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Q9CQY1 (ATG12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-like protein ATG12
Alternative name(s):
Autophagy-related protein 12
Short name=APG12-like
Gene names
Name:Atg12
Synonyms:Apg12, Apg12l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.10

Subunit structure

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. Ref.4 Ref.6

Subcellular location

Cytoplasm By similarity. Preautophagosomal structure membrane; Peripheral membrane protein By similarity. Note: TECPR1 recruits the ATG12-ATG5 conjugate to the autolysosomal membrane By similarity. Ref.1

Tissue specificity

Ubiquitous.

Domain

Shares weak sequence similarity with ubiquitin family, but contains an 'ubiquitin superfold' and the C-terminal Gly is required for isopeptide linkage. Ref.7

Post-translational modification

Acetylated by EP300 By similarity.

Sequence similarities

Belongs to the ATG12 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 141141Ubiquitin-like protein ATG12
PRO_0000212472

Amino acid modifications

Cross-link141Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor protein)

Experimental info

Sequence conflict44 – 485GTEEP → ERGT in BAB25839. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9CQY1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 440F9A625624A78B

FASTA14115,207
        10         20         30         40         50         60 
MSEDSEVVLQ LPSAPVGAGG ESLPELSPET ATPEPPSSAA VSPGTEEPPG DTKKKIDILL 

        70         80         90        100        110        120 
KAVGDTPIMK TKKWAVERTR TIQGLIDFIK KFLKLVASEQ LFIYVNQSFA PSPDQEVGTL 

       130        140 
YECFGSDGKL VLHYCKSQAW G 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS37811.1.
RefSeqNP_080493.2. NM_026217.3.
UniGeneMm.9852.

3D structure databases

ProteinModelPortalQ9CQY1.
SMRQ9CQY1. Positions 54-141.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212249. 4 interactions.
IntActQ9CQY1. 8 interactions.
MINTMINT-4613690.
STRING10090.ENSMUSP00000038489.

PTM databases

PhosphoSiteQ9CQY1.

Proteomic databases

PaxDbQ9CQY1.
PRIDEQ9CQY1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035648; ENSMUSP00000038489; ENSMUSG00000032905.
GeneID67526.
KEGGmmu:67526.
UCSCuc008evu.1. mouse.

Organism-specific databases

CTD9140.
MGIMGI:1914776. Atg12.

Phylogenomic databases

eggNOGNOG236266.
GeneTreeENSGT00390000016654.
HOGENOMHOG000234863.
HOVERGENHBG080875.
InParanoidQ9CQY1.
KOK08336.
OMAPWRKARP.
OrthoDBEOG7XPZ7X.
PhylomeDBQ9CQY1.
TreeFamTF325131.

Gene expression databases

BgeeQ9CQY1.
CleanExMM_ATG12.
GenevestigatorQ9CQY1.

Family and domain databases

InterProIPR007242. Atg12.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR13385. PTHR13385. 1 hit.
PfamPF04110. APG12. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
ProtoNetSearch...

Other

ChiTaRSATG12. mouse.
NextBio324820.
PROQ9CQY1.
SOURCESearch...

Entry information

Entry nameATG12_MOUSE
AccessionPrimary (citable) accession number: Q9CQY1
Secondary accession number(s): Q3TKE5, Q9D7Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot