EXOC4_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EXOC4_DROME
• UniProt AC: Q9VNH6
• Protein Name: Exocyst complex component 4
• Gene Name: Sec8 {ECO:0000312|FlyBase:FBgn0266672}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 985
• Protein Description: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Involved in regulation of synaptic microtubule formation, and also regulation of synaptic growth and glutamate receptor trafficking. Does not appear to be required for basal neurotransmission..
• Protein Sequence: MDAPPPTKPPRGVKYGKDESAGCGFLVNVIKSLGFSETTEERQKEKQKIEAEFKRSDLRLNELVSRHDQQLTQVLPLFSQVSSEVTASRERIHAVKENLGVCKRLLQCRRDELRKMWMDAVQHKYVLEMLEQIQELRKVPQRVVGYTAKRQYLHASKALTDALTTLNGPLQAVEGLSDLRTDLQTRRQQLYQRLHEELVTQVYTNSANEALSSFQRTNSSRLNSSFTRGIGARRSTDRIEANARVRKALAEMAQSFDLDKAEVIEDADLIYPELSMSYFVAIIVESFGMLHKVPDSLETLRVQIQTELLNVVRHTTHQLSVSGATADTNPLLSLLEVIFKQFKAIAKTHSLLLKNYLSVGQKYSVVGPQPYDLTDFWAQAQSVLQLLLTDYLDIQNAAADESAQTGFSEPTSNINSYFLRRKVPSTKRSMFKFDKSSHVGTSNNSDAFKEHRRNASDASVDDNLAGQLGGSGKGSTSGLFPHEKKQREKILICTPDQSIITKVYLPLMGYIKEIENFMKCKPGQPCSLHDFLDNYIKDTFLTKGHNRNLQLTIESLSKNQDAWRTIISPEEIKALNLSRPLLQSTVMVERRLMETKNLIQDLPCYSEDLLKMVCALLKAYREICQAAYRGIVQPDSEDKRIYSVAWLKDEDISRFLKTLPNWTDLKTYSQKSRHNRKLHRGSFEPSEEESPLQVQQRNIREAEMLTSNLGEGGITQQEILVEISVLKELAILQESMEWFSCRVSEFANDLRRPLVNGLNAVPAECGADIAVKDGTIKVMTNLALEFDELANTCLLVLHLEVRVQCFHYLRSKSSVRTNSYVGSKDDILEPDRQVQVLTKRLSEMDEAFSATLHPRKTRYIFEGLAHLASRILIQASNYLEHIDQITVQRMCRNAIALQQTLSNITASREVALDQARHFYELLCMEPDEILNALLERGTQFSEMQLLNALQLSCKSFGITDANLLASYQQKLSDILGAKPSKGVVV

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
219	Phosphorylation	SSFQRTNSSRLNSSF HHHHHCCHHHCCCCC	19.07	27626673
224	Phosphorylation	TNSSRLNSSFTRGIG CCHHHCCCCCCCCCC	31.27	29892262
225	Phosphorylation	NSSRLNSSFTRGIGA CHHHCCCCCCCCCCC	29.57	22668510
227	Phosphorylation	SRLNSSFTRGIGARR HHCCCCCCCCCCCCC	29.90	29892262
235	Phosphorylation	RGIGARRSTDRIEAN CCCCCCCCCHHHHHH	29.16	19429919
236	Phosphorylation	GIGARRSTDRIEANA CCCCCCCCHHHHHHH	27.73	19429919
456	Phosphorylation	KEHRRNASDASVDDN HHHHHCCCCCCCCCC	36.94	19429919
459	Phosphorylation	RRNASDASVDDNLAG HHCCCCCCCCCCCCC	30.94	22668510
475	Phosphorylation	LGGSGKGSTSGLFPH CCCCCCCCCCCCCCC	23.92	19429919
476	Phosphorylation	GGSGKGSTSGLFPHE CCCCCCCCCCCCCCC	35.17	19429919
477	Phosphorylation	GSGKGSTSGLFPHEK CCCCCCCCCCCCCCH	34.89	19429919
682	Phosphorylation	NRKLHRGSFEPSEEE CCCCCCCCCCCCCCC	26.79	19429919
686	Phosphorylation	HRGSFEPSEEESPLQ CCCCCCCCCCCCCCH	50.90	22668510

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EXOC4_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EXOC4_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EXOC4_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EXD_DROME	exd	physical	14605208

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-235; SER-456; SER-459;SER-682 AND SER-686, AND MASS SPECTROMETRY.
PubMed: 18327897