Protein detail
MUC18
Cell surface glycoprotein MUC18 (Cell surface glycoprotein P1H12) (Melanoma cell adhesion molecule) (Melanoma-associated antigen A32) (Melanoma-associated antigen MUC18) (S-endo 1 endothelial-associated antigen) (CD antigen CD146)
Entry name MUC18 | UniProt ID | EVMP score 0.50 |
Frequency 1 | Transmembrane count 1 | Protein classification CD markersPlasma proteinsPredicted membrane proteins |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Cell surface glycoprotein MUC18 (Cell surface glycoprotein P1H12) (Melanoma cell adhesion molecule) (Melanoma-associated antigen A32) (Melanoma-associated antigen MUC18) (S-endo 1 endothelial-associated antigen) (CD antigen CD146)
Protein Class
CD markersPlasma proteinsPredicted membrane proteins
Protein Function
CD markers
Transmembrane
560..583; Helical
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Gene Synonym
CD146HEMCAMMelCAMMETCAMMUC18
Gene Description
Melanoma cell adhesion molecule
Chromosome
11
Position
119308529-119321521
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Tissue Specificlymphoid tissueCell SpecificT-cellsSingle-Nuclei Brain SpecificleukocyteBlood Cell SpecificgdT-cellBlood Lineage SpecificT-cells
Function & Pathway
Protein Function
CD markers
Cellular Component
Molecular Function
Biological Process
Reactome
- R-hsa-9013149 rac1 gtpase cycle
- R-hsa-9013404 rac2 gtpase cycle
- R-hsa-9013423 rac3 gtpase cycle
- R-hsa-8980692 rhoa gtpase cycle
- R-hsa-9013026 rhob gtpase cycle
- R-hsa-9013106 rhoc gtpase cycle
- R-hsa-9013405 rhod gtpase cycle
- R-hsa-9035034 rhof gtpase cycle
- R-hsa-9013408 rhog gtpase cycle
- R-hsa-9012999 rho gtpase cycle
- R-hsa-9716542 signaling by rho gtpases miro gtpases and rhobtb3
Canonical Pathways
M10 Pid bcr 5pathway
Mediation Categories
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
49 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| receptor | receptor | Cellinker | No | Yes | No | Yes | No |
| receptor | receptor | scConnect | No | Yes | No | Yes | No |
| receptor | receptor | connectomeDB2020 | No | Yes | No | Yes | No |
| receptor | receptor | iTALK | No | Yes | No | Yes | No |
| receptor | receptor | EMBRACE | No | Yes | No | Yes | No |
| transmembrane | transmembrane_predicted | Phobius | No | No | No | Yes | No |
| transmembrane_phobius | transmembrane_predicted | Almen2009 | No | No | No | Yes | No |
| transmembrane_sosui | transmembrane_predicted | Almen2009 | No | No | No | Yes | No |
| transmembrane_tmhmm | transmembrane_predicted | Almen2009 | No | No | No | Yes | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Mass spectrometry | 0 |
Sequence, Structure & Domains
Sequences
Length
646
Mass
71,607
Sequence
MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRPLKEEKNRVHIQSSQTVESSGLYTLQSILKAQLVKEDKDAQFYCELNYRLPSGNHMKESREVTVPVFYPTEKVWLEVEPVGMLKEGDRVEIRCLADGNPPPHFSISKQNPSTREAEEETTNDNGVLVLEPARKEHSGRYECQGLDLDTMISLLSEPQELLVNYVSDVRVSPAAPERQEGSSLTLTCEAESSQDLEFQWLREETGQVLERGPVLQLHDLKREAGGGYRCVASVPSIPGLNRTQLVNVAIFGPPWMAFKERKVWVKENMVLNLSCEASGHPRPTISWNVNGTASEQDQDPQRVLSTLNVLVTPELLETGVECTASNDLGKNTSILFLELVNLTTLTPDSNTTTGLSTSTASPHTRANSTSTERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITLPPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P43121-1; Sequence=Displayed; Name=2; IsoId=P43121-2; Sequence=VSP_016938, VSP_016939
Alternative Sequence
1..187; MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRPLKEEKNR -> MVYIVRQFLLYNVSGSVYLDQLIVLLTAKFSILRIAGSRVHHSPFSGHLDGCSFLSLQHSLHTSLDMSRHENVFLGLTLSSKSAGLKGFQLAFVPGLLQGTGGYLDGPLPTPVDNPRVGLEVGLRLSLPPLPPCPG (in isoform 2); 549..646; ERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITLPPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH -> GKPGLAREQGCARASFLPCPSPESPVQKGE (in isoform 2)
3D Structural Models
Helix
399..401; 490..495
Beta Strand
343..352; 361..371; 374..379; 382..394; 403..410; 418..427; 429..434; 436..441; 447..458; 461..468; 471..476; 479..487; 497..503; 506..515
3D Structure
X-ray crystallography (1)
Domain & Motif Annotations
Compositional Bias
533..547; Polar residues; 629..646; Basic and acidic residues
Domain (FT)
24..129; Ig-like V-type 1; 139..242; Ig-like V-type 2; 244..330; Ig-like C2-type 1; 335..424; Ig-like C2-type 2; 430..510; Ig-like C2-type 3
Region
278..299; Disordered; 525..554; Disordered; 620..646; Disordered