ATG13_HUMAN
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 03-AUG-2022, entry version 174.
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};
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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. [O75143-5]
DR RefSeq; XP_005253323.1; XM_005253266.2. [O75143-5]
DR RefSeq; XP_005253325.1; XM_005253268.2. [O75143-5]
DR RefSeq; XP_006718459.1; XM_006718396.2. [O75143-5]
DR RefSeq; XP_011518795.1; XM_011520493.1. [O75143-5]
DR RefSeq; XP_011518798.1; XM_011520496.2. [O75143-5]
DR RefSeq; XP_011518801.1; XM_011520499.2. [O75143-5]
DR RefSeq; XP_016874088.1; XM_017018599.1. [O75143-5]
DR RefSeq; XP_016874092.1; XM_017018603.1. [O75143-1]
DR RefSeq; XP_016874096.1; XM_017018607.1. [O75143-1]
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 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 AlphaFoldDB; O75143; -.
DR SMR; O75143; -.
DR BioGRID; 115120; 44.
DR ComplexPortal; CPX-373; ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex.
DR CORUM; O75143; -.
DR DIP; DIP-60540N; -.
DR ELM; O75143; -.
DR IntAct; O75143; 27.
DR MINT; O75143; -.
DR STRING; 9606.ENSP00000432412; -.
DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; O75143; -.
DR PhosphoSitePlus; O75143; -.
DR BioMuta; ATG13; -.
DR EPD; O75143; -.
DR jPOST; O75143; -.
DR MassIVE; O75143; -.
DR MaxQB; O75143; -.
DR PeptideAtlas; O75143; -.
DR PRIDE; O75143; -.
DR ProteomicsDB; 23169; -.
DR ProteomicsDB; 4042; -.
DR ProteomicsDB; 49803; -. [O75143-1]
DR ProteomicsDB; 49804; -. [O75143-2]
DR ProteomicsDB; 49805; -. [O75143-3]
DR Antibodypedia; 26361; 633 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 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; ICYRIYM; -.
DR OrthoDB; 926357at2759; -.
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; 31 hits in 1087 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 202 other tissues.
DR ExpressionAtlas; O75143; baseline and differential.
DR Genevisible; O75143; HS.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IPI:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000407; C:phagophore assembly site; IDA:ComplexPortal.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:ComplexPortal.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:1903059; P:regulation of protein lipidation; IDA:ComplexPortal.
DR GO; GO:0098780; P:response to mitochondrial depolarisation; IEA:Ensembl.
DR DisProt; DP01731; -.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR040182; ATG13.
DR InterPro; IPR018731; Atg13_N.
DR InterPro; IPR036570; HORMA_dom_sf.
DR PANTHER; PTHR13430; PTHR13430; 1.
DR Pfam; PF10033; ATG13; 1.
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
