NRCAM_MOUSE - dbPTM
NRCAM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRCAM_MOUSE
UniProt AC Q810U4
Protein Name Neuronal cell adhesion molecule
Gene Name Nrcam
Organism Mus musculus (Mouse).
Sequence Length 1256
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, axon . Secreted . Detected at nodes of Ranvier (PubMed:14602817, PubMed:20188654, PubMed:24719088).
Protein Description Cell adhesion protein that is required for normal responses to cell-cell contacts in brain and in the peripheral nervous system. Plays a role in neurite outgrowth in response to contactin binding. [PubMed: 11564762 Plays a role in mediating cell-cell contacts between Schwann cells and axons]
Protein Sequence MQLKIMPKKKHLSAGGVPLILFLCQMISALDVPLDLVQPPTITQQSPKDYIIDPRENIVIQCEAKGKPPPSFSWTRNGTHFDIDKDPLVTMKPGSGTLVINIMSEGKAETYEGVYQCTARNERGAAVSNNIVVRPSRSPLWTKERLEPIVLQNGQSLVLPCRPPIGLPPAIIFWMDNSFQRLPQSERVSQGLNGDLYFSNVLPEDTREDYICYARFNHTQTIQQKQPISLKVISVDELNDTIAANLSDTEFYGAKSSKERPPTFLTPEGNESHKEELRGNVLSLECIAEGLPTPIIYWIKEDGMLPANRTFYRNFKKTLQITHVSEADSGNYQCIAKNALGAVHHTISVTVKAAPYWIVAPQNLVLSPGENGTLICRANGNPKPRISWLTNGVPIEIALDDPSRKIDGDTIIFSNVQESSSAVYQCNASNKYGYLLANAFVNVLAEPPRILTSANTLYQVIANRPALLDCAFFGSPMPTIEWFKGTKGSALHEDIYVLHDNGTLEIPVAQKDSTGTYTCVARNKLGMAKNEVHLEIKDPTRIIKQPEYAVVQRGSKVSFECRVKHDHTLIPTIMWLKDNGELPNDERFSTDKDHLVVSDVKDDDGGTYTCTANTTLDSASASAVLRVVAPTPTPAPIYDVPNPPFDLELTNQLDKSVQLTWTPGDDNNSPITKFIIEYEDAMHDAGLWRHQAEVSGTQTTAQLKLSPYVNYSFRVMAENSIGRSMPSEASEQYLTKAAEPDQNPMAVEGLGTEPDNLVITWKPLNGFQSNGPGLQYKVSWRQKDGDDEWTSVVVANVSKYIVSGTPTFVPYLIKVQALNDVGFAPEPAAVMGHSGEDLPMVAPGNVRVSVVNSTLAEVHWDPVPPKSVRGHLQGYRIYYWKTQSSSKRNRRHIEKKILTFQGTKTHGMLPGLQPYSHYALNVRVVNGKGEGPASTDRGFHTPEGVPSAPSSLKIVNPTLDSLTLEWDPPSHPNGILTEYILQYQPINSTHELGPLVDLKIPANKTRWTLKNLNFSTRYKFYFYAQTSVGPGSQITEEAITTVDEAGIPPPDVGAGKGKEEWRKEIVNGSRSFFGLKGLMPGTAYKVRVGAEGDSGFVSSEDVFETGPAMASRQVDIATQGWFIGLMCAVALLILILLIVCFIRRNKGGKYPVKEKEDAHADPEIQPMKEDDGTFGEYSDAEDHKPLKKGSRTPSDRTVKKEDSDDSLVDYGEGVNGQFNEDGSFIGQYSGKKEKEPAEGNESSEAPSPVNAMNSFV
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
77N-linked_GlycosylationPSFSWTRNGTHFDID
CCCCCCCCCCCCCCC
52.95-
217N-linked_GlycosylationYICYARFNHTQTIQQ
EEEEEECCCCCEECC
31.57-
239N-linked_GlycosylationVISVDELNDTIAANL
EEEHHHCCCEEECCC
42.19-
245N-linked_GlycosylationLNDTIAANLSDTEFY
CCCEEECCCCCCCCC
30.93-
270N-linked_GlycosylationTFLTPEGNESHKEEL
CEECCCCCHHHHHHH
46.03-
308N-linked_GlycosylationEDGMLPANRTFYRNF
CCCCCCCCHHHHHHH
41.40-
371N-linked_GlycosylationLVLSPGENGTLICRA
EEECCCCCCEEEEEC
55.45-
410PhosphorylationSRKIDGDTIIFSNVQ
CCCCCCCEEEECCCC
22.8517242355
419PhosphorylationIFSNVQESSSAVYQC
EECCCCCCCCCEEEE
16.7017242355
420PhosphorylationFSNVQESSSAVYQCN
ECCCCCCCCCEEEEC
22.8917242355
421PhosphorylationSNVQESSSAVYQCNA
CCCCCCCCCEEEECC
30.9117242355
427N-linked_GlycosylationSSAVYQCNASNKYGY
CCCEEEECCCCCHHE
30.77-
501N-linked_GlycosylationDIYVLHDNGTLEIPV
CEEEEECCCEEEEEC
34.30-
613N-linked_GlycosylationGTYTCTANTTLDSAS
CEEEEECCCEECCCC
18.55-
706PhosphorylationTTAQLKLSPYVNYSF
EEEEEEECCCCCCEE
16.7628059163
710N-linked_GlycosylationLKLSPYVNYSFRVMA
EEECCCCCCEEEEEE
22.38-
720PhosphorylationFRVMAENSIGRSMPS
EEEEEECCCCCCCCC
20.2328059163
796N-linked_GlycosylationWTSVVVANVSKYIVS
CEEEEEEEEEEEEEC
27.30-
811PhosphorylationGTPTFVPYLIKVQAL
CCCCCHHEEEEEEEC
18.7628576409
852N-linked_GlycosylationNVRVSVVNSTLAEVH
CEEEEEECCCCEEEE
27.41-
987N-linked_GlycosylationILQYQPINSTHELGP
HHHHCCCCCCCCCCC
47.76-
1003N-linked_GlycosylationVDLKIPANKTRWTLK
EEEECCCCCCEEEEE
40.66-
1013N-linked_GlycosylationRWTLKNLNFSTRYKF
EEEEECCCCCCCEEE
37.91-
1067N-linked_GlycosylationEWRKEIVNGSRSFFG
HHHHHHHCCCCCCCC
48.67-
1168UbiquitinationDPEIQPMKEDDGTFG
CCCCCCCCCCCCCCC
65.7522790023
1168 (in isoform 3)Ubiquitination-65.7522790023
1173PhosphorylationPMKEDDGTFGEYSDA
CCCCCCCCCCCCCCC
35.1524925903
1177PhosphorylationDDGTFGEYSDAEDHK
CCCCCCCCCCCCCCC
16.5424925903
1178PhosphorylationDGTFGEYSDAEDHKP
CCCCCCCCCCCCCCC
26.4925521595
1179 (in isoform 3)Phosphorylation-53.7420415495
1182 (in isoform 3)Phosphorylation-57.7520415495
1190PhosphorylationHKPLKKGSRTPSDRT
CCCCCCCCCCCCCCC
41.6929899451
1192PhosphorylationPLKKGSRTPSDRTVK
CCCCCCCCCCCCCCC
28.9229899451
1194PhosphorylationKKGSRTPSDRTVKKE
CCCCCCCCCCCCCHH
38.8329899451
1197PhosphorylationSRTPSDRTVKKEDSD
CCCCCCCCCCHHHCC
41.4922324799
1203PhosphorylationRTVKKEDSDDSLVDY
CCCCHHHCCCCCCCC
44.3919060867
1206PhosphorylationKKEDSDDSLVDYGEG
CHHHCCCCCCCCCCC
34.9719060867
1210PhosphorylationSDDSLVDYGEGVNGQ
CCCCCCCCCCCCCCC
15.0329899451
1223PhosphorylationGQFNEDGSFIGQYSG
CCCCCCCCCCCCCCC
26.4719060867
1228PhosphorylationDGSFIGQYSGKKEKE
CCCCCCCCCCCCCCC
17.74-
1242PhosphorylationEPAEGNESSEAPSPV
CCCCCCCCCCCCCCC
37.1625521595
1243PhosphorylationPAEGNESSEAPSPVN
CCCCCCCCCCCCCCC
31.4425521595
1247PhosphorylationNESSEAPSPVNAMNS
CCCCCCCCCCCCCCC
48.8325521595
1254PhosphorylationSPVNAMNSFV-----
CCCCCCCCCC-----
17.8225521595

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 NRCAM_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRCAM_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 NRCAM_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG4_MOUSEDlg4physical
16882004
DLG1_MOUSEDlg1physical
16882004

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NRCAM_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, AND MASSSPECTROMETRY.

TOP