PLIN5_MOUSE - dbPTM
PLIN5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLIN5_MOUSE
UniProt AC Q8BVZ1
Protein Name Perilipin-5
Gene Name Plin5
Organism Mus musculus (Mouse).
Sequence Length 463
Subcellular Localization Lipid droplet . Cytoplasm . Mitochondrion . Lipid droplet surface-associated (PubMed:17234449, PubMed:17130488, PubMed:16571721). Exchanges between lipid droplets and the cytoplasm (PubMed:19717842).
Protein Description Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE..
Protein Sequence MDQRGEDTTLAPHSRMSGDQTAQDPGSSLGELDQQNVVNRVVALPLVKATCTAVSSAYNSAKDRHPLLGSACRLAEHCVCSVTTCALDHAQPLLEHLQPQLATVNDLACRGLDKLEEKLPFLQQPSDMVVTSAKDTVAKSVTGMVDLAQRGRRWSGELRRSMSQAMDMVLGKSEKLVDRFLPMTEAELAVLAAEAEGPEVGTVEEQRQQQGYFVRLGSLSARLRHLAYEHSLGKLRQSKHRTQEMLAQLQETLELIQHMQRGASPSPTFHPPKTQELWGSWSPCLENGRSHSEVELETLALSRSLTLELQNAVDALAGCVRGLPPSAQAKVAEVQRSVDALQATFADAHCLGDVAPTALAEGRGSVARAHACVDEFLDLVLRAMPLPWLVGPFAPILVEQSEPLINLATCVDEVVGDPDPRWAHMDWPAQKRAWEAESADPGGQEAEPPRGQGKHTMMPELDF
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
17PhosphorylationLAPHSRMSGDQTAQD
CCCCCCCCCCCCCCC		37.8027742792
21PhosphorylationSRMSGDQTAQDPGSS
CCCCCCCCCCCCCCC		30.9021082442
51S-nitrosocysteineLPLVKATCTAVSSAY
HHHHHHHHHHHHHHH		2.48-
51S-nitrosylationLPLVKATCTAVSSAY
HHHHHHHHHHHHHHH		2.4821278135
70PhosphorylationDRHPLLGSACRLAEH
CCCCCHHHHHHHHHH		24.9429472430
118UbiquitinationGLDKLEEKLPFLQQP
CHHHHHHHCCCCCCC		52.6822790023
139UbiquitinationSAKDTVAKSVTGMVD
CCHHHHHHHHHCHHH		40.9122790023
155PhosphorylationAQRGRRWSGELRRSM
HHHCHHHCHHHHHHH		22.1523737553
161PhosphorylationWSGELRRSMSQAMDM
HCHHHHHHHHHHHHH		19.1522324799
162OxidationSGELRRSMSQAMDMV
CHHHHHHHHHHHHHH		3.0617242355
163PhosphorylationGELRRSMSQAMDMVL
HHHHHHHHHHHHHHH		18.9425521595
168OxidationSMSQAMDMVLGKSEK
HHHHHHHHHHCCHHH		1.4017242355
172UbiquitinationAMDMVLGKSEKLVDR
HHHHHHCCHHHHHHH		51.8122790023
173PhosphorylationMDMVLGKSEKLVDRF
HHHHHCCHHHHHHHH		37.8628059163
203UbiquitinationEGPEVGTVEEQRQQQ
CCCCCCCHHHHHHHC		6.6627667366
218PhosphorylationGYFVRLGSLSARLRH
CCEEEHHHHHHHHHH		24.6022942356
220PhosphorylationFVRLGSLSARLRHLA
EEEHHHHHHHHHHHH		17.0322817900
234UbiquitinationAYEHSLGKLRQSKHR
HHHCHHHHHHHCHHH		45.8722790023
264PhosphorylationQHMQRGASPSPTFHP
HHHHCCCCCCCCCCC		28.8327742792
266PhosphorylationMQRGASPSPTFHPPK
HHCCCCCCCCCCCCC		33.7925521595
268PhosphorylationRGASPSPTFHPPKTQ
CCCCCCCCCCCCCHH		38.6227742792
273UbiquitinationSPTFHPPKTQELWGS
CCCCCCCCHHHHHCC		68.2622790023
280PhosphorylationKTQELWGSWSPCLEN
CHHHHHCCCCHHHHC		16.8823984901
282PhosphorylationQELWGSWSPCLENGR
HHHHCCCCHHHHCCC		13.8723984901
284S-palmitoylationLWGSWSPCLENGRSH
HHCCCCHHHHCCCCC		6.5928526873
290PhosphorylationPCLENGRSHSEVELE
HHHHCCCCCCCHHHH		32.5327742792
292PhosphorylationLENGRSHSEVELETL
HHCCCCCCCHHHHHH		44.5825521595
298PhosphorylationHSEVELETLALSRSL
CCCHHHHHHHHHHHH		29.9223984901
319S-palmitoylationAVDALAGCVRGLPPS
HHHHHHHHHHCCCHH		1.2428526873
329UbiquitinationGLPPSAQAKVAEVQR
CCCHHHHHHHHHHHH		14.1727667366
330UbiquitinationLPPSAQAKVAEVQRS
CCHHHHHHHHHHHHH		29.8722790023
337PhosphorylationKVAEVQRSVDALQAT
HHHHHHHHHHHHHHH		13.78-
454UbiquitinationEPPRGQGKHTMMPEL
CCCCCCCCCCCCCCC		28.1922790023
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
155SPhosphorylationKinasePKACAP05132
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLIN5_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 PLIN5_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLPL2_MOUSEPnpla2physical
21148142
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLIN5_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-292, ANDMASS SPECTROMETRY.

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