NMDA1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NMDA1_DROME
• UniProt AC: Q24418
• Protein Name: Glutamate [NMDA] receptor subunit 1 {ECO:0000303|PubMed:15823532}
• Gene Name: Nmdar1 {ECO:0000312|EMBL:AAF52016.1, ECO:0000312|FlyBase:FBgn0010399}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 997
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein . Cell junction, synapse, postsynaptic cell membrane . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density .
• Protein Description: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors. Plays a role in associative learning and in long-term memory consolidation..
• Protein Sequence: MAMAEFVFCRPLFGLAIVLLVAPIDAAQRHTASDNPSTYNIGGVLSNSDSEEHFSTTIKHLNFDQQYVPRKVTYYDKTIRMDKNPIKTVFNVCDKLIENRVYAVVVSHEQTSGDLSPAAVSYTSGFYSIPVIGISSRDAAFSDKNIHVSFLRTVPPYYHQADVWLEMLSHFAYTKVIIIHSSDTDGRAILGRFQTTSQTYYDDVDVRATVELIVEFEPKLESFTEHLIDMKTAQSRVYLMYASTEDAQVIFRDAGEYNMTGEGHVWIVTEQALFSNNTPDGVLGLQLEHAHSDKGHIRDSVYVLASAIKEMISNETIAEAPKDCGDSAVNWESGKRLFQYLKSRNITGETGQVAFDDNGDRIYAGYDVINIREQQKKHVVGKFSYDSMRAKMRMRINDSEIIWPGKQRRKPEGIMIPTHLRLLTIEEKPFVYVRRMGDDEFRCEPDERPCPLFNNSDATANEFCCRGYCIDLLIELSKRINFTYDLALSPDGQFGHYILRNNTGAMTLRKEWTGLIGELVNERADMIVAPLTINPERAEYIEFSKPFKYQGITILEKKPSRSSTLVSFLQPFSNTLWILVMVSVHVVALVLYLLDRFSPFGRFKLSHSDSNEEKALNLSSAVWFAWGVLLNSGIGEGTPRSFSARVLGMVWAGFAMIIVASYTANLAAFLVLERPKTKLSGINDARLRNTMENLTCATVKGSSVDMYFRRQVELSNMYRTMEANNYATAEQAIQDVKKGKLMAFIWDSSRLEYEASKDCELVTAGELFGRSGYGIGLQKGSPWTDAVTLAILEFHESGFMEKLDKQWIFHGHVQQNCELFEKTPNTLGLKNMAGVFILVGVGIAGGVGLIIIEVIYKKHQVKKQKRLDIARHAADKWRGTIEKRKTIRASLAMQRQYNVGLNSTHAPGTISLAVDKRRYPRLGQRLGPERAWPGDAADVLRIRRPYELGNPGQSPKVMAANQPGMPMPMLGKTRPQQSVLPPRYSPGYTSDVSHLVV

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
258	N-linked_Glycosylation	FRDAGEYNMTGEGHV EECCCCCCCCCCEEE	19.76	-
314	N-linked_Glycosylation	AIKEMISNETIAEAP HHHHHHCCCCHHHCC	39.23	-
345	N-linked_Glycosylation	FQYLKSRNITGETGQ HHHHHHCCCCCCCCC	43.17	-
384	Phosphorylation	KHVVGKFSYDSMRAK HHEEEECCHHHHHHH	31.36	22817900
385	Phosphorylation	HVVGKFSYDSMRAKM HEEEECCHHHHHHHH	18.37	22817900
387	Phosphorylation	VGKFSYDSMRAKMRM EEECCHHHHHHHHEE	11.26	22817900
397	N-linked_Glycosylation	AKMRMRINDSEIIWP HHHEECCCCCCCCCC	36.07	-
454	N-linked_Glycosylation	ERPCPLFNNSDATAN CCCCCCCCCCCCCCC	55.57	-
481	N-linked_Glycosylation	IELSKRINFTYDLAL HHHHHHCCEEEEEEE	27.52	-
501	N-linked_Glycosylation	FGHYILRNNTGAMTL CCEEEEECCCCCCEE	47.14	-
693	N-linked_Glycosylation	RLRNTMENLTCATVK HHHHHHHCCEEEEEC	29.81	17893096
919	Phosphorylation	LAVDKRRYPRLGQRL EEEECCCCCCHHHHC	9.20	22817900

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

Oops, there are no upstream regulatory protein records of NMDA1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NMDA1_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 NMDA1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CYA1_DROME	rut	genetic	20015341

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-693, AND MASSSPECTROMETRY.
PubMed: 17893096