PCAT2_HUMAN - dbPTM
PCAT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCAT2_HUMAN
UniProt AC Q7L5N7
Protein Name Lysophosphatidylcholine acyltransferase 2
Gene Name LPCAT2
Organism Homo sapiens (Human).
Sequence Length 544
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein . Golgi apparatus membrane
Single-pass type II membrane protein. Lipid droplet .
Protein Description Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet-activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases. Also catalyzes the conversion of 1-acyl-sn-glycero-3-phosphocholine to 1,2-diacyl-sn-glycero-3-phosphocholine..
Protein Sequence MSRCAQAAEVAATVPGAGVGNVGLRPPMVPRQASFFPPPVPNPFVQQTQIGSARRVQIVLLGIILLPIRVLLVALILLLAWPFAAISTVCCPEKLTHPITGWRRKITQTALKFLGRAMFFSMGFIVAVKGKIASPLEAPVFVAAPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDSRKNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTFCQLFTKVEVEFMPVQVPNDEEKNDPVLFANKVRNLMAEALGIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGVRKHLDEYASIASSSKGGRIGIEEFAKYLKLPVSDVLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDVSGLFKEIAQGDSISYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPKEVQTTPSTASNKVSPEKHEESTSDKKDD
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
2Phosphorylation------MSRCAQAAE
------CCHHHHHHH		35.7522210691
13PhosphorylationQAAEVAATVPGAGVG
HHHHHHHCCCCCCCC		19.9324719451
34PhosphorylationPMVPRQASFFPPPVP
CCCCCCCCCCCCCCC		21.0526657352
49UbiquitinationNPFVQQTQIGSARRV
CCCCCCCCCCCHHHH		33.4427667366
105 (in isoform 2)Ubiquitination-41.3421890473
105UbiquitinationPITGWRRKITQTALK
CCCCHHHHHHHHHHH		41.3427667366
116 (in isoform 2)Ubiquitination-25.6521890473
116UbiquitinationTALKFLGRAMFFSMG
HHHHHHHHHHHHHHC		25.6521890473
119 (in isoform 2)Ubiquitination-3.9121890473
119UbiquitinationKFLGRAMFFSMGFIV
HHHHHHHHHHHCEEE		3.9121890473
121PhosphorylationLGRAMFFSMGFIVAV
HHHHHHHHHCEEEEE		13.51-
148UbiquitinationFVAAPHSTFFDGIAC
EEECCCCCCCCCHHH		25.8622817900
204AcetylationNTINEIIKRTTSGGE
CHHHHHHHHHCCCCC		49.727976715
204 (in isoform 1)Ubiquitination-49.7221890473
204UbiquitinationNTINEIIKRTTSGGE
CHHHHHHHHHCCCCC		49.7221906983
228S-palmitoylationGTCTNRSCLITFKPG
CCCCCCCEEEEECCC		2.6229575903
250PhosphorylationVQPVLLRYPNKLDTV
CCCEEECCCCCCCCE		15.89-
319UbiquitinationEALGIPVTDHTYEDC
HHHCCCCCCCCHHHH		19.4021963094
330UbiquitinationYEDCRLMISAGQLTL
HHHHEEEEECCCCEE		2.7821890473
333UbiquitinationCRLMISAGQLTLPME
HEEEEECCCCEECCC		19.0821890473
362UbiquitinationLDWDGVRKHLDEYAS
CCHHHHHHHHHHHHH		46.2229967540
362AcetylationLDWDGVRKHLDEYAS
CCHHHHHHHHHHHHH		46.2226822725
362MalonylationLDWDGVRKHLDEYAS
CCHHHHHHHHHHHHH		46.2226320211
367PhosphorylationVRKHLDEYASIASSS
HHHHHHHHHHHHHCC		12.8127642862
375UbiquitinationASIASSSKGGRIGIE
HHHHHCCCCCCCCHH		68.2921906983
375 (in isoform 1)Ubiquitination-68.2921890473
386UbiquitinationIGIEEFAKYLKLPVS
CCHHHHHHHHCCCHH		57.3422817900
386 (in isoform 1)Ubiquitination-57.3421890473
389 (in isoform 1)Ubiquitination-47.8821890473
389UbiquitinationEEFAKYLKLPVSDVL
HHHHHHHCCCHHHHH		47.8822817900
482PhosphorylationIAQGDSISYEEFKSF
HHCCCCCCHHHHHHH		30.37-
483PhosphorylationAQGDSISYEEFKSFA
HCCCCCCHHHHHHHH		20.15-
487UbiquitinationSISYEEFKSFALKHP
CCCHHHHHHHHHHCH		48.2029967540
513PhosphorylationLQTCHVFSLPKEVQT
CCCCEEEECCCCCCC		42.5524719451
520PhosphorylationSLPKEVQTTPSTASN
ECCCCCCCCCCCCCC		45.9421815630
521PhosphorylationLPKEVQTTPSTASNK
CCCCCCCCCCCCCCC		9.7328450419
523PhosphorylationKEVQTTPSTASNKVS
CCCCCCCCCCCCCCC		34.2223401153
524PhosphorylationEVQTTPSTASNKVSP
CCCCCCCCCCCCCCH		35.0028450419
526PhosphorylationQTTPSTASNKVSPEK
CCCCCCCCCCCCHHH		36.9529255136
528UbiquitinationTPSTASNKVSPEKHE
CCCCCCCCCCHHHCC		41.4132015554
530PhosphorylationSTASNKVSPEKHEES
CCCCCCCCHHHCCCC		29.0229255136
537PhosphorylationSPEKHEESTSDKKDD
CHHHCCCCCCCCCCC		30.1723312004
538PhosphorylationPEKHEESTSDKKDD-
HHHCCCCCCCCCCC-		44.2023312004
539PhosphorylationEKHEESTSDKKDD--
HHCCCCCCCCCCC--		57.6323312004
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 PCAT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCAT2_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 PCAT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PCAT2_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 PCAT2_HUMAN

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Related Literatures of Post-Translational Modification

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