ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9Y624


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name JAM1_HUMAN
Primary accession number Q9Y624
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 100)
Name and origin of the protein
Protein name Junctional adhesion molecule A [Precursor]
Synonyms JAM-A
Junctional adhesion molecule 1
JAM-1
Platelet adhesion molecule 1
PAM-1
Platelet F11 receptor
CD321 antigen
Gene name
Name: F11R
Synonyms: JAM1, JCAM
ORFNames: UNQ264/PRO301
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10395639 [NCBI, ExPASy, EBI, Israel, Japan]
Ozaki H., Ishii K., Horiuchi H., Arai H., Kawamoto T., Okawa K., Iwamatsu A., Kita T.;
"Combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells.";
J. Immunol. 163:553-557(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10753840 [NCBI, ExPASy, EBI, Israel, Japan]
Sobocka M.B., Sobocki T., Banerjee P., Weiss C., Rushbrook J.I., Norin A.J., Hartwig J., Salifu M.O., Markell M.S., Babinska A., Ehrlich Y.H., Kornecki E.;
"Cloning of the human platelet F11 receptor: a cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation.";
Blood 95:2600-2609(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=11171323 [NCBI, ExPASy, EBI, Israel, Japan]
Naik U.P., Naik M.U., Eckfeld K., Martin-DeLeon P., Spychala J.;
"Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody.";
J. Cell Sci. 114:539-547(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 28-103 AND 123-130, AND GLYCOSYLATION.
PubMed=7646439 [NCBI, ExPASy, EBI, Israel, Japan]
Naik U.P., Ehrlich Y.H., Kornecki E.;
"Mechanisms of platelet activation by a stimulatory antibody: cross-linking of a novel platelet receptor for monoclonal antibody F11 with the Fc gamma RII receptor.";
Biochem. J. 310:155-162(1995).
[8]
PROTEIN SEQUENCE OF 28-42.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[9]
PROTEIN SEQUENCE OF 28-39.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[10]
INTERACTION WITH MPDZ.
DOI=10.1083/jcb.200103047; PubMed=11489913 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh M., Sasaki H., Furuse M., Ozaki H., Kita T., Tsukita S.;
"Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions.";
J. Cell Biol. 154:491-497(2001).
[11]
REVIEW, AND NOMENCLATURE.
DOI=10.1016/S1471-4906(03)00117-0; PubMed=12810109 [NCBI, ExPASy, EBI, Israel, Japan]
Muller W.A.;
"Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response.";
Trends Immunol. 24:327-334(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-280, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; SER-275; TYR-280; SER-281; SER-284 AND SER-287, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-191, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[17]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 28-233.
DOI=10.1073/pnas.0937718100; PubMed=12697893 [NCBI, ExPASy, EBI, Israel, Japan]
Prota A.E., Campbell J.A., Schelling P., Forrest J.C., Watson M.J., Peters T.R., Aurrand-Lions M.A., Imhof B.A., Dermody T.S., Stehle T.;
"Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding.";
Proc. Natl. Acad. Sci. U.S.A. 100:5366-5371(2003).
Comments
  • FUNCTION: Seems to plays a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. 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. Involved in platelet activation. In case of orthoreovirus infection, serves as receptor for the virus.
  • SUBUNIT: Interacts with the ninth PDZ domain of MPDZ. Interacts with the first PDZ domain of PARD3. The association between PARD3 and PARD6B probably disrupts this interaction. Interacts with the orthoreovirus sigma-1 capsid protein (By similarity).
  • SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Single-pass type I membrane protein. Note=Localized at tight junctions of both epithelial and endothelial cells.
  • PTM: N-glycosylated.
  • SIMILARITY: Belongs to the immunoglobulin superfamily.
  • SIMILARITY: Contains 2 Ig-like V-type (immunoglobulin-like) domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF111713; AAD42050.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF207907; AAF22829.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172398; AAD48877.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136649; CAB66584.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358896; AAQ89255.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001533; AAH01533.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00001754; -.
PIR A59406; S56749.
RefSeq NP_058642.1; -.
UniGene Hs.517293
3D structure databases
PDB
1NBQ; X-ray; 2.90 A; A/B=27-233.[ExPASy / RCSB / EBI]
3EOY; X-ray; 3.40 A; G/H/I/J/K/L=28-129.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1NBQ; -.
3EOY; -.
ModBase Q9Y624.
Protein-protein interaction databases
IntAct Q9Y624; 1.
PTM databases
PhosphoSite Q9Y624; -.
Enzyme and pathway databases
Pathway_Interaction_DB avb3_integrin_pathway; Integrins in angiogenesis.
Reactome REACT_13552; Integrin cell surface interactions.
REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC01M159231; -.
H-InvDB HIX0001225; -.
HGNC HGNC:14685; F11R.
GenAtlas F11R.
HPA CAB004671; -.
MIM 605721; gene. [NCBI / EBI]
PharmGKB PA29991; -.
Gene expression databases
ArrayExpress Q9Y624; -.
Bgee Q9Y624; -.
CleanEx HS_F11R; -.
GermOnline ENSG00000158769; Homo sapiens.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005923; Cellular component: tight junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0006954; Biological process: inflammatory response (traceable author statement from ProtInc).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR003598; Ig_sub2.
IPR013106; Ig_V-set.
IPR003596; Ig_V-set_sub.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 2.
Pfam PF00047; ig; 1.
PF07686; V-set; 1.
Pfam graphical view of domain structure.
SMART SM00408; IGc2; 1.
SM00406; IGv; 1.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q9Y624; -.
PRIDE Q9Y624; -.
Genome annotation databases
Ensembl ENSG00000158769; Homo sapiens. [Contig view]
GeneID 50848; -.
KEGG hsa:50848; -.
Phylogenomic databases
HOGENOM Q9Y624; -.
HOVERGEN Q9Y624; -.
OMA Q9Y624; RVEWKFV.
Other
NextBio 53317; -.
SOURCE F11R; Homo sapiens.
ProtoNet Q9Y624.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell junction; Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; Host-virus interaction; Immunoglobulin domain; Membrane; Phosphoprotein; Repeat; Signal; Tight junction; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    27  27      
CHAIN   28   299  272     Junctional adhesion molecule A. PRO_0000015066
TOPO_DOM   28   238  211     Extracellular (Potential). 
TRANSMEM   239   259  21     Potential. 
TOPO_DOM   260   299  40     Cytoplasmic (Potential). 
DOMAIN   28   125  98     Ig-like V-type 1. 
DOMAIN   135   228  94     Ig-like V-type 2. 
MOD_RES   273   273        Phosphothreonine. 
MOD_RES   275   275        Phosphoserine. 
MOD_RES   280   280        Phosphotyrosine. 
MOD_RES   281   281        Phosphoserine. 
MOD_RES   284   284        Phosphoserine. 
MOD_RES   287   287        Phosphoserine. 
CARBOHYD   185   185        N-linked (GlcNAc...). 
CARBOHYD   191   191        N-linked (GlcNAc...). 
DISULFID   50   109         
DISULFID   153   212         
STRAND   30    32  3      
STRAND   47    49  3      
STRAND   51    54  4      
STRAND   56    66  11      
STRAND   69    75  7      
TURN   81    86  6      
STRAND   88    90  3      
STRAND   93    95  3      
STRAND   105   113  9      
STRAND   123   125  3      
STRAND   128   130  3      
STRAND   140   144  5      
STRAND   149   151  3      
STRAND   163   168  6      
STRAND   177   182  6      
TURN   192   194  3      
STRAND   197   201  5      
HELIX   204   206  3      
STRAND   210   215  6      
STRAND   217   219  3      
STRAND   230   232  3      
Sequence information
Length: 299 AA [This is the length of the unprocessed precursor] Molecular weight: 32583 Da [This is the MW of the unprocessed precursor] CRC64: D95DE2FEA23D2851 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC AYSGFSSPRV 

        70         80         90        100        110        120 
EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT REDTGTYTCM VSEEGGNSYG 

       130        140        150        160        170        180 
EVKVKLIVLV PPSKPTVNIP SSATIGNRAV LTCSEQDGSP PSEYTWFKDG IVMPTNPKST 

       190        200        210        220        230        240 
RAFSNSSYVL NPTTGELVFD PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGVIV 

       250        260        270        280        290 
AAVLVTLILL GILVFGIWFA YSRGHFDRTK KGTSSKKVIY SQPSARSEGE FKQTSSFLV 

Q9Y624 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!