TRPL_DROME - dbPTM
TRPL_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRPL_DROME
UniProt AC P48994
Protein Name Transient-receptor-potential-like protein
Gene Name trpl
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1124
Subcellular Localization Membrane
Multi-pass membrane protein . In the dark, there is 20 fold more rhabdomeral trpl protein forming plasma membrane channels than in the light. In the light, the protein translocates to an intracellular compartment. Protein levels remain unc
Protein Description A light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. Required for vision in the dark and in dim light. Binds calmodulin. Trp and trpl act together in the light response, although it is unclear whether as heteromultimers or distinct units. Also forms a functional cation channel with Trpgamma. Activated by fatty acids, metabolic stress, inositols and GTP-binding proteins..
Protein Sequence MGRKKKLPTGVSSGVSHASSAPKSVGGCCVPLGLPQPLLLEEKKFLLAVERGDMPNVRRILQKALRHQHININCMDPLGRRALTLAIDNENLEMVELLVVMGVETKDALLHAINAEFVEAVELLLEHEELIYKEGEPYSWQKVDINTAMFAPDITPLMLAAHKNNFEILRILLDRGAAVPVPHDIRCGCEECVRLTAEDSLRHSLSRVNIYRALCSPSLICLTSNDPIITAFQLSWELRNLALTEQECKSEYMDLRRQCQKFAVDLLDQTRTSNELAIILNYDPQMSSYEPGDRMSLTRLVQAISYKQKKFVAHSNIQQLLSSIWYDGLPGFRRKSIVDKVICIAQVAVLFPLYCLIYMCAPNCRTGQLMRKPFMKFLIHASSYLFFLFILILVSQRADDDFVRIFGTTRMKKELAEQELRQRGQTPSKLELIVVMYVIGFVWEEVQEIFAVGMKSYLRNMWNFIDFLRNSLYVSVMCLRAFAYIQQATEIARDPQMAYIPREKWHDFDPQLIAEGLFAAANVFSALKLVHLFSINPHLGPLQISLGRMVIDIVKFFFIYTLVLFAFACGLNQLLWYFAALEKSKCYVLPGGEADWGSHGDSCMKWRRFGNLFESSQSLFWASFGMVGLDDFELSGIKSYTRFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKFARTKLWMSYFEDSATLPPPFNVLPSVKWVIRIFRKSSKTIDRQRSKKRKEQEQFSEYDNIMRSLVWRYVAAMHRKFENNPVSEDDINEVKSEINTMRYEMLEIFENSGMDVSSANKKERQPRPRRIKVWERRLMKGFQVAPVQNGCELDAFGNVNGQGEMQEIKVESIPSKPAKETAKERFQRVARTVLLQSTTHKWNVVLRAAKDSQIGRCTKNERKSLQNLGRAIEEAKRLIMLNPGCPSGRESPIRIEFEDEKTSTLLELLNQISAEISDSEKPKIRPIWRPPLKTVPARAMAANNTRSLTAPELKISRKSSPAPTPTPTPGVSHTALSQFRNRELPLCPSKLIANSAPSAPTAPPKKSAPTAPTPTYKPTTHAPFSVEGGNRENTRASDGVRSDNSNFDIHVVDLDEKGGHLGRDNVSDISSIASTSPQRPKHRN
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
730PhosphorylationKTIDRQRSKKRKEQE
CHHHHHHHHHHHHHH
33.9027794539
1116PhosphorylationISSIASTSPQRPKHR
HHHHHCCCCCCCCCC
19.2827794539

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 TRPL_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRPL_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 TRPL_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRP_DROMEtrpgenetic
10557345
TRPL_DROMEtrplphysical
23687378
INAD_DROMEinaDphysical
9679151

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

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Related Literatures of Post-Translational Modification

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