PLPR4_HUMAN - dbPTM
PLPR4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLPR4_HUMAN
UniProt AC Q7Z2D5
Protein Name Phospholipid phosphatase-related protein type 4 {ECO:0000305}
Gene Name PLPPR4 {ECO:0000312|HGNC:HGNC:23496}
Organism Homo sapiens (Human).
Sequence Length 763
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Hydrolyzes lysophosphatidic acid (LPA). Facilitates axonal outgrowth during development and regenerative sprouting. In the outgrowing axons acts as an ecto-enzyme and attenuates phospholipid-induced axon collapse in neurons and facilitates outgrowth in the hippocampus..
Protein Sequence MQRAGSSGGRGECDISGAGRLGLEEAARLSCAVHTSPGGGRRPGQAAGMSAKERPKGKVIKDSVTLLPCFYFVELPILASSVVSLYFLELTDVFKPVHSGFSCYDRSLSMPYIEPTQEAIPFLMLLSLAFAGPAITIMVGEGILYCCLSKRRNGVGLEPNINAGGCNFNSFLRRAVRFVGVHVFGLCSTALITDIIQLSTGYQAPYFLTVCKPNYTSLNVSCKENSYIVEDICSGSDLTVINSGRKSFPSQHATLAAFAAVYVSMYFNSTLTDSSKLLKPLLVFTFIICGIICGLTRITQYKNHPVDVYCGFLIGGGIALYLGLYAVGNFLPSDESMFQHRDALRSLTDLNQDPNRLLSAKNGSSSDGIAHTEGILNRNHRDASSLTNLKRANADVEIITPRSPMGKENMVTFSNTLPRANTPSVEDPVRRNASIHASMDSARSKQLLTQWKNKNESRKLSLQVIEPEPGQSPPRSIEMRSSSEPSRVGVNGDHHGPGNQYLKIQPGAVPGCNNSMPGGPRVSIQSRPGSSQLVHIPEETQENISTSPKSSSARAKWLKAAEKTVACNRSNSQPRIMQVIAMSKQQGVLQSSPKNTEGSTVSCTGSIRYKTLTDHEPSGIVRVEAHPENNRPIIQIPSTEGEGSGSWKWKAPEKGSLRQTYELNDLNRDSESCESLKDSFGSGDRKRSNIDSNEHHHHGITTIRVTPVEGSEIGSETLSISSSRDSTLRRKGNIILIPERSNSPENTRNIFYKGTSPTRAYKD
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
36PhosphorylationLSCAVHTSPGGGRRP
HHEEEECCCCCCCCC
-
50PhosphorylationPGQAAGMSAKERPKG
CCCCCCCCCCCCCCC
29759185
209PhosphorylationYQAPYFLTVCKPNYT
CCCCEEEEEECCCCE
-
214N-linked_GlycosylationFLTVCKPNYTSLNVS
EEEEECCCCEEEEEE
UniProtKB CARBOHYD
219N-linked_GlycosylationKPNYTSLNVSCKENS
CCCCEEEEEEECCCE
UniProtKB CARBOHYD
226PhosphorylationNVSCKENSYIVEDIC
EEEECCCEEEEEEEC
-
247PhosphorylationVINSGRKSFPSQHAT
EEECCCCCCCCHHHH
-
254PhosphorylationSFPSQHATLAAFAAV
CCCCHHHHHHHHHHH
22210691
264PhosphorylationAFAAVYVSMYFNSTL
HHHHHHHHHHHCCCC
22210691
266PhosphorylationAAVYVSMYFNSTLTD
HHHHHHHHHCCCCCC
22210691
268N-linked_GlycosylationVYVSMYFNSTLTDSS
HHHHHHHCCCCCCHH
UniProtKB CARBOHYD
346PhosphorylationQHRDALRSLTDLNQD
HCHHHHHHHHHCCCC
27732954
348PhosphorylationRDALRSLTDLNQDPN
HHHHHHHHHCCCCHH
27732954
362N-linked_GlycosylationNRLLSAKNGSSSDGI
HHHHHCCCCCCCCCC
UniProtKB CARBOHYD
364PhosphorylationLLSAKNGSSSDGIAH
HHHCCCCCCCCCCCH
27732954
365PhosphorylationLSAKNGSSSDGIAHT
HHCCCCCCCCCCCHH
27732954
366PhosphorylationSAKNGSSSDGIAHTE
HCCCCCCCCCCCHHH
27732954
384PhosphorylationNRNHRDASSLTNLKR
CCCCCCHHHHHCHHH
27732954
385PhosphorylationRNHRDASSLTNLKRA
CCCCCHHHHHCHHHH
22617229
387PhosphorylationHRDASSLTNLKRANA
CCCHHHHHCHHHHCC
27732954
400PhosphorylationNADVEIITPRSPMGK
CCCEEEECCCCCCCC
24719451
403PhosphorylationVEIITPRSPMGKENM
EEEECCCCCCCCCCE
24117733
412PhosphorylationMGKENMVTFSNTLPR
CCCCCEEEECCCCCC
27732954
414PhosphorylationKENMVTFSNTLPRAN
CCCEEEECCCCCCCC
27732954
416PhosphorylationNMVTFSNTLPRANTP
CEEEECCCCCCCCCC
27732954
432N-linked_GlycosylationVEDPVRRNASIHASM
CCCCHHHCCCCCCCC
UniProtKB CARBOHYD
434PhosphorylationDPVRRNASIHASMDS
CCHHHCCCCCCCCCC
24719451
438PhosphorylationRNASIHASMDSARSK
HCCCCCCCCCCHHHH
30387612
449PhosphorylationARSKQLLTQWKNKNE
HHHHHHHHHHHCCCH
24719451
455N-linked_GlycosylationLTQWKNKNESRKLSL
HHHHHCCCHHCCEEE
UniProtKB CARBOHYD
461PhosphorylationKNESRKLSLQVIEPE
CCHHCCEEEEEECCC
27732954
472PhosphorylationIEPEPGQSPPRSIEM
ECCCCCCCCCCCEEE
27732954
501PhosphorylationHHGPGNQYLKIQPGA
CCCCCCCCEEECCCC
25884760
513N-linked_GlycosylationPGAVPGCNNSMPGGP
CCCCCCCCCCCCCCC
UniProtKB CARBOHYD
540PhosphorylationLVHIPEETQENISTS
EEECCHHHHHCCCCC
27732954
543N-linked_GlycosylationIPEETQENISTSPKS
CCHHHHHCCCCCCCC
UniProtKB CARBOHYD
545PhosphorylationEETQENISTSPKSSS
HHHHHCCCCCCCCHH
26699800
546PhosphorylationETQENISTSPKSSSA
HHHHCCCCCCCCHHH
26699800
547PhosphorylationTQENISTSPKSSSAR
HHHCCCCCCCCHHHH
26699800
568N-linked_GlycosylationAEKTVACNRSNSQPR
HHHHHHCCCCCCCCC
UniProtKB CARBOHYD
583PhosphorylationIMQVIAMSKQQGVLQ
HHHHHHHHHHCCCCC
29978859
591PhosphorylationKQQGVLQSSPKNTEG
HHCCCCCCCCCCCCC
27732954
592PhosphorylationQQGVLQSSPKNTEGS
HCCCCCCCCCCCCCC
27732954
606PhosphorylationSTVSCTGSIRYKTLT
CEEECCEEEEEEECC
-
638PhosphorylationRPIIQIPSTEGEGSG
CCCEECCCCCCCCCC
24425749
646PhosphorylationTEGEGSGSWKWKAPE
CCCCCCCCCEECCCC
24425749
661PhosphorylationKGSLRQTYELNDLNR
CCCCCEEEECCCCCC
25884760
670PhosphorylationLNDLNRDSESCESLK
CCCCCCCCHHHHHHH
27732954
672PhosphorylationDLNRDSESCESLKDS
CCCCCCHHHHHHHHH
27732954
675PhosphorylationRDSESCESLKDSFGS
CCCHHHHHHHHHCCC
27732954
679PhosphorylationSCESLKDSFGSGDRK
HHHHHHHHCCCCCCC
27732954
721PhosphorylationGSETLSISSSRDSTL
CCEEEEEECCCCCCC
24905233
722PhosphorylationSETLSISSSRDSTLR
CEEEEEECCCCCCCC
24905233
723PhosphorylationETLSISSSRDSTLRR
EEEEEECCCCCCCCC
24905233
726PhosphorylationSISSSRDSTLRRKGN
EEECCCCCCCCCCCE
21406692
727PhosphorylationISSSRDSTLRRKGNI
EECCCCCCCCCCCEE
21406692
741PhosphorylationIILIPERSNSPENTR
EEEECCCCCCCCCCC
22617229

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 PLPR4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLPR4_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 PLPR4_HUMAN !!

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

Oops, there are no PPI records of PLPR4_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLPR4_HUMAN

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Related Literatures of Post-Translational Modification

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