PCAT1_HUMAN - dbPTM
PCAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCAT1_HUMAN
UniProt AC Q8NF37
Protein Name Lysophosphatidylcholine acyltransferase 1
Gene Name LPCAT1
Organism Homo sapiens (Human).
Sequence Length 534
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein . Golgi apparatus membrane
Single-pass type II membrane protein . Lipid droplet . May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with b
Protein Description Possesses both acyltransferase and acetyltransferase activities. [PubMed: 16864775]
Protein Sequence MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLVAAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAEALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERARMKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFAEMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
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
14PhosphorylationGPRAAPASSAGASDA
CCCCCCCCCCCCCCC
21.4729396449
15PhosphorylationPRAAPASSAGASDAR
CCCCCCCCCCCCCCE
32.5929396449
19PhosphorylationPASSAGASDARLLAP
CCCCCCCCCCEECCC
30.7729396449
39PhosphorylationFVHELRLSALQKAQV
CHHHHHHHHHHHHHH
22.0920860994
50PhosphorylationKAQVALMTLTLFPVR
HHHHHHHHHCHHHHH
19.9020860994
52PhosphorylationQVALMTLTLFPVRLL
HHHHHHHCHHHHHHH
19.72-
93UbiquitinationQPPALWRKVVDFLLK
CCCHHHHHHHHHHHH
34.72-
191UbiquitinationRKTVEEIKRRAQSNG
HHHHHHHHHHHHHCC
38.83-
199UbiquitinationRRAQSNGKWPQIMIF
HHHHHCCCCCEEEEE
61.01-
216S-palmitoylationGTCTNRTCLITFKPG
CCCCCCEEEEEECCC
2.0329575903
221AcetylationRTCLITFKPGAFIPG
CEEEEEECCCCCCCC
33.6126051181
221UbiquitinationRTCLITFKPGAFIPG
CEEEEEECCCCCCCC
33.61-
292PhosphorylationRNPALYASNVRRVMA
CCHHHHHHHHHHHHH
23.46-
330GlutathionylationLRLPADTCLLEFARL
CCCCHHHHHHHHHHH
4.1422555962
344UbiquitinationLVRGLGLKPEKLEKD
HHHHCCCCHHHHHHH
49.70-
347UbiquitinationGLGLKPEKLEKDLDR
HCCCCHHHHHHHHHH
71.16-
362UbiquitinationYSERARMKGGEKIGI
HHHHHHHCCCCEEEH
59.20-
381PhosphorylationASLEVPVSDLLEDMF
HHCCCCHHHHHHHHH
19.2322210691
381O-linked_GlycosylationASLEVPVSDLLEDMF
HHCCCCHHHHHHHHH
19.2329351928
394PhosphorylationMFSLFDESGSGEVDL
HHHHHCCCCCCCCCH
39.8522210691
396PhosphorylationSLFDESGSGEVDLRE
HHHCCCCCCCCCHHH
40.8522210691
409O-linked_GlycosylationRECVVALSVVCRPAR
HHHHHHHHHHCCCCC
11.6329351928
443GlutathionylationVGEGDLSCILKTALG
CCCCHHHHHHHHHHC
5.7022555962
447PhosphorylationDLSCILKTALGVAEL
HHHHHHHHHHCCEEE
24.5420860994
4702-HydroxyisobutyrylationIDQEEKGKITFADFH
CCHHHCCCCCHHHHH
50.03-
470UbiquitinationIDQEEKGKITFADFH
CCHHHCCCCCHHHHH
50.03-

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
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:21068446

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCAT1_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 PCAT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BBS2_HUMANBBS2physical
26186194
MSTO1_HUMANMSTO1physical
26186194
S27A2_HUMANSLC27A2physical
26186194
DOCK7_HUMANDOCK7physical
26186194
DIP2A_HUMANDIP2Aphysical
26186194
FBW1A_HUMANBTRCphysical
21068446
S27A2_HUMANSLC27A2physical
28514442
MSTO1_HUMANMSTO1physical
28514442
METH_HUMANMTRphysical
28514442
DIP2A_HUMANDIP2Aphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCAT1_HUMAN

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Related Literatures of Post-Translational Modification

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