ID ATG13_YEAST Reviewed; 738 AA. AC Q06628; D6W4I5; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 177. DE RecName: Full=Autophagy-related protein 13; GN Name=ATG13; Synonyms=APG13; OrderedLocusNames=YPR185W; 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]. RX PubMed=9224892; DOI=10.1016/s0378-1119(97)00031-0; RA Funakoshi T., Matsuura A., Noda T., Ohsumi Y.; RT "Analyses of APG13 gene involved in autophagy in yeast, Saccharomyces RT cerevisiae."; RL Gene 192:207-213(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] 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 [4] 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 [5] RP FUNCTION, INTERACTION WITH VAC8, AND PHOSPHORYLATION. 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 [6] RP FUNCTION. RX PubMed=11086004; DOI=10.1083/jcb.151.5.1025; RA Abeliovich H., Dunn W.A. Jr., Kim J., Klionsky D.J.; RT "Dissection of autophagosome biogenesis into distinct nucleation and RT expansion steps."; RL J. Cell Biol. 151:1025-1034(2000). RN [7] RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH ATG1. 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 [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] RP FUNCTION, AND INTERACTION WITH ATG1 AND ATG17. RX PubMed=15743910; DOI=10.1091/mbc.e04-08-0669; RA Kabeya Y., Kamada Y., Baba M., Takikawa H., Sasaki M., Ohsumi Y.; RT "Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy."; RL Mol. Biol. Cell 16:2544-2553(2005). RN [14] RP INTERACTION WITH ATG1 AND ATG17. RX PubMed=15901835; DOI=10.1091/mbc.e04-10-0894; RA Cheong H., Yorimitsu T., Reggiori F., Legakis J.E., Wang C.W., RA Klionsky D.J.; RT "Atg17 regulates the magnitude of the autophagic response."; RL Mol. Biol. Cell 16:3438-3453(2005). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, 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 [16] RP FUNCTION. RX PubMed=17426440; DOI=10.4161/auto.4129; RA Legakis J.E., Yen W.L., Klionsky D.J.; RT "A cycling protein complex required for selective autophagy."; RL Autophagy 3:422-432(2007). RN [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY RP 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 [19] RP FUNCTION, AND PHOSPHORYLATION. 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 [20] RP FUNCTION. 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 [21] RP FUNCTION OF THE ATG1-ATG13 COMPLEX. RX PubMed=18287526; DOI=10.1091/mbc.e07-10-1048; RA Kawamata T., Kamada Y., Kabeya Y., Sekito T., Ohsumi Y.; RT "Organization of the pre-autophagosomal structure responsible for RT autophagosome formation."; RL Mol. Biol. Cell 19:2039-2050(2008). RN [22] RP INTERACTION WITH ATG1. RX PubMed=18829864; DOI=10.1091/mbc.e08-05-0544; RA He C., Baba M., Cao Y., Klionsky D.J.; RT "Self-interaction is critical for Atg9 transport and function at the RT phagophore assembly site during autophagy."; RL Mol. Biol. Cell 19:5506-5516(2008). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-461; SER-554 AND RP SER-649, AND IDENTIFICATION BY 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 [24] RP INTERACTION WITH THE ATG17-ATG29-ATG31 COMPLEX. RX PubMed=19755117; DOI=10.1016/j.bbrc.2009.09.034; RA Kabeya Y., Noda N.N., Fujioka Y., Suzuki K., Inagaki F., Ohsumi Y.; RT "Characterization of the Atg17-Atg29-Atg31 complex specifically required RT for starvation-induced autophagy in Saccharomyces cerevisiae."; RL Biochem. Biophys. Res. Commun. 389:612-615(2009). RN [25] RP PHOSPHORYLATION AT SER-344; SER-437 AND SER-581 BY PKA, MUTAGENESIS OF RP SER-344; SER-437 AND SER-581, FUNCTION, AND INTERACTION WITH ATG17. RX PubMed=19805182; DOI=10.1073/pnas.0903316106; RA Stephan J.S., Yeh Y.Y., Ramachandran V., Deminoff S.J., Herman P.K.; RT "The Tor and PKA signaling pathways independently target the Atg1/Atg13 RT protein kinase complex to control autophagy."; RL Proc. Natl. Acad. Sci. U.S.A. 106:17049-17054(2009). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-461 AND SER-649, 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 [27] RP FUNCTION. RX PubMed=20647741; DOI=10.4161/auto.6.7.12753; RA Ecker N., Mor A., Journo D., Abeliovich H.; RT "Induction of autophagic flux by amino acid deprivation is distinct from RT nitrogen starvation-induced macroautophagy."; RL Autophagy 6:879-890(2010). RN [28] RP INTERACTION WITH ATG1. RX PubMed=20953146; DOI=10.4161/auto.6.8.13849; RA Kijanska M., Dohnal I., Reiter W., Kaspar S., Stoffel I., Ammerer G., RA Kraft C., Peter M.; RT "Activation of Atg1 kinase in autophagy by regulated phosphorylation."; RL Autophagy 6:1168-1178(2010). RN [29] RP FUNCTION, AND INTERACTION WITH ATG1. 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 [30] 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 [31] RP PHOSPHORYLATION AT SER-348; SER-437; SER-438; SER-496; SER-535; SER-541; RP SER-646 AND SER-649, MUTAGENESIS OF SER-348; SER-437; SER-438; SER-496; RP SER-535; SER-541; SER-646 AND SER-649, AND FUNCTION. RX PubMed=19995911; DOI=10.1128/mcb.01344-09; RA Kamada Y., Yoshino K., Kondo C., Kawamata T., Oshiro N., Yonezawa K., RA Ohsumi Y.; RT "Tor directly controls the Atg1 kinase complex to regulate autophagy."; RL Mol. Cell. Biol. 30:1049-1058(2010). RN [32] RP PHOSPHORYLATION BY ATG1. 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 [33] RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION OF THE ATG1-ATG13 RP COMPLEX. RX PubMed=21468027; DOI=10.1038/emboj.2011.104; RA Graef M., Nunnari J.; RT "Mitochondria regulate autophagy by conserved signalling pathways."; RL EMBO J. 30:2101-2114(2011). RN [34] RP PHOSPHORYLATION, AND DEPHOSPHORYLATION. RX PubMed=21078689; DOI=10.1534/genetics.110.123372; RA Ramachandran V., Herman P.K.; RT "Antagonistic interactions between the cAMP-dependent protein kinase and RT Tor signaling pathways modulate cell growth in Saccharomyces cerevisiae."; RL Genetics 187:441-454(2011). RN [35] RP FUNCTION, AND INTERACTION WITH ATG1. 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 [36] RP PHOSPHORYLATION, AND DEPHOSPHORYLATION. RX PubMed=21900499; DOI=10.1091/mbc.e11-06-0525; RA Wu X., Tu B.P.; RT "Selective regulation of autophagy by the Iml1-Npr2-Npr3 complex in the RT absence of nitrogen starvation."; RL Mol. Biol. Cell 22:4124-4133(2011). RN [37] RP INTERACTION WITH THE ATG17-ATG29-ATG31 COMPLEX. RX PubMed=23219485; DOI=10.1016/j.cell.2012.11.028; RA Ragusa M.J., Stanley R.E., Hurley J.H.; RT "Architecture of the Atg17 complex as a scaffold for autophagosome RT biogenesis."; RL Cell 151:1501-1512(2012). RN [38] RP FUNCTION, INTERACTION WITH ATG1, AND MUTAGENESIS OF PHE-468 AND VAL-469. 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 [39] RP FUNCTION, AND PHOSPHORYLATION BY TORC1 COMPLEX. RX PubMed=22447937; DOI=10.1074/jbc.m112.344952; RA Umekawa M., Klionsky D.J.; RT "Ksp1 kinase regulates autophagy via the target of rapamycin complex 1 RT (TORC1) pathway."; RL J. Biol. Chem. 287:16300-16310(2012). RN [40] RP FUNCTION, AND INTERACTION WITH ATG1. 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 [41] RP FUNCTION, AND PHOSPHORYLATION. RX PubMed=22782902; DOI=10.1074/jbc.m112.344192; RA Lisa-Santamaria P., Jimenez A., Revuelta J.L.; RT "The protein factor-arrest 11 (Far11) is essential for the toxicity of RT human caspase-10 in yeast and participates in the regulation of autophagy RT and the DNA damage signaling."; RL J. Biol. Chem. 287:29636-29647(2012). RN [42] RP PHOSPHORYLATION. RX PubMed=22727621; DOI=10.1016/j.molcel.2012.05.019; RA Takahara T., Maeda T.; RT "Transient sequestration of TORC1 into stress granules during heat RT stress."; RL Mol. Cell 47:242-252(2012). RN [43] RP PHOSPHORYLATION. RX PubMed=29698392; DOI=10.1371/journal.pgen.1007334; RA Ukai H., Araki Y., Kira S., Oikawa Y., May A.I., Noda T.; RT "Gtr/Ego-independent TORC1 activation is achieved through a glutamine- RT sensitive interaction with Pib2 on the vacuolar membrane."; RL PLoS Genet. 14:e1007334-e1007334(2018). RN [44] {ECO:0007744|PDB:6KBM, ECO:0007744|PDB:6KBN} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 567-695 IN COMPLEX WITH VA8, RP FUNCTION, INTERACTION WITH ATG13, AND DOMAIN. RX PubMed=31512555; DOI=10.1080/15548627.2019.1659615; RA Park J., Kim H.I., Jeong H., Lee M., Jang S.H., Yoon S.Y., Kim H., RA Park Z.Y., Jun Y., Lee C.; RT "Quaternary structures of Vac8 differentially regulate the Cvt and PMN RT pathways."; RL Autophagy 16:991-1006(2020). CC -!- FUNCTION: Activates the ATG1 kinase in a nutritional condition CC dependent manner through the TOR pathway, leading to autophagy CC (PubMed:10995454, PubMed:11086004, PubMed:15743910, PubMed:17295840, CC PubMed:18077553, PubMed:18287526, PubMed:19805182, PubMed:19995911, CC PubMed:20647741, PubMed:20855505, PubMed:22447937, PubMed:22778255, CC PubMed:22782902, PubMed:22885598, PubMed:8224160, PubMed:21468027). CC Required for autophosphorylation of ATG1 at 'Thr-226' and its CC dimerization (PubMed:20439775, PubMed:17699586, PubMed:21712380). May CC also be involved in the regulation of autophagy through SNF1 CC (PubMed:11486014). Involved in ATG9 and ATG23 cycling through the pre- CC autophagosomal structure (PubMed:14723849, PubMed:17426440). Also CC involved in cytoplasm to vacuole transport (Cvt) and more specifically CC in Cvt vesicle formation (PubMed:10837477). Seems to play a role in the CC switching machinery regulating the conversion between the Cvt pathway CC and autophagy (PubMed:10837477, PubMed:31512555). Finally, ATG13 is CC also required for glycogen storage during stationary phase CC (PubMed:11486014). {ECO:0000269|PubMed:10837477, CC ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:11086004, CC ECO:0000269|PubMed:11486014, ECO:0000269|PubMed:14723849, CC ECO:0000269|PubMed:15743910, ECO:0000269|PubMed:17295840, CC ECO:0000269|PubMed:17426440, ECO:0000269|PubMed:17699586, CC ECO:0000269|PubMed:18077553, ECO:0000269|PubMed:18287526, CC ECO:0000269|PubMed:19805182, ECO:0000269|PubMed:19995911, CC ECO:0000269|PubMed:20439775, ECO:0000269|PubMed:20647741, CC ECO:0000269|PubMed:20855505, ECO:0000269|PubMed:21468027, CC ECO:0000269|PubMed:21712380, ECO:0000269|PubMed:22447937, CC ECO:0000269|PubMed:22778255, ECO:0000269|PubMed:22782902, CC ECO:0000269|PubMed:22885598, ECO:0000269|PubMed:31512555, CC ECO:0000269|PubMed:8224160}. CC -!- SUBUNIT: Hypophosphorylated form interacts with ATG1 to form the ATG1- CC ATG13 kinase complex (PubMed:10995454, PubMed:15743910, CC PubMed:15901835, PubMed:18829864, PubMed:20439775, PubMed:20953146, CC PubMed:21712380, PubMed:22778255, PubMed:22885598). The ATG1-ATG13 CC complex interacts with the ATG17-ATG29-ATG31 complex through direct CC interaction with ATG17 (PubMed:23219485, PubMed:15743910, CC PubMed:15901835, PubMed:19755117, PubMed:19805182). Interacts with VAC8 CC and forms heterotetramers of two VAC8 and two ATG13 (PubMed:10837477, CC PubMed:31512555). {ECO:0000269|PubMed:10837477, CC ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:15743910, CC ECO:0000269|PubMed:15901835, ECO:0000269|PubMed:18829864, CC ECO:0000269|PubMed:19755117, ECO:0000269|PubMed:19805182, CC ECO:0000269|PubMed:20439775, ECO:0000269|PubMed:20953146, CC ECO:0000269|PubMed:21712380, ECO:0000269|PubMed:22778255, CC ECO:0000269|PubMed:22885598, ECO:0000269|PubMed:23219485, CC ECO:0000269|PubMed:31512555}. CC -!- INTERACTION: CC Q06628; P53104: ATG1; NbExp=18; IntAct=EBI-36188, EBI-2657; CC Q06628; Q06410: ATG17; NbExp=6; IntAct=EBI-36188, EBI-30856; CC Q06628; P39968: VAC8; NbExp=7; IntAct=EBI-36188, EBI-20212; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC Preautophagosomal structure {ECO:0000269|PubMed:17295840, CC ECO:0000269|PubMed:21468027}. CC -!- DOMAIN: The extended 70 Angstroms-longloop of ATG13 specifically binds CC the highly conserved innergroove formed by the armadillo repeats of CC VAC8. {ECO:0000269|PubMed:31512555}. CC -!- PTM: Phosphorylated; hyperphosphorylated by the TORC1 kinase complex to CC repress the induction of autophagy in nutrient-replete conditions CC (PubMed:10995454, PubMed:19995911, PubMed:19805182, PubMed:22447937, CC PubMed:22727621, PubMed:29698392). Starvation and TOR inactivation CC results in ATG13 partial dephosphorylation leading to ATG1-binding CC (PubMed:10995454). Rephosphorylated by ATG1 during prolonged nitrogen CC starvation (PubMed:21490424). Also phosphorylated by PKA CC (PubMed:17699586, PubMed:19805182, PubMed:21078689). PKA CC phosphorylation regulates the association of ATG13 with the PAS CC (PubMed:21900499). Within this regulatory network, mitochondrial CC respiratory deficiency suppresses autophagic flux (PubMed:21468027). CC Hyperphosphorylation in rich medium is impaired in the absence of VAC8 CC (PubMed:10837477). Dephosphorylation is dependent on FAR11 CC (PubMed:22782902). {ECO:0000269|PubMed:10837477, CC ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:17699586, CC ECO:0000269|PubMed:19805182, ECO:0000269|PubMed:19995911, CC ECO:0000269|PubMed:21078689, ECO:0000269|PubMed:21468027, CC ECO:0000269|PubMed:21490424, ECO:0000269|PubMed:21900499, CC ECO:0000269|PubMed:22447937, ECO:0000269|PubMed:22727621, CC ECO:0000269|PubMed:22782902, ECO:0000269|PubMed:29698392}. CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily. CC {ECO:0000305}. 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; U25842; AAB68118.1; -; Genomic_DNA. DR EMBL; D88025; BAA21485.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11601.1; -; Genomic_DNA. DR PIR; S59842; S59842. DR RefSeq; NP_015511.1; NM_001184282.1. DR PDB; 6KBM; X-ray; 2.90 A; B=567-695. DR PDB; 6KBN; X-ray; 3.20 A; B/D=567-695. DR PDBsum; 6KBM; -. DR PDBsum; 6KBN; -. DR AlphaFoldDB; Q06628; -. DR SMR; Q06628; -. DR BioGRID; 36357; 210. DR ComplexPortal; CPX-1676; ATG1 protein kinase complex. DR DIP; DIP-1191N; -. DR IntAct; Q06628; 10. DR MINT; Q06628; -. DR STRING; 4932.YPR185W; -. DR TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family. DR iPTMnet; Q06628; -. DR MaxQB; Q06628; -. DR PaxDb; 4932-YPR185W; -. DR PeptideAtlas; Q06628; -. DR TopDownProteomics; Q06628; -. DR EnsemblFungi; YPR185W_mRNA; YPR185W; YPR185W. DR GeneID; 856315; -. DR KEGG; sce:YPR185W; -. DR AGR; SGD:S000006389; -. DR SGD; S000006389; ATG13. DR VEuPathDB; FungiDB:YPR185W; -. DR eggNOG; KOG4573; Eukaryota. DR HOGENOM; CLU_411076_0_0_1; -. DR InParanoid; Q06628; -. DR OMA; WNVCKGT; -. DR OrthoDB; 1411563at2759; -. DR BioCyc; YEAST:G3O-34308-MONOMER; -. DR Reactome; R-SCE-1632852; Macroautophagy. DR BioGRID-ORCS; 856315; 1 hit in 10 CRISPR screens. DR PRO; PR:Q06628; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; Q06628; Protein. DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:SGD. DR GO; GO:0005829; C:cytosol; HDA:SGD. DR GO; GO:0070772; C:PAS complex; IDA:DisProt. DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD. DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IDA:SGD. DR GO; GO:0008289; F:lipid binding; IMP:DisProt. DR GO; GO:0019887; F:protein kinase regulator activity; IDA:SGD. DR GO; GO:0000045; P:autophagosome assembly; IDA:SGD. DR GO; GO:0006914; P:autophagy; IMP:UniProtKB. DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD. DR GO; GO:0071255; P:Cvt vesicle assembly; IMP:SGD. DR GO; GO:0016236; P:macroautophagy; IMP:SGD. DR GO; GO:0000423; P:mitophagy; IBA:GO_Central. DR GO; GO:0044804; P:nucleophagy; IMP:SGD. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD. DR GO; GO:0010508; P:positive regulation of autophagy; IDA:DisProt. DR GO; GO:0034497; P:protein localization to phagophore assembly site; IGI:SGD. DR GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IMP:SGD. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0060341; P:regulation of cellular localization; IDA:DisProt. DR GO; GO:0042594; P:response to starvation; NAS:ComplexPortal. DR DisProt; DP01732; -. DR Gene3D; 6.10.140.1900; -; 1. DR Gene3D; 3.30.900.10; HORMA domain; 1. DR InterPro; IPR040182; ATG13. DR InterPro; IPR018731; Atg13_N. DR InterPro; IPR036570; HORMA_dom_sf. DR PANTHER; PTHR13430:SF4; AUTOPHAGY-RELATED PROTEIN 13; 1. DR PANTHER; PTHR13430; UNCHARACTERIZED; 1. DR Pfam; PF10033; ATG13; 1. PE 1: Evidence at protein level; KW 3D-structure; Autophagy; Cytoplasm; Phosphoprotein; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..738 FT /note="Autophagy-related protein 13" FT /id="PRO_0000157972" FT REGION 279..359 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 377..462 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 432..520 FT /note="Interaction with ATG1" FT REGION 521..599 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 690..719 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..438 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 532..592 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 692..710 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 344 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:19805182" FT MOD_RES 348 FT /note="Phosphoserine; by TORC1" FT /evidence="ECO:0000269|PubMed:19995911" FT MOD_RES 355 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 437 FT /note="Phosphoserine; by TORC1 and PKA" FT /evidence="ECO:0000269|PubMed:19805182, FT ECO:0000269|PubMed:19995911" FT MOD_RES 438 FT /note="Phosphoserine; by TORC1" FT /evidence="ECO:0000269|PubMed:19995911" FT MOD_RES 461 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 496 FT /note="Phosphoserine; by TORC1" FT /evidence="ECO:0000269|PubMed:19995911" FT MOD_RES 535 FT /note="Phosphoserine; by TORC1" FT /evidence="ECO:0000269|PubMed:19995911" FT MOD_RES 541 FT /note="Phosphoserine; by TORC1" FT /evidence="ECO:0000269|PubMed:19995911" FT MOD_RES 554 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 581 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:19805182" FT MOD_RES 646 FT /note="Phosphoserine; by TORC1" FT /evidence="ECO:0000269|PubMed:19995911" FT MOD_RES 649 FT /note="Phosphoserine; by TORC1" FT /evidence="ECO:0000269|PubMed:19995911, FT ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MUTAGEN 344 FT /note="S->A: Decreases phosphorylation by PKA." FT /evidence="ECO:0000269|PubMed:19805182" FT MUTAGEN 348 FT /note="S->A: Leads to constitutive activation of autophagy; FT when associated with A-437; A-438; A-496; A-535; A-541; FT A-646 and A-649." FT /evidence="ECO:0000269|PubMed:19995911" FT MUTAGEN 437 FT /note="S->A: Decreases phosphorylation by PKA. Leads to FT constitutive activation of autophagy; when associated with FT A-348; A-438; A-496; A-535; A-541; A-646 and A-649." FT /evidence="ECO:0000269|PubMed:19805182, FT ECO:0000269|PubMed:19995911" FT MUTAGEN 438 FT /note="S->A: Leads to constitutive activation of autophagy; FT when associated with A-348; A-437; A-496; A-535; A-541; FT A-646 and A-649." FT /evidence="ECO:0000269|PubMed:19995911" FT MUTAGEN 468 FT /note="F->A: Impairs binding to ATG1; when associated with FT A-469." FT /evidence="ECO:0000269|PubMed:22885598" FT MUTAGEN 469 FT /note="V->A: Impairs binding to ATG1; when associated with FT A-468." FT /evidence="ECO:0000269|PubMed:22885598" FT MUTAGEN 496 FT /note="S->A: Leads to constitutive activation of autophagy; FT when associated with A-348; A-437; A-438; A-535; A-541; FT A-646 and A-649." FT /evidence="ECO:0000269|PubMed:19995911" FT MUTAGEN 535 FT /note="S->A: Leads to constitutive activation of autophagy; FT when associated with A-348; A-437; A-438; A-496; A-541; FT A-646 and A-649." FT /evidence="ECO:0000269|PubMed:19995911" FT MUTAGEN 541 FT /note="S->A: Leads to constitutive activation of autophagy; FT when associated with A-348; A-437; A-438; A-496; A-535; FT A-646 and A-649." FT /evidence="ECO:0000269|PubMed:19995911" FT MUTAGEN 581 FT /note="S->A: Decreases phosphorylation by PKA." FT /evidence="ECO:0000269|PubMed:19805182" FT MUTAGEN 646 FT /note="S->A: Leads to constitutive activation of autophagy; FT when associated with A-348; A-437; A-438; A-496; A-535; FT A-541 and A-649." FT /evidence="ECO:0000269|PubMed:19995911" FT MUTAGEN 649 FT /note="S->A: Leads to constitutive activation of autophagy; FT when associated with A-348; A-437; A-438; A-496; A-535; FT A-541, and A-646." FT /evidence="ECO:0000269|PubMed:19995911" SQ SEQUENCE 738 AA; 83281 MW; 45CD16F69B795E62 CRC64; MVAEEDIEKQ VLQLIDSFFL KTTLLICSTE SSRYQSSTEN IFLFDDTWFE DHSELVSELP EIISKWSHYD GRKELPPLVV ETYLDLRQLN SSHLVRLKDH EGHLWNVCKG TKKQEIVMER WLIELDNSSP TFKSYSEDET DVNELSKQLV LLFRYLLTLI QLLPTTELYQ LLIKSYNGPQ NEGSSNPITS TGPLVSIRTC VLDGSKPILS KGRIGLSKPI INTYSNALNE SNLPAHLDQK KITPVWTKFG LLRVSVSYRR DWKFEINNTN DELFSARHAS VSHNSQGPQN QPEQEGQSDQ DIGKRQPQFQ QQQQPQQQQQ QQQQQQRQHQ VQTQQQRQIP DRRSLSLSPC TRANSFEPQS WQKKVYPISR PVQPFKVGSI GSQSASRNPS NSSFFNQPPV HRPSMSSNYG PQMNIEGTSV GSTSKYSSSF GNIRRHSSVK TTENAEKVSK AVKSPLQPQE SQEDLMDFVK LLEEKPDLTI KKTSGNNPPN INISDSLIRY QNLKPSNDLL SEDLSVSLSM DPNHTYHRGR SDSHSPLPSI SPSMHYGSLN SRMSQGANAS HLIARGGGNS STSALNSRRN SLDKSSNKQG MSGLPPIFGG ESTSYHHDNK IQKYNQLGVE EDDDDENDRL LNQMGNSATK FKSSISPRSI DSISSSFIKS RIPIRQPYHY SQPTTAPFQA QAKFHKPANK LIDNGNRSNS NNNNHNGNDA VGVMHNDEDD QDDDLVFFMS DMNLSKEG //