Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ubiquitin-like modifier-activating enzyme ATG7  

UniProtKB / Swiss-Prot ID :  ATG7_HUMAN

Gene Name (Synonyms) : 
ATG7, APG7L  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (Probable). 

Protein Function :  Functions as an E1 enzyme essential for multisubstrates such as ATG8-like proteins and ATG12. Forms intermediate conjugates with ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). PE-conjugation to ATG8-like proteins is essential for autophagy. Also acts as an E1 enzyme for ATG12 conjugation to ATG5 and ATG3 (By similarity). 

Protein Sequence MAAATGDPGLSKLQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAF...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHCCCCCCCEEEEEEECCCCCCCCCEEEEEECCC...
Protein Variant
LocationDescription
471V -> A (in dbSNP:rs36117895). VAR_053014
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAATG
---CCCCCC
13.05UniProtKB
Link-
306N6-acetyllysineVGWEKNQKG
EEEEECCCC
59.16HPRD
Link-
306N6-acetyllysineVGWEKNQKG
EEEEECCCC
59.16Phosphositeplus
Link-
306N6-acetyllysine.VGWEKNQKG
EEEEECCCC
59.16UniProtKB
Link-
698PhosphoserineIWDMSDDET
HCCCCCCCC
39.16HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ATG12_HUMANin vivo
yeast 2-hybrid
HPRD:12293HPRD12482611
11890701
GBRAP_HUMANin vitro
in vivo
HPRD:12293HPRD11890701
16303767
ATG12_HUMANENSP00000346437STRING
ATG3_HUMANENSP00000346437STRING
GBRAP_HUMANENSP00000346437STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-306, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures