PLBL1_HUMAN - dbPTM
PLBL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLBL1_HUMAN
UniProt AC Q6P4A8
Protein Name Phospholipase B-like 1
Gene Name PLBD1
Organism Homo sapiens (Human).
Sequence Length 553
Subcellular Localization Lysosome.
Protein Description In view of the small size of the putative binding pocket, it has been proposed that it may act as an amidase or a peptidase (By similarity). Exhibits a weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids..
Protein Sequence MTRGGPGGRPGLPQPPPLLLLLLLLPLLLVTAEPPKPAGVYYATAYWMPAEKTVQVKNVMDKNGDAYGFYNNSVKTTGWGILEIRAGYGSQTLSNEIIMFVAGFLEGYLTAPHMNDHYTNLYPQLITKPSIMDKVQDFMEKQDKWTRKNIKEYKTDSFWRHTGYVMAQIDGLYVGAKKRAILEGTKPMTLFQIQFLNSVGDLLDLIPSLSPTKNGSLKVFKRWDMGHCSALIKVLPGFENILFAHSSWYTYAAMLRIYKHWDFNVIDKDTSSSRLSFSSYPGFLESLDDFYILSSGLILLQTTNSVFNKTLLKQVIPETLLSWQRVRVANMMADSGKRWADIFSKYNSGTYNNQYMVLDLKKVKLNHSLDKGTLYIVEQIPTYVEYSEQTDVLRKGYWPSYNVPFHEKIYNWSGYPLLVQKLGLDYSYDLAPRAKIFRRDQGKVTDTASMKYIMRYNNYKKDPYSRGDPCNTICCREDLNSPNPSPGGCYDTKVADIYLASQYTSYAISGPTVQGGLPVFRWDRFNKTLHQGMPEVYNFDFITMKPILKLDIK
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
57UbiquitinationAEKTVQVKNVMDKNG
CCCEEEEEECCCCCC		27.0830230243
71N-linked_GlycosylationGDAYGFYNNSVKTTG
CCEEEEECCCCCCCE		31.85UniProtKB CARBOHYD
162PhosphorylationTDSFWRHTGYVMAQI
CCCHHHHHCCEEEEE		22.9525332170
164PhosphorylationSFWRHTGYVMAQIDG
CHHHHHCCEEEEECC		6.5518083107
173PhosphorylationMAQIDGLYVGAKKRA
EEEECCEEECCCHHH		11.4518083107
210PhosphorylationLDLIPSLSPTKNGSL
HHHCHHCCCCCCCCE		34.5624719451
270PhosphorylationFNVIDKDTSSSRLSF
CEEECCCCCCCCEEC		35.9325852190
271PhosphorylationNVIDKDTSSSRLSFS
EEECCCCCCCCEECC		36.1325852190
272PhosphorylationVIDKDTSSSRLSFSS
EECCCCCCCCEECCC		22.9025852190
273PhosphorylationIDKDTSSSRLSFSSY
ECCCCCCCCEECCCC		36.6925852190
308N-linked_GlycosylationQTTNSVFNKTLLKQV
ECCCHHCCHHHHHHH		33.96UniProtKB CARBOHYD
344PhosphorylationKRWADIFSKYNSGTY
CCHHHHHHHHCCCCC		34.2724719451
362AcetylationYMVLDLKKVKLNHSL
EEEEECCEEEECCCC		52.487826099
366N-linked_GlycosylationDLKKVKLNHSLDKGT
ECCEEEECCCCCCCC		19.58UniProtKB CARBOHYD
375PhosphorylationSLDKGTLYIVEQIPT
CCCCCCEEEEEECCC		11.6220736484
383PhosphorylationIVEQIPTYVEYSEQT
EEEECCCEEEHHHCC		5.9720736484
386PhosphorylationQIPTYVEYSEQTDVL
ECCCEEEHHHCCCHH		13.8920736484
397PhosphorylationTDVLRKGYWPSYNVP
CCHHHCCCCCCCCCC		19.72-
411N-linked_GlycosylationPFHEKIYNWSGYPLL
CHHHHHHCCCCCCHH		29.8819159218
426PhosphorylationVQKLGLDYSYDLAPR
HHHHCCCCCCCCCCC		17.74-
428PhosphorylationKLGLDYSYDLAPRAK
HHCCCCCCCCCCCCE		14.56-
445PhosphorylationRRDQGKVTDTASMKY
ECCCCCCCCHHHHHH		30.9929759185
447PhosphorylationDQGKVTDTASMKYIM
CCCCCCCHHHHHHHH		15.9729759185
449PhosphorylationGKVTDTASMKYIMRY
CCCCCHHHHHHHHHH		20.2124114839
452PhosphorylationTDTASMKYIMRYNNY
CCHHHHHHHHHHCCC		7.42-
456PhosphorylationSMKYIMRYNNYKKDP
HHHHHHHHCCCCCCC		7.1525884760
526N-linked_GlycosylationVFRWDRFNKTLHQGM
EEEHHHHCCHHHCCC		36.98UniProtKB CARBOHYD
528PhosphorylationRWDRFNKTLHQGMPE
EHHHHCCHHHCCCCC		30.4923663014
537PhosphorylationHQGMPEVYNFDFITM
HCCCCCEECCEEEEE		14.4023663014
543PhosphorylationVYNFDFITMKPILKL
EECCEEEEEEEEEEC		21.0923663014
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 PLBL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLBL1_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 PLBL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TCPW_HUMANCCT6Bphysical
26186194
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 PLBL1_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-411, AND MASSSPECTROMETRY.

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