PLIN3_HUMAN - dbPTM
PLIN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLIN3_HUMAN
UniProt AC O60664
Protein Name Perilipin-3
Gene Name PLIN3
Organism Homo sapiens (Human).
Sequence Length 434
Subcellular Localization Cytoplasm . Endosome membrane
Peripheral membrane protein
Cytoplasmic side . Lipid droplet . Membrane associated on endosomes. Detected in the envelope and the core of lipid bodies and in lipid sails.
Protein Description Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network..
Protein Sequence MSADGAEADGSTQVTVEEPVQQPSVVDRVASMPLISSTCDMVSAAYASTKESYPHIKTVCDAAEKGVRTLTAAAVSGAQPILSKLEPQIASASEYAHRGLDKLEENLPILQQPTEKVLADTKELVSSKVSGAQEMVSSAKDTVATQLSEAVDATRGAVQSGVDKTKSVVTGGVQSVMGSRLGQMVLSGVDTVLGKSEEWADNHLPLTDAELARIATSLDGFDVASVQQQRQEQSYFVRLGSLSERLRQHAYEHSLGKLRATKQRAQEALLQLSQVLSLMETVKQGVDQKLVEGQEKLHQMWLSWNQKQLQGPEKEPPKPEQVESRALTMFRDIAQQLQATCTSLGSSIQGLPTNVKDQVQQARRQVEDLQATFSSIHSFQDLSSSILAQSRERVASAREALDHMVEYVAQNTPVTWLVGPFAPGITEKAPEEKK
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
2Acetylation------MSADGAEAD
------CCCCCCCCC		34.7618491316
2Phosphorylation------MSADGAEAD
------CCCCCCCCC		34.7629743597
11O-linked_GlycosylationDGAEADGSTQVTVEE
CCCCCCCCCEEEEEC		19.0630059200
11PhosphorylationDGAEADGSTQVTVEE
CCCCCCCCCEEEEEC		19.0618491316
12O-linked_GlycosylationGAEADGSTQVTVEEP
CCCCCCCCEEEEECC		32.3730059200
12PhosphorylationGAEADGSTQVTVEEP
CCCCCCCCEEEEECC		32.3718491316
15O-linked_GlycosylationADGSTQVTVEEPVQQ
CCCCCEEEEECCCCC		16.6330059200
15PhosphorylationADGSTQVTVEEPVQQ
CCCCCEEEEECCCCC		16.6325867546
31PhosphorylationSVVDRVASMPLISST
CHHHHHHCCCCHHHH		20.3421712546
36PhosphorylationVASMPLISSTCDMVS
HHCCCCHHHHHHHHH		27.5521712546
37PhosphorylationASMPLISSTCDMVSA
HCCCCHHHHHHHHHH		26.5126657352
38PhosphorylationSMPLISSTCDMVSAA
CCCCHHHHHHHHHHH		13.0126657352
43O-linked_GlycosylationSSTCDMVSAAYASTK
HHHHHHHHHHHHCCH		10.6730059200
43PhosphorylationSSTCDMVSAAYASTK
HHHHHHHHHHHHCCH		10.6728796482
46PhosphorylationCDMVSAAYASTKESY
HHHHHHHHHCCHHHC		10.7828796482
48PhosphorylationMVSAAYASTKESYPH
HHHHHHHCCHHHCCC		27.6028796482
49PhosphorylationVSAAYASTKESYPHI
HHHHHHCCHHHCCCH		30.5728796482
65AcetylationTVCDAAEKGVRTLTA
HHHHHHHHHHHHHHH		58.9619608861
65UbiquitinationTVCDAAEKGVRTLTA
HHHHHHHHHHHHHHH		58.9619608861
69O-linked_GlycosylationAAEKGVRTLTAAAVS
HHHHHHHHHHHHHHH		26.5030059200
69PhosphorylationAAEKGVRTLTAAAVS
HHHHHHHHHHHHHHH		26.5028555341
71PhosphorylationEKGVRTLTAAAVSGA
HHHHHHHHHHHHHCC		17.4028555341
76O-linked_GlycosylationTLTAAAVSGAQPILS
HHHHHHHHCCHHHHH		24.5530059200
76PhosphorylationTLTAAAVSGAQPILS
HHHHHHHHCCHHHHH		24.5529514088
83PhosphorylationSGAQPILSKLEPQIA
HCCHHHHHHCCHHHH		35.5927251275
84AcetylationGAQPILSKLEPQIAS
CCHHHHHHCCHHHHC		54.1223236377
84UbiquitinationGAQPILSKLEPQIAS
CCHHHHHHCCHHHHC		54.1221906983
84 (in isoform 1)Ubiquitination-54.1221890473
84 (in isoform 3)Ubiquitination-54.12-
91PhosphorylationKLEPQIASASEYAHR
HCCHHHHCHHHHHHH		33.6828152594
93PhosphorylationEPQIASASEYAHRGL
CHHHHCHHHHHHHHH		28.7528152594
95PhosphorylationQIASASEYAHRGLDK
HHHCHHHHHHHHHHH		12.7625159151
102UbiquitinationYAHRGLDKLEENLPI
HHHHHHHHHHHHCCC		63.94-
116UbiquitinationILQQPTEKVLADTKE
CCCCCCHHHHHCHHH		45.0521906983
116 (in isoform 1)Ubiquitination-45.0521890473
122AcetylationEKVLADTKELVSSKV
HHHHHCHHHHHHHHC		49.9923236377
122SumoylationEKVLADTKELVSSKV
HHHHHCHHHHHHHHC		49.9925114211
122UbiquitinationEKVLADTKELVSSKV
HHHHHCHHHHHHHHC		49.9921890473
122 (in isoform 1)Ubiquitination-49.9921890473
122 (in isoform 3)Ubiquitination-49.99-
126PhosphorylationADTKELVSSKVSGAQ
HCHHHHHHHHCCCHH		36.7523927012
127PhosphorylationDTKELVSSKVSGAQE
CHHHHHHHHCCCHHH		29.6023401153
128AcetylationTKELVSSKVSGAQEM
HHHHHHHHCCCHHHH		32.6825953088
128MalonylationTKELVSSKVSGAQEM
HHHHHHHHCCCHHHH		32.6826320211
128UbiquitinationTKELVSSKVSGAQEM
HHHHHHHHCCCHHHH		32.68-
128 (in isoform 1)Ubiquitination-32.6821890473
128 (in isoform 3)Ubiquitination-32.68-
130PhosphorylationELVSSKVSGAQEMVS
HHHHHHCCCHHHHHH		31.9529255136
135SulfoxidationKVSGAQEMVSSAKDT
HCCCHHHHHHHCHHH		2.0521406390
137PhosphorylationSGAQEMVSSAKDTVA
CCHHHHHHHCHHHHH		24.2223927012
138PhosphorylationGAQEMVSSAKDTVAT
CHHHHHHHCHHHHHH		28.1125159151
140UbiquitinationQEMVSSAKDTVATQL
HHHHHHCHHHHHHHH		56.742190698
140 (in isoform 1)Ubiquitination-56.7421890473
142PhosphorylationMVSSAKDTVATQLSE
HHHHCHHHHHHHHHH		16.0121406692
145PhosphorylationSAKDTVATQLSEAVD
HCHHHHHHHHHHHHH		26.2121406692
148PhosphorylationDTVATQLSEAVDATR
HHHHHHHHHHHHHHH		17.4325159151
154PhosphorylationLSEAVDATRGAVQSG
HHHHHHHHHHHHHHC		25.7721406692
160PhosphorylationATRGAVQSGVDKTKS
HHHHHHHHCCCCCCC		33.9020068231
164AcetylationAVQSGVDKTKSVVTG
HHHHCCCCCCCHHHC		56.2823749302
164UbiquitinationAVQSGVDKTKSVVTG
HHHHCCCCCCCHHHC		56.28-
165PhosphorylationVQSGVDKTKSVVTGG
HHHCCCCCCCHHHCC		24.8820068231
167PhosphorylationSGVDKTKSVVTGGVQ
HCCCCCCCHHHCCHH		27.3520068231
170PhosphorylationDKTKSVVTGGVQSVM
CCCCCHHHCCHHHHC		26.5121601212
175PhosphorylationVVTGGVQSVMGSRLG
HHHCCHHHHCCHHHH		16.2121082442
177SulfoxidationTGGVQSVMGSRLGQM
HCCHHHHCCHHHHHH		4.9628465586
179PhosphorylationGVQSVMGSRLGQMVL
CHHHHCCHHHHHHHH		13.2621082442
184SulfoxidationMGSRLGQMVLSGVDT
CCHHHHHHHHHCCCH		2.8821406390
187PhosphorylationRLGQMVLSGVDTVLG
HHHHHHHHCCCHHCC		25.9228102081
191PhosphorylationMVLSGVDTVLGKSEE
HHHHCCCHHCCCCHH		18.4123403867
195UbiquitinationGVDTVLGKSEEWADN
CCCHHCCCCHHHHHH		51.00-
195 (in isoform 3)Ubiquitination-51.00-
196PhosphorylationVDTVLGKSEEWADNH
CCHHCCCCHHHHHHC		38.6629496963
207PhosphorylationADNHLPLTDAELARI
HHHCCCCCHHHHHHH		31.0923090842
216PhosphorylationAELARIATSLDGFDV
HHHHHHHHHCCCCCH		27.7030266825
217PhosphorylationELARIATSLDGFDVA
HHHHHHHHCCCCCHH		18.5530266825
225PhosphorylationLDGFDVASVQQQRQE
CCCCCHHHHHHHHHH		21.9528555341
241PhosphorylationSYFVRLGSLSERLRQ
HHHHHHHCHHHHHHH		33.0623401153
243PhosphorylationFVRLGSLSERLRQHA
HHHHHCHHHHHHHHH		23.5123927012
245MethylationRLGSLSERLRQHAYE
HHHCHHHHHHHHHHH		31.62115487007
257AcetylationAYEHSLGKLRATKQR
HHHHHHHHHHHHHHH		39.8425953088
283UbiquitinationLSLMETVKQGVDQKL
HHHHHHHHHCCCHHH		49.07-
289AcetylationVKQGVDQKLVEGQEK
HHHCCCHHHHHHHHH		50.4623236377
289MalonylationVKQGVDQKLVEGQEK
HHHCCCHHHHHHHHH		50.4626320211
289UbiquitinationVKQGVDQKLVEGQEK
HHHCCCHHHHHHHHH		50.46-
303PhosphorylationKLHQMWLSWNQKQLQ
HHHHHHHHHHHHHHC		14.4129514088
307UbiquitinationMWLSWNQKQLQGPEK
HHHHHHHHHHCCCCC		50.16-
314AcetylationKQLQGPEKEPPKPEQ
HHHCCCCCCCCCHHH		77.8623236377
314UbiquitinationKQLQGPEKEPPKPEQ
HHHCCCCCCCCCHHH		77.86-
318AcetylationGPEKEPPKPEQVESR
CCCCCCCCHHHHHHH		72.4226051181
342PhosphorylationQQLQATCTSLGSSIQ
HHHHHHHHHCCHHHC		23.7221712546
347PhosphorylationTCTSLGSSIQGLPTN
HHHHCCHHHCCCCCC		19.6821712546
356UbiquitinationQGLPTNVKDQVQQAR
CCCCCCHHHHHHHHH		44.50-
372PhosphorylationQVEDLQATFSSIHSF
HHHHHHHHHHHHHHH		15.8727251275
374PhosphorylationEDLQATFSSIHSFQD
HHHHHHHHHHHHHHH		24.8320068231
375PhosphorylationDLQATFSSIHSFQDL
HHHHHHHHHHHHHHH		21.8226434776
378PhosphorylationATFSSIHSFQDLSSS
HHHHHHHHHHHHCHH		23.9626657352
383PhosphorylationIHSFQDLSSSILAQS
HHHHHHHCHHHHHHH		30.2620068231
384PhosphorylationHSFQDLSSSILAQSR
HHHHHHCHHHHHHHH		28.7920068231
385PhosphorylationSFQDLSSSILAQSRE
HHHHHCHHHHHHHHH		20.4626657352
390PhosphorylationSSSILAQSRERVASA
CHHHHHHHHHHHHHH		30.4220068231
404SulfoxidationAREALDHMVEYVAQN
HHHHHHHHHHHHHHC		2.1531801345
412PhosphorylationVEYVAQNTPVTWLVG
HHHHHHCCCCEEEEC		13.68-
415PhosphorylationVAQNTPVTWLVGPFA
HHHCCCCEEEECCCC		17.81-
428UbiquitinationFAPGITEKAPEEKK-
CCCCCCCCCCCCCC-		61.67-
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

Oops, there are no upstream regulatory protein records of PLIN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLIN3_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 PLIN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB9A_HUMANRAB9Aphysical
12032303
PLIN3_HUMANPLIN3physical
12535272
A4_HUMANAPPphysical
21832049
VMA21_HUMANVMA21physical
22939629
PP4R2_HUMANPPP4R2physical
22939629
RHOA_HUMANRHOAphysical
22939629
SPART_HUMANSPG20physical
23890011
PUR8_HUMANADSLphysical
22863883
ANKY2_HUMANANKMY2physical
22863883
AN32A_HUMANANP32Aphysical
22863883
CALU_HUMANCALUphysical
22863883
CBS_HUMANCBSphysical
22863883
IF4A3_HUMANEIF4A3physical
22863883
LRSM1_HUMANLRSAM1physical
22863883
MTMR2_HUMANMTMR2physical
22863883
PDLI5_HUMANPDLIM5physical
22863883
RD23B_HUMANRAD23Bphysical
22863883
SRP14_HUMANSRP14physical
22863883
SAE2_HUMANUBA2physical
22863883
VAT1_HUMANVAT1physical
22863883
WDR4_HUMANWDR4physical
22863883
CKLF5_HUMANCMTM5physical
25416956
CCHL_HUMANHCCSphysical
26186194
MTCH2_HUMANMTCH2physical
26186194
VDAC1_HUMANVDAC1physical
26186194
TMM43_HUMANTMEM43physical
26186194
PMYT1_HUMANPKMYT1physical
26186194
PUR9_HUMANATICphysical
26344197
DUT_HUMANDUTphysical
26344197
EF1A1_HUMANEEF1A1physical
26344197
JUPI1_HUMANHN1physical
26344197
IMPA2_HUMANIMPA2physical
26344197
LEG3_HUMANLGALS3physical
26344197
MP2K1_HUMANMAP2K1physical
26344197
IPYR_HUMANPPA1physical
26344197
IPYR2_HUMANPPA2physical
26344197
RAB1A_HUMANRAB1Aphysical
26344197
RAB1B_HUMANRAB1Bphysical
26344197
PMYT1_HUMANPKMYT1physical
28514442
CCHL_HUMANHCCSphysical
28514442
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
DB01279Galsulfase
DB01271Idursulfase
Regulatory Network of PLIN3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; THR-170; SER-175AND SER-179, AND MASS SPECTROMETRY.

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