PLPL2_MOUSE - dbPTM
PLPL2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLPL2_MOUSE
UniProt AC Q8BJ56
Protein Name Patatin-like phospholipase domain-containing protein 2
Gene Name Pnpla2
Organism Mus musculus (Mouse).
Sequence Length 486
Subcellular Localization Lipid droplet. Cell membrane
Single-pass type II membrane protein.
Protein Description Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. [PubMed: 15550674 Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion.]
Protein Sequence MFPRETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSFNLVKTIRGCLLKTLPADCHERANGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLRFLRRNGLLNQPNPLLALPPVVPQEEDAEEAAVVEERAGEEDQLQPYRKDRILEHLPARLNEALLEACVEPKDLMTTLSNMLPVRLATAMMVPYTLPLESAVSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGDHLPSRLSEQVELRRAQSLPSVPLSCATYSEALPNWVRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPDALRMRAPASPTAADPATPQDPPGLPPC
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
39N-linked_GlycosylationHAPFLVANATHIYGA
HCCEEEEECCEEECC
37.58-
87PhosphorylationFLGPLHPSFNLVKTI
HCCCCCCCHHHHHHH
18.93-
101PhosphorylationIRGCLLKTLPADCHE
HHHHHHHCCCCCHHH
37.63-
210PhosphorylationHELRVTNTSIQFNLR
EEEEECCCEEEEEHH
20.17-
224UbiquitinationRNLYRLSKALFPPEP
HHHHHHHHHHCCCCH
54.4222790023
295UbiquitinationDQLQPYRKDRILEHL
CCCCCHHHHHHHHHH
45.5822790023
372PhosphorylationIRWMKEQTGSICQYL
HHHHHHHHHCHHHHH
33.71-
374PhosphorylationWMKEQTGSICQYLVM
HHHHHHHCHHHHHHH
24.4722733971
378PhosphorylationQTGSICQYLVMRAKR
HHHCHHHHHHHHHHH
9.24-
393PhosphorylationKLGDHLPSRLSEQVE
HHCCCCCHHHHHHHH
52.81-
396PhosphorylationDHLPSRLSEQVELRR
CCCCHHHHHHHHHHH
25.5222733971
406PhosphorylationVELRRAQSLPSVPLS
HHHHHHHCCCCCCCC
41.0627087446
409PhosphorylationRRAQSLPSVPLSCAT
HHHHCCCCCCCCCCC
41.4821082442
413PhosphorylationSLPSVPLSCATYSEA
CCCCCCCCCCCHHHH
8.8125159016
416PhosphorylationSVPLSCATYSEALPN
CCCCCCCCHHHHCCH
31.7225159016
417PhosphorylationVPLSCATYSEALPNW
CCCCCCCHHHHCCHH
5.9825159016
418PhosphorylationPLSCATYSEALPNWV
CCCCCCHHHHCCHHH
16.4325159016
430PhosphorylationNWVRNNLSLGDALAK
HHHHCCCCHHHHHHH
32.2227742792
468PhosphorylationLRMRAPASPTAADPA
HHCCCCCCCCCCCCC
23.0225619855
470PhosphorylationMRAPASPTAADPATP
CCCCCCCCCCCCCCC
31.7925619855
476PhosphorylationPTAADPATPQDPPGL
CCCCCCCCCCCCCCC
27.2025619855

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
396SPhosphorylationKinasePKA-Uniprot
406SPhosphorylationKinaseAMPKA1Q13131
PSP
406SPhosphorylationKinasePRKAA1Q5EG47
GPS
406SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
406SPhosphorylation

21183079

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 PLPL2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLPL2_MOUSEPnpla2physical
19692632
PLIN5_MOUSEPlin5physical
21393244
G0S2_MOUSEG0s2physical
20197052
ABHD5_MOUSEAbhd5physical
24440819

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLPL2_MOUSE

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Related Literatures of Post-Translational Modification

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