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 27-MAR-2024, entry version 210. 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}, AUT3 GN {ECO:0000303|PubMed:9190802}, CVT10 {ECO:0000303|PubMed:8663607}; GN OrderedLocusNames=YGL180W {ECO:0000312|SGD:S000003148}; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 639. DR ComplexPortal; CPX-1676; ATG1 protein 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; 4932-YGL180W; -. DR PeptideAtlas; P53104; -. DR EnsemblFungi; YGL180W_mRNA; YGL180W; YGL180W. DR GeneID; 852695; -. DR KEGG; sce:YGL180W; -. DR AGR; SGD:S000003148; -. 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 OrthoDB; 2786057at2759; -. DR BioCyc; YEAST:G3O-30667-MONOMER; -. DR BRENDA; 2.7.11.1; 984. DR Reactome; R-SCE-1632852; Macroautophagy. DR Reactome; R-SCE-8934903; Receptor Mediated Mitophagy. DR BioGRID-ORCS; 852695; 6 hits in 13 CRISPR screens. 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:0005776; C:autophagosome; IBA:GO_Central. 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: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:0016236; P:macroautophagy; IMP:SGD. DR GO; GO:0044804; P:nucleophagy; IMP:SGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central. DR GO; GO:0042594; P:response to starvation; IBA:GO_Central. DR GO; GO:0061709; P:reticulophagy; IMP:SGD. DR CDD; cd14009; STKc_ATG1_ULK_like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR045269; Atg1-like. DR InterPro; IPR048941; ATG1-like_MIT2. DR InterPro; IPR022708; Atg1-like_tMIT. 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 PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1. DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1. DR Pfam; PF12063; ATG1-like_MIT1; 1. DR Pfam; PF21127; ATG1-like_MIT2; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //