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P55290

- CAD13_HUMAN

UniProt

P55290 - CAD13_HUMAN

Protein

Cadherin-13

Gene

CDH13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May act as a negative regulator of neural cell growth.1 Publication

    GO - Molecular functioni

    1. adiponectin binding Source: BHF-UCL
    2. cadherin binding Source: BHF-UCL
    3. calcium ion binding Source: InterPro
    4. lipoprotein particle binding Source: UniProtKB
    5. low-density lipoprotein particle binding Source: BHF-UCL

    GO - Biological processi

    1. adherens junction organization Source: Reactome
    2. calcium-dependent cell-cell adhesion Source: BHF-UCL
    3. cell-cell junction organization Source: Reactome
    4. cell junction assembly Source: Reactome
    5. endothelial cell migration Source: BHF-UCL
    6. homophilic cell adhesion Source: BHF-UCL
    7. keratinocyte proliferation Source: BHF-UCL
    8. lamellipodium assembly Source: BHF-UCL
    9. localization within membrane Source: BHF-UCL
    10. low-density lipoprotein particle mediated signaling Source: BHF-UCL
    11. mitotic cell cycle Source: Ensembl
    12. negative regulation of cell adhesion Source: BHF-UCL
    13. negative regulation of cell proliferation Source: BHF-UCL
    14. positive regulation of calcium-mediated signaling Source: BHF-UCL
    15. positive regulation of cell-matrix adhesion Source: BHF-UCL
    16. positive regulation of cell migration Source: BHF-UCL
    17. positive regulation of endothelial cell proliferation Source: BHF-UCL
    18. positive regulation of positive chemotaxis Source: BHF-UCL
    19. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
    20. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    21. Rac protein signal transduction Source: BHF-UCL
    22. regulation of cell growth Source: Ensembl
    23. regulation of endocytosis Source: BHF-UCL
    24. regulation of epidermal growth factor receptor signaling pathway Source: BHF-UCL
    25. Rho protein signal transduction Source: BHF-UCL
    26. sprouting angiogenesis Source: BHF-UCL

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_19195. Adherens junctions interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cadherin-13
    Alternative name(s):
    Heart cadherin
    Short name:
    H-cadherin
    P105
    Truncated cadherin
    Short name:
    T-cad
    Short name:
    T-cadherin
    Gene namesi
    Name:CDH13
    Synonyms:CDHH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:1753. CDH13.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. caveola Source: BHF-UCL
    3. cytoplasm Source: BHF-UCL
    4. external side of plasma membrane Source: Ensembl
    5. extracellular space Source: BHF-UCL
    6. extracellular vesicular exosome Source: UniProt
    7. neuron projection Source: BHF-UCL
    8. perinuclear region of cytoplasm Source: Ensembl
    9. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26287.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 138116PRO_0000003793Add
    BLAST
    Chaini139 – 693555Cadherin-13PRO_0000003794Add
    BLAST
    Propeptidei694 – 71320Removed in mature formCuratedPRO_0000003795Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi86 – 861N-linked (GlcNAc...)1 Publication
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi500 – 5001N-linked (GlcNAc...)1 Publication
    Glycosylationi530 – 5301N-linked (GlcNAc...)1 Publication
    Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi638 – 6381N-linked (GlcNAc...)2 Publications
    Glycosylationi671 – 6711N-linked (GlcNAc...)Sequence Analysis
    Lipidationi693 – 6931GPI-anchor amidated glycine1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiP55290.
    PaxDbiP55290.
    PeptideAtlasiP55290.
    PRIDEiP55290.

    PTM databases

    PhosphoSiteiP55290.

    Expressioni

    Tissue specificityi

    Highly expressed in heart. In the CNS, expressed in cerebral cortex, medulla, hippocampus, amygdala, thalamus and substantia nigra. No expression detected in cerebellum or spinal cord.2 Publications

    Developmental stagei

    Expressed at higher levels in adult brain than in developing brain.1 Publication

    Gene expression databases

    ArrayExpressiP55290.
    BgeeiP55290.
    CleanExiHS_CDH13.
    GenevestigatoriP55290.

    Organism-specific databases

    HPAiCAB025863.
    HPA001380.

    Interactioni

    Subunit structurei

    By contrast to classical cadherins, homodimerization in trans is not mediated by cadherin EC1 domain strand-swapping, but instead through a homophilic adhesive interface which joins two elongated EC1-EC2 domains through a region near their Ca2+-binding sites to form a tetrahedral, X-like shape.By similarity

    Protein-protein interaction databases

    BioGridi107447. 1 interaction.
    IntActiP55290. 1 interaction.
    MINTiMINT-7004770.
    STRINGi9606.ENSP00000268613.

    Structurei

    Secondary structure

    1
    713
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi145 – 1484
    Beta strandi157 – 1615
    Beta strandi163 – 1675
    Beta strandi172 – 1787
    Turni179 – 1813
    Beta strandi182 – 1843
    Beta strandi187 – 1904
    Turni192 – 1943
    Beta strandi196 – 1994
    Turni205 – 2073
    Beta strandi209 – 21810
    Beta strandi224 – 23613
    Beta strandi238 – 2414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V37NMR-A139-243[»]
    ProteinModelPortaliP55290.
    SMRiP55290. Positions 21-111, 139-680.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55290.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini139 – 245107Cadherin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini246 – 363118Cadherin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini364 – 477114Cadherin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini478 – 585108Cadherin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini584 – 694111Cadherin 5PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.By similarity

    Sequence similaritiesi

    Contains 5 cadherin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG304703.
    HOGENOMiHOG000169079.
    HOVERGENiHBG106438.
    InParanoidiP55290.
    KOiK06808.
    OMAiTIATYQL.
    OrthoDBiEOG7MH0XG.
    PhylomeDBiP55290.

    Family and domain databases

    Gene3Di2.60.40.60. 6 hits.
    InterProiIPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR020894. Cadherin_CS.
    IPR014868. Cadherin_pro_dom.
    [Graphical view]
    PfamiPF00028. Cadherin. 5 hits.
    PF08758. Cadherin_pro. 1 hit.
    [Graphical view]
    PRINTSiPR00205. CADHERIN.
    SMARTiSM00112. CA. 5 hits.
    SM01055. Cadherin_pro. 1 hit.
    [Graphical view]
    SUPFAMiSSF49313. SSF49313. 6 hits.
    PROSITEiPS00232. CADHERIN_1. 3 hits.
    PS50268. CADHERIN_2. 5 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 1 (identifier: P55290-1) [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

    MQPRTPLVLC VLLSQVLLLT SAEDLDCTPG FQQKVFHINQ PAEFIEDQSI    50
    LNLTFSDCKG NDKLRYEVSS PYFKVNSDGG LVALRNITAV GKTLFVHART 100
    PHAEDMAELV IVGGKDIQGS LQDIFKFART SPVPRQKRSI VVSPILIPEN 150
    QRQPFPRDVG KVVDSDRPER SKFRLTGKGV DQEPKGIFRI NENTGSVSVT 200
    RTLDREVIAV YQLFVETTDV NGKTLEGPVP LEVIVIDQND NRPIFREGPY 250
    IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY 300
    IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT 350
    IMIDDKNDHS PKFTKKEFQA TVEEGAVGVI VNLTVEDKDD PTTGAWRAAY 400
    TIINGNPGQS FEIHTNPQTN EGMLSVVKPL DYEISAFHTL LIKVENEDPL 450
    VPDVSYGPSS TATVHITVLD VNEGPVFYPD PMMVTRQEDL SVGSVLLTVN 500
    ATDPDSLQHQ TIRYSVYKDP AGWLNINPIN GTVDTTAVLD RESPFVDNSV 550
    YTALFLAIDS GNPPATGTGT LLITLEDVND NAPFIYPTVA EVCDDAKNLS 600
    VVILGASDKD LHPNTDPFKF EIHKQAVPDK VWKISKINNT HALVSLLQNL 650
    NKANYNLPIM VTDSGKPPMT NITDLRVQVC SCRNSKVDCN AAGALRFSLP 700
    SVLLLSLFSL ACL 713
    Length:713
    Mass (Da):78,287
    Last modified:October 1, 1996 - v1
    Checksum:iCEB662D77824CB60
    GO
    Isoform 2 (identifier: P55290-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         162-190: VVDSDRPERSKFRLTGKGVDQEPKGIFRI → RTHNPINSELLLNEGITADLNPCITILAI
         191-713: Missing.

    Show »
    Length:190
    Mass (Da):21,058
    Checksum:iC7DA89A2C0C036E9
    GO
    Isoform 3 (identifier: P55290-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         162-175: VVDSDRPERSKFRL → MKIWQVLCLARWLT
         176-713: Missing.

    Show »
    Length:175
    Mass (Da):19,660
    Checksum:i0038FABE744ECAE0
    GO
    Isoform 4 (identifier: P55290-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: MQPRTPLVLCVLLS → MKTPPGASSRTKCSRELRSFCAFSCPRAKQPTCTAWFPQQEHPSENGPQMPGRDPPAASTM

    Note: Gene prediction based on EST data.

    Show »
    Length:760
    Mass (Da):83,397
    Checksum:iB4BB30012F3D4560
    GO
    Isoform 5 (identifier: P55290-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         123-161: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:674
    Mass (Da):73,787
    Checksum:i4C15F7C62AE5B0AA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti199 – 1991V → M in AAH28624. 1 PublicationCurated
    Sequence conflicti199 – 1991V → M in AAH30653. 1 PublicationCurated
    Sequence conflicti288 – 2881Q → R in AAH28624. 1 PublicationCurated
    Sequence conflicti288 – 2881Q → R in AAH30653. 1 PublicationCurated
    Sequence conflicti392 – 3921T → A in AAH28624. 1 PublicationCurated
    Sequence conflicti392 – 3921T → A in AAH30653. 1 PublicationCurated
    Sequence conflicti544 – 5441P → T in AAH28624. 1 PublicationCurated
    Sequence conflicti544 – 5441P → T in AAH30653. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651R → C in a patient with amyotrophic lateral sclerosis. 1 Publication
    VAR_065747
    Natural varianti103 – 1031A → V in a patient with amyotrophic lateral sclerosis. 1 Publication
    VAR_065748
    Natural varianti113 – 1131G → R in a patient with amyotrophic lateral sclerosis. 1 Publication
    Corresponds to variant rs183971768 [ dbSNP | Ensembl ].
    VAR_065749
    Natural varianti121 – 1211L → S.
    Corresponds to variant rs7197352 [ dbSNP | Ensembl ].
    VAR_030632
    Natural varianti246 – 2461R → W in a patient with amyotrophic lateral sclerosis. 1 Publication
    VAR_065750
    Natural varianti367 – 3671E → Q in a patient with amyotrophic lateral sclerosis. 1 Publication
    VAR_065751
    Natural varianti376 – 3761A → T.1 Publication
    Corresponds to variant rs35549391 [ dbSNP | Ensembl ].
    VAR_065752
    Natural varianti643 – 6431L → R.1 Publication
    Corresponds to variant rs34106627 [ dbSNP | Ensembl ].
    VAR_065753

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1414MQPRT…CVLLS → MKTPPGASSRTKCSRELRSF CAFSCPRAKQPTCTAWFPQQ EHPSENGPQMPGRDPPAAST M in isoform 4. CuratedVSP_046714Add
    BLAST
    Alternative sequencei123 – 16139Missing in isoform 5. 1 PublicationVSP_053739Add
    BLAST
    Alternative sequencei162 – 19029VVDSD…GIFRI → RTHNPINSELLLNEGITADL NPCITILAI in isoform 2. 1 PublicationVSP_042696Add
    BLAST
    Alternative sequencei162 – 17514VVDSD…SKFRL → MKIWQVLCLARWLT in isoform 3. 1 PublicationVSP_042794Add
    BLAST
    Alternative sequencei176 – 713538Missing in isoform 3. 1 PublicationVSP_042795Add
    BLAST
    Alternative sequencei191 – 713523Missing in isoform 2. 1 PublicationVSP_042697Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34058 mRNA. Translation: AAA35624.1.
    U59289 mRNA. Translation: AAB18912.1.
    U59288 mRNA. Translation: AAB18911.1.
    AB001103 Genomic DNA. Translation: BAA32411.1.
    EU190357 mRNA. Translation: ABW97440.1.
    EU190358 mRNA. Translation: ABW97441.1.
    AK298612 mRNA. Translation: BAH12826.1.
    AC009028 Genomic DNA. No translation available.
    AC009063 Genomic DNA. No translation available.
    AC009119 Genomic DNA. No translation available.
    AC009142 Genomic DNA. No translation available.
    AC087189 Genomic DNA. No translation available.
    AC092340 Genomic DNA. No translation available.
    AC092351 Genomic DNA. No translation available.
    AC098804 Genomic DNA. No translation available.
    AC099506 Genomic DNA. No translation available.
    AC106814 Genomic DNA. No translation available.
    AC125793 Genomic DNA. No translation available.
    BC028624 mRNA. Translation: AAH28624.1.
    BC030653 mRNA. Translation: AAH30653.1.
    CCDSiCCDS56009.1. [P55290-3]
    CCDS56010.1. [P55290-2]
    CCDS58485.1. [P55290-4]
    CCDS58486.1. [P55290-1]
    CCDS58487.1. [P55290-5]
    PIRiB38992.
    RefSeqiNP_001207418.1. NM_001220489.1. [P55290-5]
    NP_001207420.1. NM_001220491.1. [P55290-2]
    NP_001207421.1. NM_001220492.1. [P55290-3]
    NP_001248.1. NM_001257.4. [P55290-1]
    UniGeneiHs.654386.
    Hs.661776.

    Genome annotation databases

    EnsembliENST00000268613; ENSP00000268613; ENSG00000140945. [P55290-4]
    ENST00000428848; ENSP00000394557; ENSG00000140945. [P55290-5]
    ENST00000431540; ENSP00000408632; ENSG00000140945. [P55290-2]
    ENST00000565636; ENSP00000456491; ENSG00000140945. [P55290-3]
    ENST00000566620; ENSP00000454435; ENSG00000140945. [P55290-1]
    GeneIDi1012.
    KEGGihsa:1012.
    UCSCiuc002fgx.3. human. [P55290-1]
    uc010chh.3. human. [P55290-2]
    uc021tlw.1. human. [P55290-3]

    Polymorphism databases

    DMDMi1705552.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34058 mRNA. Translation: AAA35624.1 .
    U59289 mRNA. Translation: AAB18912.1 .
    U59288 mRNA. Translation: AAB18911.1 .
    AB001103 Genomic DNA. Translation: BAA32411.1 .
    EU190357 mRNA. Translation: ABW97440.1 .
    EU190358 mRNA. Translation: ABW97441.1 .
    AK298612 mRNA. Translation: BAH12826.1 .
    AC009028 Genomic DNA. No translation available.
    AC009063 Genomic DNA. No translation available.
    AC009119 Genomic DNA. No translation available.
    AC009142 Genomic DNA. No translation available.
    AC087189 Genomic DNA. No translation available.
    AC092340 Genomic DNA. No translation available.
    AC092351 Genomic DNA. No translation available.
    AC098804 Genomic DNA. No translation available.
    AC099506 Genomic DNA. No translation available.
    AC106814 Genomic DNA. No translation available.
    AC125793 Genomic DNA. No translation available.
    BC028624 mRNA. Translation: AAH28624.1 .
    BC030653 mRNA. Translation: AAH30653.1 .
    CCDSi CCDS56009.1. [P55290-3 ]
    CCDS56010.1. [P55290-2 ]
    CCDS58485.1. [P55290-4 ]
    CCDS58486.1. [P55290-1 ]
    CCDS58487.1. [P55290-5 ]
    PIRi B38992.
    RefSeqi NP_001207418.1. NM_001220489.1. [P55290-5 ]
    NP_001207420.1. NM_001220491.1. [P55290-2 ]
    NP_001207421.1. NM_001220492.1. [P55290-3 ]
    NP_001248.1. NM_001257.4. [P55290-1 ]
    UniGenei Hs.654386.
    Hs.661776.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V37 NMR - A 139-243 [» ]
    ProteinModelPortali P55290.
    SMRi P55290. Positions 21-111, 139-680.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107447. 1 interaction.
    IntActi P55290. 1 interaction.
    MINTi MINT-7004770.
    STRINGi 9606.ENSP00000268613.

    PTM databases

    PhosphoSitei P55290.

    Polymorphism databases

    DMDMi 1705552.

    Proteomic databases

    MaxQBi P55290.
    PaxDbi P55290.
    PeptideAtlasi P55290.
    PRIDEi P55290.

    Protocols and materials databases

    DNASUi 1012.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268613 ; ENSP00000268613 ; ENSG00000140945 . [P55290-4 ]
    ENST00000428848 ; ENSP00000394557 ; ENSG00000140945 . [P55290-5 ]
    ENST00000431540 ; ENSP00000408632 ; ENSG00000140945 . [P55290-2 ]
    ENST00000565636 ; ENSP00000456491 ; ENSG00000140945 . [P55290-3 ]
    ENST00000566620 ; ENSP00000454435 ; ENSG00000140945 . [P55290-1 ]
    GeneIDi 1012.
    KEGGi hsa:1012.
    UCSCi uc002fgx.3. human. [P55290-1 ]
    uc010chh.3. human. [P55290-2 ]
    uc021tlw.1. human. [P55290-3 ]

    Organism-specific databases

    CTDi 1012.
    GeneCardsi GC16P082660.
    HGNCi HGNC:1753. CDH13.
    HPAi CAB025863.
    HPA001380.
    MIMi 601364. gene.
    neXtProti NX_P55290.
    PharmGKBi PA26287.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304703.
    HOGENOMi HOG000169079.
    HOVERGENi HBG106438.
    InParanoidi P55290.
    KOi K06808.
    OMAi TIATYQL.
    OrthoDBi EOG7MH0XG.
    PhylomeDBi P55290.

    Enzyme and pathway databases

    Reactomei REACT_19195. Adherens junctions interactions.

    Miscellaneous databases

    ChiTaRSi CDH13. human.
    EvolutionaryTracei P55290.
    GeneWikii T-cadherin.
    GenomeRNAii 1012.
    NextBioi 35534829.
    PROi P55290.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55290.
    Bgeei P55290.
    CleanExi HS_CDH13.
    Genevestigatori P55290.

    Family and domain databases

    Gene3Di 2.60.40.60. 6 hits.
    InterProi IPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR020894. Cadherin_CS.
    IPR014868. Cadherin_pro_dom.
    [Graphical view ]
    Pfami PF00028. Cadherin. 5 hits.
    PF08758. Cadherin_pro. 1 hit.
    [Graphical view ]
    PRINTSi PR00205. CADHERIN.
    SMARTi SM00112. CA. 5 hits.
    SM01055. Cadherin_pro. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49313. SSF49313. 6 hits.
    PROSITEi PS00232. CADHERIN_1. 3 hits.
    PS50268. CADHERIN_2. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of five human cadherins clarifies characteristic features of cadherin extracellular domain and provides further evidence for two structurally different types of cadherin."
      Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S.
      Cell Adhes. Commun. 2:15-26(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "H-cadherin, a novel cadherin with growth inhibitory functions and diminished expression in human breast cancer."
      Lee S.W.
      Nat. Med. 2:776-782(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    3. "The H-cadherin (CDH13) gene is inactivated in human lung cancer."
      Sato M., Mori Y., Sakurada A., Fujimura S., Horii A.
      Hum. Genet. 103:96-101(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Differential alternative splicing of Cadherin 13 gene in aging and Alzheimer's disease."
      Liu Q.-R., Liu J.J., Zhu X.-G., Uhl G.R.
      Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
    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 5).
    6. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      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 1).
      Tissue: Brain and Testis.
    8. "Identification of an atypical lipoprotein-binding protein from human aortic smooth muscle as T-cadherin."
      Tkachuk V.A., Bochkov V.N., Philippova M.P., Stambolsky D.V., Kuzmenko E.S., Sidorova M.V., Molokoedov A.S., Spirov V.G., Resink T.J.
      FEBS Lett. 421:208-212(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 140-149; 162-169 AND 284-287 (ISOFORM 1).
      Tissue: Aorta.
    9. "Expression of T-cadherin (CDH13, H-Cadherin) in human brain and its characteristics as a negative growth regulator of epidermal growth factor in neuroblastoma cells."
      Takeuchi T., Misaki A., Liang S.-B., Tachibana A., Hayashi N., Sonobe H., Ohtsuki Y.
      J. Neurochem. 74:1489-1497(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Brain.
    10. "The glycosyl phosphatidylinositol anchor of human T-cadherin binds lipoproteins."
      Niermann T., Kern F., Erne P., Resink T.
      Biochem. Biophys. Res. Commun. 276:1240-1247(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "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-86; ASN-500 AND ASN-638.
      Tissue: Plasma.
    12. "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
      Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
      J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-530 AND ASN-638.
      Tissue: Liver.
    14. "Resequencing of 29 candidate genes in patients with familial and sporadic amyotrophic lateral sclerosis."
      Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D., Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A., Rouleau G.A.
      Arch. Neurol. 68:587-593(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CYS-65; VAL-103; ARG-113; TRP-246; GLN-367; THR-376 AND ARG-643.

    Entry informationi

    Entry nameiCAD13_HUMAN
    AccessioniPrimary (citable) accession number: P55290
    Secondary accession number(s): A8W476
    , A8W477, B7Z590, C9JRI6, J3KN62, Q6GTW4, Q8TBX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 142 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 chromosome 16
      Human chromosome 16: 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