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Protein

Junctional adhesion molecule A

Gene

F11R

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seems to play 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.By similarity

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cell adhesion Source: Ensembl
  3. cell-cell junction organization Source: Reactome
  4. cell junction assembly Source: Reactome
  5. epithelial cell differentiation Source: Ensembl
  6. extracellular matrix organization Source: Reactome
  7. inflammatory response Source: ProtInc
  8. leukocyte migration Source: Reactome
  9. positive regulation of blood pressure Source: Ensembl
  10. response to radiation Source: Ensembl
  11. tight junction assembly Source: Reactome
  12. transforming growth factor beta receptor signaling pathway Source: Reactome
  13. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_13552. Integrin cell surface interactions.
REACT_19373. Tight junction interactions.

Names & Taxonomyi

Protein namesi
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 namesi
Name:F11R
Synonyms:JAM1, JCAM
ORF Names:UNQ264/PRO301
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14685. F11R.

Subcellular locationi

Cell junctiontight junction 1 Publication. Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
Note: Localized at tight junctions of both epithelial and endothelial cells.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 238211ExtracellularSequence AnalysisAdd
BLAST
Transmembranei239 – 25921HelicalSequence AnalysisAdd
BLAST
Topological domaini260 – 29940CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: ProtInc
  2. cell junction Source: HPA
  3. cytoplasmic vesicle Source: Ensembl
  4. extracellular vesicular exosome Source: UniProtKB
  5. integral component of membrane Source: UniProtKB-KW
  6. microtubule cytoskeleton Source: HPA
  7. plasma membrane Source: LIFEdb
  8. slit diaphragm Source: Ensembl
  9. tight junction Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29991.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27273 PublicationsAdd
BLAST
Chaini28 – 299272Junctional adhesion molecule APRO_0000015066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 109
Disulfide bondi153 ↔ 212
Glycosylationi185 – 1851N-linked (GlcNAc...)1 Publication
Glycosylationi191 – 1911N-linked (GlcNAc...)1 Publication
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei284 – 2841Phosphoserine4 Publications
Modified residuei287 – 2871Phosphoserine1 Publication

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9Y624.
PaxDbiQ9Y624.
PeptideAtlasiQ9Y624.
PRIDEiQ9Y624.

PTM databases

PhosphoSiteiQ9Y624.

Expressioni

Gene expression databases

BgeeiQ9Y624.
CleanExiHS_F11R.
ExpressionAtlasiQ9Y624. baseline and differential.
GenevestigatoriQ9Y624.

Organism-specific databases

HPAiCAB004671.
HPA043616.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PARD3Q8TEW02EBI-742600,EBI-81968
PRKCZQ055132EBI-742600,EBI-295351

Protein-protein interaction databases

BioGridi119153. 11 interactions.
IntActiQ9Y624. 5 interactions.
MINTiMINT-154235.
STRINGi9606.ENSP00000289779.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi36 – 405Combined sources
Beta strandi47 – 493Combined sources
Beta strandi51 – 544Combined sources
Beta strandi56 – 6611Combined sources
Beta strandi69 – 757Combined sources
Beta strandi76 – 794Combined sources
Turni81 – 866Combined sources
Beta strandi88 – 903Combined sources
Beta strandi93 – 953Combined sources
Helixi101 – 1033Combined sources
Beta strandi105 – 1139Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi163 – 1686Combined sources
Beta strandi177 – 1826Combined sources
Turni192 – 1943Combined sources
Beta strandi197 – 2015Combined sources
Helixi204 – 2063Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi230 – 2323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NBQX-ray2.90A/B27-233[»]
3EOYX-ray3.40G/H/I/J/K/L28-129[»]
3TSZX-ray2.50B288-299[»]
ProteinModelPortaliQ9Y624.
SMRiQ9Y624. Positions 25-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y624.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 12598Ig-like V-type 1Add
BLAST
Domaini135 – 22894Ig-like V-type 2Add
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG150281.
GeneTreeiENSGT00730000110678.
HOVERGENiHBG000518.
InParanoidiQ9Y624.
KOiK06089.
OMAiSCSYSGF.
OrthoDBiEOG7MH0Z1.
PhylomeDBiQ9Y624.
TreeFamiTF343984.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00408. IGc2. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y624-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC
60 70 80 90 100
AYSGFSSPRV EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT
110 120 130 140 150
REDTGTYTCM VSEEGGNSYG EVKVKLIVLV PPSKPTVNIP SSATIGNRAV
160 170 180 190 200
LTCSEQDGSP PSEYTWFKDG IVMPTNPKST RAFSNSSYVL NPTTGELVFD
210 220 230 240 250
PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGVIV AAVLVTLILL
260 270 280 290
GILVFGIWFA YSRGHFDRTK KGTSSKKVIY SQPSARSEGE FKQTSSFLV
Length:299
Mass (Da):32,583
Last modified:November 1, 1999 - v1
Checksum:iD95DE2FEA23D2851
GO
Isoform 2 (identifier: Q9Y624-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-129: Missing.

Note: No experimental confirmation available.

Show »
Length:250
Mass (Da):27,208
Checksum:i548D39B300559F53
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei81 – 12949Missing in isoform 2. 1 PublicationVSP_056218Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK304412 mRNA. Translation: BAH14177.1.
AL591806 Genomic DNA. No translation available.
BC001533 mRNA. Translation: AAH01533.1.
CCDSiCCDS1213.1. [Q9Y624-1]
PIRiA59406. S56749.
RefSeqiNP_058642.1. NM_016946.4. [Q9Y624-1]
UniGeneiHs.517293.

Genome annotation databases

EnsembliENST00000368026; ENSP00000357005; ENSG00000158769. [Q9Y624-1]
ENST00000537746; ENSP00000440812; ENSG00000158769. [Q9Y624-2]
GeneIDi50848.
KEGGihsa:50848.
UCSCiuc001fxf.4. human. [Q9Y624-1]
uc010pjv.2. human.

Polymorphism databases

DMDMi10720061.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
AK304412 mRNA. Translation: BAH14177.1.
AL591806 Genomic DNA. No translation available.
BC001533 mRNA. Translation: AAH01533.1.
CCDSiCCDS1213.1. [Q9Y624-1]
PIRiA59406. S56749.
RefSeqiNP_058642.1. NM_016946.4. [Q9Y624-1]
UniGeneiHs.517293.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NBQX-ray2.90A/B27-233[»]
3EOYX-ray3.40G/H/I/J/K/L28-129[»]
3TSZX-ray2.50B288-299[»]
ProteinModelPortaliQ9Y624.
SMRiQ9Y624. Positions 25-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119153. 11 interactions.
IntActiQ9Y624. 5 interactions.
MINTiMINT-154235.
STRINGi9606.ENSP00000289779.

PTM databases

PhosphoSiteiQ9Y624.

Polymorphism databases

DMDMi10720061.

Proteomic databases

MaxQBiQ9Y624.
PaxDbiQ9Y624.
PeptideAtlasiQ9Y624.
PRIDEiQ9Y624.

Protocols and materials databases

DNASUi50848.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368026; ENSP00000357005; ENSG00000158769. [Q9Y624-1]
ENST00000537746; ENSP00000440812; ENSG00000158769. [Q9Y624-2]
GeneIDi50848.
KEGGihsa:50848.
UCSCiuc001fxf.4. human. [Q9Y624-1]
uc010pjv.2. human.

Organism-specific databases

CTDi50848.
GeneCardsiGC01M160965.
HGNCiHGNC:14685. F11R.
HPAiCAB004671.
HPA043616.
MIMi605721. gene.
neXtProtiNX_Q9Y624.
PharmGKBiPA29991.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG150281.
GeneTreeiENSGT00730000110678.
HOVERGENiHBG000518.
InParanoidiQ9Y624.
KOiK06089.
OMAiSCSYSGF.
OrthoDBiEOG7MH0Z1.
PhylomeDBiQ9Y624.
TreeFamiTF343984.

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_13552. Integrin cell surface interactions.
REACT_19373. Tight junction interactions.

Miscellaneous databases

ChiTaRSiF11R. human.
EvolutionaryTraceiQ9Y624.
GeneWikiiF11_receptor.
GenomeRNAii50848.
NextBioi35480641.
PROiQ9Y624.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y624.
CleanExiHS_F11R.
ExpressionAtlasiQ9Y624. baseline and differential.
GenevestigatoriQ9Y624.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
[Graphical view]
PfamiPF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00408. IGc2. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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.
    , 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] (ISOFORM 2).
    Tissue: Trachea.
  7. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Ovary.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-103 AND 123-130, GLYCOSYLATION.
  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 28-42.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-39.
    Tissue: Platelet.
  12. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPDZ.
  13. "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.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281; SER-284 AND SER-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-191.
    Tissue: Liver.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 28-233.

Entry informationi

Entry nameiJAM1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y624
Secondary accession number(s): B7Z941
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: January 7, 2015
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.