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Protein

Ubiquitin-like-conjugating enzyme ATG10

Gene

Atg10

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

Functioni

E2-like enzyme involved in autophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for autophagy. Likely serves as an ATG5-recognition molecule. Not involved in ATG12 conjugation to ATG3. Plays a role in adenovirus-mediated cell lysis.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei165 – 1651Glycyl thioester intermediateCurated

GO - Molecular functioni

  • Atg12 transferase activity Source: UniProtKB
  • ligase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Autophagy, Protein transport, Transport, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like-conjugating enzyme ATG10 (EC:6.3.2.-)
Alternative name(s):
Autophagy-related protein 10
Short name:
APG10-like
Short name:
mAPG10
Gene namesi
Name:Atg10
Synonyms:Apg10l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1914045. Atg10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651C → S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG10 (E2-like enzyme) and ATG12 (substrate), a stable complex with an O-ester bond is formed. Does not affect ATG12 conjugation to ATG3. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Ubiquitin-like-conjugating enzyme ATG10PRO_0000096184Add
BLAST

Proteomic databases

MaxQBiQ8R1P4.
PaxDbiQ8R1P4.
PRIDEiQ8R1P4.

PTM databases

iPTMnetiQ8R1P4.

Expressioni

Gene expression databases

BgeeiQ8R1P4.
CleanExiMM_ATG10.

Interactioni

Subunit structurei

Interacts with MAP1LC3A. By interacting with MAP1LC3A, it plays a role in the conjugation of ATG12 to ATG5. Also able to directly interact either with ATG5 or ATG7.2 Publications

Protein-protein interaction databases

BioGridi211724. 3 interactions.
IntActiQ8R1P4. 3 interactions.
STRINGi10090.ENSMUSP00000022119.

Structurei

3D structure databases

ProteinModelPortaliQ8R1P4.
SMRiQ8R1P4. Positions 93-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATG10 family.Curated

Phylogenomic databases

eggNOGiKOG4741. Eukaryota.
ENOG4111W4Q. LUCA.
HOGENOMiHOG000034127.
HOVERGENiHBG080874.
InParanoidiQ8R1P4.
KOiK17888.
OrthoDBiEOG7K3TN4.
PhylomeDBiQ8R1P4.
TreeFamiTF314016.

Family and domain databases

InterProiIPR007135. Autophagy-rel_prot_3.
[Graphical view]
PfamiPF03987. Autophagy_act_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R1P4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDEFFGEKS FQHYCAEFIR HSQQIGDGWE WRTAKECSDG YMCKTQFRIK
60 70 80 90 100
NEASTPHVGT PASVLTCLPT EENLELPMDD SEVTRPAAVA EVIKHEYHVL
110 120 130 140 150
YSCSYQVPVL YFRASFLDGR PLALEDIWEG VHECYKPRLL QGPWDTITQQ
160 170 180 190 200
EHPILGQPFF VLHPCKTNEF MTAVLKNSQK INRNVNYITS WLSLVGPVVG
210
LNLPLSYAKA TSQSE
Length:215
Mass (Da):24,577
Last modified:June 1, 2002 - v1
Checksum:i8239CC22A8727B2C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421M → I in BAB30705 (PubMed:16141072).Curated
Sequence conflicti53 – 542AS → TL in BAC77060 (PubMed:12890687).Curated
Sequence conflicti53 – 542AS → TL in BAB30705 (PubMed:16141072).Curated
Sequence conflicti53 – 542AS → TL in BAC36756 (PubMed:16141072).Curated
Sequence conflicti58 – 614Missing in BAC77060 (PubMed:12890687).Curated
Sequence conflicti58 – 614Missing in BAB30705 (PubMed:16141072).Curated
Sequence conflicti58 – 614Missing in BAC36756 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091691 mRNA. Translation: BAC55163.1.
AB079383 mRNA. Translation: BAC77060.1.
AK017355 mRNA. Translation: BAB30705.1.
AK077333 mRNA. Translation: BAC36756.1.
BC023455 mRNA. Translation: AAH23455.1.
RefSeqiNP_080046.3. NM_025770.3.
XP_006517389.1. XM_006517326.2.
UniGeneiMm.235385.

Genome annotation databases

GeneIDi66795.
KEGGimmu:66795.
UCSCiuc007rjr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091691 mRNA. Translation: BAC55163.1.
AB079383 mRNA. Translation: BAC77060.1.
AK017355 mRNA. Translation: BAB30705.1.
AK077333 mRNA. Translation: BAC36756.1.
BC023455 mRNA. Translation: AAH23455.1.
RefSeqiNP_080046.3. NM_025770.3.
XP_006517389.1. XM_006517326.2.
UniGeneiMm.235385.

3D structure databases

ProteinModelPortaliQ8R1P4.
SMRiQ8R1P4. Positions 93-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211724. 3 interactions.
IntActiQ8R1P4. 3 interactions.
STRINGi10090.ENSMUSP00000022119.

PTM databases

iPTMnetiQ8R1P4.

Proteomic databases

MaxQBiQ8R1P4.
PaxDbiQ8R1P4.
PRIDEiQ8R1P4.

Protocols and materials databases

DNASUi66795.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi66795.
KEGGimmu:66795.
UCSCiuc007rjr.1. mouse.

Organism-specific databases

CTDi83734.
MGIiMGI:1914045. Atg10.

Phylogenomic databases

eggNOGiKOG4741. Eukaryota.
ENOG4111W4Q. LUCA.
HOGENOMiHOG000034127.
HOVERGENiHBG080874.
InParanoidiQ8R1P4.
KOiK17888.
OrthoDBiEOG7K3TN4.
PhylomeDBiQ8R1P4.
TreeFamiTF314016.

Enzyme and pathway databases

ReactomeiR-MMU-1632852. Macroautophagy.

Miscellaneous databases

PROiQ8R1P4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R1P4.
CleanExiMM_ATG10.

Family and domain databases

InterProiIPR007135. Autophagy-rel_prot_3.
[Graphical view]
PfamiPF03987. Autophagy_act_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ATG12; ATG5 AND ATG7, MUTAGENESIS OF CYS-165.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ATG12 AND MAP1LC3A, MUTAGENESIS OF CYS-165.
    Tissue: Brain.
  3. "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: Head and Pituitary.
  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].
    Strain: FVB/N.
    Tissue: Mammary cancer.
  5. "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, MUTAGENESIS OF CYS-165.
  6. "Human adenovirus type 5 induces cell lysis through autophagy and autophagy-triggered caspase activity."
    Jiang H., White E.J., Rios-Vicil C.I., Xu J., Gomez-Manzano C., Fueyo J.
    J. Virol. 85:4720-4729(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiATG10_MOUSE
AccessioniPrimary (citable) accession number: Q8R1P4
Secondary accession number(s): Q8BPA9, Q9D3J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 100 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

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.