NRCAM_HUMAN - dbPTM
NRCAM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRCAM_HUMAN
UniProt AC Q92823
Protein Name Neuronal cell adhesion molecule
Gene Name NRCAM
Organism Homo sapiens (Human).
Sequence Length 1304
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, axon . Secreted . Detected at nodes of Ranvier.
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. Plays a role in mediating cell-cell contacts between Schwann cells and axons. Plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with GLDN, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier..
Protein Sequence MQLKIMPKKKRLSAGRVPLILFLCQMISALEVPLDPKLLEDLVQPPTITQQSPKDYIIDPRENIVIQCEAKGKPPPSFSWTRNGTHFDIDKDPLVTMKPGTGTLIINIMSEGKAETYEGVYQCTARNERGAAVSNNIVVRPSRSPLWTKEKLEPITLQSGQSLVLPCRPPIGLPPPIIFWMDNSFQRLPQSERVSQGLNGDLYFSNVLPEDTREDYICYARFNHTQTIQQKQPISVKVISVDELNDTIAANLSDTEFYGAKSSRERPPTFLTPEGNASNKEELRGNVLSLECIAEGLPTPIIYWAKEDGMLPKNRTVYKNFEKTLQIIHVSEADSGNYQCIAKNALGAIHHTISVRVKAAPYWITAPQNLVLSPGEDGTLICRANGNPKPRISWLTNGVPIEIAPDDPSRKIDGDTIIFSNVQERSSAVYQCNASNEYGYLLANAFVNVLAEPPRILTPANTLYQVIANRPALLDCAFFGSPLPTIEWFKGAKGSALHEDIYVLHENGTLEIPVAQKDSTGTYTCVARNKLGMAKNEVHLEIKDPTWIVKQPEYAVVQRGSMVSFECKVKHDHTLSLTVLWLKDNRELPSDERFTVDKDHLVVADVSDDDSGTYTCVANTTLDSVSASAVLSVVAPTPTPAPVYDVPNPPFDLELTDQLDKSVQLSWTPGDDNNSPITKFIIEYEDAMHKPGLWHHQTEVSGTQTTAQLKLSPYVNYSFRVMAVNSIGKSLPSEASEQYLTKASEPDKNPTAVEGLGSEPDNLVITWKPLNGFESNGPGLQYKVSWRQKDGDDEWTSVVVANVSKYIVSGTPTFVPYLIKVQALNDMGFAPEPAVVMGHSGEDLPMVAPGNVRVNVVNSTLAEVHWDPVPLKSIRGHLQGYRIYYWKTQSSSKRNRRHIEKKILTFQGSKTHGMLPGLEPFSHYTLNVRVVNGKGEGPASPDRVFNTPEGVPSAPSSLKIVNPTLDSLTLEWDPPSHPNGILTEYTLKYQPINSTHELGPLVDLKIPANKTRWTLKNLNFSTRYKFYFYAQTSAGSGSQITEEAVTTVDEAGILPPDVGAGKVQAVNPRISNLTAAAAETYANISWEYEGPEHVNFYVEYGVAGSKEEWRKEIVNGSRSFFGLKGLMPGTAYKVRVGAVGDSGFVSSEDVFETGPAMASRQVDIATQGWFIGLMCAVALLILILLIVCFIRRNKGGKYPVKEKEDAHADPEIQPMKEDDGTFGEYSDAEDHKPLKKGSRTPSDRTVKKEDSDDSLVDYGEGVNGQFNEDGSFIGQYSGKKEKEPAEGNESSEAPSPVNAMNSFV
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
83N-linked_GlycosylationPSFSWTRNGTHFDID
CCCCCCCCCCEEECC		52.95UniProtKB CARBOHYD
92 (in isoform 4)Ubiquitination-37.7121906983
98UbiquitinationKDPLVTMKPGTGTLI
CCCCEEECCCCCEEE		30.812190698
98 (in isoform 5)Ubiquitination-30.8121906983
98 (in isoform 1)Ubiquitination-30.8121906983
98 (in isoform 2)Ubiquitination-30.8121906983
98 (in isoform 3)Ubiquitination-30.8121906983
223N-linked_GlycosylationYICYARFNHTQTIQQ
EEEEEECCCCEEECC		31.57UniProtKB CARBOHYD
245N-linked_GlycosylationVISVDELNDTIAANL
EEEHHHCCCEEECCC		42.19UniProtKB CARBOHYD
251N-linked_GlycosylationLNDTIAANLSDTEFY
CCCEEECCCCCCCCC		30.93UniProtKB CARBOHYD
276N-linked_GlycosylationTFLTPEGNASNKEEL
CCCCCCCCCCCHHHH		38.2316335952
314N-linked_GlycosylationEDGMLPKNRTVYKNF
CCCCCCCCCCCCCCH		42.80UniProtKB CARBOHYD
316PhosphorylationGMLPKNRTVYKNFEK
CCCCCCCCCCCCHHH		37.2721214269
318PhosphorylationLPKNRTVYKNFEKTL
CCCCCCCCCCHHHEE		10.2921214269
433N-linked_GlycosylationSSAVYQCNASNEYGY
CCCEEECCCCCHHHH		30.77UniProtKB CARBOHYD
507N-linked_GlycosylationDIYVLHENGTLEIPV
CEEEEEECCEEEEEC		37.69UniProtKB CARBOHYD
619N-linked_GlycosylationGTYTCVANTTLDSVS
CEEEEEEECEECEEC		17.13UniProtKB CARBOHYD
639O-linked_GlycosylationSVVAPTPTPAPVYDV
EEECCCCCCCCCCCC		34.26OGP
712PhosphorylationTTAQLKLSPYVNYSF
EEEEEEECCCCCCEE		16.76-
714PhosphorylationAQLKLSPYVNYSFRV
EEEEECCCCCCEEEE		9.65-
716N-linked_GlycosylationLKLSPYVNYSFRVMA
EEECCCCCCEEEEEE		22.38UniProtKB CARBOHYD
733PhosphorylationSIGKSLPSEASEQYL
CCCCCCCCHHHHHHH		51.6025332170
739PhosphorylationPSEASEQYLTKASEP
CCHHHHHHHHHCCCC		16.58-
783MethylationNGPGLQYKVSWRQKD
CCCCCEEEEEEEECC		19.48-
802N-linked_GlycosylationWTSVVVANVSKYIVS
CEEEEEEEEEEEEEC		27.30UniProtKB CARBOHYD
858N-linked_GlycosylationNVRVNVVNSTLAEVH
CEEEEEECCCCEEEC		25.6219139490
872AcetylationHWDPVPLKSIRGHLQ
CCCCCCHHHHHHHCC		37.4519825007
881PhosphorylationIRGHLQGYRIYYWKT
HHHHCCEEEEEEEEC		4.8525884760
940PhosphorylationGKGEGPASPDRVFNT
CCCCCCCCCCCCCCC		30.3922210691
943MethylationEGPASPDRVFNTPEG
CCCCCCCCCCCCCCC		38.01115485543
956PhosphorylationEGVPSAPSSLKIVNP
CCCCCCCCCCEECCC		48.2822210691
957PhosphorylationGVPSAPSSLKIVNPT
CCCCCCCCCEECCCC		32.4022210691
993N-linked_GlycosylationTLKYQPINSTHELGP
EEEEECCCCCCCCCC		47.76UniProtKB CARBOHYD
1009N-linked_GlycosylationVDLKIPANKTRWTLK
EEEECCCCCCEEEEE		40.66UniProtKB CARBOHYD
1019N-linked_GlycosylationRWTLKNLNFSTRYKF
EEEEECCCCCCCEEE		37.91UniProtKB CARBOHYD
1072N-linked_GlycosylationAVNPRISNLTAAAAE
ECCHHHHHHHHHHHH		38.75UniProtKB CARBOHYD
1083N-linked_GlycosylationAAAETYANISWEYEG
HHHHHHCCCCEEECC		20.57UniProtKB CARBOHYD
1115N-linked_GlycosylationEWRKEIVNGSRSFFG
HHHHHHHCCCCCCCC		48.67UniProtKB CARBOHYD
1155 (in isoform 3)Ubiquitination-26.70-
1158 (in isoform 3)Ubiquitination-12.03-
1221PhosphorylationPMKEDDGTFGEYSDA
CCCCCCCCCCCCCCC		35.1525849741
1225PhosphorylationDDGTFGEYSDAEDHK
CCCCCCCCCCCCCCC		16.5425884760
1226PhosphorylationDGTFGEYSDAEDHKP
CCCCCCCCCCCCCCC		26.4928355574
1227 (in isoform 5)Phosphorylation-53.7430206219
1230 (in isoform 5)Phosphorylation-57.7530206219
1232 (in isoform 2)Phosphorylation-65.4529691806
1233 (in isoform 2)Phosphorylation-46.0929691806
1235 (in isoform 2)Phosphorylation-64.7129691806
1240PhosphorylationPLKKGSRTPSDRTVK
CCCCCCCCCCCCCCC		28.9225849741
1245PhosphorylationSRTPSDRTVKKEDSD
CCCCCCCCCCHHCCC		41.4925849741
1251PhosphorylationRTVKKEDSDDSLVDY
CCCCHHCCCCCCCCC		44.3920363803
1254PhosphorylationKKEDSDDSLVDYGEG
CHHCCCCCCCCCCCC		34.9720363803
1258PhosphorylationSDDSLVDYGEGVNGQ
CCCCCCCCCCCCCCC		15.0326471730
1271PhosphorylationGQFNEDGSFIGQYSG
CCCCCCCCCCCCCCC		26.4727422710
1276PhosphorylationDGSFIGQYSGKKEKE
CCCCCCCCCCCCCCC		17.74-
1290PhosphorylationEPAEGNESSEAPSPV
CCCCCCCCCCCCCCC		37.1628857561
1291PhosphorylationPAEGNESSEAPSPVN
CCCCCCCCCCCCCCC		31.4428857561
1295PhosphorylationNESSEAPSPVNAMNS
CCCCCCCCCCCCCCC		48.8322617229
1302PhosphorylationSPVNAMNSFV-----
CCCCCCCCCC-----		17.8225002506
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRCAM_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 NRCAM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTPRB_HUMANPTPRBphysical
9049255
HS12A_HUMANHSPA12Aphysical
12421765
MACF1_HUMANMACF1physical
12421765
MAGI3_HUMANMAGI3physical
12421765
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 NRCAM_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-276, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-276, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory