dbPTM

FAS1_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FAS1_DROME
UniProt AC	P10674
Protein Name	Fasciclin-1
Gene Name	Fas1
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	652
Subcellular Localization	Cell membrane Lipid-anchor, GPI-anchor.
Protein Description	Neural cell adhesion molecule..
Protein Sequence	MLNAAALLLALLCAANAAAAADLADKLRDDSELSQFYSLLESNQIANSTLSLRSCTIFVPTNEAFQRYKSKTAHVLYHITTEAYTQKRLPNTVSSDMAGNPPLYITKNSNGDIFVNNARIIPSLSVETNSDGKRQIMHIIDEVLEPLTVKAGHSDTPNNPNALKFLKNAEEFNVDNIGVRTYRSQVTMAKKESVYDAAGQHTFLVPVDEGFKLSARSSLVDGKVIDGHVIPNTVIFTAAAQHDDPKASAAFEDLLKVTVSFFKQKNGKMYVKSNTIVGDAKHRVGVVLAEIVKANIPVSNGVVHLIHRPLMIIDTTVTQFLQSFKENAENGALRKFYEVIMDNGGAVLDDINSLTEVTILAPSNEAWNSSNINNVLRDRNKMRQILNMHIIKDRLNVDKIRQKNANLIAQVPTVNNNTFLYFNVRGEGSDTVITVEGGGVNATVIQADVAQTNGYVHIIDHVLGVPYTTVLGKLESDPMMSDTYKMGKFSHFNDQLNNTQRRFTYFVPRDKGWQKTELDYPSAHKKLFMADFSYHSKSILERHLAISDKEYTMKDLVKFSQESGSVILPTFRDSLSIRVEEEAGRYVIIWNYKKINVYRPDVECTNGIIHVIDYPLLEEKDVVVAGGSYLPESSICIILANLIMITVAKFLN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	N-linked_Glycosylation	LESNQIANSTLSLRS HHHCCCCCCEEECCC	36.84	-
164	Acetylation	PNNPNALKFLKNAEE CCCCCHHHHHHCHHH	46.36	21791702
368	N-linked_Glycosylation	APSNEAWNSSNINNV CCCCCCCCCCCHHHH	42.48	-
416	N-linked_Glycosylation	AQVPTVNNNTFLYFN EECCEECCCEEEEEE	44.58	-
441	N-linked_Glycosylation	TVEGGGVNATVIQAD EEECCCEEEEEEECC	32.92	12575939
493	N-linked_Glycosylation	MGKFSHFNDQLNNTQ CCCCCCCHHHCCCCE	30.60	19349973
497	N-linked_Glycosylation	SHFNDQLNNTQRRFT CCCHHHCCCCEECEE	43.82	17893096
625	GPI-anchor	EEKDVVVAGGSYLPE CCCCEEEECCCCCCH	12.67	-

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 FAS1_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FAS1_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 FAS1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
APLP_DROME	Rfabg	physical	15875013

Drug and Disease Associations

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

Regulatory Network of FAS1_DROME

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Novel fold revealed by the structure of a FAS1 domain pair from theinsect cell adhesion molecule fasciclin I."; Clout N.J., Tisi D., Hohenester E.; Structure 11:197-203(2003). Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 314-628, AND GLYCOSYLATION ATASN-441.	12575939 [Abstract]
"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-493 AND ASN-497, AND MASSSPECTROMETRY.	19349973 [Abstract]
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster."; Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.; Glycobiology 17:1388-1403(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497, AND MASSSPECTROMETRY.	17893096 [Abstract]