LIG_DROME - dbPTM
LIG_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIG_DROME
UniProt AC Q86S05
Protein Name Protein lingerer
Gene Name lig {ECO:0000312|EMBL:AAO23023.1, ECO:0000312|FlyBase:FBgn0020279}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1375
Subcellular Localization Cytoplasm . Found in the cytoplasm of many neuronal and glial cells in the brain and ventral ganglion, and in imaginal disks.
Protein Description Acts in the nervous system to mediate the control of copulatory organs during courtship..
Protein Sequence MSTQTRSGGGGGGGHARNQKKSNASNSGGGGTGHHDGVSHAAAAGKKGGQDASKTDKPEKAQPKATTEQLRIAQITNSTTEDPQINEKVLLLLTMTQRSEEEVCCALNECDYDLEAAANFLIEELPQGAFAKYEKKRKNKAANNTADGAAGDGDWADGNGNADRREKSRNRSSNRGGTRGSSDSRGWRGRETRENERNQRESREPWSGQNAGQDRGDDRANDNYRGQRNGGGRSGPGGGGRGGGFVSRSGRGGGRMGGRTGGPRGDRGSGGPGGAYGSGRGGNANEDHHEVELWDNTIAQNAEKQQQAHDDAWGDWNNEEYEGSLKDSKVFTTSNLATQSAANVVSGTGASVTAVPAAAGTEISAPPGLEHQLVQQGSHLEESSSSGPAAVTPPATLSGSATTPLLQYSAAVSNPPPQLQSQGTQSGAGTGASAAAGGGAGSTPSSFVSASPDTFSSAASAAATLVHQAQKQQQLQQQTTPIKPSATLSVEQSQYFNSLASQGVSPGSVPVQSAPAGYAQNPVAAYSQTSTSVGVSQYPNTYANVFASGTAAGAGTAEQSQQQPQIRRARVKLPPPSKIPASAVEMPGDNALNNIGYLDVQFGALDFGTDDGFEPLPEKVGSGFSIDGQQQQQQPDDYQSKSQQQQQVTLAAGLQSSQISDALNAAGYTSRSTSQQQQGVSSAVNATIDQLTKSDPYGQTGGSGNAYQNAYQSSGASKTASGFPTTAPGGYSSSTYANVQSSVANSYQQQGYGSYQPSSYQQQAGSGAQSGTGAVSGGGGTATQNIPVGGSSSQNSTSGNASSAYLTSGYSTPQSAYQSSQSVYGNTGLSNSSGFSGSASNASSQYANFSASAKLKDATTASSAAHYDSVSTSSGVSSNSGSTGNGGVVSGQTGANQAAVSNNNSVSGSSSVSNVTAGVASGNVAGVGGGVSQSGVSSGVGVPGGSASSVGVNVNNNSSSASSVGAATVAQTATGTTAAVLASLTNKNTSSSNSSGSGGSAATTTGNASGQGAGASTGGVGSSSGAGGAGSGGGSGSGLVPTNIQMVSQYIQTGLPYYQQPVYSYEELQMMQQRVPHVQGYYDLNYPPASLGAGRDNLGSVTYSAMNDGRFARTDNNSSPVGNVSSTMSQQAGSSAPMLNVPYAYFYGGNVMPGSFQYGTPAIYPQIPAANTASGQQFPKPSYSAGYGSTSYDTLSQTTQDYSKGGYSSSVNQQSKTQTVSNQSQAGTGSDLTSSMYGKGHVALNKVNSYEKQSFHSGTPPPFNMPNTQTAGGTSAQPYGMYLPMPAAGHHNMIHQPIHQVHSELPLQVVVGGGTESHVLIHGNVNGPQVTYHRIWQTEPVQCQNQLVAAHCNNFEPNIDCCVHDNNNDLSFFAD
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
22PhosphorylationHARNQKKSNASNSGG
CCCCCCCCCCCCCCC		44.6719429919
25PhosphorylationNQKKSNASNSGGGGT
CCCCCCCCCCCCCCC		35.4619429919
27PhosphorylationKKSNASNSGGGGTGH
CCCCCCCCCCCCCCC		36.0021082442
32PhosphorylationSNSGGGGTGHHDGVS
CCCCCCCCCCCCCHH		36.2921082442
55PhosphorylationGGQDASKTDKPEKAQ
CCCCCCCCCCCCCCC		46.9222817900
78PhosphorylationRIAQITNSTTEDPQI
HHHHHCCCCCCCHHH		28.2321082442
202PhosphorylationNERNQRESREPWSGQ
HHHHHHHHCCCCCCC		44.1022817900
269PhosphorylationGPRGDRGSGGPGGAY
CCCCCCCCCCCCCCC		41.2819429919
276PhosphorylationSGGPGGAYGSGRGGN
CCCCCCCCCCCCCCC		18.3318281928
278PhosphorylationGPGGAYGSGRGGNAN
CCCCCCCCCCCCCCC		16.7925749252
321PhosphorylationGDWNNEEYEGSLKDS
CCCCCCCCCCCCCCC		21.2922817900
324PhosphorylationNNEEYEGSLKDSKVF
CCCCCCCCCCCCCEE		21.9519429919
479PhosphorylationQQQLQQQTTPIKPSA
HHHHHHCCCCCCCCC		30.1519429919
480PhosphorylationQQLQQQTTPIKPSAT
HHHHHCCCCCCCCCE		20.7619429919
622PhosphorylationPLPEKVGSGFSIDGQ
CCCCCCCCCCCCCCC		39.3919429919
625PhosphorylationEKVGSGFSIDGQQQQ
CCCCCCCCCCCCCCC		24.2419429919
670PhosphorylationLNAAGYTSRSTSQQQ
HHHCCCCCCCHHHHH		18.7521082442
672PhosphorylationAAGYTSRSTSQQQQG
HCCCCCCCHHHHHHH		31.9819429919
673PhosphorylationAGYTSRSTSQQQQGV
CCCCCCCHHHHHHHH		29.4619429919
674PhosphorylationGYTSRSTSQQQQGVS
CCCCCCHHHHHHHHH		27.5219429919
697PhosphorylationQLTKSDPYGQTGGSG
HHHHCCCCCCCCCCC		27.1918281928
707PhosphorylationTGGSGNAYQNAYQSS
CCCCCCHHHHHHHCC		13.2918281928
711PhosphorylationGNAYQNAYQSSGASK
CCHHHHHHHCCCCCC		19.2418281928
1082PhosphorylationVPHVQGYYDLNYPPA
CCCCCCCCCCCCCCH		22.3018281928
1090PhosphorylationDLNYPPASLGAGRDN
CCCCCCHHHCCCCCC		32.8621082442
1207PhosphorylationQDYSKGGYSSSVNQQ
CCHHCCCCCCCCCCC		17.6618281928
1210PhosphorylationSKGGYSSSVNQQSKT
HCCCCCCCCCCCCCC		21.1022817900
1233PhosphorylationAGTGSDLTSSMYGKG
CCCCCCCCHHHHCCC		24.6021082442
1237PhosphorylationSDLTSSMYGKGHVAL
CCCCHHHHCCCEEEE		20.0318281928
1249PhosphorylationVALNKVNSYEKQSFH
EEECCCCCCCCCCCC		37.3425749252
1250PhosphorylationALNKVNSYEKQSFHS
EECCCCCCCCCCCCC		23.1818281928
1313 (in isoform 2)Phosphorylation-28.3919429919
1323 (in isoform 3)Phosphorylation-32.5519429919
1324 (in isoform 3)Phosphorylation-15.2119429919
1326 (in isoform 3)Phosphorylation-61.5019429919
1327 (in isoform 3)Phosphorylation-15.1019429919
1334 (in isoform 2)Phosphorylation-22.7919429919
1335 (in isoform 2)Phosphorylation-1.7219429919
1337 (in isoform 2)Phosphorylation-33.3519429919
1338 (in isoform 2)Phosphorylation-27.5319429919
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 LIG_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIG_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 LIG_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNE_DROMECycEgenetic
23874212
DIAP1_DROMEthgenetic
23874212
SAV_DROMEsavphysical
26117838
FMR1_DROMEFmr1physical
23874212
FMR1_DROMEFmr1physical
26117838
FMR1_DROMEFmr1physical
24913805
ORB2_DROMEorb2physical
24913805
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIG_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321 AND SER-324, ANDMASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; THR-673 ANDSER-674, AND MASS SPECTROMETRY.

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