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Q9BY67

- CADM1_HUMAN

UniProt

Q9BY67 - CADM1_HUMAN

Protein

Cell adhesion molecule 1

Gene

CADM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      Previous versions | rss
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    Functioni

    Mediates homophilic cell-cell adhesion in a Ca2+-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca2+-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly By similarity. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa.By similarity7 Publications

    GO - Molecular functioni

    1. PDZ domain binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. receptor binding Source: UniProtKB

    GO - Biological processi

    1. adherens junction organization Source: Reactome
    2. apoptotic process Source: UniProtKB-KW
    3. bone development Source: Ensembl
    4. brain development Source: Ensembl
    5. calcium-independent cell-cell adhesion Source: Ensembl
    6. cell-cell junction organization Source: Reactome
    7. cell differentiation Source: UniProtKB-KW
    8. cell junction assembly Source: Reactome
    9. cell recognition Source: UniProtKB
    10. detection of stimulus Source: UniProtKB
    11. heterophilic cell-cell adhesion Source: UniProtKB
    12. homophilic cell adhesion Source: UniProtKB
    13. immune system process Source: UniProtKB-KW
    14. liver development Source: Ensembl
    15. positive regulation of cytokine secretion Source: UniProtKB
    16. positive regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
    17. spermatogenesis Source: UniProtKB-KW
    18. susceptibility to natural killer cell mediated cytotoxicity Source: UniProtKB
    19. synapse assembly Source: Ensembl
    20. unidimensional cell growth Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Apoptosis, Cell adhesion, Differentiation, Immunity, Spermatogenesis

    Enzyme and pathway databases

    ReactomeiREACT_19195. Adherens junctions interactions.
    REACT_19268. Nectin/Necl trans heterodimerization.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell adhesion molecule 1
    Alternative name(s):
    Immunoglobulin superfamily member 4
    Short name:
    IgSF4
    Nectin-like protein 2
    Short name:
    NECL-2
    Spermatogenic immunoglobulin superfamily
    Short name:
    SgIgSF
    Synaptic cell adhesion molecule
    Short name:
    SynCAM
    Tumor suppressor in lung cancer 1
    Short name:
    TSLC-1
    Gene namesi
    Name:CADM1Imported
    Synonyms:IGSF4By similarity, IGSF4A, NECL21 Publication, SYNCAMBy similarity, TSLC11 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:5951. CADM1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell junctionsynapse By similarity
    Note: Associates with perinuclear and plasma membranes in vivo. Localized to the basolateral plasma membrane of epithelial cells in gall bladder.By similarity1 PublicationSequence Analysis

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. basolateral plasma membrane Source: UniProtKB
    3. cell-cell junction Source: UniProtKB
    4. dendrite Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. integral component of membrane Source: UniProtKB-KW
    7. plasma membrane Source: UniProtKB
    8. synaptic vesicle Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi406 – 4061Y → A: Nearly abolishes EPB41L3 binding. 1 Publication
    Mutagenesisi408 – 4081T → A: Strongly reduced affinity for EPB41L3. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA29764.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4444Sequence AnalysisAdd
    BLAST
    Chaini45 – 442398Cell adhesion molecule 1Sequence AnalysisPRO_0000291968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi64 ↔ 124PROSITE-ProRule annotation
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi101 – 1011N-linked (GlcNAc...)4 Publications
    Glycosylationi113 – 1131N-linked (GlcNAc...)4 Publications
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi166 ↔ 220PROSITE-ProRule annotation
    Disulfide bondi267 ↔ 313PROSITE-ProRule annotation
    Glycosylationi301 – 3011N-linked (GlcNAc...); atypical2 Publications
    Glycosylationi302 – 3021N-linked (GlcNAc...); atypical2 Publications
    Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
    Modified residuei434 – 4341PhosphoserineBy similarity

    Post-translational modificationi

    Glycosylation at Asn-67 and Asn-101 promotes adhesive binding and synapse induction.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BY67.
    PaxDbiQ9BY67.
    PRIDEiQ9BY67.

    PTM databases

    PhosphoSiteiQ9BY67.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BY67.
    BgeeiQ9BY67.
    CleanExiHS_CADM1.
    GenevestigatoriQ9BY67.

    Organism-specific databases

    HPAiCAB037266.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with FARP1 By similarity. Interacts with CRTAM. Interacts (via C-terminus) with EPB41L3/DAL1. The interaction with EPB41L3/DAL1 may act to anchor CADM1 to the actin cytoskeleton. Interacts via its C-terminus with the PDZ domain of MPP3 and the PDZ domain of MPP6.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi117218. 3 interactions.
    DIPiDIP-57599N.
    IntActiQ9BY67. 4 interactions.
    MINTiMINT-1184987.
    STRINGi9606.ENSP00000329797.

    Structurei

    Secondary structure

    1
    442
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi52 – 554
    Beta strandi60 – 689
    Beta strandi74 – 774
    Beta strandi83 – 864
    Beta strandi97 – 1037
    Beta strandi106 – 1138
    Helixi116 – 1183
    Beta strandi120 – 1267
    Beta strandi128 – 1303
    Beta strandi132 – 14110
    Beta strandi405 – 4073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BINX-ray2.30B400-411[»]
    4H5SX-ray1.70B45-144[»]
    ProteinModelPortaliQ9BY67.
    SMRiQ9BY67. Positions 45-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BY67.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini45 – 374330ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini396 – 44247CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei375 – 39521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 13995Ig-like V-typeSequence AnalysisAdd
    BLAST
    Domaini144 – 23895Ig-like C2-type 1Sequence AnalysisAdd
    BLAST
    Domaini243 – 32987Ig-like C2-type 2Sequence AnalysisAdd
    BLAST

    Domaini

    The cytoplasmic domain appears to play a critical role in proapoptosis and tumor suppressor activity in NSCLC.2 Publications

    Sequence similaritiesi

    Belongs to the nectin family.Curated
    Contains 2 Ig-like C2-type (immunoglobulin-like) domains.Sequence Analysis
    Contains 1 Ig-like V-type (immunoglobulin-like) domain.Sequence Analysis

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG69486.
    HOGENOMiHOG000036057.
    HOVERGENiHBG057086.
    KOiK06781.
    OMAiEIYTTIT.
    OrthoDBiEOG7PVWPD.
    PhylomeDBiQ9BY67.
    TreeFamiTF334317.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR013162. CD80_C2-set.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR003585. Neurexin-like.
    [Graphical view]
    PfamiPF08205. C2-set_2. 1 hit.
    PF07679. I-set. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    SMARTiSM00294. 4.1m. 1 hit.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9BY67-1) [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

    MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGDGQNLFTK    50
    DVTVIEGEVA TISCQVNKSD DSVIQLLNPN RQTIYFRDFR PLKDSRFQLL 100
    NFSSSELKVS LTNVSISDEG RYFCQLYTDP PQESYTTITV LVPPRNLMID 150
    IQKDTAVEGE EIEVNCTAMA SKPATTIRWF KGNTELKGKS EVEEWSDMYT 200
    VTSQLMLKVH KEDDGVPVIC QVEHPAVTGN LQTQRYLEVQ YKPQVHIQMT 250
    YPLQGLTREG DALELTCEAI GKPQPVMVTW VRVDDEMPQH AVLSGPNLFI 300
    NNLNKTDNGT YRCEASNIVG KAHSDYMLYV YDPPTTIPPP TTTTTTTTTT 350
    TTTILTIITD SRAGEEGSIR AVDHAVIGGV VAVVVFAMLC LLIILGRYFA 400
    RHKGTYFTHE AKGADDAADA DTAIINAEGG QNNSEEKKEY FI 442
    Length:442
    Mass (Da):48,509
    Last modified:June 26, 2007 - v2
    Checksum:iCDEDE1E0C08BDD3A
    GO
    Isoform 21 Publication (identifier: Q9BY67-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         332-333: DP → GT
         334-442: Missing.

    Show »
    Length:333
    Mass (Da):36,915
    Checksum:iD7C1102F46D08492
    GO
    Isoform 3 (identifier: Q9BY67-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         359-359: T → TDTTATTEPAVHGLTQLPNSAEELDSEDLS

    Show »
    Length:471
    Mass (Da):51,533
    Checksum:i322A71AB89E8B21F
    GO
    Isoform 4 (identifier: Q9BY67-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         359-359: T → TDTTATTEPAVH

    Show »
    Length:453
    Mass (Da):49,633
    Checksum:i466DC2D374481CFB
    GO
    Isoform 5 (identifier: Q9BY67-5) [UniParc]FASTAAdd to Basket

    Also known as: E

    The sequence of this isoform differs from the canonical sequence as follows:
         333-360: Missing.

    Show »
    Length:414
    Mass (Da):45,624
    Checksum:i4C5AB05F34BA714A
    GO

    Sequence cautioni

    The sequence AAI25103.1 differs from that shown. Reason: Frameshift at position 1.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131A → V in CCD32613. (PubMed:22438059)Curated
    Sequence conflicti153 – 1531K → R in AAF69029. (PubMed:15893517)Curated
    Sequence conflicti333 – 35927PPTTI…LTIIT → TTATTEPAVHGLTQLPNSAE ELDSEDLS in BAC11657. (PubMed:14702039)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti285 – 2851D → E.
    Corresponds to variant rs45525440 [ dbSNP | Ensembl ].
    VAR_061309

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei332 – 3332DP → GT in isoform 2. 1 PublicationVSP_052461
    Alternative sequencei333 – 36028Missing in isoform 5. 2 PublicationsVSP_047405Add
    BLAST
    Alternative sequencei334 – 442109Missing in isoform 2. 1 PublicationVSP_052462Add
    BLAST
    Alternative sequencei359 – 3591T → TDTTATTEPAVHGLTQLPNS AEELDSEDLS in isoform 3. 1 PublicationVSP_047406
    Alternative sequencei359 – 3591T → TDTTATTEPAVH in isoform 4. 1 PublicationVSP_047407

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132811 mRNA. Translation: AAF69029.1.
    HE586496 mRNA. Translation: CCD32610.1.
    HE586497 mRNA. Translation: CCD32611.1.
    HE586498 mRNA. Translation: CCD32612.1.
    HE586499 mRNA. Translation: CCD32613.1.
    KJ534791 mRNA. Translation: AHW56431.1.
    KJ534794 mRNA. Translation: AHW56434.1.
    AB094146 mRNA. Translation: BAC66178.1.
    AK075502 mRNA. Translation: BAC11657.1.
    AP000462 Genomic DNA. No translation available.
    AP000465 Genomic DNA. No translation available.
    AP003174 Genomic DNA. No translation available.
    AP003179 Genomic DNA. No translation available.
    AP005020 Genomic DNA. No translation available.
    BC125102 mRNA. Translation: AAI25103.1. Frameshift.
    CCDSiCCDS53711.1. [Q9BY67-5]
    CCDS8373.1. [Q9BY67-1]
    RefSeqiNP_001091987.1. NM_001098517.1. [Q9BY67-5]
    NP_055148.3. NM_014333.3. [Q9BY67-1]
    XP_005271548.1. XM_005271491.2. [Q9BY67-3]
    XP_005271549.1. XM_005271492.2. [Q9BY67-4]
    XP_005271550.1. XM_005271493.2.
    UniGeneiHs.370510.

    Genome annotation databases

    EnsembliENST00000331581; ENSP00000329797; ENSG00000182985. [Q9BY67-3]
    ENST00000452722; ENSP00000395359; ENSG00000182985. [Q9BY67-1]
    ENST00000537058; ENSP00000439817; ENSG00000182985. [Q9BY67-4]
    ENST00000542447; ENSP00000439176; ENSG00000182985. [Q9BY67-5]
    GeneIDi23705.
    KEGGihsa:23705.
    UCSCiuc001pph.5. human.
    uc001ppi.4. human. [Q9BY67-1]
    uc001ppj.4. human.
    uc001ppl.3. human. [Q9BY67-2]

    Polymorphism databases

    DMDMi150438862.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132811 mRNA. Translation: AAF69029.1 .
    HE586496 mRNA. Translation: CCD32610.1 .
    HE586497 mRNA. Translation: CCD32611.1 .
    HE586498 mRNA. Translation: CCD32612.1 .
    HE586499 mRNA. Translation: CCD32613.1 .
    KJ534791 mRNA. Translation: AHW56431.1 .
    KJ534794 mRNA. Translation: AHW56434.1 .
    AB094146 mRNA. Translation: BAC66178.1 .
    AK075502 mRNA. Translation: BAC11657.1 .
    AP000462 Genomic DNA. No translation available.
    AP000465 Genomic DNA. No translation available.
    AP003174 Genomic DNA. No translation available.
    AP003179 Genomic DNA. No translation available.
    AP005020 Genomic DNA. No translation available.
    BC125102 mRNA. Translation: AAI25103.1 . Frameshift.
    CCDSi CCDS53711.1. [Q9BY67-5 ]
    CCDS8373.1. [Q9BY67-1 ]
    RefSeqi NP_001091987.1. NM_001098517.1. [Q9BY67-5 ]
    NP_055148.3. NM_014333.3. [Q9BY67-1 ]
    XP_005271548.1. XM_005271491.2. [Q9BY67-3 ]
    XP_005271549.1. XM_005271492.2. [Q9BY67-4 ]
    XP_005271550.1. XM_005271493.2.
    UniGenei Hs.370510.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BIN X-ray 2.30 B 400-411 [» ]
    4H5S X-ray 1.70 B 45-144 [» ]
    ProteinModelPortali Q9BY67.
    SMRi Q9BY67. Positions 45-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117218. 3 interactions.
    DIPi DIP-57599N.
    IntActi Q9BY67. 4 interactions.
    MINTi MINT-1184987.
    STRINGi 9606.ENSP00000329797.

    PTM databases

    PhosphoSitei Q9BY67.

    Polymorphism databases

    DMDMi 150438862.

    Proteomic databases

    MaxQBi Q9BY67.
    PaxDbi Q9BY67.
    PRIDEi Q9BY67.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331581 ; ENSP00000329797 ; ENSG00000182985 . [Q9BY67-3 ]
    ENST00000452722 ; ENSP00000395359 ; ENSG00000182985 . [Q9BY67-1 ]
    ENST00000537058 ; ENSP00000439817 ; ENSG00000182985 . [Q9BY67-4 ]
    ENST00000542447 ; ENSP00000439176 ; ENSG00000182985 . [Q9BY67-5 ]
    GeneIDi 23705.
    KEGGi hsa:23705.
    UCSCi uc001pph.5. human.
    uc001ppi.4. human. [Q9BY67-1 ]
    uc001ppj.4. human.
    uc001ppl.3. human. [Q9BY67-2 ]

    Organism-specific databases

    CTDi 23705.
    GeneCardsi GC11M115044.
    HGNCi HGNC:5951. CADM1.
    HPAi CAB037266.
    MIMi 605686. gene.
    neXtProti NX_Q9BY67.
    PharmGKBi PA29764.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69486.
    HOGENOMi HOG000036057.
    HOVERGENi HBG057086.
    KOi K06781.
    OMAi EIYTTIT.
    OrthoDBi EOG7PVWPD.
    PhylomeDBi Q9BY67.
    TreeFami TF334317.

    Enzyme and pathway databases

    Reactomei REACT_19195. Adherens junctions interactions.
    REACT_19268. Nectin/Necl trans heterodimerization.

    Miscellaneous databases

    ChiTaRSi CADM1. human.
    EvolutionaryTracei Q9BY67.
    GeneWikii Cell_adhesion_molecule_1.
    GenomeRNAii 23705.
    NextBioi 35461775.
    PROi Q9BY67.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BY67.
    Bgeei Q9BY67.
    CleanExi HS_CADM1.
    Genevestigatori Q9BY67.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR013162. CD80_C2-set.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    IPR003585. Neurexin-like.
    [Graphical view ]
    Pfami PF08205. C2-set_2. 1 hit.
    PF07679. I-set. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    SMARTi SM00294. 4.1m. 1 hit.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nectin-like molecule 1 is a protein 4.1N associated protein and recruits protein 4.1N from cytoplasm to the plasma membrane."
      Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B., Fan M., Peng X., Qiang B., Yuan J.
      Biochim. Biophys. Acta 1669:142-154(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "CADM1 isoforms differentially regulate human mast cell survival and homotypic adhesion."
      Moiseeva E.P., Leyland M.L., Bradding P.
      Cell. Mol. Life Sci. 69:2751-2764(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
      Tissue: Mast cell.
    3. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
      Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
      , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
      Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: Fetal brain.
    4. "Cloning of a secretory isoform of SgIGSF/TSLC-1."
      Ito A., Koma Y., Nagano T.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: LungImported.
    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.
      , 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 1).
      Tissue: EmbryoImported.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 5).
    8. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Direct association of TSLC1 and DAL-1, two distinct tumor suppressor proteins in lung cancer."
      Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H., Maruyama T., Shibuya M., Murakami Y.
      Cancer Res. 62:5129-5133(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EPB41L3.
    10. "The tumor suppressor protein TSLC1 is involved in cell-cell adhesion."
      Masuda M., Yageta M., Fukuhara H., Kuramochi M., Maruyama T., Nomoto A., Murakami Y.
      J. Biol. Chem. 277:31014-31019(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, GLYCOSYLATION.
    11. "The cytoplasmic domain is critical to the tumor suppressor activity of TSLC1 in non-small cell lung cancer."
      Mao X., Seidlitz E., Ghosh K., Murakami Y., Ghosh H.P.
      Cancer Res. 63:7979-7985(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    12. "Promoter methylation of the TSLC1 gene in advanced lung tumors and various cancer cell lines."
      Fukami T., Fukuhara H., Kuramochi M., Maruyama T., Isogai K., Sakamoto M., Takamoto S., Murakami Y.
      Int. J. Cancer 107:53-59(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE.
    13. "Expression of the TSLC1 adhesion molecule in pulmonary epithelium and its down-regulation in pulmonary adenocarcinoma other than bronchioloalveolar carcinoma."
      Ito A., Okada M., Uchino K., Wakayama T., Koma Y., Iseki S., Tsubota N., Okita Y., Kitamura Y.
      Lab. Invest. 83:1175-1183(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Association of a lung tumor suppressor TSLC1 with MPP3, a human homologue of Drosophila tumor suppressor Dlg."
      Fukuhara H., Masuda M., Yageta M., Fukami T., Kuramochi M., Maruyama T., Kitamura T., Murakami Y.
      Oncogene 22:6160-6165(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPP3.
    15. "Re-expression of TSLC1 in a non-small-cell lung cancer cell line induces apoptosis and inhibits tumor growth."
      Mao X., Seidlitz E., Truant R., Hitt M., Ghosh H.P.
      Oncogene 23:5632-5642(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    16. "The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell responses through the cell-surface receptor CRTAM."
      Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M.
      Blood 106:779-786(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CRTAM.
    17. "Nectin-like protein 2 defines a subset of T-cell zone dendritic cells and is a ligand for class-I-restricted T-cell-associated molecule."
      Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T., Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A., Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M., Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W.
      J. Biol. Chem. 280:21955-21964(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRTAM.
    18. "The spermatogenic Ig superfamily/synaptic cell adhesion molecule mast-cell adhesion molecule promotes interaction with nerves."
      Furuno T., Ito A., Koma Y., Watabe K., Yokozaki H., Bienenstock J., Nakanishi M., Kitamura Y.
      J. Immunol. 174:6934-6942(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113.
      Tissue: Plasma1 Publication.
    20. "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-101 AND ASN-113.
      Tissue: Liver.
    21. "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-101; ASN-113; ASN-301 AND ASN-302.
      Tissue: Leukemic T-cell.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B)."
      Busam R.D., Thorsell A.G., Flores A., Hammarstrom M., Persson C., Obrink B., Hallberg B.M.
      J. Biol. Chem. 286:4511-4516(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 400-411 IN COMPLEX WITH EPB41L3, MUTAGENESIS OF TYR-406 AND THR-408, INTERACTION WITH EPB41L3.

    Entry informationi

    Entry nameiCADM1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BY67
    Secondary accession number(s): A4FVB5
    , F5H0J4, H0YGA7, H1ZZV9, H1ZZW1, H1ZZW2, Q86WB8, Q8N2F4, X5D2C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3