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Q9BX67 (JAM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Junctional adhesion molecule C

Short name=JAM-C
Alternative name(s):
JAM-2
Junctional adhesion molecule 3
Short name=JAM-3
Gene names
Name:JAM3
ORF Names:UNQ859/PRO1868
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in cell-cell adhesion. It is a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). The soluble form is a mediator of angiogenesis. Ref.3 Ref.12 Ref.16

Subunit structure

Interacts with JAM2. Interacts with ITGAM. Ref.1 Ref.3 Ref.12

Subcellular location

Cell membrane; Single-pass type I membrane protein Potential. Cell junctiondesmosome. Secretedextracellular space. Note: In epithelial cells, it is expressed at desmosomes but not at tight junctions. Localizes at the cell surface of endothelial cells; treatment of endothelial cells with vascular endothelial growth factor stimulates recruitment of JAM3 to cell-cell contacts. Ref.12 Ref.13 Ref.16

Tissue specificity

Highest expression in placenta, brain and kidney. Significant expression is detected on platelets. Expressed in intestinal mucosa cells. Expressed in the vascular endothelium. Found in serum (at protein level). Also detected in the synovial fluid of patients with rheumatoid arthritis, psoriatic arthritis or ostearthritis (at protein level). Ref.1 Ref.3 Ref.4 Ref.12 Ref.13 Ref.16

Post-translational modification

Proteolytically cleaved from endothelial cells surface into a soluble form by ADAM10 and ADAM17; the release of soluble JAM3 is increased by proinflammatory factors. Ref.16

Involvement in disease

Hemorrhagic destruction of the brain with subependymal calcification and cataracts (HDBSCC) [MIM:613730]: A syndrome characterized by congenital cataracts and severe brain abnormalities apparently resulting from hemorrhagic destruction of the brain parenchyma, including the cerebral white matter and basal ganglia. Patients manifest profound developmental delay, and other neurologic features included seizures, spasticity, and hyperreflexia. The clinical course is very severe resulting in death in infancy. Brain imaging shows multifocal intraparenchymal hemorrhage with associated liquefaction and massive cystic degeneration, and calcification in the subependymal region and in brain tissue.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.18

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 caution

The sequence CAC94776.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAngiogenesis
Cell adhesion
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainImmunoglobulin domain
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadaptive immune response

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from direct assay Ref.16. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

establishment of cell polarity

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

leukocyte migration involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

myelination

Inferred from electronic annotation. Source: Ensembl

myeloid progenitor cell differentiation

Inferred from electronic annotation. Source: Ensembl

neutrophil homeostasis

Inferred from electronic annotation. Source: Ensembl

regulation of actin cytoskeleton organization by cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of neutrophil chemotaxis

Inferred from direct assay Ref.12. Source: UniProtKB

spermatid development

Inferred from electronic annotation. Source: Ensembl

transmission of nerve impulse

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSchmidt-Lanterman incisure

Inferred from electronic annotation. Source: Ensembl

cell-cell contact zone

Inferred from direct assay Ref.13. Source: UniProtKB

desmosome

Inferred from direct assay Ref.12. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.16. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

paranodal junction

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

tight junction

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionintegrin binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

JAM2P570872EBI-4314733,EBI-3918416

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BX67-1)

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.
Isoform 2 (identifier: Q9BX67-2)

The sequence of this isoform differs from the canonical sequence as follows:
     85-135: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.10
Chain32 – 310279Junctional adhesion molecule C
PRO_0000015071

Regions

Topological domain32 – 241210Extracellular Potential
Transmembrane242 – 26221Helical; Potential
Topological domain263 – 31048Cytoplasmic Potential
Domain35 – 12793Ig-like V-type
Domain139 – 23698Ig-like C2-type

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Ref.14
Glycosylation1981N-linked (GlcNAc...); atypical Ref.14
Disulfide bond53 ↔ 115 Potential
Disulfide bond160 ↔ 219 Potential

Natural variations

Alternative sequence85 – 13551Missing in isoform 2.
VSP_042561
Natural variant1161E → K in HDBSCC. Ref.18
VAR_069529
Natural variant2191C → Y in HDBSCC; the mutant is retained in the endoplasmic reticulum. Ref.18
VAR_069530

Experimental info

Sequence conflict1361Q → R in AAH10690. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: CE39ADF33EA1DAB9

FASTA31035,020
        10         20         30         40         50         60 
MALRRPPRLR LCARLPDFFL LLLFRGCLIG AVNLKSSNRT PVVQEFESVE LSCIITDSQT 

        70         80         90        100        110        120 
SDPRIEWKKI QDEQTTYVFF DNKIQGDLAG RAEILGKTSL KIWNVTRRDS ALYRCEVVAR 

       130        140        150        160        170        180 
NDRKEIDEIV IELTVQVKPV TPVCRVPKAV PVGKMATLHC QESEGHPRPH YSWYRNDVPL 

       190        200        210        220        230        240 
PTDSRANPRF RNSSFHLNSE TGTLVFTAVH KDDSGQYYCI ASNDAGSARC EEQEMEVYDL 

       250        260        270        280        290        300 
NIGGIIGGVL VVLAVLALIT LGICCAYRRG YFINNKQDGE SYKNPGKPDG VNYIRTDEEG 

       310 
DFRHKSSFVI 

« Hide

Isoform 2 [UniParc].

Checksum: 00F852424B415045
Show »

FASTA25929,223

References

« Hide 'large scale' references
[1]"Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor."
Arrate M.P., Rodriguez J.M., Tran T.M., Brock T.A., Cunningham S.A.
J. Biol. Chem. 276:45826-45832(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH JAM2, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members."
Aurrand-Lions M.A., Johnson-Leger C., Wong C., Du Pasquier L., Imhof B.A.
Blood 98:3699-3707(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1."
Santoso S., Sachs U.J.H., Kroll H., Linder M., Ruf A., Preissner K.T., Chavakis T.
J. Exp. Med. 196:679-691(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ITGAM.
[4]"Narrowing the critical region within 11q24-qter for hypoplastic left heart and identification of a candidate gene, JAM3, expressed during cardiogenesis."
Phillips H.M., Renforth G.L., Spalluto C., Hearn T., Curtis A.R.J., Craven L., Havarani B., Clement-Jones M., English C., Stumper O., Salmon T., Hutchinson S., Jackson M.S., Wilson D.I.
Genomics 79:475-478(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Thalamus.
[6]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORM 1).
Tissue: Eye and Uterus.
[10]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-46.
[11]"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.
[12]"JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated neutrophil transepithelial migration."
Zen K., Babbin B.A., Liu Y., Whelan J.B., Nusrat A., Parkos C.A.
Mol. Biol. Cell 15:3926-3937(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEUTROPHIL TRANSEPITHELIAL MIGRATION, INTERACTION WITH ITGAM, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[13]"Antibody against junctional adhesion molecule-C inhibits angiogenesis and tumor growth."
Lamagna C., Hodivala-Dilke K.M., Imhof B.A., Aurrand-Lions M.
Cancer Res. 65:5703-5710(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[14]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192 AND ASN-198.
Tissue: Leukemic T-cell.
[15]"A homozygous mutation in the tight-junction protein JAM3 causes hemorrhagic destruction of the brain, subependymal calcification, and congenital cataracts."
Mochida G.H., Ganesh V.S., Felie J.M., Gleason D., Hill R.S., Clapham K.R., Rakiec D., Tan W.H., Akawi N., Al-Saffar M., Partlow J.N., Tinschert S., Barkovich A.J., Ali B., Al-Gazali L., Walsh C.A.
Am. J. Hum. Genet. 87:882-889(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HDBSCC.
[16]"Junctional adhesion molecule-C is a soluble mediator of angiogenesis."
Rabquer B.J., Amin M.A., Teegala N., Shaheen M.K., Tsou P.S., Ruth J.H., Lesch C.A., Imhof B.A., Koch A.E.
J. Immunol. 185:1777-1785(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE BY ADAM10 AND ADAM17.
[17]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Delineation of the clinical, molecular and cellular aspects of novel JAM3 mutations underlying the autosomal recessive hemorrhagic destruction of the brain, subependymal calcification, and congenital cataracts."
Akawi N.A., Canpolat F.E., White S.M., Quilis-Esquerra J., Morales Sanchez M., Gamundi M.J., Mochida G.H., Walsh C.A., Ali B.R., Al-Gazali L.
Hum. Mutat. 34:498-505(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HDBSCC LYS-116 AND TYR-219, CHARACTERIZATION OF VARIANT HDBSCC TYR-219.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF356518 mRNA. Translation: AAK27221.1.
AJ344431 mRNA. Translation: CAC69845.1.
AF448478 mRNA. Translation: AAM20925.1.
AJ416101 mRNA. Translation: CAC94776.1. Different initiation.
AK074769 mRNA. Translation: BAC11195.1.
AK075309 mRNA. Translation: BAC11538.1.
AK125071 mRNA. Translation: BAG54131.1.
AY358335 mRNA. Translation: AAQ88701.1.
AP000911 Genomic DNA. No translation available.
AP001775 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67820.1.
BC010690 mRNA. Translation: AAH10690.1.
BC012147 mRNA. Translation: AAH12147.1.
RefSeqNP_001192258.1. NM_001205329.1.
NP_116190.3. NM_032801.4.
UniGeneHs.150718.

3D structure databases

ProteinModelPortalQ9BX67.
SMRQ9BX67. Positions 43-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123734. 6 interactions.
IntActQ9BX67. 2 interactions.
MINTMINT-4085421.
STRING9606.ENSP00000299106.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ9BX67.

Polymorphism databases

DMDM51701611.

Proteomic databases

PaxDbQ9BX67.
PRIDEQ9BX67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299106; ENSP00000299106; ENSG00000166086. [Q9BX67-1]
ENST00000441717; ENSP00000395742; ENSG00000166086. [Q9BX67-2]
ENST00000529443; ENSP00000431883; ENSG00000166086.
GeneID83700.
KEGGhsa:83700.
UCSCuc001qhb.3. human. [Q9BX67-1]
uc009zcz.2. human. [Q9BX67-2]

Organism-specific databases

CTD83700.
GeneCardsGC11P133972.
HGNCHGNC:15532. JAM3.
HPAHPA003417.
MIM606871. gene.
613730. phenotype.
neXtProtNX_Q9BX67.
Orphanet306547. Porencephaly-microcephaly-bilateral congenital cataract syndrome.
PharmGKBPA29993.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147320.
HOGENOMHOG000247041.
HOVERGENHBG000518.
InParanoidQ9BX67.
KOK06785.
OrthoDBEOG7DZ8KX.
PhylomeDBQ9BX67.
TreeFamTF331459.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9BX67.
BgeeQ9BX67.
CleanExHS_JAM3.
GenevestigatorQ9BX67.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF07686. 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

ChiTaRSJAM3. human.
GeneWikiJAM3.
GenomeRNAi83700.
NextBio72688.
PROQ9BX67.
SOURCESearch...

Entry information

Entry nameJAM3_HUMAN
AccessionPrimary (citable) accession number: Q9BX67
Secondary accession number(s): B3KWG9, Q8WWL8, Q96FL1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM