PLIN1_MOUSE - dbPTM
PLIN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLIN1_MOUSE
UniProt AC Q8CGN5
Protein Name Perilipin-1
Gene Name Plin1
Organism Mus musculus (Mouse).
Sequence Length 517
Subcellular Localization Endoplasmic reticulum . Lipid droplet . Lipid droplet surface-associated.
Protein Description Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness (By similarity). Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels..
Protein Sequence MSMNKGPTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYNSTKEAHPLVASVCNAYEKGVQGASNLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKGTISTRLRSARNSISVPIASTSDKVLGATLAGCELALGMAKETAEYAANTRVGRLASGGADLALGSIEKVVEFLLPPDKESAPSSGRQRTQKAPKAKPSLVRRVSTLANTLSRHTMQTTAWALKQGHSLAMWIPGVAPLSSLAQWGASAAMQVVSRRQSEVRVPWLHNLAASQDESHDDQTDTEGEETDDEEEEEESEAEENVLREVTALPNPRGLLGGVVHTVQNTLRNTISAVTWAPAAVLGTVGRILHLTPAQAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFRDIDNPSAEAERKGSGARPASPESTPRPGQPRGSLRSVRGLSAPSCPGLDDKTEASARPGFLAMPREKPARRVSDSFFRPSVMEPILGRAQYSQLRKKS
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
53PhosphorylationEAHPLVASVCNAYEK
CHHHHHHHHHHHHHH		21.52-
66PhosphorylationEKGVQGASNLAAWSM
HHHCCCHHHHHHHHH		38.9228285833
72PhosphorylationASNLAAWSMEPVVRR
HHHHHHHHHHHHHHH		14.4527717184
81PhosphorylationEPVVRRLSTQFTAAN
HHHHHHHHHHHHHHH		20.5319921680
82PhosphorylationPVVRRLSTQFTAANE
HHHHHHHHHHHHHHH		32.0926643407
85PhosphorylationRRLSTQFTAANELAC
HHHHHHHHHHHHHHH		18.2926643407
114PhosphorylationYPPEKIASELKGTIS
CCHHHHHHHHCCHHH		47.1122817900
126PhosphorylationTISTRLRSARNSISV
HHHHHHHHHHCCCCC		35.8527742792
130PhosphorylationRLRSARNSISVPIAS
HHHHHHCCCCCEEEC		15.6427742792
132PhosphorylationRSARNSISVPIASTS
HHHHCCCCCEEECCC		22.9727742792
137PhosphorylationSISVPIASTSDKVLG
CCCCEEECCCCHHHH		29.2122817900
138PhosphorylationISVPIASTSDKVLGA
CCCEEECCCCHHHHH		31.7421082442
139PhosphorylationSVPIASTSDKVLGAT
CCEEECCCCHHHHHH		32.7021082442
146PhosphorylationSDKVLGATLAGCELA
CCHHHHHHHHHHHHH		18.4921082442
174PhosphorylationTRVGRLASGGADLAL
CCHHHHHHCCCCCCC		42.2123926118
183PhosphorylationGADLALGSIEKVVEF
CCCCCCCCHHHHHHH		28.5526060331
202PhosphorylationDKESAPSSGRQRTQK
CCCCCCCCCCCCCCC		36.6222817900
222PhosphorylationPSLVRRVSTLANTLS
HHHHHHHHHHHHHHH		18.8519921680
223PhosphorylationSLVRRVSTLANTLSR
HHHHHHHHHHHHHHH		27.3426745281
227PhosphorylationRVSTLANTLSRHTMQ
HHHHHHHHHHHHHHH		22.0926745281
229PhosphorylationSTLANTLSRHTMQTT
HHHHHHHHHHHHHHH		21.7026745281
245PhosphorylationWALKQGHSLAMWIPG
HHHHCCCCEEEEECC		25.3430635358
257PhosphorylationIPGVAPLSSLAQWGA
ECCCCCHHHHHHHHH		23.4230635358
258PhosphorylationPGVAPLSSLAQWGAS
CCCCCHHHHHHHHHH		35.0930635358
265PhosphorylationSLAQWGASAAMQVVS
HHHHHHHHHHHHHHH		16.7830635358
276PhosphorylationQVVSRRQSEVRVPWL
HHHHHCCCCCCCCHH		35.9323737553
289PhosphorylationWLHNLAASQDESHDD
HHHHHHCCCCCCCCC		32.3426525534
293PhosphorylationLAASQDESHDDQTDT
HHCCCCCCCCCCCCC		40.2726525534
298PhosphorylationDESHDDQTDTEGEET
CCCCCCCCCCCCCCC		52.4626525534
300PhosphorylationSHDDQTDTEGEETDD
CCCCCCCCCCCCCCC		49.6426525534
305PhosphorylationTDTEGEETDDEEEEE
CCCCCCCCCCHHHHH		44.4426525534
314PhosphorylationDEEEEEESEAEENVL
CHHHHHHHHHHHHHH		45.4426525534
325 (in isoform 3)Phosphorylation-20.0923684622
327 (in isoform 3)Phosphorylation-2.8427681418
329 (in isoform 3)Phosphorylation-39.4923684622
334 (in isoform 3)Phosphorylation-6.6323684622
348PhosphorylationVQNTLRNTISAVTWA
HHHHHHHHHHHHHHH		15.18-
379UbiquitinationAQAVSSTKGRAMSLS
HHHHHCCCCCCCCHH		48.6322790023
384PhosphorylationSTKGRAMSLSDALKG
CCCCCCCCHHHHHCC		24.6027742792
386PhosphorylationKGRAMSLSDALKGVT
CCCCCCHHHHHCCCC		17.3327742792
399PhosphorylationVTDNVVDTVVHYVPL
CCCCCCCHHHHCCCC		16.9026060331
403PhosphorylationVVDTVVHYVPLPRLS
CCCHHHHCCCCCCCC		7.6726060331
410PhosphorylationYVPLPRLSLMEPESE
CCCCCCCCCCCCHHH		27.2727742792
416PhosphorylationLSLMEPESEFRDIDN
CCCCCCHHHHCCCCC		53.3926060331
425PhosphorylationFRDIDNPSAEAERKG
HCCCCCCCHHHHHCC		45.0226643407
431AcetylationPSAEAERKGSGARPA
CCHHHHHCCCCCCCC		49.27-
433PhosphorylationAEAERKGSGARPASP
HHHHHCCCCCCCCCC		32.1122817900
439PhosphorylationGSGARPASPESTPRP
CCCCCCCCCCCCCCC		31.7023737553
442PhosphorylationARPASPESTPRPGQP
CCCCCCCCCCCCCCC		47.2823737553
443PhosphorylationRPASPESTPRPGQPR
CCCCCCCCCCCCCCC		22.9623737553
452PhosphorylationRPGQPRGSLRSVRGL
CCCCCCCCCCCCCCC		23.1422817900
455PhosphorylationQPRGSLRSVRGLSAP
CCCCCCCCCCCCCCC		22.8127681418
457MethylationRGSLRSVRGLSAPSC
CCCCCCCCCCCCCCC		41.40-
460PhosphorylationLRSVRGLSAPSCPGL
CCCCCCCCCCCCCCC		40.7423926118
463PhosphorylationVRGLSAPSCPGLDDK
CCCCCCCCCCCCCCC		32.4322817900
471PhosphorylationCPGLDDKTEASARPG
CCCCCCCCCHHCCCC		43.7222817900
492PhosphorylationEKPARRVSDSFFRPS
CCCCCCCCCCCCCHH		26.2321082442
492O-linked_GlycosylationEKPARRVSDSFFRPS
CCCCCCCCCCCCCHH		26.2331924761
494PhosphorylationPARRVSDSFFRPSVM
CCCCCCCCCCCHHHH		20.8311641724
499PhosphorylationSDSFFRPSVMEPILG
CCCCCCHHHHHHHHC		29.8222817900
511PhosphorylationILGRAQYSQLRKKS-
HHCHHHHHHHHHCC-		15.6222817900
517PhosphorylationYSQLRKKS-------
HHHHHHCC-------		48.7919850935
517O-linked_GlycosylationYSQLRKKS-------
HHHHHHCC-------		48.7931924761
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
492SPhosphorylationKinasePKACAP17612
PSP
492SPhosphorylationKinasePRKACAP05132
GPS
517SPhosphorylationKinasePKACAP17612
PSP
517SPhosphorylationKinasePRKACAP05132
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLIN1_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 PLIN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PLIN1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLIN1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The stoichiometry of protein phosphorylation in adipocyte lipiddroplets: analysis by N-terminal isotope tagging and enzymaticdephosphorylation.";
Kanshin E., Wang S., Ashmarina L., Fedjaev M., Nifant'ev I.,Mitchell G.A., Pshezhetsky A.V.;
Proteomics 9:5067-5077(2009).
Cited for: PHOSPHORYLATION AT SER-410 AND SER-460.

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