LPAR2_HUMAN - dbPTM
LPAR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LPAR2_HUMAN
UniProt AC Q9HBW0
Protein Name Lysophosphatidic acid receptor 2
Gene Name LPAR2
Organism Homo sapiens (Human).
Sequence Length 351
Subcellular Localization Cell surface . Cell membrane
Multi-pass membrane protein . Prior to LPA treatment found predominantly at the cell surface but in the presence of LPA colocalizes with RALA in the endocytic vesicles.
Protein Description Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway. Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation..
Protein Sequence MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASNRRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVATLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSRMAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLVKTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDAEMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
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
10N-linked_GlycosylationIMGQCYYNETIGFFY
CCEEEEECCEEEEEE
17.29UniProtKB CARBOHYD
18N-linked_GlycosylationETIGFFYNNSGKELS
CEEEEEECCCCCCCH
30.91UniProtKB CARBOHYD
232PhosphorylationHVSCHPRYRETTLSL
HHCCCHHHHHHHHHH
19.7730631047
235PhosphorylationCHPRYRETTLSLVKT
CCHHHHHHHHHHHHH
24.8422210691
236PhosphorylationHPRYRETTLSLVKTV
CHHHHHHHHHHHHHH
15.0326699800
238PhosphorylationRYRETTLSLVKTVVI
HHHHHHHHHHHHHHH
29.0826699800
295PhosphorylationSLVNAAVYSCRDAEM
HHHHHHHHHCCHHHH
9.42-
311S-palmitoylationRTFRRLLCCACLRQS
HHHHHHHHHHHHHHH
1.31-
318PhosphorylationCCACLRQSTRESVHY
HHHHHHHHCCCEEEE
24.0123403867
319PhosphorylationCACLRQSTRESVHYT
HHHHHHHCCCEEEEC
30.0728857561
322PhosphorylationLRQSTRESVHYTSSA
HHHHCCCEEEECCCC
15.7623403867
325PhosphorylationSTRESVHYTSSAQGG
HCCCEEEECCCCCCC
13.2323403867
326PhosphorylationTRESVHYTSSAQGGA
CCCEEEECCCCCCCC
11.0023403867
327PhosphorylationRESVHYTSSAQGGAS
CCEEEECCCCCCCCC
19.2628857561
328PhosphorylationESVHYTSSAQGGAST
CEEEECCCCCCCCCE
19.4628857561
334PhosphorylationSSAQGGASTRIMLPE
CCCCCCCCEEEECCC
22.8428857561
335PhosphorylationSAQGGASTRIMLPEN
CCCCCCCEEEECCCC
24.5523312004
349PhosphorylationNGHPLMDSTL-----
CCCCCCCCCC-----
20.0422617229
350PhosphorylationGHPLMDSTL------
CCCCCCCCC------
32.0222617229

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 LPAR2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LPAR2_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 LPAR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRIP6_HUMANTRIP6physical
14688263
TRIP6_HUMANTRIP6physical
19293149
SIVA_HUMANSIVA1physical
19293149
NHRF2_RATSlc9a3r2physical
15143197
NHRF2_HUMANSLC9A3R2physical
15143197
PLCB3_HUMANPLCB3physical
15143197
HBB_HUMANHBBphysical
28514442
LEG3_HUMANLGALS3physical
28514442

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 LPAR2_HUMAN

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Related Literatures of Post-Translational Modification

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