ATGA1_HUMAN
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 03-AUG-2022, entry version 145.
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};
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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 PDBsum; 4WZG; -.
DR PDBsum; 5C50; -.
DR PDBsum; 5XUY; -.
DR PDBsum; 5XV1; -.
DR PDBsum; 5XV3; -.
DR PDBsum; 5XV4; -.
DR PDBsum; 5XV6; -.
DR AlphaFoldDB; Q9BSB4; -.
DR SMR; Q9BSB4; -.
DR BioGRID; 121948; 77.
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; Q9BSB4; -.
DR PeptideAtlas; Q9BSB4; -.
DR PRIDE; Q9BSB4; -.
DR ProteomicsDB; 78873; -.
DR Antibodypedia; 43032; 92 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 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; PWEVWNL; -.
DR OrthoDB; 1539728at2759; -.
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; 29 hits in 1064 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 199 other tissues.
DR ExpressionAtlas; Q9BSB4; baseline and differential.
DR Genevisible; Q9BSB4; HS.
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; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:1903059; P:regulation of protein lipidation; IDA:ComplexPortal.
DR InterPro; IPR012445; ATG101.
DR PANTHER; PTHR13292; PTHR13292; 1.
DR Pfam; PF07855; ATG101; 1.
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 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
