NCAM1_HUMAN - dbPTM
NCAM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCAM1_HUMAN
UniProt AC P13591
Protein Name Neural cell adhesion molecule 1
Gene Name NCAM1
Organism Homo sapiens (Human).
Sequence Length 858
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Cell membrane
Single-pass type I membrane protein.
Isoform 3: Cell membrane
Lipid-anchor, GPI-anchor.
Isoform 4: Cell membrane
Lipid-anchor, GPI-anchor .
Isoform 5: Secreted
Protein Description This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.; (Microbial infection) Acts as a receptor for rabies virus..
Protein Sequence MLQTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQKLMFKNAPTPQEFREGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTIQARQNIVNATANLGQSVTLVCDAEGFPEPTMSWTKDGEQIEQEEDDEKYIFSDDSSQLTIKKVDKNDEAEYICIAENKAGEQDATIHLKVFAKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEVQYAPKLQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFILVQADTPSSPSIDQVEPYSSTAQVQFDEPEATGGVPILKYKAEWRAVGEEVWHSKWYDAKEASMEGIVTIVGLKPETTYAVRLAALNGKGLGEISAASEFKTQPVQGEPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRYRALSSEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSAQPTAIPANGSPTSGLSTGAIVGILIVIFVLLLVVVDITCYFLNKCGLFMCIAVNLCGKAGPGAKGKDMEEGKAAFSKDESKEPIVEVRTEEERTPNHDGGKHTEPNETTPLTEPEKGPVEAKPECQETETKPAPAEVKTVPNDATQTKENESKA
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
121AcetylationIFQKLMFKNAPTPQE
HHHHHHCCCCCCCHH		37.9325953088
125O-linked_GlycosylationLMFKNAPTPQEFREG
HHCCCCCCCHHHHCC		34.88OGP
130MethylationAPTPQEFREGEDAVI
CCCCHHHHCCCCEEE		50.704199167
130DimethylationAPTPQEFREGEDAVI
CCCCHHHHCCCCEEE		50.70-
170PhosphorylationDVRFIVLSNNYLQIR
CCEEEEECCCEEEEC		16.4922210691
222N-linked_GlycosylationQARQNIVNATANLGQ
HHHHHHHHHHCCCCC		27.98UniProtKB CARBOHYD
315N-linked_GlycosylationPKITYVENQTAMELE
CEEEEEECCEEEEEE		34.16UniProtKB CARBOHYD
328PhosphorylationLEEQVTLTCEASGDP
EEEEEEEEEECCCCC		10.03-
347N-linked_GlycosylationTWRTSTRNISSEEKA
EEEECCCCCCHHHHC		38.28UniProtKB CARBOHYD
379PhosphorylationRSHARVSSLTLKSIQ
ECCCEECEEEEEEEE		23.6324719451
393PhosphorylationQYTDAGEYICTASNT
EECCCCCEEEEECCC		10.6124275569
398PhosphorylationGEYICTASNTIGQDS
CCEEEEECCCCCCCC		19.1624275569
400PhosphorylationYICTASNTIGQDSQS
EEEEECCCCCCCCCC		24.8024275569
405PhosphorylationSNTIGQDSQSMYLEV
CCCCCCCCCCEEEEE		19.1024275569
409PhosphorylationGQDSQSMYLEVQYAP
CCCCCCEEEEEEECC		12.6424275569
433N-linked_GlycosylationTWEGNQVNITCEVFA
EECCCEEEEEEEEEE		17.68UniProtKB CARBOHYD
449N-linked_GlycosylationPSATISWFRDGQLLP
CCCEEEEEECCCCCC		3.999774483
449N-linked_GlycosylationPSATISWFRDGQLLP
CCCEEEEEECCCCCC		3.999774483
459N-linked_GlycosylationGQLLPSSNYSNIKIY
CCCCCCCCCCCEEEE		48.9017623646
478N-linked_GlycosylationASYLEVTPDSENDFG
CCEEEECCCCCCCCC		48.599774483
488N-linked_GlycosylationENDFGNYNCTAVNRI
CCCCCCCCCCCEEEC		22.219774483
566PhosphorylationWYDAKEASMEGIVTI
CCCHHHHHCCEEEEE		20.6126074081
572PhosphorylationASMEGIVTIVGLKPE
HHCCEEEEEEECCCC		14.1826074081
598PhosphorylationGKGLGEISAASEFKT
CCCCCEEEECCCCCC		17.3024114839
605PhosphorylationSAASEFKTQPVQGEP
EECCCCCCCCCCCCC		43.35-
613PhosphorylationQPVQGEPSAPKLEGQ
CCCCCCCCCCCCCCC		53.56-
673PhosphorylationSDHVMLKSLDWNAEY
CCEEEEEECCCCCEE		27.8328842319
702PhosphorylationAAHFVFRTSAQPTAI
EEEEEEECCCCCCEE		19.56-
706 (in isoform 4)GPI-anchor-24.42-
734PhosphorylationILIVIFVLLLVVVDI
HHHHHHHHHHHHHHH		1.8215313190
741 (in isoform 3)GPI-anchor-1.61-
744PhosphorylationVVVDITCYFLNKCGL
HHHHHHHHHHHHCCH		11.4915313190
770PhosphorylationAGPGAKGKDMEEGKA
CCCCCCCCCHHHHHC		53.8718510355
771 (in isoform 1)Ubiquitination-59.39-
774PhosphorylationAKGKDMEEGKAAFSK
CCCCCHHHHHCCCCC		60.4018510355
775 (in isoform 1)Ubiquitination-16.17-
776UbiquitinationGKDMEEGKAAFSKDE
CCCHHHHHCCCCCCC		39.56-
780PhosphorylationEEGKAAFSKDESKEP
HHHHCCCCCCCCCCC		34.1730266825
781UbiquitinationEGKAAFSKDESKEPI
HHHCCCCCCCCCCCC		60.09-
784PhosphorylationAAFSKDESKEPIVEV
CCCCCCCCCCCCEEE		53.0730266825
785UbiquitinationAFSKDESKEPIVEVR
CCCCCCCCCCCEEEE		66.51-
793PhosphorylationEPIVEVRTEEERTPN
CCCEEEECCCCCCCC		53.5824117733
798PhosphorylationVRTEEERTPNHDGGK
EECCCCCCCCCCCCC		31.5529900121
807PhosphorylationNHDGGKHTEPNETTP
CCCCCCCCCCCCCCC		57.5323312004
812PhosphorylationKHTEPNETTPLTEPE
CCCCCCCCCCCCCCC		40.1127732954
813PhosphorylationHTEPNETTPLTEPEK
CCCCCCCCCCCCCCC		15.3227732954
816PhosphorylationPNETTPLTEPEKGPV
CCCCCCCCCCCCCCC		51.1827732954
849PhosphorylationKTVPNDATQTKENES
EECCCCCCCCHHHHC		39.3724719451
851PhosphorylationVPNDATQTKENESKA
CCCCCCCCHHHHCCC		35.6529759185
856PhosphorylationTQTKENESKA-----
CCCHHHHCCC-----		45.5229759185
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
803TPhosphorylationKinaseERK2P28482
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCAM1_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 NCAM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPCB_HUMANPRKCBphysical
12743109
FGFR1_HUMANFGFR1physical
12121226
PLCG1_HUMANPLCG1physical
23061666
SPTB1_HUMANSPTBphysical
23061666
TBB5_HUMANTUBBphysical
23061666
PP1A_HUMANPPP1CAphysical
23061666
UCHL1_HUMANUCHL1physical
23061666
RHEB_HUMANRHEBphysical
21988832
Drug and Disease Associations
Kegg Disease
H00010 Multiple myeloma
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D09927 Lorvotuzumab mertansine (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NCAM1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-459, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex.";
DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.;
J. Proteome Res. 4:306-315(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, AND MASSSPECTROMETRY.

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