ID ATGA1_HUMAN Reviewed; 218 AA. AC Q9BSB4; Q9HAE2; Q9HBN1; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 154. DE RecName: Full=Autophagy-related protein 101; GN Name=ATG101; Synonyms=C12orf44; ORFNames=PP894; 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]. RC TISSUE=Embryo; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Uterus; 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 [5] RP FUNCTION, INTERACTION WITH ATG13, AND COMPLEX FORMATION WITH ULK1 AND RP RB1CC1. 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 [6] RP FUNCTION AS AUTOPHAGY FACTOR, SUBCELLULAR LOCATION, SUBUNIT, AND RP INTERACTION WITH ATG13. 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] {ECO:0007744|PDB:4WZG} 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 [9] {ECO:0007744|PDB:5C50} RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 1-198 IN COMPLEX WITH ATG13, RP INTERACTION WITH ATG13, AND MUTAGENESIS OF HIS-31; ASP-54; ILE-152; ILE-153 RP AND VAL-156. 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. CC Stabilizes ATG13, protecting it from proteasomal degradation. CC {ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:19597335}. CC -!- SUBUNIT: Interacts with ATG13 (PubMed:19287211, PubMed:19597335, CC PubMed:26299944). Associates with a complex composed of ATG13, ULK1 and CC RB1CC1; the association with this complex requires the presence of CC ATG13 (PubMed:19287211, PubMed:19597335). {ECO:0000269|PubMed:19287211, CC ECO:0000269|PubMed:19597335, ECO:0000269|PubMed:26299944}. CC -!- INTERACTION: CC Q9BSB4; Q9BSB4: ATG101; NbExp=2; IntAct=EBI-2946739, EBI-2946739; CC Q9BSB4; O75143: ATG13; NbExp=16; IntAct=EBI-2946739, EBI-2798775; CC Q9BSB4; O75143-2: ATG13; NbExp=3; IntAct=EBI-2946739, EBI-20151086; CC Q9BSB4; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-2946739, EBI-2603996; CC Q9BSB4; Q8TDY2: RB1CC1; NbExp=7; IntAct=EBI-2946739, EBI-1047793; CC Q9BSB4; Q91YI1: Atg13; Xeno; NbExp=2; IntAct=EBI-2946739, EBI-8391007; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19597335}. CC Preautophagosomal structure {ECO:0000269|PubMed:19597335}. Note=Under CC starvation conditions, it 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:19597335}. CC -!- SIMILARITY: Belongs to the ATG101 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG17273.1; Type=Frameshift; 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; AK021835; BAB13907.1; -; mRNA. DR EMBL; AF218031; AAG17273.1; ALT_FRAME; mRNA. DR EMBL; AC025259; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005151; AAH05151.1; -; mRNA. DR EMBL; BC009937; AAH09937.1; -; mRNA. DR CCDS; CCDS8820.1; -. DR RefSeq; NP_001092143.1; NM_001098673.1. DR RefSeq; NP_068753.2; NM_021934.4. DR PDB; 4WZG; X-ray; 1.90 A; A=1-218. DR PDB; 5C50; X-ray; 1.63 A; A=1-198. DR PDB; 5XUY; X-ray; 2.20 A; B/D=1-218. DR PDB; 5XV1; X-ray; 2.51 A; B/D=1-218. DR PDB; 5XV3; X-ray; 2.57 A; B/D=1-218. DR PDB; 5XV4; X-ray; 2.95 A; B/D/F/H/J/L/N/P=1-218. DR PDB; 5XV6; X-ray; 2.46 A; B=1-218. DR PDB; 8DO8; X-ray; 2.41 A; A/C/E/F=1-198. DR PDBsum; 4WZG; -. DR PDBsum; 5C50; -. DR PDBsum; 5XUY; -. DR PDBsum; 5XV1; -. DR PDBsum; 5XV3; -. DR PDBsum; 5XV4; -. DR PDBsum; 5XV6; -. DR PDBsum; 8DO8; -. DR AlphaFoldDB; Q9BSB4; -. DR SMR; Q9BSB4; -. DR BioGRID; 121948; 96. DR ComplexPortal; CPX-373; ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex. DR CORUM; Q9BSB4; -. DR DIP; DIP-60653N; -. DR IntAct; Q9BSB4; 45. DR MINT; Q9BSB4; -. DR STRING; 9606.ENSP00000338990; -. DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family. DR iPTMnet; Q9BSB4; -. DR PhosphoSitePlus; Q9BSB4; -. DR BioMuta; ATG101; -. DR DMDM; 74732983; -. DR EPD; Q9BSB4; -. DR jPOST; Q9BSB4; -. DR MassIVE; Q9BSB4; -. DR MaxQB; Q9BSB4; -. DR PaxDb; 9606-ENSP00000338990; -. DR PeptideAtlas; Q9BSB4; -. DR ProteomicsDB; 78873; -. DR Pumba; Q9BSB4; -. DR Antibodypedia; 43032; 111 antibodies from 26 providers. DR DNASU; 60673; -. DR Ensembl; ENST00000336854.9; ENSP00000338990.4; ENSG00000123395.15. DR GeneID; 60673; -. DR KEGG; hsa:60673; -. DR MANE-Select; ENST00000336854.9; ENSP00000338990.4; NM_021934.5; NP_068753.2. DR UCSC; uc001rzu.5; human. DR AGR; HGNC:25679; -. DR CTD; 60673; -. DR DisGeNET; 60673; -. DR GeneCards; ATG101; -. DR HGNC; HGNC:25679; ATG101. DR HPA; ENSG00000123395; Low tissue specificity. DR MIM; 615089; gene. DR neXtProt; NX_Q9BSB4; -. DR OpenTargets; ENSG00000123395; -. DR PharmGKB; PA143485374; -. DR VEuPathDB; HostDB:ENSG00000123395; -. DR eggNOG; KOG4493; Eukaryota. DR GeneTree; ENSGT00390000016511; -. DR InParanoid; Q9BSB4; -. DR OMA; EDVDCDF; -. DR OrthoDB; 3133133at2759; -. DR PhylomeDB; Q9BSB4; -. DR TreeFam; TF320996; -. DR PathwayCommons; Q9BSB4; -. DR Reactome; R-HSA-1632852; Macroautophagy. DR SignaLink; Q9BSB4; -. DR SIGNOR; Q9BSB4; -. DR BioGRID-ORCS; 60673; 35 hits in 1143 CRISPR screens. DR ChiTaRS; ATG101; human. DR GeneWiki; Autophagy-related_protein_101; -. DR GenomeRNAi; 60673; -. DR Pharos; Q9BSB4; Tbio. DR PRO; PR:Q9BSB4; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9BSB4; Protein. DR Bgee; ENSG00000123395; Expressed in stromal cell of endometrium and 201 other cell types or tissues. DR ExpressionAtlas; Q9BSB4; baseline and differential. DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IPI:ComplexPortal. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB. DR GO; GO:0000045; P:autophagosome assembly; IDA:ComplexPortal. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:ComplexPortal. DR GO; GO:0010508; P:positive regulation of autophagy; ISO:ComplexPortal. DR GO; GO:1903059; P:regulation of protein lipidation; IDA:ComplexPortal. DR InterPro; IPR012445; ATG101. DR PANTHER; PTHR13292:SF0; AUTOPHAGY-RELATED PROTEIN 101; 1. DR PANTHER; PTHR13292; UNCHARACTERIZED; 1. DR Pfam; PF07855; ATG101; 1. DR Genevisible; Q9BSB4; HS. PE 1: Evidence at protein level; KW 3D-structure; Autophagy; Cytoplasm; Reference proteome. FT CHAIN 1..218 FT /note="Autophagy-related protein 101" FT /id="PRO_0000294322" FT REGION 152..156 FT /note="Important for interaction with ATG13" FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 31 FT /note="H->S: Impairs interaction with ATG13; when FT associated with R-54." FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 54 FT /note="D->R: Impairs interaction with ATG13; when FT associated with S-31." FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 152 FT /note="I->D: Abolishes interaction with ATG13; when FT associated with D-153 and D-156." FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 153 FT /note="I->D: Abolishes interaction with ATG13; when FT associated with D-152 and D-156." FT /evidence="ECO:0000269|PubMed:26299944" FT MUTAGEN 156 FT /note="V->D: Abolishes interaction with ATG13; when FT associated with D-152 and D-152." FT /evidence="ECO:0000269|PubMed:26299944" FT CONFLICT 47 FT /note="I -> T (in Ref. 1; BAB13907)" FT /evidence="ECO:0000305" FT STRAND 4..13 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 17..31 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:5XUY" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:4WZG" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 52..56 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 70..89 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 92..105 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 113..129 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 134..161 FT /evidence="ECO:0007829|PDB:5C50" FT HELIX 171..176 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:8DO8" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 190..198 FT /evidence="ECO:0007829|PDB:5C50" FT STRAND 202..207 FT /evidence="ECO:0007829|PDB:4WZG" FT HELIX 208..214 FT /evidence="ECO:0007829|PDB:5XUY" SQ SEQUENCE 218 AA; 25003 MW; 69A881EAF9A07659 CRC64; MNCRSEVLEV SVEGRQVEEA MLAVLHTVLL HRSTGKFHYK KEGTYSIGTV GTQDVDCDFI DFTYVRVSSE ELDRALRKVV GEFKDALRNS GGDGLGQMSL EFYQKKKSRW PFSDECIPWE VWTVKVHVVA LATEQERQIC REKVGEKLCE KIINIVEVMN RHEYLPKMPT QSEVDNVFDT GLRDVQPYLY KISFQITDAL GTSVTTTMRR LIKDTLAL //