PLB1_HUMAN - dbPTM
PLB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLB1_HUMAN
UniProt AC Q6P1J6
Protein Name Phospholipase B1, membrane-associated
Gene Name PLB1
Organism Homo sapiens (Human).
Sequence Length 1458
Subcellular Localization Apical cell membrane
Single-pass type I membrane protein. Present in the intestinal brush border membranes..
Protein Description Membrane-associated phospholipase. Exhibits a calcium-independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids (By similarity)..
Protein Sequence MGLRPGIFLLELLLLLGQGTPQIHTSPRKSTLEGQLWPETLKNSPFPCNPNKLGVNMPSKSVHSLKPSDIKFVAAIGNLEIPPDPGTGDLEKQDWTERPQQVCMGVMTVLSDIIRYFSPSVPMPVCHTGKRVIPHDGAEDLWIQAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLCPSAQQNGLAAGGVDELMGVLDYLQQEVPRAFVNLVDLSEVAEVSRQYHGTWLSPAPEPCNCSEETTRLAKVVMQWSYQEAWNSLLASSRYSEQESFTVVFQPFFYETTPSLHSEDPRLQDSTTLAWHLWNRMMEPAGEKDEPLSVKHGRPMKCPSQESPYLFSYRNSNYLTRLQKPQDKLEVREGAEIRCPDKDPSDTVPTSVHRLKPADINVIGALGDSLTAGNGAGSTPGNVLDVLTQYRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKETSPNAFLNQAVAGGRAEDLPVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDILHAEVPRAFVNLVTVLEIVNLRELYQEKKVYCPRMILRSLCPCVLKFDDNSTELATLIEFNKKFQEKTHQLIESGRYDTREDFTVVVQPFFENVDMPKTSEGLPDNSFFAPDCFHFSSKSHSRAASALWNNMLEPVGQKTTRHKFENKINITCPNQVQPFLRTYKNSMQGHGTWLPCRDRAPSALHPTSVHALRPADIQVVAALGDSLTAGNGIGSKPDDLPDVTTQYRGLSYSAGGDGSLENVTTLPNILREFNRNLTGYAVGTGDANDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKDDHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVLHREVPRVLVNLVDFLNPTIMRQVFLGNPDKCPVQQASVLCNCVLTLRENSQELARLEAFSRAYRSSMRELVGSGRYDTQEDFSVVLQPFFQNIQLPVLADGLPDTSFFAPDCIHPNQKFHSQLARALWTNMLEPLGSKTETLDLRAEMPITCPTQNEPFLRTPRNSNYTYPIKPAIENWGSDFLCTEWKASNSVPTSVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTTLPNILKKFNPYLLGFSTSTWEGTAGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKDWKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSEELPRAFVNVVEVMELASLYQGQGGKCAMLAAQNNCTCLRHSQSSLEKQELKKVNWNLQHGISSFSYWHQYTQREDFAVVVQPFFQNTLTPLNERGDTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVGRKTTSNNFTHSRAKLKCPSPESPYLYTLRNSRLLPDQAEEAPEVLYWAVPVAAGVGLVVGIIGTVVWRCRRGGRREDPPMSLRTVAL
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
130SumoylationMPVCHTGKRVIPHDG
CCCCCCCCCCCCCCC
44.65-
130SumoylationMPVCHTGKRVIPHDG
CCCCCCCCCCCCCCC
44.65-
173N-linked_GlycosylationLINVFFSNASQCYLC
HHHHHCCCCCCEEEC
38.15-
240N-linked_GlycosylationSPAPEPCNCSEETTR
CCCCCCCCCCHHHHH
42.96UniProtKB CARBOHYD
464 (in isoform 2)Phosphorylation-43.5229083192
470 (in isoform 2)Phosphorylation-39.0829083192
472 (in isoform 2)Phosphorylation-3.5129083192
475 (in isoform 2)Phosphorylation-18.8529083192
493N-linked_GlycosylationRLVDLMKNDTRIHFQ
HHHHHHHCCCEEEEC
41.75UniProtKB CARBOHYD
529N-linked_GlycosylationLVHYSPQNFTDNIGK
HHCCCCCCCCCCHHH
45.21UniProtKB CARBOHYD
590N-linked_GlycosylationCVLKFDDNSTELATL
EEEECCCCCHHHHHH
53.31-
690N-linked_GlycosylationHKFENKINITCPNQV
CCCCCCCCCCCCCCH
25.73-
723PhosphorylationPCRDRAPSALHPTSV
ECCCCCCCCCCCCCC
42.3422673903
728PhosphorylationAPSALHPTSVHALRP
CCCCCCCCCCCCCCH
32.4122673903
729PhosphorylationPSALHPTSVHALRPA
CCCCCCCCCCCCCHH
19.1622673903
783N-linked_GlycosylationGGDGSLENVTTLPNI
CCCCCCHHHHCHHHH
41.55-
797N-linked_GlycosylationILREFNRNLTGYAVG
HHHHHHHCCCCEEEC
42.96UniProtKB CARBOHYD
809N-linked_GlycosylationAVGTGDANDTNAFLN
EECCCCCCCHHHHHH
62.47-
961PhosphorylationSMRELVGSGRYDTQE
HHHHHHCCCCCCCHH
16.7727251275
1017PhosphorylationQLARALWTNMLEPLG
HHHHHHHHHHCCCCC
16.1725954137
1029PhosphorylationPLGSKTETLDLRAEM
CCCCCCCEEEEEECC
30.7025954137
1055N-linked_GlycosylationLRTPRNSNYTYPIKP
CCCCCCCCCCCCCCC
36.39UniProtKB CARBOHYD
1113N-linked_GlycosylationTAVGARPNNSSDLPT
HHCCCCCCCCCCCCC
56.30-
1115PhosphorylationVGARPNNSSDLPTSW
CCCCCCCCCCCCCCC
31.6928842319
1116PhosphorylationGARPNNSSDLPTSWR
CCCCCCCCCCCCCCC
45.3428842319
1128PhosphorylationSWRGLSWSIGGDGNL
CCCCCEEECCCCCCC
14.15-
1139PhosphorylationDGNLETHTTLPNILK
CCCCCCCCCHHHHHH
37.13-
1140PhosphorylationGNLETHTTLPNILKK
CCCCCCCCHHHHHHH
32.39-
1192PhosphorylationLVERMKNSPDINLEK
HHHHHHCCCCCCCHH
20.5929743597
1275N-linked_GlycosylationAMLAAQNNCTCLRHS
HHHHHHCCCEECCCC
15.47-
1378N-linked_GlycosylationGRKTTSNNFTHSRAK
CCCCCCCCCCCCCCC
42.85-
1398PhosphorylationPESPYLYTLRNSRLL
CCCCCEEEECCCCCC
19.3524719451

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 PLB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLB1_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 PLB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CGAT2_HUMANCSGALNACT2physical
28514442
PERM_HUMANMPOphysical
28514442
WDR47_HUMANWDR47physical
28514442
GILT_HUMANIFI30physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPW_HUMANCCT6Bphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLB1_HUMAN

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Related Literatures of Post-Translational Modification

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