PLCE_HUMAN - dbPTM
PLCE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLCE_HUMAN
UniProt AC Q9NUQ2
Protein Name 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Gene Name AGPAT5
Organism Homo sapiens (Human).
Sequence Length 364
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Nucleus envelope . Mitochondrion .
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 C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor. Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA. Activity toward lysophosphatidylglycerol not detectable..
Protein Sequence MLLSLVLHTYSMRYLLPSVVLLGTAPTYVLAWGVWRLLSAFLPARFYQALDDRLYCVYQSMVLFFFENYTGVQILLYGDLPKNKENIIYLANHQSTVDWIVADILAIRQNALGHVRYVLKEGLKWLPLYGCYFAQHGGIYVKRSAKFNEKEMRNKLQSYVDAGTPMYLVIFPEGTRYNPEQTKVLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDCMKNYLDAIYDVTVVYEGKDDGGQRRESPTMTEFLCKECPKIHIHIDRIDKKDVPEEQEHMRRWLHERFEIKDKMLIEFYESPDPERRKRFPGKSVNSKLSIKKTLPSMLILSGLTAGMLMTDAGRKLYVNTWIYGTLLGCLWVTIKA
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
4Phosphorylation----MLLSLVLHTYS
----CCHHHHHHHHH		16.6923663014
9PhosphorylationLLSLVLHTYSMRYLL
CHHHHHHHHHHHHHH		17.0923663014
10PhosphorylationLSLVLHTYSMRYLLP
HHHHHHHHHHHHHHH		6.9623663014
11PhosphorylationSLVLHTYSMRYLLPS
HHHHHHHHHHHHHHH		9.6523663014
14PhosphorylationLHTYSMRYLLPSVVL
HHHHHHHHHHHHHHH		12.1624043423
18PhosphorylationSMRYLLPSVVLLGTA
HHHHHHHHHHHCCCC		25.4824043423
24PhosphorylationPSVVLLGTAPTYVLA
HHHHHCCCCCHHHHH		29.4524043423
27PhosphorylationVLLGTAPTYVLAWGV
HHCCCCCHHHHHHHH		24.6524043423
28PhosphorylationLLGTAPTYVLAWGVW
HCCCCCHHHHHHHHH		7.7524043423
39PhosphorylationWGVWRLLSAFLPARF
HHHHHHHHHHHCHHH		22.90110759125
120UbiquitinationGHVRYVLKEGLKWLP
CCHHHHHHHCCCCHH		39.4321890473
120MalonylationGHVRYVLKEGLKWLP
CCHHHHHHHCCCCHH		39.4326320211
150UbiquitinationRSAKFNEKEMRNKLQ
ECCCCCHHHHHHHHH		58.8921890473
155UbiquitinationNEKEMRNKLQSYVDA
CHHHHHHHHHHHHCC		37.2221890473
164PhosphorylationQSYVDAGTPMYLVIF
HHHHCCCCCEEEEEC		13.45110759131
183AcetylationRYNPEQTKVLSASQA
CCCHHHHHCCCHHHH		40.6526051181
183UbiquitinationRYNPEQTKVLSASQA
CCCHHHHHCCCHHHH		40.6521890473
183MalonylationRYNPEQTKVLSASQA
CCCHHHHHCCCHHHH		40.6526320211
201UbiquitinationQRGLAVLKHVLTPRI
HHHHHHHHHHCCHHH		25.68-
201AcetylationQRGLAVLKHVLTPRI
HHHHHHHHHHCCHHH		25.6825825284
205PhosphorylationAVLKHVLTPRIKATH
HHHHHHCCHHHCHHH		14.9422210691
209UbiquitinationHVLTPRIKATHVAFD
HHCCHHHCHHHHHHH		48.81-
221PhosphorylationAFDCMKNYLDAIYDV
HHHHHHHHHHHHCEE		10.637331141
232PhosphorylationIYDVTVVYEGKDDGG
HCEEEEEEECCCCCC		18.037331151
253UbiquitinationTMTEFLCKECPKIHI
CHHHHHHHHCCCEEE		65.58-
257UbiquitinationFLCKECPKIHIHIDR
HHHHHCCCEEEEEEE		59.58-
290UbiquitinationERFEIKDKMLIEFYE
HHHCCCCHHHHHECC		30.51-
296PhosphorylationDKMLIEFYESPDPER
CHHHHHECCCCCHHH		11.6026471730
298PhosphorylationMLIEFYESPDPERRK
HHHHECCCCCHHHHH		24.1926471730
310UbiquitinationRRKRFPGKSVNSKLS
HHHCCCCCCCCCHHC		52.01-
315UbiquitinationPGKSVNSKLSIKKTL
CCCCCCCHHCCCCHH		40.84-
321PhosphorylationSKLSIKKTLPSMLIL
CHHCCCCHHCHHHHH		38.6126552605
324PhosphorylationSIKKTLPSMLILSGL
CCCCHHCHHHHHHCC		29.3668739317
329PhosphorylationLPSMLILSGLTAGML
HCHHHHHHCCHHHHE		25.4330257219
332PhosphorylationMLILSGLTAGMLMTD
HHHHHCCHHHHECCH		25.3726552605
338PhosphorylationLTAGMLMTDAGRKLY
CHHHHECCHHCCHHH		20.8026552605
351PhosphorylationLYVNTWIYGTLLGCL
HHHHHHHHHHHHHHH		8.8120049867
353PhosphorylationVNTWIYGTLLGCLWV
HHHHHHHHHHHHHEE		11.2220049867
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 PLCE_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of PLCE_HUMAN !!
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 PLCE_HUMAN

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Related Literatures of Post-Translational Modification

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