BAKOR_HUMAN
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 03-AUG-2022, entry version 146.
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).
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). Modulates the hepatic lipid metabolism (By
CC 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 -!- 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). Interacts with NRBF2 (By
CC similarity). Interacts with PIK3C3 and BECN1; this interaction is
CC increased in the absence of TMEM39A (PubMed:31806350). Interacts with
CC STEEP1; the interaction is required for trafficking of STING1 from the
CC endoplasmic reticulum (PubMed:32690950). {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:0000305}.
CC -!- INTERACTION:
CC Q6ZNE5; Q14457: BECN1; NbExp=47; 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=27; IntAct=EBI-2690371, EBI-1056470;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19050071}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:19270696,
CC ECO:0000269|PubMed:20713597}; Peripheral membrane protein
CC {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). Localizes also 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 -!- 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};
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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_011536563.2. [Q6ZNE5-2]
DR PDB; 6HOL; X-ray; 1.40 A; C/D=429-443.
DR PDBsum; 6HOL; -.
DR AlphaFoldDB; Q6ZNE5; -.
DR SMR; Q6ZNE5; -.
DR BioGRID; 116531; 65.
DR ComplexPortal; CPX-73; Phosphatidylinositol 3-kinase complex, class III, ATG14 variant.
DR CORUM; Q6ZNE5; -.
DR DIP; DIP-48651N; -.
DR IntAct; Q6ZNE5; 18.
DR MINT; Q6ZNE5; -.
DR STRING; 9606.ENSP00000247178; -.
DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; Q6ZNE5; -.
DR PhosphoSitePlus; Q6ZNE5; -.
DR BioMuta; ATG14; -.
DR DMDM; 67461020; -.
DR EPD; Q6ZNE5; -.
DR jPOST; Q6ZNE5; -.
DR MassIVE; Q6ZNE5; -.
DR MaxQB; Q6ZNE5; -.
DR PaxDb; Q6ZNE5; -.
DR PeptideAtlas; Q6ZNE5; -.
DR PRIDE; Q6ZNE5; -.
DR ProteomicsDB; 68016; -. [Q6ZNE5-1]
DR ProteomicsDB; 68017; -. [Q6ZNE5-2]
DR Antibodypedia; 24031; 224 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 CTD; 22863; -.
DR DisGeNET; 22863; -.
DR GeneCards; ATG14; -.
DR HGNC; HGNC:19962; ATG14.
DR HPA; ENSG00000126775; Low tissue specificity.
DR MIM; 613515; gene.
DR neXtProt; NX_Q6ZNE5; -.
DR OpenTargets; ENSG00000126775; -.
DR PharmGKB; PA165478560; -.
DR VEuPathDB; HostDB:ENSG00000126775; -.
DR eggNOG; KOG4398; Eukaryota.
DR GeneTree; ENSGT00390000011854; -.
DR HOGENOM; CLU_046719_1_0_1; -.
DR InParanoid; Q6ZNE5; -.
DR OMA; PWITLPN; -.
DR OrthoDB; 1332122at2759; -.
DR PhylomeDB; Q6ZNE5; -.
DR TreeFam; TF323392; -.
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 BioGRID-ORCS; 22863; 31 hits in 1083 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 203 other tissues.
DR Genevisible; Q6ZNE5; HS.
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; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
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:0000045; P:autophagosome assembly; IMP:UniProtKB.
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:0045022; P:early endosome to late endosome transport; IDA:ComplexPortal.
DR GO; GO:0008333; P:endosome to lysosome transport; IGI:MGI.
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:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
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:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0006622; P:protein targeting to lysosome; IC:ComplexPortal.
DR GO; GO:0016241; P:regulation of macroautophagy; IDA:ComplexPortal.
DR GO; GO:0061635; P:regulation of protein complex stability; IC:ParkinsonsUK-UCL.
DR GO; GO:0001932; P:regulation of protein phosphorylation; 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 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 Reference proteome.
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 443..473
FT /note="Polar residues"
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 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
