PLPL8_HUMAN - dbPTM
PLPL8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLPL8_HUMAN
UniProt AC Q9NP80
Protein Name Calcium-independent phospholipase A2-gamma
Gene Name PNPLA8
Organism Homo sapiens (Human).
Sequence Length 782
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein. Golgi apparatus membrane
Single-pass membrane protein. Cytoplasm, perinuclear region.
Protein Description Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids..
Protein Sequence MSINLTVDIYIYLLSNARSVCGKQRSKQLYFLFSPKHYWRISHISLQRGFHTNIIRCKWTKSEAHSCSKHCYSPSNHGLHIGILKLSTSAPKGLTKVNICMSRIKSTLNSVSKAVFGNQNEMISRLAQFKPSSQILRKVSDSGWLKQKNIKQAIKSLKKYSDKSAEKSPFPEEKSHIIDKEEDIGKRSLFHYTSSITTKFGDSFYFLSNHINSYFKRKEKMSQQKENEHFRDKSELEDKKVEEGKLRSPDPGILAYKPGSESVHTVDKPTSPSAIPDVLQVSTKQSIANFLSRPTEGVQALVGGYIGGLVPKLKYDSKSQSEEQEEPAKTDQAVSKDRNAEEKKRLSLQREKIIARVSIDNRTRALVQALRRTTDPKLCITRVEELTFHLLEFPEGKGVAVKERIIPYLLRLRQIKDETLQAAVREILALIGYVDPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFSQNVIVGTVKMSWSHAFYDSQTWENILKDRMGSALMIETARNPTCPKVAAVSTIVNRGITPKAFVFRNYGHFPGINSHYLGGCQYKMWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDVPLECIVSLGTGRYESDVRNTVTYTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLDESRNEKLDQLQLEGLKYIERNEQKMKKVAKILSQEKTTLQKINDWIKLKTDMYEGLPFFSKL
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------MSINLTVDI
------CCCEEEEEE
21.8624043423
4N-linked_Glycosylation----MSINLTVDIYI
----CCCEEEEEEHH
23.50UniProtKB CARBOHYD
6Phosphorylation--MSINLTVDIYIYL
--CCCEEEEEEHHHH
16.1924043423
19PhosphorylationYLLSNARSVCGKQRS
HHHHCCHHHHCCCCC
21.2424043423
34PhosphorylationKQLYFLFSPKHYWRI
CEEEEEECHHHEEEE
34.8824719451
45PhosphorylationYWRISHISLQRGFHT
EEEEEEEEECCCCCC
17.0224719451
87PhosphorylationHIGILKLSTSAPKGL
EEEEEEECCCCCCCC
20.8027251275
88PhosphorylationIGILKLSTSAPKGLT
EEEEEECCCCCCCCC
39.0727251275
89PhosphorylationGILKLSTSAPKGLTK
EEEEECCCCCCCCCH
38.9227251275
102PhosphorylationTKVNICMSRIKSTLN
CHHHHHHHHHHHHHH
26.8329083192
106PhosphorylationICMSRIKSTLNSVSK
HHHHHHHHHHHHHHH
35.4429083192
107PhosphorylationCMSRIKSTLNSVSKA
HHHHHHHHHHHHHHH
25.5929083192
110PhosphorylationRIKSTLNSVSKAVFG
HHHHHHHHHHHHHHC
30.7729083192
112PhosphorylationKSTLNSVSKAVFGNQ
HHHHHHHHHHHHCCH
18.0829083192
125DimethylationNQNEMISRLAQFKPS
CHHHHHHHHHCCCCH
24.10-
125MethylationNQNEMISRLAQFKPS
CHHHHHHHHHCCCCH
24.1024410469
156PhosphorylationNIKQAIKSLKKYSDK
CHHHHHHHHHHHCCC
39.0324702127
168PhosphorylationSDKSAEKSPFPEEKS
CCCCCCCCCCCHHHH
24.2328348404
168O-linked_GlycosylationSDKSAEKSPFPEEKS
CCCCCCCCCCCHHHH
24.2331492838
188PhosphorylationEEDIGKRSLFHYTSS
CHHCCCHHHHEEEEE
38.5828450419
192PhosphorylationGKRSLFHYTSSITTK
CCHHHHEEEEECEEC
10.8628450419
193PhosphorylationKRSLFHYTSSITTKF
CHHHHEEEEECEECC
13.8728450419
194PhosphorylationRSLFHYTSSITTKFG
HHHHEEEEECEECCC
16.7528450419
195PhosphorylationSLFHYTSSITTKFGD
HHHEEEEECEECCCC
19.0228450419
197PhosphorylationFHYTSSITTKFGDSF
HEEEEECEECCCCHH
26.3628450419
198PhosphorylationHYTSSITTKFGDSFY
EEEEECEECCCCHHH
23.7828450419
233UbiquitinationENEHFRDKSELEDKK
HHHHCCCHHHHCCHH
41.39-
239UbiquitinationDKSELEDKKVEEGKL
CHHHHCCHHCCCCCC
49.71-
245UbiquitinationDKKVEEGKLRSPDPG
CHHCCCCCCCCCCCC
43.96-
347PhosphorylationAEEKKRLSLQREKII
HHHHHHHHHHHHHHH
26.8724719451
358PhosphorylationEKIIARVSIDNRTRA
HHHHHEEECCHHHHH
20.7627251275
361N-linked_GlycosylationIARVSIDNRTRALVQ
HHEEECCHHHHHHHH
45.62UniProtKB CARBOHYD
381PhosphorylationTDPKLCITRVEELTF
CCCCCEEEEHHHHEE
27.89-
438UbiquitinationIGYVDPVKGRGIRIL
HCCCCCCCCCCEEEE
48.56-
511PhosphorylationELYRKLGSDVFSQNV
HHHHHHCCCHHHCCE
40.83-
515PhosphorylationKLGSDVFSQNVIVGT
HHCCCHHHCCEEEEE
22.24-
558PhosphorylationIETARNPTCPKVAAV
EECCCCCCCCCHHHH
45.0128509920
561UbiquitinationARNPTCPKVAAVSTI
CCCCCCCCHHHHHHH
46.80-
663PhosphorylationVSLGTGRYESDVRNT
EEECCCCCCCCCCCC
22.56-
664 (in isoform 2)Ubiquitination-38.8221906983
670PhosphorylationYESDVRNTVTYTSLK
CCCCCCCCEEEECHH
12.03-
672PhosphorylationSDVRNTVTYTSLKTK
CCCCCCEEEECHHHH
21.0221964256
673PhosphorylationDVRNTVTYTSLKTKL
CCCCCEEEECHHHHH
7.0426356563
674PhosphorylationVRNTVTYTSLKTKLS
CCCCEEEECHHHHHH
20.4426356563
677MalonylationTVTYTSLKTKLSNVI
CEEEECHHHHHHHHH
43.3026320211
726UbiquitinationLDESRNEKLDQLQLE
CCCCCCCCCHHHHHH
62.002190698
726 (in isoform 1)Ubiquitination-62.0021906983
736SuccinylationQLQLEGLKYIERNEQ
HHHHHHHHHHHHCHH
55.85-
736SuccinylationQLQLEGLKYIERNEQ
HHHHHHHHHHHHCHH
55.85-
736UbiquitinationQLQLEGLKYIERNEQ
HHHHHHHHHHHHCHH
55.85-
736AcetylationQLQLEGLKYIERNEQ
HHHHHHHHHHHHCHH
55.8525038526
756UbiquitinationAKILSQEKTTLQKIN
HHHHHCCCHHHHHHH
38.89-
767UbiquitinationQKINDWIKLKTDMYE
HHHHHHHHHCCCCCC
39.41-

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
511SPhosphorylationKinaseMKNK1Q9BUB5
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLPL8_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 PLPL8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PLPL8_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
251950Mitochondrial myopathy with lactic acidosis (MMLA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLPL8_HUMAN

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Related Literatures of Post-Translational Modification

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