ATG7_HUMAN - dbPTM
ATG7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG7_HUMAN
UniProt AC O95352
Protein Name Ubiquitin-like modifier-activating enzyme ATG7
Gene Name ATG7
Organism Homo sapiens (Human).
Sequence Length 703
Subcellular Localization Cytoplasm. Preautophagosomal structure. Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme..
Protein Description 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..
Protein Sequence MAAATGDPGLSKLQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDMSAPTPARCCPAIGTLYNTNTLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGLDQRFSLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVSLLKHYSDFFQGQRTKITIGVYDPCNLAQYPGWPLRNFLVLAAHRWSSSFQSVEVVCFRDRTMQGARDVAHSIIFEVKLPEMAFSPDCPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLGGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVNFSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPKQQGAGDLCPNHPVASADLLGSSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEREGFNFLAKVFNSSHSFLEDLTGLTLLHQETQAAEIWDMSDDETI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAATGDPG
------CCCCCCCCC		13.0522223895
5Phosphorylation---MAAATGDPGLSK
---CCCCCCCCCCCC		37.07-
11PhosphorylationATGDPGLSKLQFAPF
CCCCCCCCCCCCCCC		36.9220860994
38PhosphorylationTQKKLNEYRLDEAPK
HHHHHHHHCCCCCCC		18.53-
120PhosphorylationWESIKSGTALENPVL
HHHHHHCCCCCCHHH		34.8523911959
135PhosphorylationLNKFLLLTFADLKKY
HHHHHHHHHHHHHHH		19.4220068231
211PhosphorylationDENMVLVSLLKHYSD
CCCCHHHHHHHHHHH		24.6724719451
267AcetylationFQSVEVVCFRDRTMQ
CCCEEEEEECCCCCC		2.5319608861
292SulfoxidationFEVKLPEMAFSPDCP
EEEECCCCCCCCCCC		4.2721406390
300AcetylationAFSPDCPKAVGWEKN
CCCCCCCCCCCCCCC		63.1326051181
300UbiquitinationAFSPDCPKAVGWEKN
CCCCCCCCCCCCCCC		63.13-
306AcetylationPKAVGWEKNQKGGMG
CCCCCCCCCCCCCCC		59.1619608861
306UbiquitinationPKAVGWEKNQKGGMG
CCCCCCCCCCCCCCC		59.1619608861
309UbiquitinationVGWEKNQKGGMGPRM
CCCCCCCCCCCCCCC		67.82-
352UbiquitinationVPTLDLDKVVSVKCL
CCCCCHHHHHHHEEE		52.40-
401PhosphorylationNPVRQPLYEFEDCLG
CCCCCCCEEHHHHCC		25.8427642862
411UbiquitinationEDCLGGGKPKALAAA
HHHCCCCCHHHHHHH		46.77-
420MethylationKALAAADRLQKIFPG
HHHHHHHHHHHHCCC		34.00-
423UbiquitinationAAADRLQKIFPGVNA
HHHHHHHHHCCCCCC		51.40-
490PhosphorylationLPAVIAASKRKLVIN
HHHHHHHHCCHHHEE		24.7924260401
531PhosphorylationCPNHPVASADLLGSS
CCCCCCCCHHHHCCH		23.6627251275
618 (in isoform 3)Phosphorylation-26.6427251275
622 (in isoform 3)Phosphorylation-3.64-
645UbiquitinationPVSLAFDKCTACSSK
EEHHHCCCCCCCCHH		27.34-
652UbiquitinationKCTACSSKVLDQYER
CCCCCCHHHHHHHHH		30.44-
671PhosphorylationFLAKVFNSSHSFLED
HHHHHHCCCCCHHHH		20.2620068231
672PhosphorylationLAKVFNSSHSFLEDL
HHHHHCCCCCHHHHH		25.0120068231
674PhosphorylationKVFNSSHSFLEDLTG
HHHCCCCCHHHHHHC		33.2120068231
680PhosphorylationHSFLEDLTGLTLLHQ
CCHHHHHHCCCHHCC		42.3320068231
683PhosphorylationLEDLTGLTLLHQETQ
HHHHHCCCHHCCCCH		28.7220068231
689PhosphorylationLTLLHQETQAAEIWD
CCHHCCCCHHHHHHC		19.5520068231
698PhosphorylationAAEIWDMSDDETI--
HHHHHCCCCCCCC--		39.1622170151
702PhosphorylationWDMSDDETI------
HCCCCCCCC------		38.6920068231
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ATG7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATG7_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ATG7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATG3_HUMANATG3physical
11825910
GBRL2_HUMANGABARAPL2physical
20562859
GBRAP_HUMANGABARAPphysical
20562859
MLP3C_HUMANMAP1LC3Cphysical
20562859
GBRL1_HUMANGABARAPL1physical
20562859
ATG3_HUMANATG3physical
20562859
ATG12_HUMANATG12physical
11096062
SIR1_HUMANSIRT1physical
18296641
GBRL1_HUMANGABARAPL1physical
16704426
A4_HUMANAPPphysical
21832049
EP300_HUMANEP300physical
19124466
FOXO1_HUMANFOXO1physical
22622204
AN32E_HUMANANP32Ephysical
22863883
SRC8_HUMANCTTNphysical
22863883
ERF3A_HUMANGSPT1physical
22863883
ERF3B_HUMANGSPT2physical
22863883
TF2AA_HUMANGTF2A1physical
22863883
MAT2B_HUMANMAT2Bphysical
22863883
NASP_HUMANNASPphysical
22863883
PP2BB_HUMANPPP3CBphysical
22863883
RADI_HUMANRDXphysical
22863883
SYSC_HUMANSARSphysical
22863883
GLYM_HUMANSHMT2physical
22863883
SNX1_HUMANSNX1physical
22863883
SNX2_HUMANSNX2physical
22863883
SNX6_HUMANSNX6physical
22863883
STAT1_HUMANSTAT1physical
22863883
TBCD_HUMANTBCDphysical
22863883
UGDH_HUMANUGDHphysical
22863883
MLP3B_HUMANMAP1LC3Bphysical
15355958
MLP3A_HUMANMAP1LC3Aphysical
16303767
GBRL2_HUMANGABARAPL2physical
16303767
GBRAP_HUMANGABARAPphysical
16303767
ATG3_HUMANATG3physical
28514442
ATP23_HUMANXRCC6BP1physical
28514442
TXLNB_HUMANTXLNBphysical
28514442
RIPK1_HUMANRIPK1physical
28514442
MICU2_HUMANMICU2physical
28514442
ALR_HUMANGFERphysical
28514442
TRIP6_HUMANTRIP6physical
28514442
DNLZ_HUMANDNLZphysical
28514442
FKBP5_HUMANFKBP5physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATG7_HUMAN

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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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