ATG5_HUMAN - dbPTM
ATG5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG5_HUMAN
UniProt AC Q9H1Y0
Protein Name Autophagy protein 5
Gene Name ATG5
Organism Homo sapiens (Human).
Sequence Length 275
Subcellular Localization Cytoplasm . Preautophagosomal structure membrane
Peripheral membrane protein. Colocalizes with nonmuscle actin. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed (By similarity). Localizes also
Protein Description Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.; May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. Plays a crucial role in IFN-gamma-induced autophagic cell death by interacting with FADD.; (Microbial infection) May act as a proviral factor. In association with ATG12, negatively regulates the innate antiviral immune response by impairing the type I IFN production pathway upon vesicular stomatitis virus (VSV) infection. [PubMed: 17709747 Required for the translation of incoming hepatitis C virus (HCV) RNA and, thereby, for initiation of HCV replication, but not required once infection is established]
Protein Sequence MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKHFQKVMRQEDISEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHCPSKDAIEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLMEYPAEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLKEVCPSAIDPEDGEKKNQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIIPQPTD
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
1Acetylation-------MTDDKDVL
-------CCCHHHHH
9.2822814378
5Ubiquitination---MTDDKDVLRDVW
---CCCHHHHHHHHH
53.17-
35PhosphorylationTEREAEPYYLLLPRV
CCCCCCCEEEECCCC
9.7630576142
36PhosphorylationEREAEPYYLLLPRVS
CCCCCCEEEECCCCC
11.1121214269
49PhosphorylationVSYLTLVTDKVKKHF
CCHHHHCHHHHHHHH
32.9630576142
60 (in isoform 2)Ubiquitination-4.7621906983
75PhosphorylationIWFEYEGTPLKWHYP
HHCEECCCCCEECCC
17.32-
81PhosphorylationGTPLKWHYPIGLLFD
CCCCEECCCHHHHHH
8.74-
93 (in isoform 2)Ubiquitination-17.6421906983
101PhosphorylationSALPWNITVHFKSFP
CCCCCEEEEEECCCC
12.52-
138UbiquitinationEADALKHKSQVINEM
HHHHHHHHHHHHHHH
40.7821906983
138 (in isoform 1)Ubiquitination-40.7821906983
147UbiquitinationQVINEMQKKDHKQLW
HHHHHHHHHHHHHHH
59.88-
171UbiquitinationQFWAINRKLMEYPAE
HHHHHHHHHHCCCHH
47.932190698
171 (in isoform 1)Ubiquitination-47.9321906983
214PhosphorylationAADGQLHTLGDLLKE
CCCCCEEEHHHHHHH
40.8227307780
220UbiquitinationHTLGDLLKEVCPSAI
EEHHHHHHHHCCCCC
56.23-

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
101TPhosphorylationKinasePAK1Q13153
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATG5_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 ATG5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMDH2_HUMANIMPDH2physical
17353931
A16L1_HUMANATG16L1physical
20562859
TCPR1_HUMANTECPR1physical
20562859
ATG12_HUMANATG12physical
20562859
TKT_HUMANTKTphysical
20562859
SIR1_HUMANSIRT1physical
18296641
TCPR1_HUMANTECPR1physical
22342342
A16L1_HUMANATG16L1physical
22342342
ATG12_HUMANATG12physical
22342342
WDFY3_HUMANWDFY3physical
20417604
A16L1_HUMANATG16L1physical
22863883
CAV1_HUMANCAV1physical
24727585
FADD_HUMANFADDphysical
15778222
KEAP1_HUMANKEAP1physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
TEKT4_HUMANTEKT4physical
25416956
A16L1_HUMANATG16L1physical
23202584
A16L1_HUMANATG16L1physical
26344197
TCPR1_HUMANTECPR1physical
25484072
A16L1_HUMANATG16L1physical
25484072
SQSTM_HUMANSQSTM1physical
27879200
CACO2_HUMANCALCOCO2physical
27879200
OPTN_HUMANOPTNphysical
27879200

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 ATG5_HUMAN

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Related Literatures of Post-Translational Modification

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