Q9Y624 · JAM1_HUMAN
- ProteinJunctional adhesion molecule A
- GeneF11R
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids299 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3 (PubMed:11489913).
The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity).
Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity).
Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (PubMed:11812992).
Involved in platelet activation (PubMed:10753840).
The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity).
Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity).
Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (PubMed:11812992).
Involved in platelet activation (PubMed:10753840).
(Microbial infection) Acts as a receptor for Mammalian reovirus sigma-1.
(Microbial infection) Acts as a receptor for Human Rotavirus strain Wa.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 285-286 | (Microbial infection) Cleavage; by H.pylori PqqE | ||||
Sequence: AR |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameJunctional adhesion molecule A
- Short namesJAM-A
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y624
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: Localized at tight junctions of both epithelial and endothelial cells.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 28-238 | Extracellular | ||||
Sequence: SVTVHSSEPEVRIPENNPVKLSCAYSGFSSPRVEWKFDQGDTTRLVCYNNKITASYEDRVTFLPTGITFKSVTREDTGTYTCMVSEEGGNSYGEVKVKLIVLVPPSKPTVNIPSSATIGNRAVLTCSEQDGSPPSEYTWFKDGIVMPTNPKSTRAFSNSSYVLNPTTGELVFDPLSASDTGEYSCEARNGYGTPMTSNAVRMEAVERNVGV | ||||||
Transmembrane | 239-259 | Helical | ||||
Sequence: IVAAVLVTLILLGILVFGIWF | ||||||
Topological domain | 260-299 | Cytoplasmic | ||||
Sequence: AYSRGHFDRTKKGTSSKKVIYSQPSARSEGEFKQTSSFLV |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 305 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-27 | UniProt | |||||
Sequence: MGTKAQVERKLLCLFILAILLCSLALG | |||||||
Chain | PRO_0000015066 | 28-299 | UniProt | Junctional adhesion molecule A | |||
Sequence: SVTVHSSEPEVRIPENNPVKLSCAYSGFSSPRVEWKFDQGDTTRLVCYNNKITASYEDRVTFLPTGITFKSVTREDTGTYTCMVSEEGGNSYGEVKVKLIVLVPPSKPTVNIPSSATIGNRAVLTCSEQDGSPPSEYTWFKDGIVMPTNPKSTRAFSNSSYVLNPTTGELVFDPLSASDTGEYSCEARNGYGTPMTSNAVRMEAVERNVGVIVAAVLVTLILLGILVFGIWFAYSRGHFDRTKKGTSSKKVIYSQPSARSEGEFKQTSSFLV | |||||||
Disulfide bond | 50↔109 | UniProt | |||||
Sequence: CAYSGFSSPRVEWKFDQGDTTRLVCYNNKITASYEDRVTFLPTGITFKSVTREDTGTYTC | |||||||
Disulfide bond | 153↔212 | UniProt | |||||
Sequence: CSEQDGSPPSEYTWFKDGIVMPTNPKSTRAFSNSSYVLNPTTGELVFDPLSASDTGEYSC | |||||||
Glycosylation | 185 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 280 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 281 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 281 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 284 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 284 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 287 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
N-glycosylated.
(Microbial infection) Cleaved by H.pylori virulence factor PqqE. Cleavage leads to altered tight junction functions.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in endothelium, epithelium and leukocytes (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with the ninth PDZ domain of MPDZ (PubMed:11489913).
Interacts with the first PDZ domain of PARD3 (PubMed:11489913).
The association between PARD3 and PARD6B probably disrupts this interaction (By similarity).
Interacts with ITGAL (via I-domain) (PubMed:15528364).
Interacts with CD151 (PubMed:35067832).
Interacts with the first PDZ domain of PARD3 (PubMed:11489913).
The association between PARD3 and PARD6B probably disrupts this interaction (By similarity).
Interacts with ITGAL (via I-domain) (PubMed:15528364).
Interacts with CD151 (PubMed:35067832).
(Microbial infection) Interacts with Mammalian reovirus sigma-1 capsid protein.
(Microbial infection) Interacts with Human Rotavirus strain Wa vp4 capsid protein.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-125 | Ig-like V-type 1 | ||||
Sequence: SVTVHSSEPEVRIPENNPVKLSCAYSGFSSPRVEWKFDQGDTTRLVCYNNKITASYEDRVTFLPTGITFKSVTREDTGTYTCMVSEEGGNSYGEVKVK | ||||||
Domain | 135-228 | Ig-like V-type 2 | ||||
Sequence: PTVNIPSSATIGNRAVLTCSEQDGSPPSEYTWFKDGIVMPTNPKSTRAFSNSSYVLNPTTGELVFDPLSASDTGEYSCEARNGYGTPMTSNAVR |
Domain
The Ig-like V-type 2 domain is necessary and sufficient for interaction with integrin alpha-L/beta-2.
Sequence similarities
Belongs to the immunoglobulin superfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9Y624-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length299
- Mass (Da)32,583
- Last updated1999-11-01 v1
- ChecksumD95DE2FEA23D2851
Q9Y624-2
- Name2
- Differences from canonical
- 81-129: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056218 | 81-129 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF111713 EMBL· GenBank· DDBJ | AAD42050.1 EMBL· GenBank· DDBJ | mRNA | ||
AF207907 EMBL· GenBank· DDBJ | AAF22829.1 EMBL· GenBank· DDBJ | mRNA | ||
AF172398 EMBL· GenBank· DDBJ | AAD48877.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136649 EMBL· GenBank· DDBJ | CAB66584.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358896 EMBL· GenBank· DDBJ | AAQ89255.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304412 EMBL· GenBank· DDBJ | BAH14177.1 EMBL· GenBank· DDBJ | mRNA | ||
AL591806 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC001533 EMBL· GenBank· DDBJ | AAH01533.1 EMBL· GenBank· DDBJ | mRNA |