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Protein

Ubiquitin-like protein ATG12

Gene

Atg12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. The ATG12-ATG5 conjugate also regulates negatively the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Plays also a role in translation or delivery of incoming viral RNA to the translation apparatus.3 Publications

GO - Molecular functioni

GO - Biological processi

  • autophagosome assembly Source: UniProtKB
  • autophagy Source: MGI
  • cellular response to nitrogen starvation Source: GO_Central
  • C-terminal protein lipidation Source: GO_Central
  • innate immune response Source: UniProtKB-KW
  • mitochondrion degradation Source: GO_Central
  • nucleophagy Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Autophagy, Immunity, Innate immunity, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_289760. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like protein ATG12
Alternative name(s):
Autophagy-related protein 12
Short name:
APG12-like
Gene namesi
Name:Atg12
Synonyms:Apg12, Apg12l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1914776. Atg12.

Subcellular locationi

GO - Cellular componenti

  • Atg12-Atg5-Atg16 complex Source: GO_Central
  • cytosol Source: Reactome
  • membrane Source: ParkinsonsUK-UCL
  • pre-autophagosomal structure membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 141141Ubiquitin-like protein ATG12PRO_0000212472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki141 – 141Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor protein)

Post-translational modificationi

Acetylated by EP300.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond

Proteomic databases

MaxQBiQ9CQY1.
PaxDbiQ9CQY1.
PRIDEiQ9CQY1.

PTM databases

PhosphoSiteiQ9CQY1.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9CQY1.
CleanExiMM_ATG12.
GenevisibleiQ9CQY1. MM.

Interactioni

Subunit structurei

Forms a conjugate with ATG5. The ATG12-ATG5 conjugate forms a complex with several units of ATG16L. Interacts with ATG3, ATG7 and ATG10. ATG12-ATG5 also interacts with MAVS, MGA, RARRES3 and TECPR1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Atg3Q9CPX63EBI-2911788,EBI-2911810
Atg5Q99J833EBI-2911788,EBI-2911848

Protein-protein interaction databases

BioGridi212249. 4 interactions.
IntActiQ9CQY1. 8 interactions.
MINTiMINT-4613690.
STRINGi10090.ENSMUSP00000038489.

Structurei

3D structure databases

ProteinModelPortaliQ9CQY1.
SMRiQ9CQY1. Positions 54-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Shares weak sequence similarity with ubiquitin family, but contains an 'ubiquitin superfold' and the C-terminal Gly is required for isopeptide linkage.1 Publication

Sequence similaritiesi

Belongs to the ATG12 family.Curated

Phylogenomic databases

eggNOGiNOG236266.
GeneTreeiENSGT00390000016654.
HOGENOMiHOG000234863.
HOVERGENiHBG080875.
InParanoidiQ9CQY1.
KOiK08336.
OMAiPWRKARP.
OrthoDBiEOG7XPZ7X.
PhylomeDBiQ9CQY1.
TreeFamiTF325131.

Family and domain databases

InterProiIPR007242. Atg12.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR13385. PTHR13385. 1 hit.
PfamiPF04110. APG12. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CQY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEDSEVVLQ LPSAPVGAGG ESLPELSPET ATPEPPSSAA VSPGTEEPPG
60 70 80 90 100
DTKKKIDILL KAVGDTPIMK TKKWAVERTR TIQGLIDFIK KFLKLVASEQ
110 120 130 140
LFIYVNQSFA PSPDQEVGTL YECFGSDGKL VLHYCKSQAW G
Length:141
Mass (Da):15,207
Last modified:June 1, 2001 - v1
Checksum:i440F9A625624A78B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 485GTEEP → ERGT in BAB25839 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB066216 mRNA. Translation: BAB62092.1.
AK008698 mRNA. Translation: BAB25839.1.
AK016474 mRNA. Translation: BAB30256.1.
AK005405 mRNA. Translation: BAB24005.1.
AK167027 mRNA. Translation: BAE39200.1.
BC070470 mRNA. Translation: AAH70470.1.
CCDSiCCDS37811.1.
RefSeqiNP_080493.2. NM_026217.3.
UniGeneiMm.9852.

Genome annotation databases

EnsembliENSMUST00000035648; ENSMUSP00000038489; ENSMUSG00000032905.
GeneIDi67526.
KEGGimmu:67526.
UCSCiuc008evu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB066216 mRNA. Translation: BAB62092.1.
AK008698 mRNA. Translation: BAB25839.1.
AK016474 mRNA. Translation: BAB30256.1.
AK005405 mRNA. Translation: BAB24005.1.
AK167027 mRNA. Translation: BAE39200.1.
BC070470 mRNA. Translation: AAH70470.1.
CCDSiCCDS37811.1.
RefSeqiNP_080493.2. NM_026217.3.
UniGeneiMm.9852.

3D structure databases

ProteinModelPortaliQ9CQY1.
SMRiQ9CQY1. Positions 54-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212249. 4 interactions.
IntActiQ9CQY1. 8 interactions.
MINTiMINT-4613690.
STRINGi10090.ENSMUSP00000038489.

PTM databases

PhosphoSiteiQ9CQY1.

Proteomic databases

MaxQBiQ9CQY1.
PaxDbiQ9CQY1.
PRIDEiQ9CQY1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035648; ENSMUSP00000038489; ENSMUSG00000032905.
GeneIDi67526.
KEGGimmu:67526.
UCSCiuc008evu.1. mouse.

Organism-specific databases

CTDi9140.
MGIiMGI:1914776. Atg12.

Phylogenomic databases

eggNOGiNOG236266.
GeneTreeiENSGT00390000016654.
HOGENOMiHOG000234863.
HOVERGENiHBG080875.
InParanoidiQ9CQY1.
KOiK08336.
OMAiPWRKARP.
OrthoDBiEOG7XPZ7X.
PhylomeDBiQ9CQY1.
TreeFamiTF325131.

Enzyme and pathway databases

ReactomeiREACT_289760. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSiAtg12. mouse.
NextBioi324820.
PROiQ9CQY1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQY1.
CleanExiMM_ATG12.
GenevisibleiQ9CQY1. MM.

Family and domain databases

InterProiIPR007242. Atg12.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR13385. PTHR13385. 1 hit.
PfamiPF04110. APG12. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells."
    Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y., Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.
    J. Cell Biol. 152:657-668(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CONJUGATION TO ATG5, FUNCTION OF THE ATG12/ATG5 CONJUGATE, SUBCELLULAR LOCATION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Blastocyst, Placenta, Stomach and Testis.
  3. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method."
    Mizushima N., Yoshimori T., Ohsumi Y.
    FEBS Lett. 532:450-454(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG10, CONJUGATION TO ATG5.
  5. "The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification."
    Nemoto T., Tanida I., Tanida-Miyake E., Minematsu-Ikeguchi N., Yokota M., Ohsumi M., Ueno T., Kominami E.
    J. Biol. Chem. 278:39517-39526(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CONJUGATION TO ATG5 BY ATG10, FUNCTION.
  6. "Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate."
    Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M., Takao T., Natsume T., Ohsumi Y., Yoshimori T.
    J. Cell Sci. 116:1679-1688(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ATG5 AND ATG16.
  7. "The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. 'Protein modifications: beyond the usual suspects' review series."
    Geng J., Klionsky D.J.
    EMBO Rep. 9:859-864(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  8. "The Atg8 conjugation system is indispensable for proper development of autophagic isolation membranes in mice."
    Sou Y.S., Waguri S., Iwata J., Ueno T., Fujimura T., Hara T., Sawada N., Yamada A., Mizushima N., Uchiyama Y., Kominami E., Tanaka K., Komatsu M.
    Mol. Biol. Cell 19:4762-4775(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CONJUGATION TO ATG5.
  9. "Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation."
    Zhang J., Randall M.S., Loyd M.R., Dorsey F.C., Kundu M., Cleveland J.L., Ney P.A.
    Blood 114:157-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CONJUGATION TO ATG5.
  10. "ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death."
    Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C., Debnath J.
    Cell 142:590-600(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiATG12_MOUSE
AccessioniPrimary (citable) accession number: Q9CQY1
Secondary accession number(s): Q3TKE5, Q9D7Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.