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Q9JI59 (JAM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Junctional adhesion molecule B

Short name=JAM-B
Alternative name(s):
Junctional adhesion molecule 2
Short name=JAM-2
Vascular endothelial junction-associated molecule
Short name=VE-JAM
CD_antigen=CD322
Gene names
Name:Jam2
Synonyms:Vejam
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the processes of lymphocyte homing to secondary lymphoid organs By similarity.

Subunit structure

Interacts with JAM3 By similarity.

Subcellular location

Cell junctiontight junction. Cell membrane; Single-pass type I membrane protein. Note: Localized at tight junctions of both epithelial and endothelial cells. Ref.2

Sequence similarities

Belongs to the immunoglobulin superfamily.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.1
Chain29 – 298270Junctional adhesion molecule B
PRO_0000015070

Regions

Topological domain29 – 236208Extracellular Potential
Transmembrane237 – 25721Helical; Potential
Topological domain258 – 29841Cytoplasmic Potential
Domain32 – 12897Ig-like V-type
Domain135 – 238104Ig-like C2-type

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 110 Potential
Disulfide bond156 ↔ 214 Potential

Experimental info

Sequence conflict1331V → M in BAC26102. Ref.3
Sequence conflict1741T → H in BAC37139. Ref.3
Sequence conflict1831G → R in BAC37139. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9JI59 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1124E0F07E6CF751

FASTA29833,047
        10         20         30         40         50         60 
MARSPQGLLM LLLLHYLIVA LDYHKANGFS ASKDHRQEVT VIEFQEAILA CKTPKKTTSS 

        70         80         90        100        110        120 
RLEWKKVGQG VSLVYYQQAL QGDFKDRAEM IDFNIRIKNV TRSDAGEYRC EVSAPTEQGQ 

       130        140        150        160        170        180 
NLQEDKVMLE VLVAPAVPAC EVPTSVMTGS VVELRCQDKE GNPAPEYIWF KDGTSLLGNP 

       190        200        210        220        230        240 
KGGTHNNSSY TMNTKSGILQ FNMISKMDSG EYYCEARNSV GHRRCPGKRM QVDVLNISGI 

       250        260        270        280        290 
IATVVVVAFV ISVCGLGTCY AQRKGYFSKE TSFQKGSPAS KVTTMSENDF KHTKSFII 

« Hide

References

« Hide 'large scale' references
[1]"Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells."
Palmeri D., van Zante A., Huang C.-C., Hemmerich S., Rosen S.D.
J. Biol. Chem. 275:19139-19145(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-33.
Strain: C57BL/6J.
[2]"Cloning of JAM-2 and JAM-3: an emerging junctional adhesion molecular family?"
Aurrand-Lions M.A., Duncan L., Du Pasquier L., Imhof B.A.
Curr. Top. Microbiol. Immunol. 251:91-98(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head, Medulla oblongata and Skin.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[6]"Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response."
Muller W.A.
Trends Immunol. 24:327-334(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF255911 mRNA. Translation: AAF81224.1.
AJ291757 mRNA. Translation: CAC20699.1.
AK010616 mRNA. Translation: BAB27064.1.
AK013914 mRNA. Translation: BAB29053.1.
AK028757 mRNA. Translation: BAC26102.1.
AK078128 mRNA. Translation: BAC37139.1.
CT027693, AC164162 Genomic DNA. Translation: CAO78081.1.
BC028778 mRNA. Translation: AAH28778.1.
CCDSCCDS37381.1.
RefSeqNP_076333.3. NM_023844.5.
UniGeneMm.41758.

3D structure databases

ProteinModelPortalQ9JI59.
SMRQ9JI59. Positions 36-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000109833.

PTM databases

PhosphoSiteQ9JI59.

Proteomic databases

PaxDbQ9JI59.
PRIDEQ9JI59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114195; ENSMUSP00000109833; ENSMUSG00000053062.
GeneID67374.
KEGGmmu:67374.
UCSCuc007ztg.2. mouse.

Organism-specific databases

CTD58494.
MGIMGI:1933820. Jam2.

Phylogenomic databases

eggNOGNOG132289.
GeneTreeENSGT00730000110678.
HOGENOMHOG000247041.
HOVERGENHBG000518.
InParanoidA6X955.
KOK06735.
OMASVGHRRC.
OrthoDBEOG7MH0Z1.
PhylomeDBQ9JI59.
TreeFamTF331459.

Gene expression databases

ArrayExpressQ9JI59.
BgeeQ9JI59.
CleanExMM_JAM2.
GenevestigatorQ9JI59.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF07679. I-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio324388.
PROQ9JI59.
SOURCESearch...

Entry information

Entry nameJAM2_MOUSE
AccessionPrimary (citable) accession number: Q9JI59
Secondary accession number(s): A6X955, Q8C5K9, Q8CE95
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot