PLBL2_HUMAN - dbPTM
PLBL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLBL2_HUMAN
UniProt AC Q8NHP8
Protein Name Putative phospholipase B-like 2
Gene Name PLBD2
Organism Homo sapiens (Human).
Sequence Length 589
Subcellular Localization Lysosome lumen .
Protein Description Putative phospholipase..
Protein Sequence MVGQMYCYPGSHLARALTRALALALVLALLVGPFLSGLAGAIPAPGGRWARDGQVPPASRSRSVLLDVSAGQLLMVDGRHPDAVAWANLTNAIRETGWAFLELGTSGQYNDSLQAYAAGVVEAAVSEELIYMHWMNTVVNYCGPFEYEVGYCERLKSFLEANLEWMQEEMESNPDSPYWHQVRLTLLQLKGLEDSYEGRVSFPAGKFTIKPLGFLLLQLSGDLEDLELALNKTKIKPSLGSGSCSALIKLLPGQSDLLVAHNTWNNYQHMLRVIKKYWLQFREGPWGDYPLVPGNKLVFSSYPGTIFSCDDFYILGSGLVTLETTIGNKNPALWKYVRPRGCVLEWVRNIVANRLASDGATWADIFKRFNSGTYNNQWMIVDYKAFIPGGPSPGSRVLTILEQIPGMVVVADKTSELYQKTYWASYNIPSFETVFNASGLQALVAQYGDWFSYDGSPRAQIFRRNQSLVQDMDSMVRLMRYNDFLHDPLSLCKACNPQPNGENAISARSDLNPANGSYPFQALRQRSHGGIDVKVTSMSLARILSLLAASGPTWDQVPPFQWSTSPFSGLLHMGQPDLWKFAPVKVSWD
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
18PhosphorylationSHLARALTRALALAL
HHHHHHHHHHHHHHH		16.95-
36PhosphorylationLLVGPFLSGLAGAIP
HHHHHHHHHHHCCCC		31.94-
59UbiquitinationDGQVPPASRSRSVLL
CCCCCCCCCCCCEEE		36.2421963094
65UbiquitinationASRSRSVLLDVSAGQ
CCCCCCEEEEECCCC		3.4021963094
75UbiquitinationVSAGQLLMVDGRHPD
ECCCCEEEECCCCCC		3.3427667366
81UbiquitinationLMVDGRHPDAVAWAN
EEECCCCCCHHHHHH		29.8727667366
88N-linked_GlycosylationPDAVAWANLTNAIRE
CCHHHHHHHHHHHHH		36.3817105447
110N-linked_GlycosylationLGTSGQYNDSLQAYA
CCCCCCCCHHHHHHH		25.2217105447
190UbiquitinationRLTLLQLKGLEDSYE
HHHHHHHCCCCCCCC		48.79-
190UbiquitinationRLTLLQLKGLEDSYE
HHHHHHHCCCCCCCC		48.7921906983
206UbiquitinationRVSFPAGKFTIKPLG
CCCCCCCCEEECCHH		41.2527667366
208PhosphorylationSFPAGKFTIKPLGFL
CCCCCCEEECCHHHH		31.42-
231N-linked_GlycosylationEDLELALNKTKIKPS
HHHHHHHHCCCCCCC		44.3217105447
234UbiquitinationELALNKTKIKPSLGS
HHHHHCCCCCCCCCC		50.7929967540
236UbiquitinationALNKTKIKPSLGSGS
HHHCCCCCCCCCCCC		30.0622817900
242UbiquitinationIKPSLGSGSCSALIK
CCCCCCCCCHHHHHH		30.7622817900
253UbiquitinationALIKLLPGQSDLLVA
HHHHHCCCCCCEEEE		39.3223503661
255PhosphorylationIKLLPGQSDLLVAHN
HHHCCCCCCEEEEEC		35.82-
259UbiquitinationPGQSDLLVAHNTWNN
CCCCCEEEEECCCCC		7.0923503661
267PhosphorylationAHNTWNNYQHMLRVI
EECCCCCHHHHHHHH		9.15-
354MethylationVRNIVANRLASDGAT
HHHHHHHHHHCCCCC		23.15115487739
357PhosphorylationIVANRLASDGATWAD
HHHHHHHCCCCCHHH		40.96-
367UbiquitinationATWADIFKRFNSGTY
CCHHHHHHHHHCCCC		57.31-
367UbiquitinationATWADIFKRFNSGTY
CCHHHHHHHHHCCCC		57.3122817900
371 (in isoform 2)Phosphorylation-29.7826437602
373 (in isoform 2)Phosphorylation-23.9326437602
374PhosphorylationKRFNSGTYNNQWMIV
HHHHCCCCCCEEEEE		18.6819413330
384UbiquitinationQWMIVDYKAFIPGGP
EEEEEEEEEECCCCC		32.1523503661
392PhosphorylationAFIPGGPSPGSRVLT
EECCCCCCCCHHHHH		45.2119413330
395PhosphorylationPGGPSPGSRVLTILE
CCCCCCCHHHHHHHH		23.7019413330
407SulfoxidationILEQIPGMVVVADKT
HHHHCCCEEEEEECC		1.4121406390
436N-linked_GlycosylationPSFETVFNASGLQAL
CCHHEECCHHHHHHH		28.9417105447
465N-linked_GlycosylationRAQIFRRNQSLVQDM
HHHHHHCCHHHHHCH		31.3817105447
467PhosphorylationQIFRRNQSLVQDMDS
HHHHCCHHHHHCHHH		33.77-
474PhosphorylationSLVQDMDSMVRLMRY
HHHHCHHHHHHHHHH		16.73-
515N-linked_GlycosylationRSDLNPANGSYPFQA
CCCCCCCCCCCCHHH		41.0017105447
517O-linked_GlycosylationDLNPANGSYPFQALR
CCCCCCCCCCHHHHH		29.4628657654
545PhosphorylationMSLARILSLLAASGP
HHHHHHHHHHHHHCC		20.97-
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 PLBL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLBL2_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 PLBL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDHD1_HUMANWDHD1physical
22939629
RBM12_HUMANRBM12physical
22939629
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 PLBL2_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-465, AND MASSSPECTROMETRY.
"Biochemical characterization and lysosomal localization of themannose-6-phosphate protein p76 (hypothetical protein LOC196463).";
Jensen A.G., Chemali M., Chapel A., Kieffer-Jaquinod S., Jadot M.,Garin J., Journet A.;
Biochem. J. 402:449-458(2007).
Cited for: PROTEIN SEQUENCE OF 42-49 AND 244-250, GLYCOSYLATION AT ASN-88;ASN-110; ASN-231; ASN-436; ASN-465 AND ASN-515, INTERACTION WITHIGF2R, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASSSPECTROMETRY.

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