SEM2A_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SEM2A_DROME
• UniProt AC: Q24323
• Protein Name: Semaphorin-2A {ECO:0000312|FlyBase:FBgn0011260}
• Gene Name: Sema2a {ECO:0000312|FlyBase:FBgn0011260}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 724
• Subcellular Localization: Secreted .
• Protein Description: Plays a role in growth cones guidance. Required for both proper adult behavior and survival. Can function in vivo as a selective target-derived signal that inhibits the formation of specific synaptic terminal arbors..
• Protein Sequence: MSLLQLSPLLALLLLLCSSVSETAADYENTWNFYYERPCCTGNDQGNNNYGKHGADHVREFNCGKLYYRTFHMNEDRDTLYVGAMDRVFRVNLQNISSSNCNRDVINLEPTRDDVVSCVSKGKSQIFDCKNHVRVIQSMDQGDRLYVCGTNAHNPKDYVIYANLTHLPRSEYVIGVGLGIAKCPYDPLDNSTAIYVENGNPGGLPGLYSGTNAEFTKADTVIFRTDLYNTSAKRLEYKFKRTLKYDSKWLDKPNFVGSFDIGEYVYFFFRETAVEYINCGKAVYSRIARVCKKDVGGKNLLAHNWATYLKARLNCSISGEFPFYFNEIQSVYQLPSDKSRFFATFTTSTNGLIGSAVCSFHINEIQAAFNGKFKEQSSSNSAWLPVLNSRVPEPRPGTCVNDTSNLPDTVLNFIRSHPLMDKAVNHEHNNPVYYKRDLVFTKLVVDKIRIDILNQEYIVYYVGTNLGRIYKIVQYYRNGESLSKLLDIFEVAPNEAIQVMEISQTRKSLYIGTDHRIKQIDLAMCNRRYDNCFRCVRDPYCGWDKEANTCRPYELDLLQDVANETSDICDSSVLKKKIVVTYGQSVHLGCFVKIPEVLKNEQVTWYHHSKDKGRYEIRYSPTKYIETTERGLVVVSVNEADGGRYDCHLGGSLLCSYNITVDAHRCTPPNKSNDYQKIYSDWCHEFEKYKTAMKSWEKKQAQCSTRQNFSSNQHPNEIFRKPNV

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
95	N-linked_Glycosylation	VFRVNLQNISSSNCN EEEEECCCCCCCCCC	39.00	19349973
163	N-linked_Glycosylation	KDYVIYANLTHLPRS CCEEEEEECCCCCCC	28.62	-
190	N-linked_Glycosylation	CPYDPLDNSTAIYVE CCCCCCCCCEEEEEE	49.28	-
229	N-linked_Glycosylation	IFRTDLYNTSAKRLE EEEEECCCCCCHHHH	34.55	-
314	N-linked_Glycosylation	TYLKARLNCSISGEF HHHHHHHCCEECCCC	16.37	-
401	N-linked_Glycosylation	PRPGTCVNDTSNLPD CCCCCCCCCCCCCCH	49.33	-
563	N-linked_Glycosylation	DLLQDVANETSDICD HHHHHHHHHCCCCCC	53.58	-
658	N-linked_Glycosylation	GSLLCSYNITVDAHR CEEEEEEEEEEECCC	13.73	-
670	N-linked_Glycosylation	AHRCTPPNKSNDYQK CCCCCCCCCCCCHHH	62.69	-
708	N-linked_Glycosylation	AQCSTRQNFSSNQHP HHHHCCCCCCCCCCC	35.16	-

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

Oops, there are no upstream regulatory protein records of SEM2A_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SEM2A_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 SEM2A_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACTZ_DROME	Arp1	physical	14605208
SRC64_DROME	Src64B	physical	14605208
NETA_DROME	NetA	genetic	9604933
PLXB_DROME	PlexB	genetic	17109838
PLXB_DROME	PlexB	genetic	16672342
PLXB_DROME	PlexB	physical	21521614

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95, AND MASS SPECTROMETRY.
PubMed: 19349973