ID ATG13_HUMAN Reviewed; 517 AA. AC O75143; B4DFI4; D3DQQ1; D3DQQ2; E9PQZ8; Q53EN6; Q9BRL3; Q9H8B0; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 182. DE RecName: Full=Autophagy-related protein 13; GN Name=ATG13; Synonyms=KIAA0652; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Brain cortex, and Thyroid; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Cervix, Lung, and Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP INTERACTION WITH ATG101; ULK1 AND RB1CC1, AND SUBUNIT. RX PubMed=19597335; DOI=10.4161/auto.5.7.9296; RA Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T., Mizushima N.; RT "Atg101, a novel mammalian autophagy protein interacting with Atg13."; RL Autophagy 5:973-979(2009). RN [9] RP FUNCTION AS AUTOPHAGY FACTOR, PHOSPHORYLATION, AND INTERACTION WITH ULK1 RP AND ATG101. RX PubMed=19287211; DOI=10.4161/auto.5.5.8249; RA Mercer C.A., Kaliappan A., Dennis P.B.; RT "A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is RT essential for macroautophagy."; RL Autophagy 5:649-662(2009). RN [10] RP FUNCTION, INTERACTION WITH ULK1 AND RB1CC1, PHOSPHORYLATION, AND RP SUBCELLULAR LOCATION. RX PubMed=19211835; DOI=10.1091/mbc.e08-12-1248; RA Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y., RA Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N., RA Mizushima N.; RT "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex RT required for autophagy."; RL Mol. Biol. Cell 20:1981-1991(2009). RN [11] RP INTERACTION WITH ULK1; ULK2 AND RB1CC1, PHOSPHORYLATION BY ULK1; ULK2 AND RP MTOR, AND FUNCTION. RX PubMed=19225151; DOI=10.1091/mbc.e08-12-1249; RA Jung C.H., Jun C.B., Ro S.H., Kim Y.M., Otto N.M., Cao J., Kundu M., RA Kim D.H.; RT "ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy RT machinery."; RL Mol. Biol. Cell 20:1992-2003(2009). RN [12] RP FUNCTION, INTERACTION WITH ULK1, AND PHOSPHORYLATION AT SER-355 BY ULK1. RX PubMed=21855797; DOI=10.1016/j.molcel.2011.06.018; RA Joo J.H., Dorsey F.C., Joshi A., Hennessy-Walters K.M., Rose K.L., RA McCastlain K., Zhang J., Iyengar R., Jung C.H., Suen D.F., Steeves M.A., RA Yang C.Y., Prater S.M., Kim D.H., Thompson C.B., Youle R.J., Ney P.A., RA Cleveland J.L., Kundu M.; RT "Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated RT mitophagy."; RL Mol. Cell 43:572-585(2011). RN [13] RP FUNCTION AS AUTOPHAGY FACTOR, INTERACTION WITH ULK1 AND ULK2, AND RP PHOSPHORYLATION BY ULK1 AND ULK2. RX PubMed=18936157; DOI=10.1128/mcb.01082-08; RA Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.; RT "Kinase-inactivated ULK proteins inhibit autophagy via their conserved C- RT terminal domains using an Atg13-independent mechanism."; RL Mol. Cell. Biol. 29:157-171(2009). RN [14] RP FUNCTION. RX PubMed=21795849; DOI=10.4161/auto.7.10.16660; RA Jung C.H., Seo M., Otto N.M., Kim D.H.; RT "ULK1 inhibits the kinase activity of mTORC1 and cell proliferation."; RL Autophagy 7:1212-1221(2011). RN [15] RP PHOSPHORYLATION, AND INTERACTION WITH ULK1 AND RB1CC1. RX PubMed=21258367; DOI=10.1038/ncb2152; RA Kim J., Kundu M., Viollet B., Guan K.L.; RT "AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1."; RL Nat. Cell Biol. 13:132-141(2011). RN [16] RP INTERACTION WITH TAB2 AND TAB3. RX PubMed=21976705; DOI=10.1093/jb/mvr123; RA Takaesu G., Kobayashi T., Yoshimura A.; RT "TGFbeta-activated kinase 1 (TAK1)-binding proteins (TAB) 2 and 3 RT negatively regulate autophagy."; RL J. Biochem. 151:157-166(2012). RN [17] RP INTERACTION WITH GABARAP; GABARAPL1; GABARAPL2 AND MAP1LC3A, DOMAIN, AND RP MUTAGENESIS. RX PubMed=23043107; DOI=10.1074/jbc.m112.378109; RA Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., RA Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.; RT "ATG8 family proteins act as scaffolds for assembly of the ULK complex: RT sequence requirements for LC3-interacting region (LIR) motifs."; RL J. Biol. Chem. 287:39275-39290(2012). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-361, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-356, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP INTERACTION WITH C9ORF72. RX PubMed=27334615; DOI=10.15252/embj.201694401; RA Webster C.P., Smith E.F., Bauer C.S., Moller A., Hautbergue G.M., RA Ferraiuolo L., Myszczynska M.A., Higginbottom A., Walsh M.J., RA Whitworth A.J., Kaspar B.K., Meyer K., Shaw P.J., Grierson A.J., RA De Vos K.J.; RT "The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate RT initiation of autophagy."; RL EMBO J. 35:1656-1676(2016). RN [22] RP INTERACTION WITH ULK1 AND RB1CC1. RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035; RA Miao G., Zhang Y., Chen D., Zhang H.; RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1."; RL Mol. Cell 0:0-0(2019). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 436-447, INTERACTION WITH RP MAP1LC3A; MAP1LC3B AND MAP1LC3C, MOTIF, SUBUNIT, AND MUTAGENESIS OF PHE-444 RP AND ILE-447. RX PubMed=24290141; DOI=10.1016/j.str.2013.09.023; RA Suzuki H., Tabata K., Morita E., Kawasaki M., Kato R., Dobson R.C., RA Yoshimori T., Wakatsuki S.; RT "Structural basis of the autophagy-related LC3/Atg13 LIR complex: RT recognition and interaction mechanism."; RL Structure 22:47-58(2014). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS). RX PubMed=26236954; DOI=10.1080/15548627.2015.1076605; RA Michel M., Schwarten M., Decker C., Nagel-Steger L., Willbold D., RA Weiergraber O.H.; RT "The mammalian autophagy initiator complex contains 2 HORMA domain RT proteins."; RL Autophagy 11:2300-2308(2015). RN [25] RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 1-198 IN COMPLEX WITH ATG101, RP INTERACTION WITH ATG101, AND MUTAGENESIS OF SER-127; ILE-131; ARG-133 AND RP VAL-134. RX PubMed=26299944; DOI=10.1016/j.str.2015.07.011; RA Qi S., Kim do J., Stjepanovic G., Hurley J.H.; RT "Structure of the human Atg13-Atg101 HORMA heterodimer: an interaction hub RT within the ULK1 complex."; RL Structure 23:1848-1857(2015). CC -!- FUNCTION: Autophagy factor required for autophagosome formation and CC mitophagy. Target of the TOR kinase signaling pathway that regulates CC autophagy through the control of the phosphorylation status of ATG13 CC and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through CC its regulation of ULK1 activity, plays a role in the regulation of the CC kinase activity of mTORC1 and cell proliferation. CC {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835, CC ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211, CC ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:21855797}. CC -!- SUBUNIT: Part of a complex consisting of ATG13, ULK1 and RB1CC1 CC (PubMed:19597335, PubMed:19211835, PubMed:19225151, PubMed:24290141). CC Interacts with ATG101 (PubMed:19597335, PubMed:19287211, CC PubMed:26299944). Interacts with ULK1 (via C-terminus); this CC interaction is increased in the absence of TMEM39A (PubMed:19287211, CC PubMed:21855797, PubMed:18936157, PubMed:31806350). Interacts with ULK2 CC (via C-terminus) (PubMed:19225151, PubMed:18936157). Interacts (via the CC LIR motif) with GABARAP, GABARAPL, GABARAPL2 (PubMed:23043107). CC Interacts (via the LIR motif) with MAP1LC3A, MAP1LC3B and MAP1LC3C CC (PubMed:24290141). Interacts with TAB2 and TAB3 (PubMed:21976705). CC Interacts with C9orf72 (PubMed:27334615). Interacts with RB1CC1; this CC interaction is increased in the absence of TMEM39A (PubMed:31806350). CC {ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835, CC ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211, CC ECO:0000269|PubMed:19597335, ECO:0000269|PubMed:21258367, CC ECO:0000269|PubMed:21855797, ECO:0000269|PubMed:21976705, CC ECO:0000269|PubMed:23043107, ECO:0000269|PubMed:26299944, CC ECO:0000269|PubMed:27334615, ECO:0000269|PubMed:31806350}. CC -!- INTERACTION: CC O75143; Q9BSB4: ATG101; NbExp=16; IntAct=EBI-2798775, EBI-2946739; CC O75143; Q96LT7-1: C9orf72; NbExp=5; IntAct=EBI-2798775, EBI-16693635; CC O75143; Q96LT7-2: C9orf72; NbExp=4; IntAct=EBI-2798775, EBI-16693673; CC O75143; O95166: GABARAP; NbExp=3; IntAct=EBI-2798775, EBI-712001; CC O75143; Q9H0R8: GABARAPL1; NbExp=2; IntAct=EBI-2798775, EBI-746969; CC O75143; P60520: GABARAPL2; NbExp=3; IntAct=EBI-2798775, EBI-720116; CC O75143; Q9H492-1: MAP1LC3A; NbExp=7; IntAct=EBI-2798775, EBI-16082793; CC O75143; Q9GZQ8: MAP1LC3B; NbExp=5; IntAct=EBI-2798775, EBI-373144; CC O75143; Q9BXW4: MAP1LC3C; NbExp=8; IntAct=EBI-2798775, EBI-2603996; CC O75143; O75665: OFD1; NbExp=4; IntAct=EBI-2798775, EBI-716327; CC O75143; Q8TDY2: RB1CC1; NbExp=10; IntAct=EBI-2798775, EBI-1047793; CC O75143; O75385: ULK1; NbExp=13; IntAct=EBI-2798775, EBI-908831; CC O75143-2; Q9BSB4: ATG101; NbExp=3; IntAct=EBI-20151086, EBI-2946739; CC O75143-2; P45973: CBX5; NbExp=3; IntAct=EBI-20151086, EBI-78219; CC O75143-2; P37173: TGFBR2; NbExp=3; IntAct=EBI-20151086, EBI-296151; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19211835}. CC Preautophagosomal structure {ECO:0000269|PubMed:19211835}. Note=Under CC starvation conditions, is localized to puncate structures primarily CC representing the isolation membrane; the isolation membrane sequesters CC a portion of the cytoplasm resulting in autophagosome formation. CC {ECO:0000269|PubMed:19211835}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=O75143-1; Sequence=Displayed; CC Name=2; CC IsoId=O75143-2; Sequence=VSP_002431; CC Name=3; CC IsoId=O75143-3; Sequence=VSP_002431, VSP_002432, VSP_002433; CC Name=4; CC IsoId=O75143-4; Sequence=VSP_044503, VSP_044504; CC Name=5; CC IsoId=O75143-5; Sequence=VSP_044640; CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the CC interaction with the ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, CC and MAP1LC3A. {ECO:0000269|PubMed:23043107}. CC -!- PTM: Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status CC depends on nutrient-rich conditions; dephosphorylated during starvation CC or following treatment with rapamycin. ULK1-mediated phosphorylation of CC ATG13 at Ser-355 is required for efficient clearance of depolarized CC mitochondria. {ECO:0000269|PubMed:18936157, CC ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19225151, CC ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:21258367, CC ECO:0000269|PubMed:21855797}. CC -!- SIMILARITY: Belongs to the ATG13 family. Metazoan subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA31627.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAD97323.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB014552; BAA31627.2; ALT_INIT; mRNA. DR EMBL; AK023867; BAB14707.1; -; mRNA. DR EMBL; AK294110; BAG57445.1; -; mRNA. DR EMBL; AK223603; BAD97323.1; ALT_INIT; mRNA. DR EMBL; AC115088; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC127035; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW67985.1; -; Genomic_DNA. DR EMBL; CH471064; EAW67986.1; -; Genomic_DNA. DR EMBL; CH471064; EAW67987.1; -; Genomic_DNA. DR EMBL; CH471064; EAW67988.1; -; Genomic_DNA. DR EMBL; CH471064; EAW67989.1; -; Genomic_DNA. DR EMBL; CH471064; EAW67990.1; -; Genomic_DNA. DR EMBL; CH471064; EAW67991.1; -; Genomic_DNA. DR EMBL; BC001331; AAH01331.1; -; mRNA. DR EMBL; BC002378; AAH02378.1; -; mRNA. DR EMBL; BC006191; AAH06191.1; -; mRNA. DR CCDS; CCDS44582.1; -. [O75143-1] DR CCDS; CCDS55760.1; -. [O75143-5] DR CCDS; CCDS55761.1; -. [O75143-4] DR CCDS; CCDS7921.1; -. [O75143-2] DR RefSeq; NP_001136145.1; NM_001142673.2. [O75143-1] DR RefSeq; NP_001192048.1; NM_001205119.1. [O75143-5] DR RefSeq; NP_001192049.1; NM_001205120.1. [O75143-1] DR RefSeq; NP_001192050.1; NM_001205121.1. [O75143-2] DR RefSeq; NP_001192051.1; NM_001205122.1. [O75143-4] DR RefSeq; NP_001333240.1; NM_001346311.1. [O75143-5] DR RefSeq; NP_001333241.1; NM_001346312.1. [O75143-5] DR RefSeq; NP_001333242.1; NM_001346313.1. [O75143-5] DR RefSeq; NP_001333243.1; NM_001346314.1. [O75143-5] DR RefSeq; NP_001333244.1; NM_001346315.1. [O75143-5] DR RefSeq; NP_001333245.1; NM_001346316.1. [O75143-5] DR RefSeq; NP_001333248.1; NM_001346319.1. [O75143-1] DR RefSeq; NP_001333249.1; NM_001346320.1. [O75143-1] DR RefSeq; NP_001333250.1; NM_001346321.1. [O75143-1] DR RefSeq; NP_001333251.1; NM_001346322.1. [O75143-1] DR RefSeq; NP_001333252.1; NM_001346323.1. [O75143-1] DR RefSeq; NP_001333253.1; NM_001346324.1. [O75143-1] DR RefSeq; NP_001333254.1; NM_001346325.1. [O75143-1] DR RefSeq; NP_001333255.1; NM_001346326.1. [O75143-1] DR RefSeq; NP_001333256.1; NM_001346327.1. [O75143-1] DR RefSeq; NP_001333257.1; NM_001346328.1. [O75143-1] DR RefSeq; NP_001333258.1; NM_001346329.1. [O75143-1] DR RefSeq; NP_001333259.1; NM_001346330.1. [O75143-1] DR RefSeq; NP_001333260.1; NM_001346331.1. [O75143-1] DR RefSeq; NP_001333261.1; NM_001346332.1. [O75143-1] DR RefSeq; NP_001333271.1; NM_001346342.1. [O75143-2] DR RefSeq; NP_001333273.1; NM_001346344.1. [O75143-2] DR RefSeq; NP_001333275.1; NM_001346346.1. [O75143-2] DR RefSeq; NP_001333277.1; NM_001346348.1. [O75143-2] DR RefSeq; NP_001333278.1; NM_001346349.1. [O75143-2] DR RefSeq; NP_001333279.1; NM_001346350.1. [O75143-2] DR RefSeq; NP_001333280.1; NM_001346351.1. [O75143-2] DR RefSeq; NP_001333281.1; NM_001346352.1. [O75143-2] DR RefSeq; NP_001333282.1; NM_001346353.1. [O75143-2] DR RefSeq; NP_001333283.1; NM_001346354.1. [O75143-2] DR RefSeq; NP_055556.2; NM_014741.4. [O75143-2] DR RefSeq; XP_005253322.1; XM_005253265.2. DR RefSeq; XP_005253323.1; XM_005253266.2. DR RefSeq; XP_005253325.1; XM_005253268.2. DR RefSeq; XP_006718459.1; XM_006718396.2. DR RefSeq; XP_011518795.1; XM_011520493.1. DR RefSeq; XP_011518798.1; XM_011520496.2. DR RefSeq; XP_011518801.1; XM_011520499.2. DR RefSeq; XP_016874088.1; XM_017018599.1. DR RefSeq; XP_016874092.1; XM_017018603.1. DR RefSeq; XP_016874096.1; XM_017018607.1. DR PDB; 3WAN; X-ray; 1.77 A; A/B=436-447. DR PDB; 3WAO; X-ray; 2.60 A; A/B/C/D=436-447. DR PDB; 3WAP; X-ray; 3.10 A; A=436-447. DR PDB; 5C50; X-ray; 1.63 A; B=12-200. DR PDB; 5XUY; X-ray; 2.20 A; A/C=1-190. DR PDB; 5XV1; X-ray; 2.51 A; A/C=1-190. DR PDB; 5XV3; X-ray; 2.57 A; A/C=1-190. DR PDB; 5XV4; X-ray; 2.95 A; A/C/E/G/I/K/M/O=1-190. DR PDB; 5XV6; X-ray; 2.46 A; A=1-190. DR PDB; 6HYN; X-ray; 1.14 A; A=441-454. DR PDB; 8DO8; X-ray; 2.41 A; B/D=1-197. DR PDB; 8SOI; EM; 4.20 A; D=462-517. DR PDB; 8SQZ; EM; 5.85 A; E/F=363-517. DR PDB; 8SRM; EM; 4.46 A; E/F=450-517. DR PDB; 8SRQ; EM; 6.20 A; D=462-517. DR PDBsum; 3WAN; -. DR PDBsum; 3WAO; -. DR PDBsum; 3WAP; -. DR PDBsum; 5C50; -. DR PDBsum; 5XUY; -. DR PDBsum; 5XV1; -. DR PDBsum; 5XV3; -. DR PDBsum; 5XV4; -. DR PDBsum; 5XV6; -. DR PDBsum; 6HYN; -. DR PDBsum; 8DO8; -. DR PDBsum; 8SOI; -. DR PDBsum; 8SQZ; -. DR PDBsum; 8SRM; -. DR PDBsum; 8SRQ; -. DR AlphaFoldDB; O75143; -. DR EMDB; EMD-40715; -. DR SMR; O75143; -. DR BioGRID; 115120; 206. DR ComplexPortal; CPX-373; ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex. DR CORUM; O75143; -. DR DIP; DIP-60540N; -. DR ELM; O75143; -. DR IntAct; O75143; 29. DR MINT; O75143; -. DR STRING; 9606.ENSP00000432412; -. DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family. DR GlyGen; O75143; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75143; -. DR PhosphoSitePlus; O75143; -. DR BioMuta; ATG13; -. DR EPD; O75143; -. DR jPOST; O75143; -. DR MassIVE; O75143; -. DR MaxQB; O75143; -. DR PaxDb; 9606-ENSP00000432412; -. DR PeptideAtlas; O75143; -. DR ProteomicsDB; 23169; -. DR ProteomicsDB; 4042; -. DR ProteomicsDB; 49803; -. [O75143-1] DR ProteomicsDB; 49804; -. [O75143-2] DR ProteomicsDB; 49805; -. [O75143-3] DR Pumba; O75143; -. DR Antibodypedia; 26361; 671 antibodies from 38 providers. DR DNASU; 9776; -. DR Ensembl; ENST00000359513.8; ENSP00000352500.4; ENSG00000175224.17. [O75143-1] DR Ensembl; ENST00000524625.5; ENSP00000433543.1; ENSG00000175224.17. [O75143-2] DR Ensembl; ENST00000526508.5; ENSP00000431974.1; ENSG00000175224.17. [O75143-1] DR Ensembl; ENST00000528494.5; ENSP00000432412.1; ENSG00000175224.17. [O75143-5] DR Ensembl; ENST00000529655.5; ENSP00000433756.1; ENSG00000175224.17. [O75143-2] DR Ensembl; ENST00000530500.5; ENSP00000434390.1; ENSG00000175224.17. [O75143-4] DR Ensembl; ENST00000683050.1; ENSP00000507809.1; ENSG00000175224.17. [O75143-5] DR GeneID; 9776; -. DR KEGG; hsa:9776; -. DR MANE-Select; ENST00000683050.1; ENSP00000507809.1; NM_001346311.2; NP_001333240.1. [O75143-5] DR UCSC; uc001ncz.4; human. [O75143-1] DR AGR; HGNC:29091; -. DR CTD; 9776; -. DR DisGeNET; 9776; -. DR GeneCards; ATG13; -. DR HGNC; HGNC:29091; ATG13. DR HPA; ENSG00000175224; Low tissue specificity. DR MIM; 615088; gene. DR neXtProt; NX_O75143; -. DR OpenTargets; ENSG00000175224; -. DR PharmGKB; PA165543187; -. DR VEuPathDB; HostDB:ENSG00000175224; -. DR eggNOG; KOG3874; Eukaryota. DR GeneTree; ENSGT00390000007055; -. DR HOGENOM; CLU_036365_0_0_1; -. DR InParanoid; O75143; -. DR OMA; SLKTSEX; -. DR OrthoDB; 3061619at2759; -. DR PhylomeDB; O75143; -. DR TreeFam; TF321599; -. DR PathwayCommons; O75143; -. DR Reactome; R-HSA-1632852; Macroautophagy. DR SignaLink; O75143; -. DR SIGNOR; O75143; -. DR BioGRID-ORCS; 9776; 33 hits in 1165 CRISPR screens. DR ChiTaRS; ATG13; human. DR GeneWiki; Autophagy-related_protein_13; -. DR GenomeRNAi; 9776; -. DR Pharos; O75143; Tbio. DR PRO; PR:O75143; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; O75143; Protein. DR Bgee; ENSG00000175224; Expressed in left testis and 204 other cell types or tissues. DR ExpressionAtlas; O75143; baseline and differential. DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IPI:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IC:UniProt. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL. DR GO; GO:0000407; C:phagophore assembly site; IDA:ComplexPortal. DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProt. DR GO; GO:0019901; F:protein kinase binding; IDA:UniProt. DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProt. DR GO; GO:0000045; P:autophagosome assembly; IDA:ComplexPortal. DR GO; GO:0000423; P:mitophagy; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:ComplexPortal. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central. DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProt. DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL. DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central. DR GO; GO:1903059; P:regulation of protein lipidation; IDA:ComplexPortal. DR GO; GO:0098780; P:response to mitochondrial depolarisation; IEA:Ensembl. 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. DR Genevisible; O75143; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Autophagy; Cytoplasm; KW Phosphoprotein; Reference proteome. FT CHAIN 1..517 FT /note="Autophagy-related protein 13" FT /id="PRO_0000050767" FT REGION 127..134 FT /note="Important for interaction with ATG101" FT /evidence="ECO:0000269|PubMed:26299944" FT REGION 305..324 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 332..361 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 405..439 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 444..447 FT /note="LIR" FT /evidence="ECO:0000305|PubMed:24290141" FT COMPBIAS 417..439 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 355 FT /note="Phosphoserine; by ULK1" FT /evidence="ECO:0000269|PubMed:21855797, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..79 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044503" FT VAR_SEQ 262 FT /note="S -> SQCVFTVTKAHFQTPTPVVTDTLRVPMAGLAFSH (in isoform FT 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_044640" FT VAR_SEQ 263..299 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044504" FT VAR_SEQ 265..301 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_002431" FT VAR_SEQ 428..442 FT /note="HSDGSSGGSSGNTHD -> PCSWPLPCLLSPSTV (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_002432" FT VAR_SEQ 443..517 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_002433" FT MUTAGEN 127 FT /note="S->H: Abolishes interaction with ATG101; when FT associated with D-133." FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 131 FT /note="I->D: Decreases interaction with ATG101; when FT associated with D-134." FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 133 FT /note="R->D: Abolishes interaction with ATG101; when FT associated with H-127." FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 134 FT /note="V->D: Decreases interaction with ATG101; when FT associated with D-131." FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 444 FT /note="F->A: Decreases interaction with MAP1LC3A." FT /evidence="ECO:0000269|PubMed:24290141" FT MUTAGEN 447 FT /note="I->A: Decreases interaction with MAP1LC3A." FT /evidence="ECO:0000269|PubMed:24290141" FT HELIX 12..30 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:5XUY" FT HELIX 59..69 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 78..88 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 93..103 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:5XV3" FT HELIX 114..131 FT /evidence="ECO:0007829|PDB:5C50" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 137..142 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 145..158 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:5XV6" FT STRAND 169..178 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 181..189 FT /evidence="ECO:0007829|PDB:5C50" FT TURN 452..454 FT /evidence="ECO:0007829|PDB:6HYN" SQ SEQUENCE 517 AA; 56572 MW; 4D6905985EAB78A7 CRC64; METDLNSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW FNLAIKDIPE VTHEAKKALA GQLPAVGRSM CVEISLKTSE GDSMELEIWC LEMNEKCDKE IKVSYTVYNR LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI LYRIYFGEVQ LSGLGEGFQT VRVGTVGTPV GTITLSCAYR INLAFMSTRQ FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAGEDTGV IYPSVEDSQE VCTTSFSTSP PSQLSSSRLS YQPAALGVGS ADLAYPVVFA AGLNATHPHQ LMVPGKEGGV PLAPNQPVHG TQADQERLAT CTPSDRTHCA ATPSSSEDTE TVSNSSEGRA SPHDVLETIF VRKVGAFVNK PINQVTLTSL DIPFAMFAPK NLELEDTDPM VNPPDSPETE SPLQGSLHSD GSSGGSSGNT HDDFVMIDFK PAFSKDDILP MDLGTFYREF QNPPQLSSLS IDIGAQSMAE DLDSLPEKLA VHEKNVREFD AFVETLQ //