PGPLC_DROME - dbPTM
PGPLC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGPLC_DROME
UniProt AC Q9GNK5
Protein Name Peptidoglycan-recognition protein LC
Gene Name PGRP-LC
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 520
Subcellular Localization Membrane
Single-pass type II membrane protein .
Protein Description Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. [PubMed: 11872802]
Protein Sequence MPFSNETEMSQCSNAKRRVNDPLTGPKNCSTSSTDSGVILNDNVAAFRPEKETKDRGTGEGQFQSKSEEKTESKRISVEHTVNITTENVGKTSSPAVSIRSTTISVVSIDDNAIDSSSIDSDSEAEAEDYTVQKLGHQVTYPPNSSHLRDLNQGLTVISRHVAPGEAAVPPPNPLEAGIVAKQILNGNLAVATPTSPAGGATQGIGSIALTNSTDVTFGDKHFYEGPVTIQQFLIDNRDKWKPGEGPAGGQDNPAFNGGPSTNGSAPGSKHEDPAQTPPICPFLPNTVGRKAVTVTVVFVTLTFLLGIVLATTTNLFGKTLNQSKIRDDDDYRQNIPINSTIDLDNIGGGLILRFVERQQWLAQPPQKEIPDLELPVGLVIALPTNSENCSTQAICVLRVRLLQTYDIESSQKCDIAYNFLIGGDGNVYVGRGWNKMGAHMNNINYDSQSLSFAYIGSFKTIQPSAKQLSVTRLLLERGVKLGKIAPSYRFTASSKLMPSVTDFKADALYASFANWTHWS
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
77PhosphorylationKTESKRISVEHTVNI
CCCCCCEEEEEEEEE
26.0319429919
94PhosphorylationENVGKTSSPAVSIRS
CCCCCCCCCCEEEEE
23.3119429919
98PhosphorylationKTSSPAVSIRSTTIS
CCCCCCEEEEECEEE
17.8719429919
224PhosphorylationTFGDKHFYEGPVTIQ
EECCCCEEECCEEEE
21.5019429919
389N-linked_GlycosylationALPTNSENCSTQAIC
ECCCCCCCCCHHHEE
25.5116556841
461PhosphorylationAYIGSFKTIQPSAKQ
EEECCCCCCCCCHHH
23.8822817900
515N-linked_GlycosylationALYASFANWTHWS--
HHHHHHCCCCCCC--
42.0116556841

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 PGPLC_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGPLC_DROME !!

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 PGPLC_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JUPIT_DROMEJupiterphysical
23749869
ATPA_DROMEblwphysical
23749869
SODC_DROMESodphysical
23749869
HCF_DROMEHcfphysical
23749869
RS16_DROMERpS16physical
23749869
ATC1_DROMECa-P60Aphysical
23749869
HCD2_DROMEscuphysical
23749869
Y3800_DROMECG3800physical
23749869
HSP7D_DROMEHsc70-4physical
23749869
RS3_DROMERpS3physical
23749869
EF2_DROMEEF2physical
23749869
RL22_DROMERpL22physical
23749869
TBA2_DROMEalphaTub85Ephysical
23749869
TBA3_DROMEalphaTub84Dphysical
23749869
IF2A_DROMEeIF-2alphaphysical
23749869
CADF_DROMEtsrphysical
23749869
RS28_DROMERpS28bphysical
23749869
CH60_DROMEHsp60physical
23749869
RS20_DROMERpS20physical
23749869
STIM_DROMEStimphysical
23749869
TBA1_DROMEalphaTub84Bphysical
23749869
TCPG_DROMECctgammaphysical
23749869
CH60C_DROMEHsp60Cphysical
23749869
TAF6_DROMETaf6physical
23749869
CATL_DROMECp1physical
23749869
CATA_DROMECatphysical
23749869
CUP_DROMEcupphysical
23749869
HSP7E_DROMEHsc70-5physical
23749869
LIG_DROMEligphysical
23749869
EF1A2_DROMEEf1alpha100Ephysical
23749869
EF1A1_DROMEEf1alpha48Dphysical
23749869
ZASP_DROMEZasp52physical
23749869
ADT_DROMEsesBphysical
23749869
RS21_DROMERpS21physical
23749869
RL7A_DROMERpL7Aphysical
23749869
RS17_DROMERpS17physical
23749869
MSL3_DROMEmsl-3physical
23749869
GALE_DROMEGalephysical
23749869
PRDX1_DROMEJafrac1physical
23749869
NCD_DROMEncdphysical
23749869
PGPLC_DROMEPGRP-LCphysical
23749869
RS10B_DROMERpS10bphysical
23749869
GBLP_DROMERack1physical
23749869
NH2L1_DROMEhoipphysical
23749869
PGPSD_DROMEPGRP-SDphysical
27851910
PGPLC_DROMEPGRP-LCphysical
15657141

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

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure of tracheal cytotoxin in complex with a heterodimericpattern-recognition receptor.";
Chang C.-I., Chelliah Y., Borek D., Mengin-Lecreulx D.,Deisenhofer J.;
Science 311:1761-1764(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 355-520 IN COMPLEX WITHPEPTIDOGLYCAN FRAGMENT, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-389AND ASN-515.

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