ID BAKOR_HUMAN Reviewed; 492 AA. AC Q6ZNE5; A6NJE4; A8K9U5; B7ZWP5; O94920; Q32MK7; Q32MK8; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-JAN-2026, entry version 162. DE RecName: Full=Beclin 1-associated autophagy-related key regulator {ECO:0000303|PubMed:19050071}; DE Short=Barkor {ECO:0000303|PubMed:19050071}; DE AltName: Full=Autophagy-related protein 14-like protein {ECO:0000303|PubMed:19270696}; DE Short=Atg14L {ECO:0000303|PubMed:19270696}; GN Name=ATG14 {ECO:0000303|PubMed:18843052}; GN Synonyms=ATG14L {ECO:0000303|PubMed:19270696}, KIAA0831; 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 2). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hippocampus, and Trachea; 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 GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [4] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [6] RP IDENTIFICATION, FUNCTION, INTERACTION WITH BECN1; PIK3C3 AND PIK3R4, AND RP SUBCELLULAR LOCATION. RX PubMed=18843052; DOI=10.1091/mbc.e08-01-0080; RA Itakura E., Kishi C., Inoue K., Mizushima N.; RT "Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with RT mammalian Atg14 and UVRAG."; RL Mol. Biol. Cell 19:5360-5372(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP FUNCTION, INTERACTION WITH BECN1, AND SUBCELLULAR LOCATION. RX PubMed=19050071; DOI=10.1073/pnas.0810452105; RA Sun Q., Fan W., Chen K., Ding X., Chen S., Zhong Q.; RT "Identification of Barkor as a mammalian autophagy-specific factor for RT Beclin 1 and class III phosphatidylinositol 3-kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 105:19211-19216(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-416 AND THR-429, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [10] RP FUNCTION, INTERACTION WITH BECN1; PIK3C3 AND PIK3R4, AND SUBCELLULAR RP LOCATION. RX PubMed=19270696; DOI=10.1038/ncb1846; RA Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N., RA Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S., Noda T., RA Yoshimori T.; RT "Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate RT autophagy at different stages."; RL Nat. Cell Biol. 11:385-396(2009). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF CYS-43; CYS-46; RP CYS-55 AND CYS-58. RX PubMed=20713597; DOI=10.1083/jcb.200911141; RA Matsunaga K., Morita E., Saitoh T., Akira S., Ktistakis N.T., Izumi T., RA Noda T., Yoshimori T.; RT "Autophagy requires endoplasmic reticulum targeting of the PI3-kinase RT complex via Atg14L."; RL J. Cell Biol. 190:511-521(2010). RN [12] RP INTERACTION WITH BECN1, AND SUBCELLULAR LOCATION. RX PubMed=22314358; DOI=10.1038/ncomms1648; RA Li X., He L., Che K.H., Funderburk S.F., Pan L., Pan N., Zhang M., Yue Z., RA Zhao Y.; RT "Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and RT heterodimer formation with Atg14L and UVRAG."; RL Nat. Commun. 3:662-662(2012). RN [13] RP INTERACTION WITH BECN2. RX PubMed=23954414; DOI=10.1016/j.cell.2013.07.035; RA He C., Wei Y., Sun K., Li B., Dong X., Zou Z., Liu Y., Kinch L.N., Khan S., RA Sinha S., Xavier R.J., Grishin N.V., Xiao G., Eskelinen E.L., Scherer P.E., RA Whistler J.L., Levine B.; RT "Beclin 2 functions in autophagy, degradation of G protein-coupled RT receptors, and metabolism."; RL Cell 154:1085-1099(2013). RN [14] RP FUNCTION, AND INTERACTION WITH BECN1. RX PubMed=23878393; DOI=10.1128/mcb.00079-13; RA Fogel A.I., Dlouhy B.J., Wang C., Ryu S.W., Neutzner A., Hasson S.A., RA Sideris D.P., Abeliovich H., Youle R.J.; RT "Role of membrane association and Atg14-dependent phosphorylation in RT beclin-1-mediated autophagy."; RL Mol. Cell. Biol. 33:3675-3688(2013). RN [15] RP RECONSTITUTION OF THE PI3K COMPLEX I, AND ELECTRON MICROSCOPY OF THE PI3K RP COMPLEX I. RX PubMed=25490155; DOI=10.7554/elife.05115; RA Baskaran S., Carlson L.A., Stjepanovic G., Young L.N., Kim do J., Grob P., RA Stanley R.E., Nogales E., Hurley J.H.; RT "Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase RT complex."; RL Elife 3:0-0(2014). RN [16] RP INTERACTION WITH BECN1; STX17 AND SNAP29, SUBCELLULAR LOCATION, FUNCTION, RP DOMAIN, SUBUNIT, AND MUTAGENESIS OF CYS-43; CYS-46; CYS-55 AND CYS-58. RX PubMed=25686604; DOI=10.1038/nature14147; RA Diao J., Liu R., Rong Y., Zhao M., Zhang J., Lai Y., Zhou Q., Wilz L.M., RA Li J., Vivona S., Pfuetzner R.A., Brunger A.T., Zhong Q.; RT "ATG14 promotes membrane tethering and fusion of autophagosomes to RT endolysosomes."; RL Nature 520:563-566(2015). RN [17] RP INTERACTION WITH BECN2. RX PubMed=28218432; DOI=10.1002/pro.3140; RA Su M., Li Y., Wyborny S., Neau D., Chakravarthy S., Levine B., RA Colbert C.L., Sinha S.C.; RT "BECN2 interacts with ATG14 through a metastable coiled-coil to mediate RT autophagy."; RL Protein Sci. 26:972-984(2017). RN [18] RP INTERACTION WITH PIK3C3 AND BECN1. 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 [19] RP PHOSPHORYLATION AT SER-29. RX PubMed=31123703; DOI=10.1126/sciadv.aau8857; RA Di Rienzo M., Antonioli M., Fusco C., Liu Y., Mari M., Orhon I., Refolo G., RA Germani F., Corazzari M., Romagnoli A., Ciccosanti F., Mandriani B., RA Pellico M.T., De La Torre R., Ding H., Dentice M., Neri M., Ferlini A., RA Reggiori F., Kulesz-Martin M., Piacentini M., Merla G., Fimia G.M.; RT "Autophagy induction in atrophic muscle cells requires ULK1 activation by RT TRIM32 through unanchored K63-linked polyubiquitin chains."; RL Sci. Adv. 5:eaau8857-eaau8857(2019). RN [20] RP INTERACTION WITH STEEP1. RX PubMed=32690950; DOI=10.1038/s41590-020-0730-5; RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L., RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F., RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T., RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T., RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O., RA Thomsen M.K., Paludan S.R.; RT "STEEP mediates STING ER exit and activation of signaling."; RL Nat. Immunol. 21:868-879(2020). RN [21] RP ERRATUM OF PUBMED:32690950. RX PubMed=32929276; DOI=10.1038/s41590-020-0803-5; RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L., RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F., RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T., RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T., RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O., RA Thomsen M.K., Paludan S.R.; RL Nat. Immunol. 21:1468-1469(2020). RN [22] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STX17, AND UBIQUITINATION. RX PubMed=37632749; DOI=10.1016/j.celrep.2023.113045; RA Shi X., Wu W., Feng Z., Fan P., Shi R., Zhang X.; RT "MARCH7-mediated ubiquitination decreases the solubility of ATG14 to RT inhibit autophagy."; RL Cell Rep. 42:113045-113045(2023). CC -!- FUNCTION: Required for both basal and inducible autophagy. Determines CC the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 CC (PubMed:18843052, PubMed:19050071). Plays a role in autophagosome CC formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine CC (PubMed:19270696, PubMed:20713597). Promotes BECN1 translocation from CC the trans-Golgi network to autophagosomes (PubMed:20713597). Enhances CC PIK3C3 activity in a BECN1-dependent manner. Essential for the CC autophagy-dependent phosphorylation of BECN1 (PubMed:23878393). CC Stimulates the phosphorylation of BECN1, but suppresses the CC phosphorylation PIK3C3 by AMPK (PubMed:23878393). Binds to STX17-SNAP29 CC binary t-SNARE complex on autophagosomes and primes it for VAMP8 CC interaction to promote autophagosome-endolysosome fusion CC (PubMed:25686604, PubMed:37632749). Modulates the hepatic lipid CC metabolism (By similarity). {ECO:0000250|UniProtKB:Q8CDJ3, CC ECO:0000269|PubMed:18843052, ECO:0000269|PubMed:19050071, CC ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:20713597, CC ECO:0000269|PubMed:23878393, ECO:0000269|PubMed:25686604, CC ECO:0000269|PubMed:37632749}. CC -!- SUBUNIT: Forms homooligomers; homo-oligomerization is essential for the CC roles in membrane tethering and enhancement of SNARE-mediated fusion CC (PubMed:25686604). Component of the PI3K (PI3KC3/PI3K-III/class III CC phosphatidylinositol 3-kinase) complex I (PI3KC3-C1) in which the core CC composed of the catalytic subunit PIK3C3, the regulatory subunit PIK3R4 CC and BECN1 is associated with ATG14 (PubMed:18843052, PubMed:19050071, CC PubMed:19270696, PubMed:22314358, PubMed:23878393). PI3KC3-C1 displays CC a V-shaped architecture with PIK3R4 serving as a bridge between PIK3C3 CC and the ATG14:BECN1 subcomplex (PubMed:25490155). PI3KC3-C1 can CC associate with further regulatory subunits. Interacts with PIK3CB (By CC similarity). Interacts (via coiled-coil domain) with BECN2 (via coiled- CC coil domain); this interaction is tighter than BECN2 self-association CC (PubMed:23954414, PubMed:28218432). Interacts with the STX17-SNAP29 CC binary t-SNARE complex (PubMed:25686604, PubMed:37632749). Interacts CC with NRBF2 (By similarity). Interacts with PIK3C3 and BECN1; this CC interaction is increased in the absence of TMEM39A (PubMed:31806350). CC Interacts with STEEP1; the interaction is required for trafficking of CC STING1 from the endoplasmic reticulum (PubMed:32690950). Interacts with CC ARMC3 (via ARM domains) (By similarity). {ECO:0000250|UniProtKB:Q8CDJ3, CC ECO:0000269|PubMed:18843052, ECO:0000269|PubMed:19050071, CC ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:22314358, CC ECO:0000269|PubMed:23878393, ECO:0000269|PubMed:23954414, CC ECO:0000269|PubMed:25490155, ECO:0000269|PubMed:25686604, CC ECO:0000269|PubMed:28218432, ECO:0000269|PubMed:31806350, CC ECO:0000269|PubMed:32690950, ECO:0000269|PubMed:37632749, ECO:0000305}. CC -!- INTERACTION: CC Q6ZNE5; Q14457: BECN1; NbExp=50; IntAct=EBI-2690371, EBI-949378; CC Q6ZNE5; A1L4K1: FSD2; NbExp=3; IntAct=EBI-2690371, EBI-5661036; CC Q6ZNE5; Q9NYP9: MIS18A; NbExp=4; IntAct=EBI-2690371, EBI-1104552; CC Q6ZNE5; Q8NEB9: PIK3C3; NbExp=30; IntAct=EBI-2690371, EBI-1056470; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19050071, CC ECO:0000269|PubMed:37632749}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:20713597}; Peripheral CC membrane protein {ECO:0000305}. Preautophagosomal structure membrane CC {ECO:0000269|PubMed:18843052, ECO:0000269|PubMed:19050071, CC ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:22314358}; Peripheral CC membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome CC membrane {ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:25686604}; CC Peripheral membrane protein {ECO:0000305}. Note=Cytosolic under CC nutrient-rich conditions (PubMed:19050071). Following autophagy CC stimuli, such as starvation or rapamycin induction, predominantly CC detected in cytoplasmic foci, identified as isolation membranes and CC autophagosomes (PubMed:19050071). Accumulates on highly curved CC PtdIns(3)P enriched autophagic membrane via its BATS domain to sense CC and maintain membrane curvature (By similarity). Also localizes to CC discrete punctae along the ciliary axoneme and to the base of the CC ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:Q8CDJ3}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6ZNE5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6ZNE5-2; Sequence=VSP_013931; CC -!- DOMAIN: The coiled-coil domain is required for BECN1- and PIK3C3- CC binding and for autophagy. {ECO:0000269|PubMed:20713597}. CC -!- DOMAIN: The final 80 residues in the C-terminus define a minimum CC required region for autophagosome binding called BATS. CC {ECO:0000269|PubMed:20713597, ECO:0000269|PubMed:25686604}. CC -!- DOMAIN: The N-terminal cysteine repeats are required for proper CC localization to the endoplasmic reticulum. CC {ECO:0000269|PubMed:20713597}. CC -!- PTM: Ubiquitinated via 'Lys-6', 'Lys-11' and 'Lys-63'-linked CC polyubiquitin chains on multiple lysines by MARCHF7, leading to ATG14 CC aggregation and loss of interaction with STX17. CC {ECO:0000269|PubMed:37632749}. CC -!- SIMILARITY: Belongs to the ATG14 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74854.2; 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; AB020638; BAA74854.2; ALT_INIT; mRNA. DR EMBL; AK131251; BAD18430.1; -; mRNA. DR EMBL; AK292810; BAF85499.1; -; mRNA. DR EMBL; AL158801; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471061; EAW80673.1; -; Genomic_DNA. DR EMBL; BC109089; AAI09090.1; -; mRNA. DR EMBL; BC109090; AAI09091.1; -; mRNA. DR EMBL; BR000826; FAA00433.1; -; mRNA. DR CCDS; CCDS32087.1; -. [Q6ZNE5-1] DR RefSeq; NP_055739.2; NM_014924.4. [Q6ZNE5-1] DR RefSeq; XP_011534865.1; XM_011536563.3. [Q6ZNE5-2] DR RefSeq; XP_054231553.1; XM_054375578.1. [Q6ZNE5-2] DR PDB; 6HOL; X-ray; 1.40 A; C/D=429-443. DR PDB; 8SOR; EM; 3.96 A; C=1-492. DR PDB; 9C82; EM; 6.84 A; C=1-492. DR PDB; 9MHF; EM; 2.73 A; C=1-492. DR PDB; 9MHG; EM; 3.20 A; C=1-492. DR PDB; 9MHH; EM; 4.50 A; C=1-492. DR PDBsum; 6HOL; -. DR PDBsum; 8SOR; -. DR PDBsum; 9C82; -. DR PDBsum; 9MHF; -. DR PDBsum; 9MHG; -. DR PDBsum; 9MHH; -. DR AlphaFoldDB; Q6ZNE5; -. DR EMDB; EMD-2846; -. DR EMDB; EMD-40669; -. DR EMDB; EMD-40738; -. DR EMDB; EMD-45297; -. DR EMDB; EMD-48276; -. DR EMDB; EMD-48277; -. DR EMDB; EMD-48278; -. DR SMR; Q6ZNE5; -. DR BioGRID; 116531; 360. DR ComplexPortal; CPX-73; Phosphatidylinositol 3-kinase complex, class III, ATG14 variant. DR CORUM; Q6ZNE5; -. DR DIP; DIP-48651N; -. DR FunCoup; Q6ZNE5; 2074. DR IntAct; Q6ZNE5; 49. DR MINT; Q6ZNE5; -. DR STRING; 9606.ENSP00000247178; -. DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family. DR GlyGen; Q6ZNE5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6ZNE5; -. DR PhosphoSitePlus; Q6ZNE5; -. DR BioMuta; ATG14; -. DR DMDM; 67461020; -. DR jPOST; Q6ZNE5; -. DR MassIVE; Q6ZNE5; -. DR PaxDb; 9606-ENSP00000247178; -. DR PeptideAtlas; Q6ZNE5; -. DR ProteomicsDB; 68016; -. [Q6ZNE5-1] DR ProteomicsDB; 68017; -. [Q6ZNE5-2] DR Pumba; Q6ZNE5; -. DR Antibodypedia; 24031; 214 antibodies from 32 providers. DR DNASU; 22863; -. DR Ensembl; ENST00000247178.6; ENSP00000247178.5; ENSG00000126775.9. [Q6ZNE5-1] DR GeneID; 22863; -. DR KEGG; hsa:22863; -. DR MANE-Select; ENST00000247178.6; ENSP00000247178.5; NM_014924.5; NP_055739.2. DR UCSC; uc001xbx.3; human. [Q6ZNE5-1] DR AGR; HGNC:19962; -. DR ClinPGx; PA165478560; -. DR CTD; 22863; -. DR DisGeNET; 22863; -. DR GeneCards; ATG14; -. DR HGNC; HGNC:19962; ATG14. DR HPA; ENSG00000126775; Tissue enhanced (bone). DR MIM; 613515; gene. DR OpenTargets; ENSG00000126775; -. DR VEuPathDB; HostDB:ENSG00000126775; -. DR eggNOG; KOG4398; Eukaryota. DR GeneTree; ENSGT00390000011854; -. DR HOGENOM; CLU_046719_1_0_1; -. DR InParanoid; Q6ZNE5; -. DR OMA; LCYSEFC; -. DR OrthoDB; 16772at2759; -. DR PAN-GO; Q6ZNE5; 9 GO annotations based on evolutionary models. DR PhylomeDB; Q6ZNE5; -. DR BRENDA; 2.7.1.137; 2681. DR PathwayCommons; Q6ZNE5; -. DR Reactome; R-HSA-1632852; Macroautophagy. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; Q6ZNE5; -. DR SIGNOR; Q6ZNE5; -. DR Agora; ENSG00000126775; -. DR BioGRID-ORCS; 22863; 31 hits in 1164 CRISPR screens. DR ChiTaRS; ATG14; human. DR GenomeRNAi; 22863; -. DR Pharos; Q6ZNE5; Tbio. DR PRO; PR:Q6ZNE5; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q6ZNE5; protein. DR Bgee; ENSG00000126775; Expressed in secondary oocyte and 205 other cell types or tissues. DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB. DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005930; C:axoneme; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0097629; C:extrinsic component of omegasome membrane; IDA:UniProtKB. DR GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IDA:UniProtKB. DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane contact site; IEA:Ensembl. DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl. DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProt. DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB. DR GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; IPI:ComplexPortal. DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB. DR GO; GO:0141039; F:phosphatidylinositol 3-kinase inhibitor activity; IDA:GO_Central. DR GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; IBA:GO_Central. DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:UniProt. DR GO; GO:0000045; P:autophagosome assembly; IDA:UniProt. DR GO; GO:0097352; P:autophagosome maturation; IDA:ComplexPortal. DR GO; GO:0016240; P:autophagosome membrane docking; IDA:GO_Central. DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB. DR GO; GO:0009267; P:cellular response to starvation; IMP:ParkinsonsUK-UCL. DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl. DR GO; GO:0045022; P:early endosome to late endosome transport; IDA:ComplexPortal. DR GO; GO:0008333; P:endosome to lysosome transport; IGI:MGI. DR GO; GO:0045087; P:innate immune response; IEA:Ensembl. DR GO; GO:0016236; P:macroautophagy; IMP:ParkinsonsUK-UCL. DR GO; GO:0000423; P:mitophagy; IMP:ParkinsonsUK-UCL. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:UniProtKB. DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IDA:ComplexPortal. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB. DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:ParkinsonsUK-UCL. DR GO; GO:0006622; P:protein targeting to lysosome; NAS:ComplexPortal. DR GO; GO:0016241; P:regulation of macroautophagy; IDA:ComplexPortal. DR GO; GO:0061635; P:regulation of protein complex stability; IMP:ParkinsonsUK-UCL. DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IEA:Ensembl. DR GO; GO:0098780; P:response to mitochondrial depolarisation; IMP:BHF-UCL. DR InterPro; IPR018791; UV_resistance/autophagy_Atg14. DR PANTHER; PTHR13664; BECLIN 1-ASSOCIATED AUTOPHAGY-RELATED KEY REGULATOR; 1. DR PANTHER; PTHR13664:SF0; BECLIN 1-ASSOCIATED AUTOPHAGY-RELATED KEY REGULATOR; 1. DR Pfam; PF10186; ATG14; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Autophagy; Coiled coil; Cytoplasm; KW Cytoplasmic vesicle; Endoplasmic reticulum; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Ubl conjugation. FT CHAIN 1..492 FT /note="Beclin 1-associated autophagy-related key regulator" FT /id="PRO_0000050774" FT REGION 43..58 FT /note="Cysteine repeats" FT REGION 410..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 413..492 FT /note="BATS" FT /evidence="ECO:0000250" FT COILED 71..180 FT /evidence="ECO:0000255" FT COMPBIAS 415..433 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 448..473 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 29 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:31123703, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19369195" FT MOD_RES 416 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 429 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19369195" FT VAR_SEQ 1..113 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10048485" FT /id="VSP_013931" FT VARIANT 59 FT /note="V -> I (in dbSNP:rs57295720)" FT /id="VAR_061240" FT VARIANT 131 FT /note="N -> K (in dbSNP:rs17675076)" FT /id="VAR_049514" FT MUTAGEN 43 FT /note="C->A: In Atg14L4C4A; fails to localize to the FT endoplasmic reticulum; when associated with A-46; A-55 and FT A-58." FT /evidence="ECO:0000269|PubMed:20713597, FT ECO:0000269|PubMed:25686604" FT MUTAGEN 46 FT /note="C->A: In Atg14L4C4A; fails to localize to the FT endoplasmic reticulum; when associated with A-43; A-55 and FT A-58." FT /evidence="ECO:0000269|PubMed:20713597, FT ECO:0000269|PubMed:25686604" FT MUTAGEN 55 FT /note="C->A: In Atg14L4C4A; fails to localize to the FT endoplasmic reticulum; when associated with A-43; A-46 and FT A-58." FT /evidence="ECO:0000269|PubMed:20713597, FT ECO:0000269|PubMed:25686604" FT MUTAGEN 58 FT /note="C->A: In Atg14L4C4A; fails to localize to the FT endoplasmic reticulum; when associated with A-43; A-46 and FT A-55." FT /evidence="ECO:0000269|PubMed:20713597, FT ECO:0000269|PubMed:25686604" FT CONFLICT 256 FT /note="N -> S (in Ref. 5; AAI09090)" FT /evidence="ECO:0000305" FT HELIX 57..61 FT /evidence="ECO:0007829|PDB:9MHG" FT HELIX 75..204 FT /evidence="ECO:0007829|PDB:9MHF" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:9MHF" FT STRAND 260..265 FT /evidence="ECO:0007829|PDB:9MHF" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:9MHF" FT HELIX 277..280 FT /evidence="ECO:0007829|PDB:9MHF" FT HELIX 299..321 FT /evidence="ECO:0007829|PDB:9MHF" FT HELIX 331..334 FT /evidence="ECO:0007829|PDB:9MHF" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:9MHF" FT HELIX 341..361 FT /evidence="ECO:0007829|PDB:9MHF" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:9MHF" FT HELIX 374..382 FT /evidence="ECO:0007829|PDB:9MHF" FT TURN 387..390 FT /evidence="ECO:0007829|PDB:9MHF" FT HELIX 399..405 FT /evidence="ECO:0007829|PDB:9MHG" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:6HOL" SQ SEQUENCE 492 AA; 55309 MW; A3EAB0580077D7A6 CRC64; MASPSGKGAR ALEAPGCGPR PLARDLVDSV DDAEGLYVAV ERCPLCNTTR RRLTCAKCVQ SGDFVYFDGR DRERFIDKKE RLSRLKSKQE EFQKEVLKAM EGKWITDQLR WKIMSCKMRI EQLKQTICKG NEEMEKNSEG LLKTKEKNQK LYSRAQRHQE KKEKIQRHNR KLGDLVEKKT IDLRSHYERL ANLRRSHILE LTSVIFPIEE VKTGVRDPAD VSSESDSAMT SSTVSKLAEA RRTTYLSGRW VCDDHNGDTS ISITGPWISL PNNGDYSAYY SWVEEKKTTQ GPDMEQSNPA YTISAALCYA TQLVNILSHI LDVNLPKKLC NSEFCGENLS KQKFTRAVKK LNANILYLCF SQHVNLDQLQ PLHTLRNLMY LVSPSSEHLG RSGPFEVRAD LEESMEFVDP GVAGESDESG DERVSDEETD LGTDWENLPS PRFCDIPSQS VEVSQSQSTQ ASPPIASSSA GGMISSAAAS VTSWFKAYTG HR //