NINAC_DROME - dbPTM
NINAC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NINAC_DROME
UniProt AC P10676
Protein Name Neither inactivation nor afterpotential protein C
Gene Name ninaC
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1501
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton. Nucleus . Membrane . Localizes in the cytoplasm or punctate structures within the nuclei in the absence of rtp. Co-localizes with rtp in the rhabdomere membrane.
Protein Description Required for photoreceptor cell function. The ninaC proteins combines putative serine/threonine-protein kinase and myosin activities. [PubMed: 2449973 Essential for the expression and stability of the rtp protein in the photoreceptors]
Protein Sequence MMYLPYAQLPDPTDKFEIYEEIAQGVNAKVFRAKELDNDRIVALKIQHYDEEHQVSIEEEYRTLRDYCDHPNLPEFYGVYKLSKPNGPDEIWFVMEYCAGGTAVDMVNKLLKLDRRMREEHIAYIIRETCRAAIELNRNHVLHRDIRGDNILLTKNGRVKLCDFGLSRQVDSTLGKRGTCIGSPCWMAPEVVSAMESREPDITVRADVWALGITTIELADGKPPFADMHPTRAMFQIIRNPPPTLMRPTNWSQQINDFISESLEKNAENRPMMVEMVEHPFLTELIENEDEMRSDIAEMLELSRDVKTLYKEPELFVDRGYVKRFDEKPEKMYPEDLAALENPVDENIIESLRHRILMGESYSFIGDILLSLNSNEIKQEFPQEFHAKYRFKSRSENQPHIFSVADIAYQDMLHHKEPQHIVLSGESYSGKSTNARLLIKHLCYLGDGNRGATGRVESSIKAILMLVNAGTPVNNDSTRCVLQYCLTFGKTGKMSGAVFNMYMLEKLRVATTDGTQHNFHIFYYFYDFINQQNQLKEYNLKADRNYRYLRVPPEVPPSKLKYRRDDPEGNVERYREFENILRDIDFNHKQLETVRKVLAAILNIGNIRFRQNGKYAEVENTDIVSRIAELLRVDEKKFMWSLTNFIMVKGGIAERRQYTTEEARDARDAVASTLYSRLVDFIINRINMNMSFPRAVFGDTNAIIIHDMFGFECFNRNGLEQLMINTLNEQMQYHYNQRIFISEMLEMEAEDIDTINLNFYDNKTALDNLLTKPDGLFYIIDDASRSCQDQDLIMDRVSEKHSQFVKKHTATEISVAHYTGRIIYDTRAFTDINRDFVPPEMIETFRSSLDESIMLMFTNQLTKAGNLTMPFEAVQHKDESERKSYALNTLSAGCISQVNNLRTLAANFRFTCLTLLKMLSQNANLGVHFVRCIRADLEYKPRSFHSDVVQQQMKALGVLDTVIARQKGFSSRLPFDEFLRRYQFLAFDFDEPVEMTKDNCRLLFLRLKMEGWALGKTKVFLRYYNDEFLARLYELQVKKVIKVQSMMRALLARKRVKGGKVFKLGKKGPEHHDVAASKIQKAFRGFRDRVRLPPLVNEKSGQLNENTADFIRPFAKKWREKSIFQVLLHYRAARFQDFVNLSQQVHIYNQRMVAGLNKCTRAVPFERINMREVNSSQLGPLPVPIKKMPFRLDQIPFYDTQYMVDPANSISRQAFPNQLLTQHMEDDEPWDSPLQRNPSMTSCALTYNAYKKEQACQTNWDRMGESDNIYNQGYFRDPQQLRRNQMQMNMNAYNNAYNSYNSNYNNQNWGVHRSGSRRNSLKGYAAPPPPPPPMPSSNYYRNNPNQQQRNYQQRSSYPPSDPVRELQNMARNEGDNSEDPPFNFKAMLRKTNYPRGSETNTYDFNNRRGSDSGDQHTFQPPKLRSTGRRYQDDEGYNSSSGNYGVSRKFGQQQRAPTLRQSPASVGRSFEDSNARSFEEAGSYVEEEIAPGITLSGYAVDI
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
172PhosphorylationGLSRQVDSTLGKRGT
CCCHHCCCCCCCCCE
27.0327794539
173PhosphorylationLSRQVDSTLGKRGTC
CCHHCCCCCCCCCEE
34.7627794539
183PhosphorylationKRGTCIGSPCWMAPE
CCCEECCCCCCCCHH
9.292449973
1410PhosphorylationDFNNRRGSDSGDQHT
CCCCCCCCCCCCCCC
27.1328490779
1412PhosphorylationNNRRGSDSGDQHTFQ
CCCCCCCCCCCCCCC
46.0628490779
1417PhosphorylationSDSGDQHTFQPPKLR
CCCCCCCCCCCCCCC
20.5228490779

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 NINAC_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NINAC_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 NINAC_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OPS3_DROMERh3genetic
18786361
CALM_DROMECamphysical
8235618
INAD_DROMEinaDphysical
23536301

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NINAC_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 SER-183, AND MASSSPECTROMETRY.

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