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P15116

- CADH2_MOUSE

UniProt

P15116 - CADH2_MOUSE

Protein

Cadherin-2

Gene

Cdh2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence (PubMed:24952463). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi262 – 2621Calcium 1
    Metal bindingi262 – 2621Calcium 2
    Metal bindingi293 – 2931Calcium 3

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct
    3. protein phosphatase binding Source: UniProtKB

    GO - Biological processi

    1. blood vessel morphogenesis Source: MGI
    2. calcium-dependent cell-cell adhesion Source: MGI
    3. cell adhesion Source: MGI
    4. cell migration Source: MGI
    5. heterophilic cell-cell adhesion Source: MGI
    6. homophilic cell adhesion Source: MGI
    7. negative regulation of canonical Wnt signaling pathway Source: MGI
    8. positive regulation of MAPK cascade Source: MGI
    9. striated muscle cell differentiation Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cadherin-2
    Alternative name(s):
    Neural cadherin
    Short name:
    N-cadherin
    CD_antigen: CD325
    Gene namesi
    Name:Cdh2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:88355. Cdh2.

    Subcellular locationi

    GO - Cellular componenti

    1. adherens junction Source: MGI
    2. apical plasma membrane Source: MGI
    3. catenin complex Source: Ensembl
    4. cell-cell junction Source: MGI
    5. fascia adherens Source: MGI
    6. integral component of membrane Source: UniProtKB-KW
    7. intercalated disc Source: BHF-UCL
    8. lamellipodium Source: MGI
    9. membrane Source: MGI
    10. synapse Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic lethality.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi262 – 2621D → A: Abolishes dimerization. 1 Publication
    Mutagenesisi293 – 2931D → A: Severely impaired the binding of calcium to all three sites. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Propeptidei26 – 159134Sequence AnalysisPRO_0000003733Add
    BLAST
    Chaini160 – 906747Cadherin-2PRO_0000003734Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi572 – 5721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi651 – 6511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi692 – 6921N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa amino-terminal soluble fragment and a 45 kDa membrane-bound carboxy-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa. Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate neural stem cell quiescence.2 Publications

    Keywords - PTMi

    Cleavage on pair of basic residues, Glycoprotein

    Proteomic databases

    MaxQBiP15116.
    PaxDbiP15116.
    PRIDEiP15116.

    PTM databases

    PhosphoSiteiP15116.

    Expressioni

    Developmental stagei

    Expressed at all stages of testicular development with highest levels found in testes of 21-day-old mice.1 Publication

    Gene expression databases

    ArrayExpressiP15116.
    BgeeiP15116.
    CleanExiMM_CDH2.
    GenevestigatoriP15116.

    Interactioni

    Subunit structurei

    Interacts with CDCP1 By similarity. Interacts with PCDH8; this complex may also include TAOK2 By similarity. The interaction with PCDH8 may lead to internalization through TAOK2/p38 MAPK pathway. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTPN1P180313EBI-397974,EBI-968788From a different organism.

    Protein-protein interaction databases

    BioGridi198637. 20 interactions.
    DIPiDIP-31564N.
    IntActiP15116. 9 interactions.
    MINTiMINT-4089694.

    Structurei

    Secondary structure

    1
    906
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 434
    Beta strandi55 – 573
    Beta strandi69 – 724
    Beta strandi76 – 827
    Turni83 – 853
    Beta strandi86 – 916
    Beta strandi96 – 983
    Beta strandi100 – 1089
    Turni109 – 1124
    Beta strandi113 – 1219
    Beta strandi166 – 1716
    Beta strandi176 – 1827
    Helixi186 – 1905
    Beta strandi194 – 1996
    Turni200 – 2023
    Beta strandi203 – 2064
    Beta strandi209 – 2124
    Turni214 – 2163
    Beta strandi218 – 2214
    Turni227 – 2293
    Beta strandi232 – 2409
    Turni242 – 2443
    Beta strandi246 – 2483
    Beta strandi251 – 2588
    Beta strandi268 – 2769
    Beta strandi285 – 2884
    Turni300 – 3023
    Beta strandi307 – 3104
    Beta strandi321 – 3233
    Turni325 – 3273
    Beta strandi329 – 3324
    Turni339 – 3413
    Beta strandi343 – 3508
    Turni353 – 3564
    Turni358 – 3603
    Beta strandi365 – 3728
    Beta strandi381 – 39414
    Beta strandi396 – 40611
    Turni414 – 4163
    Beta strandi421 – 4255
    Beta strandi431 – 4355
    Turni437 – 4393
    Beta strandi441 – 4466
    Turni452 – 4543
    Beta strandi456 – 4638
    Beta strandi466 – 4683
    Helixi478 – 4803
    Beta strandi481 – 4899
    Beta strandi496 – 50813
    Beta strandi515 – 5184
    Beta strandi526 – 5283
    Beta strandi532 – 5387
    Beta strandi544 – 5463
    Turni548 – 5503
    Beta strandi552 – 5576
    Beta strandi561 – 5633
    Beta strandi568 – 57912
    Beta strandi581 – 5833
    Beta strandi586 – 59611
    Beta strandi604 – 6063
    Beta strandi621 – 6233
    Beta strandi633 – 6364
    Beta strandi638 – 6403
    Beta strandi643 – 6453
    Helixi646 – 6516
    Beta strandi652 – 6565
    Beta strandi658 – 6603
    Beta strandi662 – 6665
    Beta strandi674 – 68310
    Beta strandi685 – 6884
    Beta strandi691 – 70010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NCGX-ray2.10A160-267[»]
    1NCHX-ray2.10A/B160-267[»]
    1NCIX-ray2.10A/B160-267[»]
    1NCJX-ray3.40A160-374[»]
    1OP4NMR-A24-159[»]
    2QVIX-ray3.01A160-374[»]
    3Q2WX-ray3.20A160-712[»]
    ProteinModelPortaliP15116.
    SMRiP15116. Positions 24-701, 818-904.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15116.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini160 – 724565ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini746 – 906161CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei725 – 74521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini160 – 267108Cadherin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini268 – 382115Cadherin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini383 – 497115Cadherin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini498 – 603106Cadherin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini604 – 717114Cadherin 5PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi863 – 87816Ser-richAdd
    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. Calcium-binding sites are occupied sequentially in the order of site 3, then site 2 and site 1.

    Sequence similaritiesi

    Contains 5 cadherin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG251747.
    GeneTreeiENSGT00740000115112.
    HOGENOMiHOG000231254.
    HOVERGENiHBG106438.
    InParanoidiQ6GU11.
    KOiK06736.
    OMAiHSGHLQR.
    OrthoDBiEOG7RJPQM.
    TreeFamiTF316817.

    Family and domain databases

    Gene3Di2.60.40.60. 6 hits.
    4.10.900.10. 1 hit.
    InterProiIPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR009124. Cadherin/Desmocollin.
    IPR020894. Cadherin_CS.
    IPR000233. Cadherin_cytoplasmic-dom.
    IPR014868. Cadherin_pro_dom.
    IPR027397. Catenin_binding_dom.
    [Graphical view]
    PfamiPF00028. Cadherin. 5 hits.
    PF01049. Cadherin_C. 1 hit.
    PF08758. Cadherin_pro. 1 hit.
    [Graphical view]
    PRINTSiPR00205. CADHERIN.
    PR01820. DESMOCOLLIN.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P15116-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCRIAGAPRT LLPLLAALLQ ASVEASGEIA LCKTGFPEDV YSAVLPKDVH    50
    EGQPLLNVKF SNCNRKRKVQ YESSEPADFK VDEDGTVYAV RSFPLTAEQA 100
    KFLIYAQDKE TQEKWQVAVN LSREPTLTEE PMKEPHEIEE IVFPRQLAKH 150
    SGALQRQKRD WVIPPINLPE NSRGPFPQEL VRIRSDRDKN LSLRYSVTGP 200
    GADQPPTGIF IINPISGQLS VTKPLDRELI ARFHLRAHAV DINGNQVENP 250
    IDIVINVIDM NDNRPEFLHQ VWNGSVPEGS KPGTYVMTVT AIDADDPNAL 300
    NGMLRYRILS QAPSTPSPNM FTINNETGDI ITVAAGLDRE KVQQYTLIIQ 350
    ATDMEGNPTY GLSNTATAVI TVTDVNDNPP EFTAMTFYGE VPENRVDVIV 400
    ANLTVTDKDQ PHTPAWNAAY RISGGDPTGR FAILTDPNSN DGLVTVVKPI 450
    DFETNRMFVL TVAAENQVPL AKGIQHPPQS TATVSVTVID VNENPYFAPN 500
    PKIIRQEEGL HAGTMLTTLT AQDPDRYMQQ NIRYTKLSDP ANWLKIDPVN 550
    GQITTIAVLD RESPNVKNNI YNATFLASDN GIPPMSGTGT LQIYLLDIND 600
    NAPQVLPQEA ETCETPEPNS INITALDYDI DPNAGPFAFD LPLSPVTIKR 650
    NWTINRLNGD FAQLNLKIKF LEAGIYEVPI IITDSGNPPK SNISILRVKV 700
    CQCDSNGDCT DVDRIVGAGL GTGAIIAILL CIIILLILVL MFVVWMKRRD 750
    KERQAKQLLI DPEDDVRDNI LKYDEEGGGE EDQDYDLSQL QQPDTVEPDA 800
    IKPVGIRRLD ERPIHAEPQY PVRSAAPHPG DIGDFINEGL KAADNDPTAP 850
    PYDSLLVFDY EGSGSTAGSL SSLNSSSSGG DQDYDYLNDW GPRFKKLADM 900
    YGGGDD 906
    Length:906
    Mass (Da):99,796
    Last modified:July 27, 2011 - v2
    Checksum:iBDAB8063A23E1F13
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 93APR → GRG in AAA37353. (PubMed:2762814)Curated
    Sequence conflicti565 – 5673NVK → YVQ in AAA37353. (PubMed:2762814)Curated
    Sequence conflicti624 – 6241T → A in AAA37353. (PubMed:2762814)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31131 mRNA. Translation: AAA37353.1.
    AB008811 mRNA. Translation: BAA23549.1.
    S45011 Genomic DNA. Translation: AAB23356.1.
    CH466557 Genomic DNA. Translation: EDK96930.1.
    BC022107 mRNA. Translation: AAH22107.1.
    CCDSiCCDS29076.1.
    PIRiA32759. IJMSCN.
    RefSeqiNP_031690.3. NM_007664.4.
    UniGeneiMm.257437.

    Genome annotation databases

    EnsembliENSMUST00000025166; ENSMUSP00000025166; ENSMUSG00000024304.
    GeneIDi12558.
    KEGGimmu:12558.
    UCSCiuc008edx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31131 mRNA. Translation: AAA37353.1 .
    AB008811 mRNA. Translation: BAA23549.1 .
    S45011 Genomic DNA. Translation: AAB23356.1 .
    CH466557 Genomic DNA. Translation: EDK96930.1 .
    BC022107 mRNA. Translation: AAH22107.1 .
    CCDSi CCDS29076.1.
    PIRi A32759. IJMSCN.
    RefSeqi NP_031690.3. NM_007664.4.
    UniGenei Mm.257437.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NCG X-ray 2.10 A 160-267 [» ]
    1NCH X-ray 2.10 A/B 160-267 [» ]
    1NCI X-ray 2.10 A/B 160-267 [» ]
    1NCJ X-ray 3.40 A 160-374 [» ]
    1OP4 NMR - A 24-159 [» ]
    2QVI X-ray 3.01 A 160-374 [» ]
    3Q2W X-ray 3.20 A 160-712 [» ]
    ProteinModelPortali P15116.
    SMRi P15116. Positions 24-701, 818-904.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198637. 20 interactions.
    DIPi DIP-31564N.
    IntActi P15116. 9 interactions.
    MINTi MINT-4089694.

    PTM databases

    PhosphoSitei P15116.

    Proteomic databases

    MaxQBi P15116.
    PaxDbi P15116.
    PRIDEi P15116.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025166 ; ENSMUSP00000025166 ; ENSMUSG00000024304 .
    GeneIDi 12558.
    KEGGi mmu:12558.
    UCSCi uc008edx.2. mouse.

    Organism-specific databases

    CTDi 1000.
    MGIi MGI:88355. Cdh2.

    Phylogenomic databases

    eggNOGi NOG251747.
    GeneTreei ENSGT00740000115112.
    HOGENOMi HOG000231254.
    HOVERGENi HBG106438.
    InParanoidi Q6GU11.
    KOi K06736.
    OMAi HSGHLQR.
    OrthoDBi EOG7RJPQM.
    TreeFami TF316817.

    Miscellaneous databases

    EvolutionaryTracei P15116.
    NextBioi 281622.
    PROi P15116.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15116.
    Bgeei P15116.
    CleanExi MM_CDH2.
    Genevestigatori P15116.

    Family and domain databases

    Gene3Di 2.60.40.60. 6 hits.
    4.10.900.10. 1 hit.
    InterProi IPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR009124. Cadherin/Desmocollin.
    IPR020894. Cadherin_CS.
    IPR000233. Cadherin_cytoplasmic-dom.
    IPR014868. Cadherin_pro_dom.
    IPR027397. Catenin_binding_dom.
    [Graphical view ]
    Pfami PF00028. Cadherin. 5 hits.
    PF01049. Cadherin_C. 1 hit.
    PF08758. Cadherin_pro. 1 hit.
    [Graphical view ]
    PRINTSi PR00205. CADHERIN.
    PR01820. DESMOCOLLIN.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Tamura K.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Genomic structure and chromosomal mapping of the mouse N-cadherin gene."
      Miyatani S., Copeland N.G., Gilbert D.J., Jenkins N.A., Takeichi M.
      Proc. Natl. Acad. Sci. U.S.A. 89:8443-8447(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/6.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Strain: FVB/N.
      Tissue: Liver.
    6. "A comprehensive survey of the cadherins expressed in the testes of fetal, immature, and adult mice utilizing the polymerase chain reaction."
      Munro S.B., Blaschuk O.W.
      Biol. Reprod. 55:822-827(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
      Strain: C57BL/6.
      Tissue: Testis.
    7. "N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling."
      Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.
      Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH FGFR4; PLCG1; FRS2; SRC; GAP43 AND CTTN.
    8. "Activity-induced protocadherin arcadlin regulates dendritic spine number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases."
      Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U., Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M., Yamagata K.
      Neuron 56:456-471(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PCDH8-MEDIATED ENDOCYTOSIS.
    9. Cited for: PROTEOLYTIC PROCESSING.
    10. "Sequential binding of calcium leads to dimerization in neural cadherin."
      Vunnam N., Pedigo S.
      Biochemistry 50:2973-2982(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CALCIUM-BINDING SITES, MUTAGENESIS OF ASP-262 AND ASP-293.
    11. "MT5-MMP regulates adult neural stem cell functional quiescence through the cleavage of N-cadherin."
      Porlan E., Marti-Prado B., Morante-Redolat J.M., Consiglio A., Delgado A.C., Kypta R., Lopez-Otin C., Kirstein M., Farinas I.
      Nat. Cell Biol. 16:629-638(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, PROTEOLYTIC PROCESSING.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-267.
    13. "Structure-function analysis of cell adhesion by neural (N-) cadherin."
      Tamura K., Shan W.S., Hendrickson W.A., Colman D.R., Shapiro L.
      Neuron 20:1153-1163(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 160-374.

    Entry informationi

    Entry nameiCADH2_MOUSE
    AccessioniPrimary (citable) accession number: P15116
    Secondary accession number(s): Q64260, Q6GU11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3