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Junctional adhesion molecule A (JAM-A) (Junctional adhesion molecule 1) (JAM-1) (Platelet F11 receptor) (Platelet adhesion molecule 1) (PAM-1) (CD antigen CD321)

 JAM1_HUMAN              Reviewed;         299 AA.
Q9Y624; B7Z941;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
27-SEP-2017, entry version 180.
RecName: Full=Junctional adhesion molecule A;
Short=JAM-A;
AltName: Full=Junctional adhesion molecule 1;
Short=JAM-1;
AltName: Full=Platelet F11 receptor;
AltName: Full=Platelet adhesion molecule 1;
Short=PAM-1;
AltName: CD_antigen=CD321;
Flags: Precursor;
Name=F11R; Synonyms=JAM1, JCAM; ORFNames=UNQ264/PRO301;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10395639;
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] (ISOFORM 1), AND FUNCTION.
PubMed=10753840;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
PubMed=11171323;
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] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
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] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
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] (ISOFORM 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[9]
PROTEIN SEQUENCE OF 28-103 AND 123-130, AND GLYCOSYLATION.
PubMed=7646439; DOI=10.1042/bj3100155;
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).
[10]
PROTEIN SEQUENCE OF 28-42.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[11]
PROTEIN SEQUENCE OF 28-39.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
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).
[12]
FUNCTION, AND INTERACTION WITH MPDZ.
PubMed=11489913; DOI=10.1083/jcb.200103047;
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).
[13]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MAMMALIAN
REOVIRUS SIGMA-1 PROTEIN.
PubMed=11239401; DOI=10.1016/S0092-8674(01)00231-8;
Barton E.S., Forrest J.C., Connolly J.L., Chappell J.D., Liu Y.,
Schnell F.J., Nusrat A., Parkos C.A., Dermody T.S.;
"Junction adhesion molecule is a receptor for reovirus.";
Cell 104:441-451(2001).
[14]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
PubMed=11812992; DOI=10.1038/ni755;
Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.;
"JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in
transendothelial migration of leukocytes.";
Nat. Immunol. 3:151-158(2002).
[15]
REVIEW, AND NOMENCLATURE.
PubMed=12810109; DOI=10.1016/S1471-4906(03)00117-0;
Muller W.A.;
"Leukocyte-endothelial-cell interactions in leukocyte transmigration
and the inflammatory response.";
Trends Immunol. 24:327-334(2003).
[16]
INTERACTION WITH ITGAL.
PubMed=15528364; DOI=10.4049/jimmunol.173.10.6259;
Fraemohs L., Koenen R.R., Ostermann G., Heinemann B., Weber C.;
"The functional interaction of the beta 2 integrin lymphocyte
function-associated antigen-1 with junctional adhesion molecule-A is
mediated by the I domain.";
J. Immunol. 173:6259-6264(2004).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281; SER-284 AND
SER-287, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-191.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-287, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-27, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ROTAVIRUS
STRAIN WA VP4 PROTEIN.
PubMed=25481868; DOI=10.1016/j.virol.2014.11.016;
Torres-Flores J.M., Silva-Ayala D., Espinoza M.A., Lopez S.,
Arias C.F.;
"The tight junction protein JAM-A functions as coreceptor for
rotavirus entry into MA104 cells.";
Virology 475:172-178(2015).
[27]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 27-233, AND DISULFIDE BONDS.
PubMed=12697893; DOI=10.1073/pnas.0937718100;
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).
-!- 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). {ECO:0000250|UniProtKB:O88792,
ECO:0000269|PubMed:10753840, ECO:0000269|PubMed:11489913,
ECO:0000269|PubMed:11812992}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Mammalian
reovirus sigma-1. {ECO:0000269|PubMed:11239401}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Human
Rotavirus strain Wa. {ECO:0000269|PubMed:25481868}.
-!- 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).
{ECO:0000250|UniProtKB:O88792, ECO:0000269|PubMed:11489913,
ECO:0000269|PubMed:15528364}.
-!- SUBUNIT: (Microbial infection) Interacts with Mammalian reovirus
sigma-1 capsid protein. {ECO:0000269|PubMed:11239401}.
-!- SUBUNIT: (Microbial infection) Interacts with Human Rotavirus
strain Wa vp4 capsid protein. {ECO:0000269|PubMed:25481868}.
-!- INTERACTION:
Q8TEW0:PARD3; NbExp=2; IntAct=EBI-742600, EBI-81968;
Q05513:PRKCZ; NbExp=2; IntAct=EBI-742600, EBI-295351;
O43765:SGTA; NbExp=9; IntAct=EBI-742600, EBI-347996;
-!- SUBCELLULAR LOCATION: Cell junction, tight junction
{ECO:0000269|PubMed:11171323}. Cell membrane
{ECO:0000269|PubMed:11171323}; Single-pass type I membrane protein
{ECO:0000269|PubMed:11171323}. Note=Localized at tight junctions
of both epithelial and endothelial cells.
{ECO:0000269|PubMed:11171323}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y624-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y624-2; Sequence=VSP_056218;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in endothelium, epithelium and
leukocytes (at protein level). {ECO:0000269|PubMed:11812992}.
-!- DOMAIN: The Ig-like V-type 2 domain is necessary and sufficient
for interaction with integrin alpha-L/beta-2.
{ECO:0000269|PubMed:11812992}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:7646439}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
{ECO:0000305}.
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EMBL; AF111713; AAD42050.1; -; mRNA.
EMBL; AF207907; AAF22829.1; -; mRNA.
EMBL; AF172398; AAD48877.1; -; mRNA.
EMBL; AL136649; CAB66584.1; -; mRNA.
EMBL; AY358896; AAQ89255.1; -; mRNA.
EMBL; AK304412; BAH14177.1; -; mRNA.
EMBL; AL591806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001533; AAH01533.1; -; mRNA.
CCDS; CCDS1213.1; -. [Q9Y624-1]
PIR; A59406; S56749.
RefSeq; NP_001335020.1; NM_001348091.1. [Q9Y624-2]
RefSeq; NP_058642.1; NM_016946.5. [Q9Y624-1]
UniGene; Hs.517293; -.
PDB; 1NBQ; X-ray; 2.90 A; A/B=27-233.
PDB; 3EOY; X-ray; 3.40 A; G/H/I/J/K/L=28-129.
PDB; 3TSZ; X-ray; 2.50 A; B=288-299.
PDB; 4ODB; X-ray; 3.20 A; D/E/F=28-129.
PDBsum; 1NBQ; -.
PDBsum; 3EOY; -.
PDBsum; 3TSZ; -.
PDBsum; 4ODB; -.
ProteinModelPortal; Q9Y624; -.
SMR; Q9Y624; -.
BioGrid; 119153; 16.
CORUM; Q9Y624; -.
IntAct; Q9Y624; 8.
MINT; MINT-154235; -.
STRING; 9606.ENSP00000289779; -.
iPTMnet; Q9Y624; -.
PhosphoSitePlus; Q9Y624; -.
SwissPalm; Q9Y624; -.
BioMuta; F11R; -.
DMDM; 10720061; -.
EPD; Q9Y624; -.
PaxDb; Q9Y624; -.
PeptideAtlas; Q9Y624; -.
PRIDE; Q9Y624; -.
DNASU; 50848; -.
Ensembl; ENST00000368026; ENSP00000357005; ENSG00000158769. [Q9Y624-1]
Ensembl; ENST00000537746; ENSP00000440812; ENSG00000158769. [Q9Y624-2]
GeneID; 50848; -.
KEGG; hsa:50848; -.
UCSC; uc009wtt.4; human. [Q9Y624-1]
CTD; 50848; -.
DisGeNET; 50848; -.
EuPathDB; HostDB:ENSG00000158769.17; -.
GeneCards; F11R; -.
HGNC; HGNC:14685; F11R.
HPA; CAB004671; -.
HPA; HPA043616; -.
HPA; HPA061700; -.
MIM; 605721; gene.
neXtProt; NX_Q9Y624; -.
OpenTargets; ENSG00000158769; -.
PharmGKB; PA29991; -.
eggNOG; ENOG410IWUE; Eukaryota.
eggNOG; ENOG410YHHV; LUCA.
GeneTree; ENSGT00730000110678; -.
HOVERGEN; HBG000518; -.
InParanoid; Q9Y624; -.
KO; K06089; -.
OMA; NRAFSNS; -.
OrthoDB; EOG091G05PI; -.
PhylomeDB; Q9Y624; -.
TreeFam; TF343984; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-420029; Tight junction interactions.
SIGNOR; Q9Y624; -.
ChiTaRS; F11R; human.
EvolutionaryTrace; Q9Y624; -.
GeneWiki; F11_receptor; -.
GenomeRNAi; 50848; -.
PRO; PR:Q9Y624; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000158769; -.
CleanEx; HS_F11R; -.
ExpressionAtlas; Q9Y624; baseline and differential.
Genevisible; Q9Y624; HS.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; TAS:Reactome.
GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
GO; GO:0036057; C:slit diaphragm; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
GO; GO:0070830; P:bicellular tight junction assembly; TAS:Reactome.
GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:UniProtKB.
GO; GO:0090002; P:establishment of protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0050892; P:intestinal absorption; IMP:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
GO; GO:0090559; P:regulation of membrane permeability; IMP:UniProtKB.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Immunoglobulin domain; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Tight junction; Transmembrane; Transmembrane helix.
SIGNAL 1 27 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:7646439}.
CHAIN 28 299 Junctional adhesion molecule A.
/FTId=PRO_0000015066.
TOPO_DOM 28 238 Extracellular. {ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TOPO_DOM 260 299 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 125 Ig-like V-type 1.
DOMAIN 135 228 Ig-like V-type 2.
MOD_RES 281 281 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 50 109 {ECO:0000269|PubMed:12697893}.
DISULFID 153 212 {ECO:0000269|PubMed:12697893}.
VAR_SEQ 81 129 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056218.
STRAND 30 32 {ECO:0000244|PDB:1NBQ}.
STRAND 36 41 {ECO:0000244|PDB:4ODB}.
STRAND 47 49 {ECO:0000244|PDB:1NBQ}.
STRAND 51 54 {ECO:0000244|PDB:1NBQ}.
STRAND 56 66 {ECO:0000244|PDB:1NBQ}.
STRAND 69 75 {ECO:0000244|PDB:1NBQ}.
STRAND 76 79 {ECO:0000244|PDB:3EOY}.
TURN 81 86 {ECO:0000244|PDB:1NBQ}.
STRAND 88 90 {ECO:0000244|PDB:1NBQ}.
STRAND 93 95 {ECO:0000244|PDB:1NBQ}.
HELIX 101 103 {ECO:0000244|PDB:4ODB}.
STRAND 105 113 {ECO:0000244|PDB:1NBQ}.
STRAND 123 125 {ECO:0000244|PDB:1NBQ}.
STRAND 128 130 {ECO:0000244|PDB:1NBQ}.
STRAND 140 144 {ECO:0000244|PDB:1NBQ}.
STRAND 149 151 {ECO:0000244|PDB:1NBQ}.
STRAND 163 168 {ECO:0000244|PDB:1NBQ}.
STRAND 177 182 {ECO:0000244|PDB:1NBQ}.
TURN 192 194 {ECO:0000244|PDB:1NBQ}.
STRAND 197 201 {ECO:0000244|PDB:1NBQ}.
HELIX 204 206 {ECO:0000244|PDB:1NBQ}.
STRAND 210 215 {ECO:0000244|PDB:1NBQ}.
STRAND 217 219 {ECO:0000244|PDB:1NBQ}.
STRAND 230 232 {ECO:0000244|PDB:1NBQ}.
SEQUENCE 299 AA; 32583 MW; D95DE2FEA23D2851 CRC64;
MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC AYSGFSSPRV
EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT REDTGTYTCM VSEEGGNSYG
EVKVKLIVLV PPSKPTVNIP SSATIGNRAV LTCSEQDGSP PSEYTWFKDG IVMPTNPKST
RAFSNSSYVL NPTTGELVFD PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGVIV
AAVLVTLILL GILVFGIWFA YSRGHFDRTK KGTSSKKVIY SQPSARSEGE FKQTSSFLV


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