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Protein

Autophagy-related protein 101

Gene

ATG101

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Autophagy factor required for autophagosome formation. Stabilizes ATG13, protecting it from proteasomal degradation.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein complex binding Source: UniProtKB

GO - Biological processi

  • autophagosome assembly Source: UniProtKB
  • macroautophagy Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Autophagy

Enzyme and pathway databases

ReactomeiR-HSA-1632852. Macroautophagy.
SIGNORiQ9BSB4.

Names & Taxonomyi

Protein namesi
Recommended name:
Autophagy-related protein 101
Gene namesi
Name:ATG101
Synonyms:C12orf44
ORF Names:PP894
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:25679. ATG101.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • pre-autophagosomal structure Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311H → S: Impairs interaction with ATG13; when associated with R-54. 1 Publication
Mutagenesisi54 – 541D → R: Impairs interaction with ATG13; when associated with S-31. 1 Publication
Mutagenesisi152 – 1521I → D: Abolishes interaction with ATG13; when associated with D-153 and D-156. 1 Publication
Mutagenesisi153 – 1531I → D: Abolishes interaction with ATG13; when associated with D-152 and D-156. 1 Publication
Mutagenesisi156 – 1561V → D: Abolishes interaction with ATG13; when associated with D-152 and D-152. 1 Publication

Organism-specific databases

PharmGKBiPA143485374.

Polymorphism and mutation databases

BioMutaiATG101.
DMDMi74732983.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Autophagy-related protein 101PRO_0000294322Add
BLAST

Proteomic databases

EPDiQ9BSB4.
MaxQBiQ9BSB4.
PaxDbiQ9BSB4.
PRIDEiQ9BSB4.

PTM databases

iPTMnetiQ9BSB4.
PhosphoSiteiQ9BSB4.

Expressioni

Gene expression databases

BgeeiQ9BSB4.
CleanExiHS_C12orf44.
ExpressionAtlasiQ9BSB4. baseline and differential.
GenevisibleiQ9BSB4. HS.

Organism-specific databases

HPAiHPA039904.

Interactioni

Subunit structurei

Interacts with ATG13 (PubMed:19287211, PubMed:19597335, PubMed:26299944). Associates with a complex composed of ATG13, ULK1 and RB1CC1; the association with this complex requires the presence of ATG13 (PubMed:19287211, PubMed:19597335).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2946739,EBI-2946739
ATG13O7514310EBI-2946739,EBI-2798775
MAP1LC3CQ9BXW42EBI-2946739,EBI-2603996
RB1CC1Q8TDY27EBI-2946739,EBI-1047793

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121948. 42 interactions.
DIPiDIP-60653N.
IntActiQ9BSB4. 40 interactions.
MINTiMINT-6780987.
STRINGi9606.ENSP00000338990.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1310Combined sources
Helixi14 – 163Combined sources
Helixi17 – 3115Combined sources
Beta strandi37 – 393Combined sources
Helixi41 – 433Combined sources
Beta strandi45 – 473Combined sources
Beta strandi52 – 565Combined sources
Beta strandi58 – 614Combined sources
Beta strandi63 – 686Combined sources
Helixi70 – 8920Combined sources
Beta strandi92 – 10514Combined sources
Beta strandi113 – 12917Combined sources
Helixi134 – 16128Combined sources
Helixi171 – 1766Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi190 – 1989Combined sources
Beta strandi202 – 2076Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WZGX-ray1.90A1-218[»]
5C50X-ray1.63A1-198[»]
ProteinModelPortaliQ9BSB4.
SMRiQ9BSB4. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni152 – 1565Important for interaction with ATG131 Publication

Sequence similaritiesi

Belongs to the ATG101 family.Curated

Phylogenomic databases

eggNOGiKOG4493. Eukaryota.
ENOG410XP6A. LUCA.
GeneTreeiENSGT00390000016511.
HOGENOMiHOG000008086.
InParanoidiQ9BSB4.
KOiK19730.
OMAiMGQISLE.
OrthoDBiEOG7DFXD6.
PhylomeDBiQ9BSB4.
TreeFamiTF320996.

Family and domain databases

InterProiIPR012445. ATG101.
[Graphical view]
PANTHERiPTHR13292. PTHR13292. 1 hit.
PfamiPF07855. DUF1649. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BSB4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNCRSEVLEV SVEGRQVEEA MLAVLHTVLL HRSTGKFHYK KEGTYSIGTV
60 70 80 90 100
GTQDVDCDFI DFTYVRVSSE ELDRALRKVV GEFKDALRNS GGDGLGQMSL
110 120 130 140 150
EFYQKKKSRW PFSDECIPWE VWTVKVHVVA LATEQERQIC REKVGEKLCE
160 170 180 190 200
KIINIVEVMN RHEYLPKMPT QSEVDNVFDT GLRDVQPYLY KISFQITDAL
210
GTSVTTTMRR LIKDTLAL
Length:218
Mass (Da):25,003
Last modified:June 1, 2001 - v1
Checksum:i69A881EAF9A07659
GO

Sequence cautioni

The sequence AAG17273.1 differs from that shown. Reason: Frameshift at position 110. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471I → T in BAB13907 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021835 mRNA. Translation: BAB13907.1.
AF218031 mRNA. Translation: AAG17273.1. Frameshift.
AC025259 Genomic DNA. No translation available.
BC005151 mRNA. Translation: AAH05151.1.
BC009937 mRNA. Translation: AAH09937.1.
CCDSiCCDS8820.1.
RefSeqiNP_001092143.1. NM_001098673.1.
NP_068753.2. NM_021934.4.
UniGeneiHs.9911.

Genome annotation databases

EnsembliENST00000336854; ENSP00000338990; ENSG00000123395.
GeneIDi60673.
KEGGihsa:60673.
UCSCiuc001rzu.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021835 mRNA. Translation: BAB13907.1.
AF218031 mRNA. Translation: AAG17273.1. Frameshift.
AC025259 Genomic DNA. No translation available.
BC005151 mRNA. Translation: AAH05151.1.
BC009937 mRNA. Translation: AAH09937.1.
CCDSiCCDS8820.1.
RefSeqiNP_001092143.1. NM_001098673.1.
NP_068753.2. NM_021934.4.
UniGeneiHs.9911.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WZGX-ray1.90A1-218[»]
5C50X-ray1.63A1-198[»]
ProteinModelPortaliQ9BSB4.
SMRiQ9BSB4. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121948. 42 interactions.
DIPiDIP-60653N.
IntActiQ9BSB4. 40 interactions.
MINTiMINT-6780987.
STRINGi9606.ENSP00000338990.

PTM databases

iPTMnetiQ9BSB4.
PhosphoSiteiQ9BSB4.

Polymorphism and mutation databases

BioMutaiATG101.
DMDMi74732983.

Proteomic databases

EPDiQ9BSB4.
MaxQBiQ9BSB4.
PaxDbiQ9BSB4.
PRIDEiQ9BSB4.

Protocols and materials databases

DNASUi60673.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336854; ENSP00000338990; ENSG00000123395.
GeneIDi60673.
KEGGihsa:60673.
UCSCiuc001rzu.5. human.

Organism-specific databases

CTDi60673.
GeneCardsiATG101.
H-InvDBHIX0010645.
HGNCiHGNC:25679. ATG101.
HPAiHPA039904.
MIMi615089. gene.
neXtProtiNX_Q9BSB4.
PharmGKBiPA143485374.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4493. Eukaryota.
ENOG410XP6A. LUCA.
GeneTreeiENSGT00390000016511.
HOGENOMiHOG000008086.
InParanoidiQ9BSB4.
KOiK19730.
OMAiMGQISLE.
OrthoDBiEOG7DFXD6.
PhylomeDBiQ9BSB4.
TreeFamiTF320996.

Enzyme and pathway databases

ReactomeiR-HSA-1632852. Macroautophagy.
SIGNORiQ9BSB4.

Miscellaneous databases

GeneWikiiAutophagy-related_protein_101.
GenomeRNAii60673.
PROiQ9BSB4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BSB4.
CleanExiHS_C12orf44.
ExpressionAtlasiQ9BSB4. baseline and differential.
GenevisibleiQ9BSB4. HS.

Family and domain databases

InterProiIPR012445. ATG101.
[Graphical view]
PANTHERiPTHR13292. PTHR13292. 1 hit.
PfamiPF07855. DUF1649. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  2. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Uterus.
  5. "A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy."
    Mercer C.A., Kaliappan A., Dennis P.B.
    Autophagy 5:649-662(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATG13, COMPLEX FORMATION WITH ULK1 AND RB1CC1.
  6. "Atg101, a novel mammalian autophagy protein interacting with Atg13."
    Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T., Mizushima N.
    Autophagy 5:973-979(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AUTOPHAGY FACTOR, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH ATG13.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "The mammalian autophagy initiator complex contains 2 HORMA domain proteins."
    Michel M., Schwarten M., Decker C., Nagel-Steger L., Willbold D., Weiergraber O.H.
    Autophagy 11:2300-2308(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
  9. "Structure of the human Atg13-Atg101 HORMA heterodimer: an interaction hub within the ULK1 complex."
    Qi S., Kim do J., Stjepanovic G., Hurley J.H.
    Structure 23:1848-1857(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 1-198 IN COMPLEX WITH ATG13, INTERACTION WITH ATG13, MUTAGENESIS OF HIS-31; ASP-54; ILE-152; ILE-153 AND VAL-156.

Entry informationi

Entry nameiATGA1_HUMAN
AccessioniPrimary (citable) accession number: Q9BSB4
Secondary accession number(s): Q9HAE2, Q9HBN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.