dbPTM

NRG_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NRG_DROME
UniProt AC	P20241
Protein Name	Neuroglian
Gene Name	Nrg
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1302
Subcellular Localization	Cell membrane Single-pass type I membrane protein. Cell junction, tight junction.
Protein Description	The long isoform may play a role in neural and glial cell adhesion in the developing embryo. The short isoform may be a more general cell adhesion molecule involved in other tissues and imaginal disk morphogenesis. Vital for embryonic development. Essential for septate junctions. Septate junctions, which are the equivalent of vertebrates tight junctions, are characterized by regular arrays of transverse structures that span the intermembrane space and form a physical barrier to diffusion. Required for the blood-brain barrier formation..
Protein Sequence	MWRQSTILAALLVALLCAGSAESKGNRPPRITKQPAPGELLFKVAQQNKESDNPFIIECEADGQPEPEYSWIKNGKKFDWQAYDNRMLRQPGRGTLVITIPKDEDRGHYQCFASNEFGTATSNSVYVRKAELNAFKDEAAKTLEAVEGEPFMLKCAAPDGFPSPTVNWMIQESIDGSIKSINNSRMTLDPEGNLWFSNVTREDASSDFYYACSATSVFRSEYKIGNKVLLDVKQMGVSASQNKHPPVRQYVSRRQSLALRGKRMELFCIYGGTPLPQTVWSKDGQRIQWSDRITQGHYGKSLVIRQTNFDDAGTYTCDVSNGVGNAQSFSIILNVNSVPYFTKEPEIATAAEDEEVVFECRAAGVPEPKISWIHNGKPIEQSTPNPRRTVTDNTIRIINLVKGDTGNYGCNATNSLGYVYKDVYLNVQAEPPTISEAPAAVSTVDGRNVTIKCRVNGSPKPLVKWLRASNWLTGGRYNVQANGDLEIQDVTFSDAGKYTCYAQNKFGEIQADGSLVVKEHTRITQEPQNYEVAAGQSATFRCNEAHDDTLEIEIDWWKDGQSIDFEAQPRFVKTNDNSLTIAKTMELDSGEYTCVARTRLDEATARANLIVQDVPNAPKLTGITCQADKAEIHWEQQGDNRSPILHYTIQFNTSFTPASWDAAYEKVPNTDSSFVVQMSPWANYTFRVIAFNKIGASPPSAHSDSCTTQPDVPFKNPDNVVGQGTEPNNLVISWTPMPEIEHNAPNFHYYVSWKRDIPAAAWENNNIFDWRQNNIVIADQPTFVKYLIKVVAINDRGESNVAAEEVVGYSGEDRPLDAPTNFTMRQITSSTSGYMAWTPVSEESVRGHFKGYKIQTWTENEGEEGLREIHVKGDTHNALVTQFKPDSKNYARILAYNGRFNGPPSAVIDFDTPEGVPSPVQGLDAYPLGSSAFMLHWKKPLYPNGKLTGYKIYYEEVKESYVGERREYDPHITDPRVTRMKMAGLKPNSKYRISITATTKMGEGSEHYIEKTTLKDAVNVAPATPSFSWEQLPSDNGLAKFRINWLPSTEGHPGTHFFTMHRIKGETQWIRENEEKNSDYQEVGGLDPETAYEFRVVSVDGHFNTESATQEIDTNTVEGPIMVANETVANAGWFIGMMLALAFIIILFIIICIIRRNRGGKYDVHDRELANGRRDYPEEGGFHEYSQPLDNKSAGRQSVSSANKPGVESDTDSMAEYGDGDTGQFTEDGSFIGQYVPGKLQPPVSPQPLNNSAAAHQAAPTAGGSGAAGSAAAAGASGGASSAGGAAASNGGAAAGAVATYV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
182	N-linked_Glycosylation	DGSIKSINNSRMTLD CCCEEEECCCCCEEC	47.73	-
198	N-linked_Glycosylation	EGNLWFSNVTREDAS CCCEEEEECCCCCCC	29.70	17893096
411	N-linked_Glycosylation	DTGNYGCNATNSLGY CCCCCCCCCCCCCCE	45.49	17893096
414	N-linked_Glycosylation	NYGCNATNSLGYVYK CCCCCCCCCCCEEEE	32.59	19349973
448	N-linked_Glycosylation	VSTVDGRNVTIKCRV EEEECCCCEEEEEEE	40.59	-
652	N-linked_Glycosylation	LHYTIQFNTSFTPAS EEEEEEECCCCCCCC	20.59	7512815
683	N-linked_Glycosylation	VQMSPWANYTFRVIA EEECCCCCEEEEEEE	32.29	7512815
821	N-linked_Glycosylation	RPLDAPTNFTMRQIT CCCCCCCCCEEEEEC	29.36	-
1125	N-linked_Glycosylation	EGPIMVANETVANAG CCCEEECCCHHHCHH	33.78	-
1211	Phosphorylation	KPGVESDTDSMAEYG CCCCCCCCCCCCCCC	38.97	18327897
1211 (in isoform 2)	Phosphorylation	-	38.97	18327897
1213	Phosphorylation	GVESDTDSMAEYGDG CCCCCCCCCCCCCCC	23.22	18327897
1213 (in isoform 2)	Phosphorylation	-	23.22	18327897
1235	Phosphorylation	DGSFIGQYVPGKLQP CCCEECCCCCCCCCC	11.91	11719549
1289	Phosphorylation	SAGGAAASNGGAAAG CHHCCHHCCCCCCCC	31.14	22817900

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 NRG_DROME !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAD6_DROME	Ak6	physical	14605208
FAS2_DROME	Fas2	genetic	15607949
FAS3_DROME	Fas3	genetic	25135978
EVE_DROME	eve	genetic	24560702
EGFR_DROME	Egfr	genetic	11163263
EGFR_DROME	Egfr	genetic	14718570
FGFR1_DROME	htl	genetic	11163263
41_DROME	cora	physical	12782686
NRX4_DROME	Nrx-IV	physical	12782686
NRX4_DROME	Nrx-IV	physical	16554482
CONT_DROME	Cont	physical	16554482

Drug and Disease Associations

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

Regulatory Network of NRG_DROME

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of tandem type III fibronectin domains fromDrosophila neuroglian at 2.0 A."; Huber A.H., Wang Y.-M.E., Bieber A.J., Bjorkman P.J.; Neuron 12:717-731(1994). Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 610-814, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-652 AND ASN-683.	7512815 [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-411 AND ASN-414, 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-198 AND ASN-411, AND MASSSPECTROMETRY.	17893096 [Abstract]