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Q9CQY1

- ATG12_MOUSE

UniProt

Q9CQY1 - ATG12_MOUSE

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Protein

Ubiquitin-like protein ATG12

Gene

Atg12

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. Atg8 ligase activity Source: RefGenome

GO - Biological processi

  1. autophagic vacuole assembly Source: UniProtKB
  2. autophagy Source: MGI
  3. cellular response to nitrogen starvation Source: RefGenome
  4. C-terminal protein lipidation Source: RefGenome
  5. innate immune response Source: UniProtKB-KW
  6. mitochondrion degradation Source: RefGenome
  7. nucleophagy Source: RefGenome
Complete GO annotation...

Keywords - Biological processi

Autophagy, Immunity, Innate immunity, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_198532. 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: Chromosome 18

Organism-specific databases

MGIiMGI:1914776. Atg12.

Subcellular locationi

Cytoplasm By similarity. Preautophagosomal structure membrane By similarity; Peripheral membrane protein By similarity
Note: TECPR1 recruits the ATG12-ATG5 conjugate to the autolysosomal membrane.By similarity

GO - Cellular componenti

  1. Atg12-Atg5-Atg16 complex Source: RefGenome
  2. cytosol Source: Reactome
  3. 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.
GenevestigatoriQ9CQY1.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS37811.1.
RefSeqi NP_080493.2. NM_026217.3.
UniGenei Mm.9852.

3D structure databases

ProteinModelPortali Q9CQY1.
SMRi Q9CQY1. Positions 54-141.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212249. 4 interactions.
IntActi Q9CQY1. 8 interactions.
MINTi MINT-4613690.
STRINGi 10090.ENSMUSP00000038489.

PTM databases

PhosphoSitei Q9CQY1.

Proteomic databases

MaxQBi Q9CQY1.
PaxDbi Q9CQY1.
PRIDEi Q9CQY1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035648 ; ENSMUSP00000038489 ; ENSMUSG00000032905 .
GeneIDi 67526.
KEGGi mmu:67526.
UCSCi uc008evu.1. mouse.

Organism-specific databases

CTDi 9140.
MGIi MGI:1914776. Atg12.

Phylogenomic databases

eggNOGi NOG236266.
GeneTreei ENSGT00390000016654.
HOGENOMi HOG000234863.
HOVERGENi HBG080875.
InParanoidi Q9CQY1.
KOi K08336.
OMAi PWRKARP.
OrthoDBi EOG7XPZ7X.
PhylomeDBi Q9CQY1.
TreeFami TF325131.

Enzyme and pathway databases

Reactomei REACT_198532. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSi ATG12. mouse.
NextBioi 324820.
PROi Q9CQY1.
SOURCEi Search...

Gene expression databases

Bgeei Q9CQY1.
CleanExi MM_ATG12.
Genevestigatori Q9CQY1.

Family and domain databases

InterProi IPR007242. Atg12.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
PANTHERi PTHR13385. PTHR13385. 1 hit.
Pfami PF04110. APG12. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
ProtoNeti Search...

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: October 29, 2014
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

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