PLCC_HUMAN - dbPTM
PLCC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLCC_HUMAN
UniProt AC Q9NRZ7
Protein Name 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Gene Name AGPAT3
Organism Homo sapiens (Human).
Sequence Length 376
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Nucleus envelope.
Protein Description Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA. [PubMed: 21173190 Has a preference for arachidonoyl-CoA as a donor. Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity]
Protein Sequence MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSLLGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE
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
57 (in isoform 2)Ubiquitination-3.1221890473
57UbiquitinationNCRLAYSLWSQLVML
CHHHHHHHHHHHHHH		3.1221890473
77PhosphorylationCTECTLFTDQATVER
CCCCCCCCCHHHHHH		30.25113136161
101UbiquitinationLNHNFEIDFLCGWTM
ECCCCEEEEECCHHC		24.2221890473
119UbiquitinationFGVLGSSKVLAKKEL
HCCCCCCHHHCCCHH		42.8621890473
123UbiquitinationGSSKVLAKKELLYVP
CCCHHHCCCHHEEEC		42.4921890473
139 (in isoform 2)Ubiquitination-2.2921890473
139 (in isoform 3)Ubiquitination-2.2921890473
139UbiquitinationIGWTWYFLEIVFCKR
CHHHHHHHHHHHHHH		2.2921890473
149UbiquitinationVFCKRKWEEDRDTVV
HHHHHHCCCCHHHHH		53.7221890473
154PhosphorylationKWEEDRDTVVEGLRR
HCCCCHHHHHHHHHH		27.6122985185
159UbiquitinationRDTVVEGLRRLSDYP
HHHHHHHHHHHHCCH		1.5021890473
174 (in isoform 2)Ubiquitination-7.2121890473
174UbiquitinationEYMWFLLYCEGTRFT
HHHHHHHHCCCCCCC		7.2121890473
183PhosphorylationEGTRFTETKHRVSME
CCCCCCCCCHHHHHH		29.1524719451
183UbiquitinationEGTRFTETKHRVSME
CCCCCCCCCHHHHHH		29.1521890473
185UbiquitinationTRFTETKHRVSMEVA
CCCCCCCHHHHHHHH		42.6821890473
185 (in isoform 2)Ubiquitination-42.6821890473
193UbiquitinationRVSMEVAAAKGLPVL
HHHHHHHHHCCCCEE		18.1921890473
195MalonylationSMEVAAAKGLPVLKY
HHHHHHHCCCCEEEE		57.1426320211
201UbiquitinationAKGLPVLKYHLLPRT
HCCCCEEEEEECCCC		30.7521890473
205UbiquitinationPVLKYHLLPRTKGFT
CEEEEEECCCCCCCH		1.3921890473
206 (in isoform 1)Ubiquitination-48.5321890473
206UbiquitinationVLKYHLLPRTKGFTT
EEEEEECCCCCCCHH		48.5321890473
209UbiquitinationYHLLPRTKGFTTAVK
EEECCCCCCCHHHHH		53.9929967540
212PhosphorylationLPRTKGFTTAVKCLR
CCCCCCCHHHHHHHH		23.6346160481
213PhosphorylationPRTKGFTTAVKCLRG
CCCCCCHHHHHHHHC		27.4846160487
218UbiquitinationFTTAVKCLRGTVAAV
CHHHHHHHHCCEEEE		4.7221890473
219 (in isoform 2)Ubiquitination-48.4821890473
221 (in isoform 3)Ubiquitination-10.6721890473
229UbiquitinationVAAVYDVTLNFRGNK
EEEEEEEEEECCCCC		17.0621890473
231UbiquitinationAVYDVTLNFRGNKNP
EEEEEEEECCCCCCH		18.4021890473
236UbiquitinationTLNFRGNKNPSLLGI
EEECCCCCCHHHHHH		73.4021890473
240UbiquitinationRGNKNPSLLGILYGK
CCCCCHHHHHHHHCC		5.5321890473
241UbiquitinationGNKNPSLLGILYGKK
CCCCHHHHHHHHCCC		4.7421890473
247UbiquitinationLLGILYGKKYEADMC
HHHHHHCCCCCCCEE		38.3321890473
251UbiquitinationLYGKKYEADMCVRRF
HHCCCCCCCEEEEEC		13.5221890473
256 (in isoform 3)Ubiquitination-29.6021890473
266UbiquitinationPLEDIPLDEKEAAQW
CCCCCCCCHHHHHHH		60.6121890473
267 (in isoform 3)Ubiquitination-61.5521890473
268UbiquitinationEDIPLDEKEAAQWLH
CCCCCCHHHHHHHHH		52.9329967540
275UbiquitinationKEAAQWLHKLYQEKD
HHHHHHHHHHHHHHH		18.3421890473
276UbiquitinationEAAQWLHKLYQEKDA
HHHHHHHHHHHHHHH		46.8721890473
277UbiquitinationAAQWLHKLYQEKDAL
HHHHHHHHHHHHHHH		3.5721890473
281UbiquitinationLHKLYQEKDALQEIY
HHHHHHHHHHHHHHH		32.542190698
287UbiquitinationEKDALQEIYNQKGMF
HHHHHHHHHHCCCCC		2.2321890473
288 (in isoform 1)Ubiquitination-15.7021890473
288UbiquitinationKDALQEIYNQKGMFP
HHHHHHHHHCCCCCC		15.7021890473
301 (in isoform 3)Ubiquitination-32.0821890473
310UbiquitinationRRPWTLLNFLSWATI
CCCHHHHHHHHHHHH		38.6421890473
321UbiquitinationWATILLSPLFSFVLG
HHHHHHHHHHHHHHH		37.0821890473
323 (in isoform 1)Ubiquitination-6.3821890473
323UbiquitinationTILLSPLFSFVLGVF
HHHHHHHHHHHHHHH		6.3821890473
334 (in isoform 1)Ubiquitination-15.1821890473
334UbiquitinationLGVFASGSPLLILTF
HHHHCCCCCHHHHHH		15.1821890473
368 (in isoform 1)Ubiquitination-31.1521890473
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 PLCC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLCC_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 PLCC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TM1L1_HUMANTOM1L1physical
28514442
SCYL1_HUMANSCYL1physical
28514442
HSP7C_HUMANHSPA8physical
28514442
NOMO1_HUMANNOMO1physical
27173435
METL9_HUMANMETTL9physical
27173435
SERC1_HUMANSERINC1physical
27173435
NCLN_HUMANNCLNphysical
27173435
T120B_HUMANTMEM120Bphysical
27173435
T120A_HUMANTMEM120Aphysical
27173435
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
There are no disease associations of PTM sites.
Regulatory Network of PLCC_HUMAN

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Related Literatures of Post-Translational Modification

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