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Q9Y624

- JAM1_HUMAN

UniProt

Q9Y624 - JAM1_HUMAN

Protein

Junctional adhesion molecule A

Gene

F11R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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 - Molecular functioni

    1. protein binding Source: IntAct

    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. tight junction assembly Source: Reactome
    10. transforming growth factor beta receptor signaling pathway Source: Reactome
    11. viral process Source: UniProtKB-KW

    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.

    GO - Cellular componenti

    1. cell-cell junction Source: ProtInc
    2. cell junction Source: HPA
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of membrane Source: UniProtKB-KW
    5. microtubule cytoskeleton Source: HPA
    6. plasma membrane Source: LIFEdb
    7. tight junction Source: UniProtKB-SubCell

    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...)2 Publications
    Glycosylationi191 – 1911N-linked (GlcNAc...)2 Publications
    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

    ArrayExpressiQ9Y624.
    BgeeiQ9Y624.
    CleanExiHS_F11R.
    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. 10 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 – 323
    Beta strandi36 – 405
    Beta strandi47 – 493
    Beta strandi51 – 544
    Beta strandi56 – 6611
    Beta strandi69 – 757
    Beta strandi76 – 794
    Turni81 – 866
    Beta strandi88 – 903
    Beta strandi93 – 953
    Helixi101 – 1033
    Beta strandi105 – 1139
    Beta strandi123 – 1253
    Beta strandi128 – 1303
    Beta strandi140 – 1445
    Beta strandi149 – 1513
    Beta strandi163 – 1686
    Beta strandi177 – 1826
    Turni192 – 1943
    Beta strandi197 – 2015
    Helixi204 – 2063
    Beta strandi210 – 2156
    Beta strandi217 – 2193
    Beta strandi230 – 2323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei239 – 25921HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC    50
    AYSGFSSPRV EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT 100
    REDTGTYTCM VSEEGGNSYG EVKVKLIVLV PPSKPTVNIP SSATIGNRAV 150
    LTCSEQDGSP PSEYTWFKDG IVMPTNPKST RAFSNSSYVL NPTTGELVFD 200
    PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGVIV AAVLVTLILL 250
    GILVFGIWFA YSRGHFDRTK KGTSSKKVIY SQPSARSEGE FKQTSSFLV 299
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiA59406. S56749.
    RefSeqiNP_058642.1. NM_016946.4.
    UniGeneiHs.517293.

    Genome annotation databases

    EnsembliENST00000368026; ENSP00000357005; ENSG00000158769.
    ENST00000537746; ENSP00000440812; ENSG00000158769.
    GeneIDi50848.
    KEGGihsa:50848.
    UCSCiuc001fxf.4. human.

    Polymorphism databases

    DMDMi10720061.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1213.1.
    PIRi A59406. S56749.
    RefSeqi NP_058642.1. NM_016946.4.
    UniGenei Hs.517293.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q9Y624.
    SMRi Q9Y624. Positions 25-233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119153. 10 interactions.
    IntActi Q9Y624. 5 interactions.
    MINTi MINT-154235.
    STRINGi 9606.ENSP00000289779.

    PTM databases

    PhosphoSitei Q9Y624.

    Polymorphism databases

    DMDMi 10720061.

    Proteomic databases

    MaxQBi Q9Y624.
    PaxDbi Q9Y624.
    PeptideAtlasi Q9Y624.
    PRIDEi Q9Y624.

    Protocols and materials databases

    DNASUi 50848.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368026 ; ENSP00000357005 ; ENSG00000158769 .
    ENST00000537746 ; ENSP00000440812 ; ENSG00000158769 .
    GeneIDi 50848.
    KEGGi hsa:50848.
    UCSCi uc001fxf.4. human.

    Organism-specific databases

    CTDi 50848.
    GeneCardsi GC01M160965.
    GC01M160975.
    HGNCi HGNC:14685. F11R.
    HPAi CAB004671.
    HPA043616.
    MIMi 605721. gene.
    neXtProti NX_Q9Y624.
    PharmGKBi PA29991.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG150281.
    HOVERGENi HBG000518.
    InParanoidi Q9Y624.
    KOi K06089.
    OMAi SCSYSGF.
    OrthoDBi EOG7MH0Z1.
    PhylomeDBi Q9Y624.
    TreeFami TF343984.

    Enzyme and pathway databases

    Reactomei REACT_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

    ChiTaRSi F11R. human.
    EvolutionaryTracei Q9Y624.
    GeneWikii F11_receptor.
    GenomeRNAii 50848.
    NextBioi 53317.
    PROi Q9Y624.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y624.
    Bgeei Q9Y624.
    CleanExi HS_F11R.
    Genevestigatori Q9Y624.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR003596. Ig_V-set_subgr.
    [Graphical view ]
    Pfami PF07686. V-set. 1 hit.
    [Graphical view ]
    SMARTi SM00408. IGc2. 1 hit.
    SM00406. IGv. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 150 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