JAM3
Junctional adhesion molecule C
Also known as: JAM-3, JAM-C, JAM3_HUMAN, JAMC
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9BX67
- Gene
- JAM3
- Ensembl
- ENSG00000166086
- Chromosome
- 11
- Canonical length
- 310 aa
- Protein class
- Disease related genes, Human disease related genes, Predicted intracellular proteins, Predicted membrane proteins, Predicted secreted proteins
- Subcellular location
- Golgi apparatus
- Secretome location
- Secreted to blood
OverviewNCBI Gene
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. Unlike other proteins in this family, the this protein is unable to adhere to leukocyte cell lines and only forms weak homotypic interactions. The encoded protein is a member of the junctional adhesion molecule protein family and acts as a receptor for another member of this family. A mutation in an intron of this gene is associated with hemorrhagic destruction of the brain, subependymal calcification, and congenital cataracts. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Apr 2011]
Canonical amino-acid sequenceUniProt
310 residues, UniProt reviewed canonical sequence.
>Q9BX67|JAM3
1 MALRRPPRLR LCARLPDFFL LLLFRGCLIG AVNLKSSNRT PVVQEFESVE LSCIITDSQT
61 SDPRIEWKKI QDEQTTYVFF DNKIQGDLAG RAEILGKTSL KIWNVTRRDS ALYRCEVVAR
121 NDRKEIDEIV IELTVQVKPV TPVCRVPKAV PVGKMATLHC QESEGHPRPH YSWYRNDVPL
181 PTDSRANPRF RNSSFHLNSE TGTLVFTAVH KDDSGQYYCI ASNDAGSARC EEQEMEVYDL
241 NIGGIIGGVL VVLAVLALIT LGICCAYRRG YFINNKQDGE SYKNPGKPDG VNYIRTDEEG
301 DFRHKSSFVILocalizationUniProt · AlphaFold · HPA
Whether an antibody against JAM3 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.4
- Highest tissue expression
- 97 nTPM
Expression across tissuesHPA
Tissue
- placenta: 97 nTPM
- blood vessel: 80 nTPM
- spinal cord: 73 nTPM
- colon: 50 nTPM
- midbrain: 48 nTPM
- choroid plexus: 47 nTPM
Single-cell type
- oligodendrocytes: 384 nCPM
- rod photoreceptor cells: 321 nCPM
- choroid plexus epithelial cells: 256 nCPM
- platelets: 217 nCPM
- sertoli cells: 204 nCPM
- respiratory ionocytes: 188 nCPM
Immune cell
- memory B-cell: 5.3 nTPM
- naive B-cell: 3 nTPM
- naive CD4 T-cell: 2.4 nTPM
- total PBMC: 1.8 nTPM
- MAIT T-cell: 1.7 nTPM
- memory CD4 T-cell: 1.7 nTPM
Brain region
- white matter: 178 nTPM
- basal ganglia: 122 nTPM
- midbrain: 104 nTPM
- medulla oblongata: 100 nTPM
- thalamus: 96 nTPM
- cerebral cortex: 93 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about JAM3.
Disease | AllUniProt
Conditions JAM3 is implicated in, by any mechanism.
- Hemorrhagic destruction of the brain with subependymal calcification and cataracts (HDBSCC) MIM:613730
Disease | GeneticClinVar
16 pathogenic / likely-pathogenic of 238 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Porencephaly-microcephaly-bilateral congenital cataract syndrome
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.84
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.87
- DepMap mean gene effect
- 0.14
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- adaptive immune response
- adherens junction assembly
- angiogenesis
- apical protein localization
- cell migration
- cell-cell adhesion
- cell-matrix adhesion
- establishment of cell polarity
- granulocyte migration
- hematopoietic stem cell migration to bone marrow
- heterotypic cell-cell adhesion
- leukocyte migration involved in inflammatory response
- maintenance of blood-brain barrier
- myelination
- myeloid progenitor cell differentiation
- negative regulation of cell adhesion mediated by integrin
- negative regulation of integrin activation
- neutrophil homeostasis
- positive regulation of membrane permeability
- positive regulation of monocyte extravasation
- protein localization to cell junction
- protein localization to cell surface
- regulation of neutrophil chemotaxis
- spermatid development
- transmission of nerve impulse
- regulation of actin cytoskeleton organization by cell-cell adhesion
Molecular functions
- cell-cell adhesion mediator activity
- integrin binding
- protein heterodimerization activity
- protein homodimerization activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of JAM3 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads JAM3 as an antibody target. Whether an autoantibody or antibody against JAM3 could matter depends on whether native JAM3 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
JAM3 is annotated at the cell surface, where native JAM3 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label JAM3 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...