ATG10_HUMAN
ID ATG10_HUMAN Reviewed; 220 AA.
AC Q9H0Y0; B2RE09; Q6PIX1; Q9H842;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ubiquitin-like-conjugating enzyme ATG10;
DE EC=2.3.2.-;
DE AltName: Full=Autophagy-related protein 10;
DE Short=APG10-like;
GN Name=ATG10; Synonyms=APG10L; ORFNames=PP12616;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-212
RP AND HIS-220.
RC TISSUE=Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=21367888; DOI=10.1128/jvi.02032-10;
RA Jiang H., White E.J., Rios-Vicil C.I., Xu J., Gomez-Manzano C., Fueyo J.;
RT "Human adenovirus type 5 induces cell lysis through autophagy and
RT autophagy-triggered caspase activity.";
RL J. Virol. 85:4720-4729(2011).
RN [6]
RP INTERACTION WITH IRGM.
RX PubMed=22174682; DOI=10.1371/journal.ppat.1002422;
RA Gregoire I.P., Richetta C., Meyniel-Schicklin L., Borel S., Pradezynski F.,
RA Diaz O., Deloire A., Azocar O., Baguet J., Le Breton M., Mangeot P.E.,
RA Navratil V., Joubert P.E., Flacher M., Vidalain P.O., Andre P., Lotteau V.,
RA Biard-Piechaczyk M., Rabourdin-Combe C., Faure M.;
RT "IRGM is a common target of RNA viruses that subvert the autophagy
RT network.";
RL PLoS Pathog. 7:E1002422-E1002422(2011).
CC -!- FUNCTION: E2-like enzyme involved in autophagy. Acts as an E2-like
CC enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12
CC conjugation to ATG5 is required for autophagy. Likely serves as an
CC ATG5-recognition molecule. Not involved in ATG12 conjugation to ATG3
CC (By similarity). Plays a role in adenovirus-mediated cell lysis.
CC {ECO:0000250, ECO:0000269|PubMed:21367888}.
CC -!- SUBUNIT: Interacts with MAP1LC3A. By interacting with MAP1LC3A, it
CC plays a role in the conjugation of ATG12 to ATG5. Also able to directly
CC interact either with ATG5 or ATG7 (By similarity). Interacts with IRGM.
CC {ECO:0000250, ECO:0000269|PubMed:22174682}.
CC -!- INTERACTION:
CC Q9H0Y0; Q9H1Y0: ATG5; NbExp=5; IntAct=EBI-1048913, EBI-1047414;
CC Q9H0Y0; P54253: ATXN1; NbExp=6; IntAct=EBI-1048913, EBI-930964;
CC Q9H0Y0; P55212: CASP6; NbExp=3; IntAct=EBI-1048913, EBI-718729;
CC Q9H0Y0; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-1048913, EBI-745535;
CC Q9H0Y0; P62879: GNB2; NbExp=3; IntAct=EBI-1048913, EBI-356942;
CC Q9H0Y0; O00291: HIP1; NbExp=3; IntAct=EBI-1048913, EBI-473886;
CC Q9H0Y0; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1048913, EBI-10975473;
CC Q9H0Y0; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1048913, EBI-21591415;
CC Q9H0Y0; O60260-5: PRKN; NbExp=3; IntAct=EBI-1048913, EBI-21251460;
CC Q9H0Y0; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-1048913, EBI-5280197;
CC Q9H0Y0; P62826: RAN; NbExp=3; IntAct=EBI-1048913, EBI-286642;
CC Q9H0Y0; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1048913, EBI-396669;
CC Q9H0Y0; P37840: SNCA; NbExp=3; IntAct=EBI-1048913, EBI-985879;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0Y0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0Y0-2; Sequence=VSP_013272, VSP_013273;
CC -!- SIMILARITY: Belongs to the ATG10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC004551; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BC027718; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF318326; AAL55833.1; -; mRNA.
DR EMBL; AK024016; BAB14778.1; -; mRNA.
DR EMBL; AK315752; BAG38106.1; -; mRNA.
DR EMBL; AL136912; CAB66846.1; -; mRNA.
DR EMBL; BC004551; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC027718; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC029268; AAH29268.1; -; mRNA.
DR CCDS; CCDS4057.1; -. [Q9H0Y0-1]
DR RefSeq; NP_001124500.1; NM_001131028.1. [Q9H0Y0-1]
DR RefSeq; NP_113670.1; NM_031482.4. [Q9H0Y0-1]
DR RefSeq; XP_005248667.1; XM_005248610.4. [Q9H0Y0-1]
DR RefSeq; XP_005248668.1; XM_005248611.4. [Q9H0Y0-1]
DR AlphaFoldDB; Q9H0Y0; -.
DR SMR; Q9H0Y0; -.
DR BioGRID; 123745; 212.
DR IntAct; Q9H0Y0; 29.
DR STRING; 9606.ENSP00000282185; -.
DR iPTMnet; Q9H0Y0; -.
DR PhosphoSitePlus; Q9H0Y0; -.
DR BioMuta; ATG10; -.
DR DMDM; 62286633; -.
DR EPD; Q9H0Y0; -.
DR MassIVE; Q9H0Y0; -.
DR MaxQB; Q9H0Y0; -.
DR PaxDb; Q9H0Y0; -.
DR PeptideAtlas; Q9H0Y0; -.
DR PRIDE; Q9H0Y0; -.
DR ProteomicsDB; 80344; -. [Q9H0Y0-1]
DR ProteomicsDB; 80345; -. [Q9H0Y0-2]
DR Antibodypedia; 24713; 394 antibodies from 33 providers.
DR DNASU; 83734; -.
DR Ensembl; ENST00000282185.8; ENSP00000282185.3; ENSG00000152348.16. [Q9H0Y0-1]
DR Ensembl; ENST00000355178.8; ENSP00000347309.4; ENSG00000152348.16. [Q9H0Y0-2]
DR Ensembl; ENST00000458350.7; ENSP00000404938.3; ENSG00000152348.16. [Q9H0Y0-1]
DR Ensembl; ENST00000513443.5; ENSP00000425182.1; ENSG00000152348.16. [Q9H0Y0-2]
DR GeneID; 83734; -.
DR KEGG; hsa:83734; -.
DR MANE-Select; ENST00000282185.8; ENSP00000282185.3; NM_031482.5; NP_113670.1.
DR UCSC; uc003khq.2; human. [Q9H0Y0-1]
DR CTD; 83734; -.
DR DisGeNET; 83734; -.
DR GeneCards; ATG10; -.
DR HGNC; HGNC:20315; ATG10.
DR HPA; ENSG00000152348; Low tissue specificity.
DR MIM; 610800; gene.
DR neXtProt; NX_Q9H0Y0; -.
DR OpenTargets; ENSG00000152348; -.
DR PharmGKB; PA134872167; -.
DR VEuPathDB; HostDB:ENSG00000152348; -.
DR eggNOG; KOG4741; Eukaryota.
DR GeneTree; ENSGT00390000000924; -.
DR HOGENOM; CLU_1991882_0_0_1; -.
DR InParanoid; Q9H0Y0; -.
DR OMA; YSCSHQV; -.
DR OrthoDB; 1538225at2759; -.
DR PhylomeDB; Q9H0Y0; -.
DR TreeFam; TF314016; -.
DR PathwayCommons; Q9H0Y0; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR SignaLink; Q9H0Y0; -.
DR SIGNOR; Q9H0Y0; -.
DR BioGRID-ORCS; 83734; 27 hits in 1085 CRISPR screens.
DR ChiTaRS; ATG10; human.
DR GeneWiki; ATG10; -.
DR GenomeRNAi; 83734; -.
DR Pharos; Q9H0Y0; Tbio.
DR PRO; PR:Q9H0Y0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H0Y0; protein.
DR Bgee; ENSG00000152348; Expressed in islet of Langerhans and 149 other tissues.
DR ExpressionAtlas; Q9H0Y0; baseline and differential.
DR Genevisible; Q9H0Y0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019777; F:Atg12 transferase activity; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0006983; P:ER overload response; IMP:BHF-UCL.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0031401; P:positive regulation of protein modification process; ISS:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; ISS:UniProtKB.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007135; Atg3/Atg10.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; Protein transport;
KW Reference proteome; Transferase; Transport; Ubl conjugation pathway.
FT CHAIN 1..220
FT /note="Ubiquitin-like-conjugating enzyme ATG10"
FT /id="PRO_0000096183"
FT ACT_SITE 166
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 73..125
FT /note="EAFELPLDDCEVIETAAASEVIKYEYHVLYSCSYQVPVLYFRASFLDGRPLT
FT L -> VKSCSVTQAGVQLRDLSSLQPPPSGFKQFSCLSLPSNWDYRGSPLHLANFLYF
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_013272"
FT VAR_SEQ 126..220
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_013273"
FT VARIANT 62
FT /note="S -> P (in dbSNP:rs3734114)"
FT /id="VAR_024370"
FT VARIANT 212
FT /note="T -> M (in dbSNP:rs1864183)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_021562"
FT VARIANT 220
FT /note="P -> H (in dbSNP:rs1864182)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_021563"
SQ SEQUENCE 220 AA; 25279 MW; 1EDA80E385779B69 CRC64;
MEEDEFIGEK TFQRYCAEFI KHSQQIGDSW EWRPSKDCSD GYMCKIHFQI KNGSVMSHLG
ASTHGQTCLP MEEAFELPLD DCEVIETAAA SEVIKYEYHV LYSCSYQVPV LYFRASFLDG
RPLTLKDIWE GVHECYKMRL LQGPWDTITQ QEHPILGQPF FVLHPCKTNE FMTPVLKNSQ
KINKNVNYIT SWLSIVGPVV GLNLPLSYAK ATSQDERNVP
