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O95352 (ATG7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-like modifier-activating enzyme ATG7
Alternative name(s):
ATG12-activating enzyme E1 ATG7
Autophagy-related protein 7
Short name=APG7-like
Short name=hAGP7
Ubiquitin-activating enzyme E1-like protein
Gene names
Name:ATG7
Synonyms:APG7L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length703 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Ref.6 Ref.9 Ref.15

Subunit structure

Homodimer. Interacts with ATG3 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. Forms intermediate conjugates with ATG8-like proteins such as GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A. Interacts with EP300 acetyltransferase. Ref.6 Ref.8 Ref.9 Ref.11

Subcellular location

Cytoplasm By similarity. Preautophagosomal structure By similarity. Note: Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme By similarity.

Tissue specificity

Widely expressed, especially in kidney, liver, lymph nodes and bone marrow. Ref.7

Induction

Expression is up-regulated by the transcription factor HSF1. Ref.17

Domain

The C-terminal part of the protein is essential for the dimerization and interaction with ATG3 and ATG12 By similarity.

The N-terminal FAP motif (residues 15 to 17) is essential for the formation of the ATG89-PE and ATG5-ATG12 conjugates (Ref.15).

Post-translational modification

Acetylated by EP300. Ref.11

Sequence similarities

Belongs to the ATG7 family.

Ontologies

Keywords
   Biological processAutophagy
Protein transport
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from electronic annotation. Source: Ensembl

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

cellular amino acid metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular protein modification process

Traceable author statement Ref.1. Source: ProtInc

central nervous system neuron axonogenesis

Inferred from electronic annotation. Source: Ensembl

cerebellar Purkinje cell layer development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

membrane fusion

Traceable author statement Ref.1. Source: ProtInc

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

neurological system process

Inferred from electronic annotation. Source: Ensembl

organelle organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of macroautophagy

Inferred from mutant phenotype PubMed 22354037. Source: BHF-UCL

positive regulation of protein modification process

Inferred from direct assay PubMed 12890687. Source: MGI

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein lipidation

Inferred from direct assay PubMed 12890687. Source: MGI

protein modification by small protein conjugation

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

pyramidal neuron development

Inferred from electronic annotation. Source: Ensembl

regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxoneme

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Traceable author statement. Source: ProtInc

pre-autophagosomal structure

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionAtg12 activating enzyme activity

Inferred from sequence or structural similarity PubMed 20723759. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6Ref.8. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.6. Source: UniProtKB

ubiquitin activating enzyme activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95352-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O95352-2)

The sequence of this isoform differs from the canonical sequence as follows:
     626-652: Missing.
Isoform 3 (identifier: O95352-3)

The sequence of this isoform differs from the canonical sequence as follows:
     138-176: Missing.
     653-693: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 703702Ubiquitin-like modifier-activating enzyme ATG7
PRO_0000212806

Regions

Motif15 – 173FAP motif

Sites

Active site5721Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.16

Natural variations

Alternative sequence138 – 17639Missing in isoform 3.
VSP_045206
Alternative sequence626 – 65227Missing in isoform 2.
VSP_013205
Alternative sequence653 – 69341Missing in isoform 3.
VSP_045207
Natural variant4711V → A.
Corresponds to variant rs36117895 [ dbSNP | Ensembl ].
VAR_053014

Experimental info

Mutagenesis151F → D: Impairs conjugation activity; when associated with D-16 and D-17. Ref.15
Mutagenesis161A → D: Impairs conjugation activity; when associated with D-15 and D-17. Ref.15
Mutagenesis171P → D: Impairs conjugation activity; when associated with D-15 and D-16. Ref.15
Sequence conflict2101V → A in BAG64682. Ref.2
Sequence conflict3461P → L in BAG64682. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: ABBD1A29A6C58356

FASTA70377,960
        10         20         30         40         50         60 
MAAATGDPGL SKLQFAPFSS ALDVGFWHEL TQKKLNEYRL DEAPKDIKGY YYNGDSAGLP 

        70         80         90        100        110        120 
ARLTLEFSAF DMSAPTPARC CPAIGTLYNT NTLESFKTAD KKLLLEQAAN EIWESIKSGT 

       130        140        150        160        170        180 
ALENPVLLNK FLLLTFADLK KYHFYYWFCY PALCLPESLP LIQGPVGLDQ RFSLKQIEAL 

       190        200        210        220        230        240 
ECAYDNLCQT EGVTALPYFL IKYDENMVLV SLLKHYSDFF QGQRTKITIG VYDPCNLAQY 

       250        260        270        280        290        300 
PGWPLRNFLV LAAHRWSSSF QSVEVVCFRD RTMQGARDVA HSIIFEVKLP EMAFSPDCPK 

       310        320        330        340        350        360 
AVGWEKNQKG GMGPRMVNLS ECMDPKRLAE SSVDLNLKLM CWRLVPTLDL DKVVSVKCLL 

       370        380        390        400        410        420 
LGAGTLGCNV ARTLMGWGVR HITFVDNAKI SYSNPVRQPL YEFEDCLGGG KPKALAAADR 

       430        440        450        460        470        480 
LQKIFPGVNA RGFNMSIPMP GHPVNFSSVT LEQARRDVEQ LEQLIESHDV VFLLMDTRES 

       490        500        510        520        530        540 
RWLPAVIAAS KRKLVINAAL GFDTFVVMRH GLKKPKQQGA GDLCPNHPVA SADLLGSSLF 

       550        560        570        580        590        600 
ANIPGYKLGC YFCNDVVAPG DSTRDRTLDQ QCTVSRPGLA VIAGALAVEL MVSVLQHPEG 

       610        620        630        640        650        660 
GYAIASSSDD RMNEPPTSLG LVPHQIRGFL SRFDNVLPVS LAFDKCTACS SKVLDQYERE 

       670        680        690        700 
GFNFLAKVFN SSHSFLEDLT GLTLLHQETQ AAEIWDMSDD ETI 

« Hide

Isoform 2 [UniParc].

Checksum: 184E1A7A3B989524
Show »

FASTA67675,002
Isoform 3 [UniParc].

Checksum: 2186C29D24B11D6E
Show »

FASTA62368,618

References

« Hide 'large scale' references
[1]"Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein."
Yuan W., Stromhaug P.E., Dunn W.A. Jr.
Mol. Biol. Cell 10:1353-1366(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Kidney.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 2).
Tissue: Placenta.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-703 (ISOFORM 1).
Tissue: Testis.
[6]"The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3."
Tanida I., Tanida-Miyake E., Ueno T., Kominami E.
J. Biol. Chem. 276:1701-1706(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH ATG12; GABARAP; GABARAPL2 AND MAP1LC3A.
[7]"Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs."
Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H., Ueno T., Kominami E.
Biochem. Biophys. Res. Commun. 292:256-262(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p."
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.
J. Biol. Chem. 277:13739-13744(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG3 AND ATG12.
Tissue: Brain.
[9]"Phosphatidylserine in addition to phosphatidylethanolamine is an in vitro target of the mammalian Atg8 modifiers, LC3, GABARAP, and GATE-16."
Sou Y.S., Tanida I., Komatsu M., Ueno T., Kominami E.
J. Biol. Chem. 281:3017-3024(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GABARAP; GABARAPL2 AND MAP1LC3A.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Regulation of autophagy by the p300 acetyltransferase."
Lee I.H., Finkel T.
J. Biol. Chem. 284:6322-6328(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION, INTERACTION WITH EP300.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is essential for the E2-substrate reaction of LC3 lipidation."
Tanida I., Yamasaki M., Komatsu M., Ueno T.
Autophagy 8:88-97(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF PHE-15; ALA-16 AND PRO-17.
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Heat shock factor 1 (HSF1) controls chemoresistance and autophagy through transcriptional regulation of autophagy-related protein 7 (ATG7)."
Desai S., Liu Z., Yao J., Patel N., Chen J., Wu Y., Ahn E.E., Fodstad O., Tan M.
J. Biol. Chem. 288:9165-9176(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF094516 mRNA. Translation: AAC69630.1.
AK303694 mRNA. Translation: BAG64682.1.
AC020750 Genomic DNA. No translation available.
AC022001 Genomic DNA. No translation available.
AC026185 Genomic DNA. No translation available.
AC083855 Genomic DNA. No translation available.
BC000091 mRNA. Translation: AAH00091.1.
AL122075 mRNA. Translation: CAB59250.1.
CCDSCCDS2605.1. [O95352-1]
CCDS46752.1. [O95352-2]
CCDS46753.1. [O95352-3]
PIRT34556.
RefSeqNP_001129503.2. NM_001136031.2. [O95352-2]
NP_001138384.1. NM_001144912.1. [O95352-3]
NP_006386.1. NM_006395.2. [O95352-1]
UniGeneHs.38032.

3D structure databases

ProteinModelPortalO95352.
SMRO95352. Positions 13-690.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115787. 43 interactions.
DIPDIP-29759N.
IntActO95352. 14 interactions.
STRING9606.ENSP00000346437.

Chemistry

ChEMBLCHEMBL2321621.

PTM databases

PhosphoSiteO95352.

Proteomic databases

MaxQBO95352.
PaxDbO95352.
PRIDEO95352.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354449; ENSP00000346437; ENSG00000197548. [O95352-1]
ENST00000354956; ENSP00000347042; ENSG00000197548. [O95352-2]
ENST00000446450; ENSP00000412580; ENSG00000197548. [O95352-3]
GeneID10533.
KEGGhsa:10533.
UCSCuc003bwc.3. human. [O95352-1]
uc003bwd.3. human. [O95352-2]

Organism-specific databases

CTD10533.
GeneCardsGC03P011313.
HGNCHGNC:16935. ATG7.
HPACAB018771.
HPA007639.
MIM608760. gene.
neXtProtNX_O95352.
PharmGKBPA134983397.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000162379.
HOVERGENHBG080877.
InParanoidO95352.
KOK08337.
OMALGCQVAR.
OrthoDBEOG7X0VGG.
PhylomeDBO95352.
TreeFamTF105689.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO95352.
BgeeO95352.
CleanExHS_ATG7.
GenevestigatorO95352.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR006285. Atg7.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PANTHERPTHR10953:SF3. PTHR10953:SF3. 1 hit.
PfamPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 2 hits.
TIGRFAMsTIGR01381. E1_like_apg7. 1 hit.
ProtoNetSearch...

Other

GeneWikiATG7.
GenomeRNAi10533.
NextBio39961.
PROO95352.
SOURCESearch...

Entry information

Entry nameATG7_HUMAN
AccessionPrimary (citable) accession number: O95352
Secondary accession number(s): B4E170 expand/collapse secondary AC list , E9PB95, Q7L8L0, Q9BWP2, Q9UFH4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM