MUC18_HUMAN - dbPTM
MUC18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MUC18_HUMAN
UniProt AC P43121
Protein Name Cell surface glycoprotein MUC18
Gene Name MCAM
Organism Homo sapiens (Human).
Sequence Length 646
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration..
Protein Sequence MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRPLKEEKNRVHIQSSQTVESSGLYTLQSILKAQLVKEDKDAQFYCELNYRLPSGNHMKESREVTVPVFYPTEKVWLEVEPVGMLKEGDRVEIRCLADGNPPPHFSISKQNPSTREAEEETTNDNGVLVLEPARKEHSGRYECQGLDLDTMISLLSEPQELLVNYVSDVRVSPAAPERQEGSSLTLTCEAESSQDLEFQWLREETGQVLERGPVLQLHDLKREAGGGYRCVASVPSIPGLNRTQLVNVAIFGPPWMAFKERKVWVKENMVLNLSCEASGHPRPTISWNVNGTASEQDQDPQRVLSTLNVLVTPELLETGVECTASNDLGKNTSILFLELVNLTTLTPDSNTTTGLSTSTASPHTRANSTSTERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITLPPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH
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
3 (in isoform 2)Phosphorylation-1.8424043423
11 (in isoform 2)Phosphorylation-1.3724043423
14 (in isoform 2)Phosphorylation-6.2024043423
16 (in isoform 2)Phosphorylation-1.9924043423
18 (in isoform 2)Phosphorylation-1.1824043423
27 (in isoform 2)Phosphorylation-42.8524043423
56N-linked_GlycosylationGLSQSQGNLSHVDWF
CCCCCCCCCCCCCEE		30.63UniProtKB CARBOHYD
93PhosphorylationGEYEQRLSLQDRGAT
CCHHHHEEHHHHCCE		26.61-
97MethylationQRLSLQDRGATLALT
HHEEHHHHCCEEEEE		24.56115482755
100PhosphorylationSLQDRGATLALTQVT
EHHHHCCEEEEEECC		18.5224043423
104PhosphorylationRGATLALTQVTPQDE
HCCEEEEEECCCCCC		18.5224043423
107PhosphorylationTLALTQVTPQDERIF
EEEEEECCCCCCEEE		12.8624043423
123PhosphorylationCQGKRPRSQEYRIQL
ECCCCCCCCCEEEEE		30.0124719451
126PhosphorylationKRPRSQEYRIQLRVY
CCCCCCCEEEEEEEE		12.8424719451
193PhosphorylationNRVHIQSSQTVESSG
CCEEEEECCEECCCC		17.3125954137
195PhosphorylationVHIQSSQTVESSGLY
EEEEECCEECCCCHH		28.3425954137
195O-linked_GlycosylationVHIQSSQTVESSGLY
EEEEECCEECCCCHH		28.34OGP
198PhosphorylationQSSQTVESSGLYTLQ
EECCEECCCCHHHHH		25.9320068231
199PhosphorylationSSQTVESSGLYTLQS
ECCEECCCCHHHHHH		21.2220068231
202PhosphorylationTVESSGLYTLQSILK
EECCCCHHHHHHHHH		14.6620068231
203PhosphorylationVESSGLYTLQSILKA
ECCCCHHHHHHHHHH		24.3025954137
206PhosphorylationSGLYTLQSILKAQLV
CCHHHHHHHHHHHHH		32.7624719451
217UbiquitinationAQLVKEDKDAQFYCE
HHHHCCCCCCCEEEE		56.93-
238PhosphorylationSGNHMKESREVTVPV
CCCCCCCCEEEEEEE		28.3724501219
290PhosphorylationSISKQNPSTREAEEE
CCCCCCCCCHHCCEE		47.8826657352
398AcetylationVLQLHDLKREAGGGY
EEEEEECCCCCCCCC		55.0027452117
418N-linked_GlycosylationVPSIPGLNRTQLVNV
CCCCCCCCCCCEEEE		51.36UniProtKB CARBOHYD
449N-linked_GlycosylationVKENMVLNLSCEASG
EEECEEEEEEEECCC		20.63UniProtKB CARBOHYD
467N-linked_GlycosylationPTISWNVNGTASEQD
CEEEEEECCCCCCCC		38.5919159218
508N-linked_GlycosylationASNDLGKNTSILFLE
ECCCCCCCCEEEEEE		36.94UniProtKB CARBOHYD
518N-linked_GlycosylationILFLELVNLTTLTPD
EEEEEEECCCEECCC		44.27UniProtKB CARBOHYD
527N-linked_GlycosylationTTLTPDSNTTTGLST
CEECCCCCCCCCCCC		49.15UniProtKB CARBOHYD
544N-linked_GlycosylationASPHTRANSTSTERK
CCCCCCCCCCCCCCC		42.40UniProtKB CARBOHYD
585AcetylationVLYFLYKKGKLPCRR
HHHHHHHCCCCCCCC		47.9619824207
593O-linked_GlycosylationGKLPCRRSGKQEITL
CCCCCCCCCCCEEEC		30.8730379171
595UbiquitinationLPCRRSGKQEITLPP
CCCCCCCCCEEECCC		46.10-
599PhosphorylationRSGKQEITLPPSRKS
CCCCCEEECCCCCCC		32.2429449344
603PhosphorylationQEITLPPSRKSELVV
CEEECCCCCCCEEEE		50.8626657352
605AcetylationITLPPSRKSELVVEV
EECCCCCCCEEEEEE		53.257668451
605UbiquitinationITLPPSRKSELVVEV
EECCCCCCCEEEEEE		53.25-
606PhosphorylationTLPPSRKSELVVEVK
ECCCCCCCEEEEEEE		34.7429255136
613AcetylationSELVVEVKSDKLPEE
CEEEEEEECCCCCHH		39.167668465
613UbiquitinationSELVVEVKSDKLPEE
CEEEEEEECCCCCHH		39.16-
614PhosphorylationELVVEVKSDKLPEEM
EEEEEEECCCCCHHH		45.1930266825
616UbiquitinationVVEVKSDKLPEEMGL
EEEEECCCCCHHHCC		73.3821906983
616 (in isoform 1)Ubiquitination-73.3821906983
627PhosphorylationEMGLLQGSSGDKRAP
HHCCCCCCCCCCCCC		20.4230266825
628PhosphorylationMGLLQGSSGDKRAPG
HCCCCCCCCCCCCCC		58.8130266825
631 (in isoform 1)Ubiquitination-54.7221906983
631UbiquitinationLQGSSGDKRAPGDQG
CCCCCCCCCCCCCCC		54.7221906983
640 (in isoform 1)Ubiquitination-55.0921906983
640AcetylationAPGDQGEKYIDLRH-
CCCCCCCCEEECCC-		55.0927452117
640UbiquitinationAPGDQGEKYIDLRH-
CCCCCCCCEEECCC-		55.092190698
641PhosphorylationPGDQGEKYIDLRH--
CCCCCCCEEECCC--		8.7225884760
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 MUC18_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MUC18_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 MUC18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FYN_HUMANFYNphysical
9756930
VPP2_HUMANATP6V0A2physical
26186194
VPP1_HUMANATP6V0A1physical
26186194
AT11C_HUMANATP11Cphysical
26186194
LAMA4_HUMANLAMA4physical
26186194
CNTN1_HUMANCNTN1physical
26186194
VA0D1_HUMANATP6V0D1physical
26186194
LAMA4_HUMANLAMA4physical
28514442
CNTN1_HUMANCNTN1physical
28514442
VPP2_HUMANATP6V0A2physical
28514442
VPP1_HUMANATP6V0A1physical
28514442
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 MUC18_HUMAN

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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-467, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606 AND SER-614, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, AND MASSSPECTROMETRY.

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