Q9Y624 (JAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Junctional adhesion molecule A
Short name=JAM-A

Alternative name(s):
Junctional adhesion molecule 1
Short name=JAM-1
Platelet F11 receptor
Platelet adhesion molecule 1
Short name=PAM-1
CD_antigen=CD321

Gene names

Name:	F11R
Synonyms:	JAM1, JCAM
ORF Names:	UNQ264/PRO301

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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 structure	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. Ref.10
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. Ref.3
Post-translational modification	N-glycosylated. Ref.7 Ref.16
Sequence similarities	Belongs to the immunoglobulin superfamily. Contains 2 Ig-like V-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell junction Cell membrane Membrane Tight junction
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome inflammatory response Traceable author statement. Source: ProtInc interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW leukocyte migration Traceable author statement. Source: Reactome tight junction assembly Traceable author statement. Source: Reactome
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Ref.7 Ref.8 Ref.9

Chain

28 – 299

272

Junctional adhesion molecule A

PRO_0000015066

Regions

Topological domain

28 – 238

211

Extracellular Potential

Transmembrane

239 – 259

21

Helical; Potential

Topological domain

260 – 299

40

Cytoplasmic Potential

Domain

28 – 125

98

Ig-like V-type 1

Domain

135 – 228

94

Ig-like V-type 2

Amino acid modifications

Modified residue

273

1

Phosphothreonine Ref.14

Modified residue

275

1

Phosphoserine Ref.14

Modified residue

280

1

Phosphotyrosine Ref.12 Ref.14 Ref.17

Modified residue

281

1

Phosphoserine Ref.14

Modified residue

284

1

Phosphoserine Ref.13 Ref.14 Ref.15

Modified residue

287

1

Phosphoserine Ref.14 Ref.15

Modified residue

296

1

Phosphoserine Ref.15

Glycosylation

185

1

N-linked (GlcNAc...) Ref.16

Glycosylation

191

1

N-linked (GlcNAc...) Ref.16

Disulfide bond

50 ↔ 109

Disulfide bond

153 ↔ 212

Secondary structure

1

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299

Helix Strand Turn

Details...

Beta strand

30 – 32

3

Beta strand

47 – 49

3

Beta strand

51 – 54

4

Beta strand

56 – 66

11

Beta strand

69 – 75

7

Turn

81 – 86

6

Beta strand

88 – 90

3

Beta strand

93 – 95

3

Beta strand

105 – 113

9

Beta strand

123 – 125

3

Beta strand

128 – 130

3

Beta strand

140 – 144

5

Beta strand

149 – 151

3

Beta strand

163 – 168

6

Beta strand

177 – 182

6

Turn

192 – 194

3

Beta strand

197 – 201

5

Helix

204 – 206

3

Beta strand

210 – 215

6

Beta strand

217 – 219

3

Beta strand

230 – 232

3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y624 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: D95DE2FEA23D2851	FASTA	299	32,583
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells." Ozaki H., Ishii K., Horiuchi H., Arai H., Kawamoto T., Okawa K., Iwamatsu A., Kita T. J. Immunol. 163:553-557(1999) [PubMed: 10395639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of the human platelet F11 receptor: a cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation." 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. Blood 95:2600-2609(2000) [PubMed: 10753840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody." Naik U.P., Naik M.U., Eckfeld K., Martin-DeLeon P., Spychala J. J. Cell Sci. 114:539-547(2001) [PubMed: 11171323] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[4]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." 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. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." 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. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[7]	"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." Naik U.P., Ehrlich Y.H., Kornecki E. Biochem. J. 310:155-162(1995) [PubMed: 7646439] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-103 AND 123-130, GLYCOSYLATION.
[8]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-42.
[9]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-39. Tissue: Platelet.
[10]	"Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions." Itoh M., Sasaki H., Furuse M., Ozaki H., Kita T., Tsukita S. J. Cell Biol. 154:491-497(2001) [PubMed: 11489913] [Abstract] Cited for: INTERACTION WITH MPDZ.
[11]	"Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response." Muller W.A. Trends Immunol. 24:327-334(2003) [PubMed: 12810109] [Abstract] Cited for: REVIEW, NOMENCLATURE.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-280, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[13]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, MASS SPECTROMETRY. Tissue: Platelet.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; SER-275; TYR-280; SER-281; SER-284 AND SER-287, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-287 AND SER-296, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-191, MASS SPECTROMETRY. Tissue: Liver.
[17]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-280, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding." 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. Proc. Natl. Acad. Sci. U.S.A. 100:5366-5371(2003) [PubMed: 12697893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 28-233.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF111713 mRNA. Translation: AAD42050.1.
AF207907 mRNA. Translation: AAF22829.1.
AF172398 mRNA. Translation: AAD48877.1.
AL136649 mRNA. Translation: CAB66584.1.
AY358896 mRNA. Translation: AAQ89255.1.
BC001533 mRNA. Translation: AAH01533.1.

IPI

IPI00001754.

PIR

S56749. A59406.

RefSeq

NP_058642.1. NM_016946.4.

UniGene

Hs.517293.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NBQ	X-ray	2.90	A/B	27-233	[»]
3EOY	X-ray	3.40	G/H/I/J/K/L	28-129	[»]
3TSZ	X-ray	2.50	B	288-299	[»]

ProteinModelPortal

Q9Y624.

SMR

Q9Y624. Positions 25-233.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y624. 3 interactions.

MINT

MINT-154235.

STRING

Q9Y624.

PTM databases

PhosphoSite

Q9Y624.

Polymorphism databases

DMDM

10720061.

Proteomic databases

PeptideAtlas

Q9Y624.

PRIDE

Q9Y624.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000289779; ENSP00000289779; ENSG00000158769.
ENST00000335772; ENSP00000337141; ENSG00000158769.
ENST00000368026; ENSP00000357005; ENSG00000158769.

GeneID

50848.

KEGG

hsa:50848.

UCSC

uc001fxf.2. human.

Organism-specific databases

CTD

50848.

GeneCards

GC01M160965.

H-InvDB

HIX0001225.

HGNC

HGNC:14685. F11R.

HPA

CAB004671.

MIM

605721. gene.

neXtProt

NX_Q9Y624.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00600000084033.

HOVERGEN

HBG000518.

InParanoid

Q9Y624.

OMA

SCSYSGF.

OrthoDB

EOG4VT5XV.

PhylomeDB

Q9Y624.

Enzyme and pathway databases

Pathway_Interaction_DB

avb3_integrin_pathway. Integrins in angiogenesis.

Reactome

REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q9Y624.

Bgee

Q9Y624.

CleanEx

HS_F11R.

Genevestigator

Q9Y624.

GermOnline

ENSG00000158769. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 2 hits.

KO

K06089.

Pfam

PF07679. I-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00408. IGc2. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

53317.

SOURCE

Search...

Entry information

Entry name

JAM1_HUMAN

Accession

Primary (citable) accession number: Q9Y624

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.