SEPT1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SEPT1_DROME
• UniProt AC: P42207
• Protein Name: Septin-1
• Gene Name: 1-Sep
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 361
• Protein Description: Involved in cytokinesis..
• Protein Sequence: MADTKGFSSIETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLVNSLFLTDLYPERIIPDAIEKQKQTVKLEASTVEIEERGVKLRLTVVDTPGFGDAIDNSNSFGAILEYIDEQYERFLRDESGLNRRNIVDNRIHCCFYFISPFGHGLKPLDVEFMKKLHSKVNIVPVIAKADCLTKKEILRLKCRIMQEIESHGIKIYPLPDCDSDEDEDYKEQVKQLKEAVPFAVCGANTLLEVKGKKVRGRLYPWGVVEVENPDHCDFIKLRTMLITHMQDLQEVTQEVHYENYRSDRLAKGIKGKENGVKAERDSSSQVVSNSVLGEKDRILQEKEAELRRMQEMLAQMQARMQAQQ

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
8	Phosphorylation	MADTKGFSSIETPGY CCCCCCCCCCCCCCC	38.79	21082442
9	Phosphorylation	ADTKGFSSIETPGYV CCCCCCCCCCCCCCC	23.37	21082442
12	Phosphorylation	KGFSSIETPGYVGFA CCCCCCCCCCCCCCC	21.97	19429919
15	Phosphorylation	SSIETPGYVGFANLP CCCCCCCCCCCCCCC	9.90	19429919
216	Phosphorylation	YPLPDCDSDEDEDYK EECCCCCCCCCHHHH	49.59	19429919
222	Phosphorylation	DSDEDEDYKEQVKQL CCCCCHHHHHHHHHH	17.87	22817900
319	Phosphorylation	GVKAERDSSSQVVSN CEECCCCCCCCCCHH	37.80	19429919
320	Phosphorylation	VKAERDSSSQVVSNS EECCCCCCCCCCHHH	29.13	19429919
321	Phosphorylation	KAERDSSSQVVSNSV ECCCCCCCCCCHHHH	30.83	19429919

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

Oops, there are no upstream regulatory protein records of SEPT1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SEPT1_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 SEPT1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SEPT2_DROME	Sep2	physical	14605208
EF1A1_DROME	Ef1alpha48D	physical	14605208
PNUT_DROME	pnut	physical	22036573
SEPT2_DROME	Sep2	physical	22036573
PNUT_DROME	pnut	physical	24633326
PNUT_DROME	pnut	physical	8590810
PNUT_DROME	pnut	physical	8636235
SEPT2_DROME	Sep2	physical	24633326
SEPT2_DROME	Sep2	physical	8636235
SEPT2_DROME	Sep2	physical	11884525

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-319, AND MASSSPECTROMETRY.
PubMed: 17372656