NPTN_HUMAN - dbPTM
NPTN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NPTN_HUMAN
UniProt AC Q9Y639
Protein Name Neuroplastin
Gene Name NPTN
Organism Homo sapiens (Human).
Sequence Length 398
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 MSGSSLPSALALSLLLVSGSLLPGPGAAQNAGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQATISVLQKPRIVTSEEVIIRDSPVLPVTLQCNLTSSSHTLTYSYWTKNGVELSATRKNASNMEYRINKPRAEDSGEYHCVYHFVSAPKANATIEVKAAPDITGHKRSENKNEGQDATMYCKSVGYPHPDWIWRKKENGMPMDIVNTSGRFFIINKENYTELNIVNLQITEDPGEYECNATNAIGSASVVTVLRVRSHLAPLWPFLGILAEIIILVVIIVVYEKRKRPDEVPDDDEPAGPMKTNSTNNHKDKNLRQRNTN
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 Orthologous
Protein Cluster
74PhosphorylationAEVNRAESFRQLWDG
EECHHHHHHHHHHHC		25.4129523821
81N-linked_GlycosylationSFRQLWDGARKRRVT
HHHHHHHCCCCCCEE		18.7219349973
95PhosphorylationTVNTAYGSNGVSVLR
EEEECCCCCCEEEEE		20.1023898821
113N-linked_GlycosylationLTLEDSGTYECRASN
EEECCCCEEEEECCC		21.7919349973
113N-linked_GlycosylationLTLEDSGTYECRASN
EEECCCCEEEEECCC		21.7919349973
119UbiquitinationGTYECRASNDPKRND
CEEEEECCCCCCCCC		23.5521963094
119 (in isoform 3)Ubiquitination-23.5521906983
119 (in isoform 1)Ubiquitination-23.5521906983
128UbiquitinationDPKRNDLRQNPSITW
CCCCCCCCCCCCCEE		36.7727667366
133UbiquitinationDLRQNPSITWIRAQA
CCCCCCCCEEEEEEE		3.7921963094
144 (in isoform 1)Ubiquitination-6.08-
144UbiquitinationRAQATISVLQKPRIV
EEEEEEEECCCCEEE		6.0821963094
153PhosphorylationQKPRIVTSEEVIIRD
CCCEEEECCEEEECC		22.3623403867
160N-linked_GlycosylationSEEVIIRDSPVLPVT
CCEEEECCCCCCEEE		47.0519349973
168N-linked_GlycosylationSPVLPVTLQCNLTSS
CCCCEEEEEEECCCC		5.7919349973
168N-linked_GlycosylationSPVLPVTLQCNLTSS
CCCCEEEEEEECCCC		5.7919349973
171N-linked_GlycosylationLPVTLQCNLTSSSHT
CEEEEEEECCCCCCE		33.13UniProtKB CARBOHYD
180N-linked_GlycosylationTSSSHTLTYSYWTKN
CCCCCEEEEEEEECC		16.1619159218
197N-linked_GlycosylationELSATRKNASNMEYR
EEEEEECCCCCCEEE		45.36UniProtKB CARBOHYD
199PhosphorylationSATRKNASNMEYRIN
EEEECCCCCCEEEEC		46.2121406692
203PhosphorylationKNASNMEYRINKPRA
CCCCCCEEEECCCCH		13.1621406692
216PhosphorylationRAEDSGEYHCVYHFV
CHHHCCCEEEEEEEE		12.2127642862
218GlutathionylationEDSGEYHCVYHFVSA
HHCCCEEEEEEEEEC		2.9622555962
220PhosphorylationSGEYHCVYHFVSAPK
CCCEEEEEEEEECCC		8.5727642862
229N-linked_GlycosylationFVSAPKANATIEVKA
EEECCCCCCEEEEEE		43.6817660510
235 (in isoform 2)Ubiquitination-26.4921906983
235 (in isoform 4)Ubiquitination-26.4921906983
235UbiquitinationANATIEVKAAPDITG
CCCEEEEEECCCCCC		26.4921906983
244UbiquitinationAPDITGHKRSENKNE
CCCCCCCCCCCCCCC		59.9927667366
2442-HydroxyisobutyrylationAPDITGHKRSENKNE
CCCCCCCCCCCCCCC		59.99-
246UbiquitinationDITGHKRSENKNEGQ
CCCCCCCCCCCCCCC		50.7723503661
248UbiquitinationTGHKRSENKNEGQDA
CCCCCCCCCCCCCCC		54.4127667366
248 (in isoform 1)Ubiquitination-54.4121906983
249UbiquitinationGHKRSENKNEGQDAT
CCCCCCCCCCCCCCC		52.9321963094
259GlutathionylationGQDATMYCKSVGYPH
CCCCCHHHHHCCCCC		1.5122555962
260UbiquitinationQDATMYCKSVGYPHP
CCCCHHHHHCCCCCC		30.5921963094
276N-linked_GlycosylationWIWRKKENGMPMDIV
HHEEECCCCCCCEEE		62.03-
284N-linked_GlycosylationGMPMDIVNTSGRFFI
CCCCEEEECCCCEEE		28.9419159218
285PhosphorylationMPMDIVNTSGRFFII
CCCEEEECCCCEEEE		22.9727134283
286PhosphorylationPMDIVNTSGRFFIIN
CCEEEECCCCEEEEE		23.8327134283
296N-linked_GlycosylationFFIINKENYTELNIV
EEEEECCCCCEEEEE		51.1119159218
317N-linked_GlycosylationDPGEYECNATNAIGS
CCCCCEECCCCCCCC		37.55UniProtKB CARBOHYD
362UbiquitinationVIIVVYEKRKRPDEV
HHHHHHHHCCCCCCC		45.6023503661
364UbiquitinationIVVYEKRKRPDEVPD
HHHHHHCCCCCCCCC		78.3727667366
364 (in isoform 2)Ubiquitination-78.3721906983
397PhosphorylationKNLRQRNTN------
CCCHHHCCC------		44.4829514088
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NPTN_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBXN1_HUMANUBXN1physical
22939629
VMA21_HUMANVMA21physical
22939629
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NPTN_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-229, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-284 AND ASN-296, AND MASSSPECTROMETRY.

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