dbPTM

NPTN_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NPTN_MOUSE
UniProt AC	P97300
Protein Name	Neuroplastin
Gene Name	Nptn
Organism	Mus musculus (Mouse).
Sequence Length	397
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Enriched at postsynaptic density..
Protein Description	Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity)..
Protein Sequence	MSGSSLPGALALSLLLVSGSLLPGPGAAQNAGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQATISVLQKPRIVTSEEVIIRESLLPVTLQCNLTSSSHTLMYSYWTRNGVELTATRKNASNMEYRINKPRAEDSGEYHCVYHFVSAPKANATIEVKAAPDITGHKRSENKNEGQDAMMYCKSVGYPHPEWIWRKKENGVFEEISNSSGRFFITNKENYTELSIVNLQITEDPGEYECNATNSIGSASVSTVLRVRSHLAPLWPFLGILAEIIILVVIIVVYEKRKRPDEVPDDDEPAGPMKTNSTNNHKDKNLRQRNTN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
147	Ubiquitination	ATISVLQKPRIVTSE EEEEECCCCCEECCC	31.91	27667366
170	N-linked_Glycosylation	LPVTLQCNLTSSSHT CCEEEEEECCCCCCE	33.13	-
186	N-linked_Glycosylation	MYSYWTRNGVELTAT EEEEEECCCEEEEEE	52.03	19656770
196	N-linked_Glycosylation	ELTATRKNASNMEYR EEEEEECCCCCCEEE	45.36	19656770
199	N-linked_Glycosylation	ATRKNASNMEYRINK EEECCCCCCEEEECC	25.54	19656770
217	S-nitrosylation	EDSGEYHCVYHFVSA HHCCCEEEEEEEEEC	2.96	24895380
228	N-linked_Glycosylation	FVSAPKANATIEVKA EEECCCCCCEEEEEE	43.68	19656770
275	N-linked_Glycosylation	WIWRKKENGVFEEIS HHEEECCCCCEEEEE	61.89	19656770
283	N-linked_Glycosylation	GVFEEISNSSGRFFI CCEEEEECCCCCEEE	45.95	16944957
295	N-linked_Glycosylation	FFITNKENYTELSIV EEEECCCCCEEEEEE	51.11	-
316	N-linked_Glycosylation	DPGEYECNATNSIGS CCCCEEECCCCCCCC	37.55	-
380	Phosphorylation	EPAGPMKTNSTNNHK CCCCCCCCCCCCCHH	28.31	25266776
382	Phosphorylation	AGPMKTNSTNNHKDK CCCCCCCCCCCHHHC	37.43	23375375
396	Phosphorylation	KNLRQRNTN------ CCCHHHCCC------	44.48	22324799

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 NPTN_MOUSE !!

Functions of PTM Sites

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

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 NPTN_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NPTN_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of NPTN_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-228; ASN-275 AND ASN-283,AND MASS SPECTROMETRY.	19349973 [Abstract]
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation."; Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.; Mol. Cell. Proteomics 8:2555-2569(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186; ASN-196; ASN-199;ASN-228; ASN-275 AND ASN-283, AND MASS SPECTROMETRY.	19656770 [Abstract]
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography."; Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.; J. Proteome Res. 5:2438-2447(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-283, AND MASSSPECTROMETRY.	16944957 [Abstract]