ATG5_MOUSE - dbPTM
ATG5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG5_MOUSE
UniProt AC Q99J83
Protein Name Autophagy protein 5
Gene Name Atg5
Organism Mus musculus (Mouse).
Sequence Length 275
Subcellular Localization Cytoplasm . Preautophagosomal structure membrane
Peripheral membrane protein . The conjugate detaches from the membrane immediately before or after autophagosome formation is completed. Localizes also to discrete punctae along the ciliary axoneme a
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 (By similarity).; (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..
Protein Sequence MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKHFQKVMRQEDVSEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHCPSKDAVEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLMEYPPEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLREVCPSAVAPEDGEKRSQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIVPQPTD
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
9.28-
44PhosphorylationLLLPRVSYLTLVTDK
EECCCCCHHHHCHHH
10.80-
75PhosphorylationIWFEYEGTPLKWHYP
HHCEECCCCCEECCC
17.32-
138UbiquitinationEADALKHKSQVINEM
HHHHHHHHHHHHHHH
40.7822790023

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
75TPhosphorylationKinaseMAPK14Q16539
GPS
75TPhosphorylationKinaseP38AP47811
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATG5_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CASP8_MOUSECasp8physical
22362782
FADD_MOUSEFaddphysical
22362782
A16L1_MOUSEAtg16l1physical
12665549
CASP8_MOUSECasp8physical
18946037
RIPK1_MOUSERipk1physical
18946037
FADD_MOUSEFaddphysical
18946037
MLP3A_MOUSEMap1lc3aphysical
18946037

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATG5_MOUSE

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Related Literatures of Post-Translational Modification

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