PHLD_HUMAN - dbPTM
PHLD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHLD_HUMAN
UniProt AC P80108
Protein Name Phosphatidylinositol-glycan-specific phospholipase D
Gene Name GPLD1
Organism Homo sapiens (Human).
Sequence Length 840
Subcellular Localization Secreted.
Protein Description This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane..
Protein Sequence MSAFRLWPGLLIMLGSLCHRGSPCGLSTHVEIGHRALEFLQLHNGRVNYRELLLEHQDAYQAGIVFPDCFYPSICKGGKFHDVSESTHWTPFLNASVHYIRENYPLPWEKDTEKLVAFLFGITSHMAADVSWHSLGLEQGFLRTMGAIDFHGSYSEAHSAGDFGGDVLSQFEFNFNYLARRWYVPVKDLLGIYEKLYGRKVITENVIVDCSHIQFLEMYGEMLAVSKLYPTYSTKSPFLVEQFQEYFLGGLDDMAFWSTNIYHLTSFMLENGTSDCNLPENPLFIACGGQQNHTQGSKMQKNDFHRNLTTSLTESVDRNINYTERGVFFSVNSWTPDSMSFIYKALERNIRTMFIGGSQLSQKHVSSPLASYFLSFPYARLGWAMTSADLNQDGHGDLVVGAPGYSRPGHIHIGRVYLIYGNDLGLPPVDLDLDKEAHRILEGFQPSGRFGSALAVLDFNVDGVPDLAVGAPSVGSEQLTYKGAVYVYFGSKQGGMSSSPNITISCQDIYCNLGWTLLAADVNGDSEPDLVIGSPFAPGGGKQKGIVAAFYSGPSLSDKEKLNVEAANWTVRGEEDFSWFGYSLHGVTVDNRTLLLVGSPTWKNASRLGHLLHIRDEKKSLGRVYGYFPPNGQSWFTISGDKAMGKLGTSLSSGHVLMNGTLKQVLLVGAPTYDDVSKVAFLTVTLHQGGATRMYALTSDAQPLLLSTFSGDRRFSRFGGVLHLSDLDDDGLDEIIMAAPLRIADVTSGLIGGEDGRVYVYNGKETTLGDMTGKCKSWITPCPEEKAQYVLISPEASSRFGSSLITVRSKAKNQVVIAAGRSSLGARLSGALHVYSLGSD
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
16PhosphorylationGLLIMLGSLCHRGSP
HHHHHHHHHHHCCCC		24.7027762562
94N-linked_GlycosylationTHWTPFLNASVHYIR
CCCCCCCCEEEEEHH		30.4616335952
231PhosphorylationAVSKLYPTYSTKSPF
HHHCCCCCCCCCCCH		19.29-
233PhosphorylationSKLYPTYSTKSPFLV
HCCCCCCCCCCCHHH		31.66-
234PhosphorylationKLYPTYSTKSPFLVE
CCCCCCCCCCCHHHH		25.73-
271N-linked_GlycosylationLTSFMLENGTSDCNL
HHHHHHHCCCCCCCC		55.89UniProtKB CARBOHYD
292N-linked_GlycosylationIACGGQQNHTQGSKM
EEECCCCCCCCCCCC		32.08UniProtKB CARBOHYD
307N-linked_GlycosylationQKNDFHRNLTTSLTE
CHHHHHHHHHHHHHH		32.92UniProtKB CARBOHYD
307N-linked_GlycosylationQKNDFHRNLTTSLTE
CHHHHHHHHHHHHHH		32.9217623646
321N-linked_GlycosylationESVDRNINYTERGVF
HHHHCCCCCCCCEEE		41.02UniProtKB CARBOHYD
491PhosphorylationAVYVYFGSKQGGMSS
EEEEEECCCCCCCCC		16.35-
501N-linked_GlycosylationGGMSSSPNITISCQD
CCCCCCCCEEEEEEE		46.08UniProtKB CARBOHYD
551PhosphorylationKGIVAAFYSGPSLSD
CCEEEEEECCCCCCC		14.1625072903
552PhosphorylationGIVAAFYSGPSLSDK
CEEEEEECCCCCCCH		37.4625072903
555PhosphorylationAAFYSGPSLSDKEKL
EEEECCCCCCCHHHH		43.9924905233
557PhosphorylationFYSGPSLSDKEKLNV
EECCCCCCCHHHHCC		51.4824905233
568N-linked_GlycosylationKLNVEAANWTVRGEE
HHCCCCCCCEECCCC		41.8417623646
568N-linked_GlycosylationKLNVEAANWTVRGEE
HHCCCCCCCEECCCC		41.84UniProtKB CARBOHYD
591N-linked_GlycosylationLHGVTVDNRTLLLVG
EEEEEECCCEEEEEC		34.20UniProtKB CARBOHYD
604N-linked_GlycosylationVGSPTWKNASRLGHL
ECCCCCCCHHHHCCC		34.41UniProtKB CARBOHYD
639PhosphorylationGQSWFTISGDKAMGK
CCCCEEEECCCCCCC		37.57-
659N-linked_GlycosylationSSGHVLMNGTLKQVL
CCCCEEECCEEEEEE		35.8219159218
683PhosphorylationVSKVAFLTVTLHQGG
HHCEEEEEEEEECCC		12.65-
747PhosphorylationPLRIADVTSGLIGGE
CEEEEECCCCCCCCC		20.0219845377
748PhosphorylationLRIADVTSGLIGGED
EEEEECCCCCCCCCC		31.3019845377
759PhosphorylationGGEDGRVYVYNGKET
CCCCCEEEEECCEEE		8.8919845377
761PhosphorylationEDGRVYVYNGKETTL
CCCEEEEECCEEEEC		10.6619845377
764AcetylationRVYVYNGKETTLGDM
EEEEECCEEEECCCC		48.5320167786
766PhosphorylationYVYNGKETTLGDMTG
EEECCEEEECCCCCC		30.7022210691
767PhosphorylationVYNGKETTLGDMTGK
EECCEEEECCCCCCC		29.8122210691
777PhosphorylationDMTGKCKSWITPCPE
CCCCCCCCCEEECCH		32.9329978859
780PhosphorylationGKCKSWITPCPEEKA
CCCCCCEEECCHHHC		16.7529978859
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 PHLD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHLD_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 PHLD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APOA1_HUMANAPOA1physical
11254757
HIF1A_HUMANHIF1Aphysical
26680696
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 PHLD_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-659, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94, AND MASS SPECTROMETRY.

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