RefSeq; NP_011335.1; NM_001181045.1.
DR AlphaFoldDB; P53104; -.
DR SMR; P53104; -.
DR BioGRID; 33074; 626.
DR ComplexPortal; CPX-1676; ATG1 kinase complex.
DR DIP; DIP-1192N; -.
DR IntAct; P53104; 24.
DR MINT; P53104; -.
DR STRING; 4932.YGL180W; -.
DR TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; P53104; -.
DR MaxQB; P53104; -.
DR PaxDb; P53104; -.
DR PRIDE; P53104; -.
DR EnsemblFungi; YGL180W_mRNA; YGL180W; YGL180W.
DR GeneID; 852695; -.
DR KEGG; sce:YGL180W; -.
DR SGD; S000003148; ATG1.
DR VEuPathDB; FungiDB:YGL180W; -.
DR eggNOG; KOG0595; Eukaryota.
DR GeneTree; ENSGT00940000157689; -.
DR HOGENOM; CLU_006447_0_0_1; -.
DR InParanoid; P53104; -.
DR OMA; INNVVQW; -.
DR BioCyc; YEAST:G3O-30667-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:P53104; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53104; protein.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:SGD.
DR GO; GO:0000421; C:autophagosome membrane; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0097635; C:extrinsic component of autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0061908; C:phagophore; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0044805; P:late nucleophagy; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IC:ComplexPortal.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IMP:SGD.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR022708; Ser/Thr_kinase_C.
DR PANTHER; PTHR24348; PTHR24348; 1.
DR Pfam; PF12063; DUF3543; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Autophagy; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transport.
FT CHAIN 1..897
FT /note="Serine/threonine-protein kinase ATG1"
FT /id="PRO_0000085655"
FT DOMAIN 24..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..886
FT /note="Required for Cvt trafficking"
FT MOTIF 429..432
FT /note="LIR"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 226
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20439775"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 356
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 390
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:21460632,
FT ECO:0000269|PubMed:24440502, ECO:0007744|PubMed:18407956"
FT MOD_RES 508
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:17699586"
FT MOD_RES 515
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:17699586,
FT ECO:0000269|PubMed:21460632"
FT MOD_RES 517
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 590
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632,
FT ECO:0007744|PubMed:15665377"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 34
FT /note="S->D,E: Impairs kinase activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 54
FT /note="K->A: Defect in the Cvt pathway."
FT /evidence="ECO:0000269|PubMed:10995454,
FT ECO:0000269|PubMed:12589048, ECO:0000269|PubMed:23549786"
FT MUTAGEN 102
FT /note="M->A: Enables the binding of the inhibitor of the
FT kinase activity 1-NA-PP1."
FT /evidence="ECO:0000269|PubMed:12589048"
FT MUTAGEN 211
FT /note="D->A: Abolished kinase activity. Loss of cell
FT viability under starvation."
FT /evidence="ECO:0000269|PubMed:23549786,
FT ECO:0000269|PubMed:24440502, ECO:0000269|PubMed:28821724,
FT ECO:0000269|PubMed:9224897"
FT MUTAGEN 226
FT /note="T->E: Leads to constitutive autophosphorylation
FT activity."
FT /evidence="ECO:0000269|PubMed:20439775"
FT MUTAGEN 237
FT /note="E->R: Loss of cell viability under starvation."
FT /evidence="ECO:0000269|PubMed:9224897"
FT MUTAGEN 429
FT /note="Y->A: Impairs interaction with ATG8 and decreases
FT autophagy efficiency; when associated with A-432."
FT /evidence="ECO:0000269|PubMed:22778255"
FT MUTAGEN 432
FT /note="V->A: Impairs interaction with ATG8 and decreases
FT autophagy efficiency; when associated with A-429."
FT /evidence="ECO:0000269|PubMed:22778255"
FT MUTAGEN 508
FT /note="S->A: Impairs autophagic activity; when associated
FT with A-515."
FT /evidence="ECO:0000269|PubMed:17699586"
FT MUTAGEN 515
FT /note="S->A: Impairs autophagic activity; when associated
FT with A-508."
FT /evidence="ECO:0000269|PubMed:17699586"
FT MUTAGEN 551
FT /note="S->A: Decreases autophagic activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 552
FT /note="S->A: Decreases autophagic activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 621
FT /note="S->A: Decreases autophagic activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 677
FT /note="S->A: Decreases autophagic activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 680
FT /note="S->A: Decreases autophagic activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 683
FT /note="S->A: Decreases autophagic activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 769
FT /note="S->A: Decreases autophagic activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 783
FT /note="S->A: Decreases autophagic activity."
FT /evidence="ECO:0000269|PubMed:21460632"
FT MUTAGEN 884
FT /note="N->A: No effect."
FT /evidence="ECO:0000269|PubMed:12589048"
FT MUTAGEN 886
FT /note="L->G: Cvt pathway specific block."
FT /evidence="ECO:0000269|PubMed:12589048"
SQ SEQUENCE 897 AA; 101717 MW; 7F4C785AA3A7CC46 CRC64;
MGDIKNKDHT TSVNHNLMAS AGNYTAEKEI GKGSFATVYR GHLTSDKSQH VAIKEVSRAK
LKNKKLLENL EIEIAILKKI KHPHIVGLID CERTSTDFYL IMEYCALGDL TFLLKRRKEL
MENHPLLRTV FEKYPPPSEN HNGLHRAFVL SYLQQLASAL KFLRSKNLVH RDIKPQNLLL
STPLIGYHDS KSFHELGFVG IYNLPILKIA DFGFARFLPN TSLAETLCGS PLYMAPEILN
YQKYNAKADL WSVGTVVFEM CCGTPPFRAS NHLELFKKIK RANDVITFPS YCNIEPELKE
LICSLLTFDP AQRIGFEEFF ANKVVNEDLS SYELEDDLPE LESKSKGIVE SNMFVSEYLS
KQPKSPNSNL AGHQSMADNP AELSDALKNS NILTAPAVKT DHTQAVDKKA SNNKYHNSLV
SDRSFEREYV VVEKKSVEVN SLADEVAQAG FNPNPIKHPT STQNQNVLLN EQFSPNNQQY
FQNQGENPRL LRATSSSSGG SDGSRRPSLV DRRLSISSLN PSNALSRALG IASTRLFGGA
NQQQQQQQIT SSPPYSQTLL NSQLFHELTE NIILRIDHLQ HPETLKLDNT NIVSILESLA
AKAFVVYSYA EVKFSQIVPL STTLKGMANF ENRRSMDSNA IAEEQDSDDA EEEDETLKKY
KEDCLSTKTF GKGRTLSATS QLSATFNKLP RSEMILLCNE AIVLYMKALS ILSKSMQVTS
NWWYESQEKS CSLRVNVLVQ WLREKFNECL EKADFLRLKI NDLRFKHASE VAENQTLEEK
GSSEEPVYLE KLLYDRALEI SKMAAHMELK GENLYNCELA YATSLWMLET SLDDDDFTNA
YGDYPFKTNI HLKSNDVEDK EKYHSVLDEN DRIIIRKYID SIANRLKILR QKMNHQN
