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UniProtKB - P15116 (CADH2_MOUSE)

Protein

Cadherin-2

Gene

Cdh2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell (PubMed:2762814, PubMed:11433297, PubMed:17988630, PubMed:9655503, PubMed:25253890). 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.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi170Calcium 1Combined sources1 Publication1
Metal bindingi170Calcium 2Combined sources1 Publication1
Metal bindingi226Calcium 1Combined sources1 Publication1
Metal bindingi228Calcium 1Combined sources1 Publication1
Metal bindingi228Calcium 2Combined sources1 Publication1
Metal bindingi259Calcium 2Combined sources1 Publication1
Metal bindingi260Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi261Calcium 3Combined sources1 Publication1
Metal bindingi262Calcium 1Combined sources2 Publications1
Metal bindingi262Calcium 2Combined sources2 Publications1
Metal bindingi263Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi293Calcium 3Combined sources2 Publications1
Metal bindingi295Calcium 2Combined sources1 Publication1
Metal bindingi301Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi353Calcium 3Combined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-375170 CDO in myogenesis
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-418990 Adherens junctions interactions
R-MMU-8957275 Post-translational protein phosphorylation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cadherin-2
Alternative name(s):
Neural cadherin
Short name:
N-cadherin
CD_antigen: CD325
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Cdh2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 18

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:88355 Cdh2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini160 – 724ExtracellularSequence analysisAdd BLAST565
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei725 – 745HelicalSequence analysisAdd BLAST21
Topological domaini746 – 906CytoplasmicSequence analysisAdd BLAST161

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Embryonic lethality.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi161W → A or Y: Loss of calcium-dependent cell-cell adhesion. 1 Publication1
Mutagenesisi161W → A: Loss of dimerization; when associated with E-173. 1 Publication1
Mutagenesisi162V → A: Decreased calcium-dependent cell-cell adhesion. 1 Publication1
Mutagenesisi173R → E: Loss of dimerization; when associated with A-161. 1 Publication1
Mutagenesisi237A → M: Loss of calcium-dependent cell-cell adhesion. 1 Publication1
Mutagenesisi239A → M: Loss of calcium-dependent cell-cell adhesion. 1 Publication1
Mutagenesisi262D → A: Abolishes dimerization. 1 Publication1
Mutagenesisi293D → A: Severely impaired the binding of calcium to all three sites. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000373326 – 159Sequence analysisAdd BLAST134
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000003734160 – 906Cadherin-2Add BLAST747

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi190N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi273N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi325N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi402N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi572N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi651N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Glycosylationi692N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
May be phosphorylated by OBSCN.1 Publication
O-glycosylated on Ser and Thr residues.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P15116

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P15116

PeptideAtlas

More...PeptideAtlasi		P15116

PRoteomics IDEntifications database

More...PRIDEi		P15116

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P15116

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P15116

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in cardiac muscle (at protein level).1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000024304 Expressed in 398 organ(s), highest expression level in cardiac ventricle

CleanEx database of gene expression profiles

More...CleanExi		MM_CDH2

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P15116 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P15116 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (via extracellular region) (PubMed:21300292, PubMed:25253890). Can also form heterodimers with other cadherins (via extracellular region) (PubMed:25253890). Dimerization occurs in trans, i.e. with a cadherin chain from another cell (PubMed:21300292, PubMed:25253890). 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 (By similarity). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (PubMed:11433297). May interact with OBSCN (via protein kinase domain 2) (PubMed:23392350).By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		198637, 26 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P15116

Database of interacting proteins

More...DIPi		DIP-31564N

Protein interaction database and analysis system

More...IntActi		P15116, 18 interactors

Molecular INTeraction database

More...MINTi		P15116

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000025166

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1906
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P15116

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P15116

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P15116

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini160 – 267Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini268 – 382Cadherin 2PROSITE-ProRule annotationAdd BLAST115
Domaini383 – 497Cadherin 3PROSITE-ProRule annotationAdd BLAST115
Domaini498 – 603Cadherin 4PROSITE-ProRule annotationAdd BLAST106
Domaini604 – 717Cadherin 5PROSITE-ProRule annotationAdd BLAST114

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi863 – 878Ser-richAdd BLAST16

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 1.2 Publications

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3594 Eukaryota
ENOG410XQHI LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155981

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231254

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG106438

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P15116

KEGG Orthology (KO)

More...KOi		K06736

Database of Orthologous Groups

More...OrthoDBi		EOG091G01FV

TreeFam database of animal gene trees

More...TreeFami		TF316817

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		4.10.900.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR039808 Cadherin
IPR002126 Cadherin-like_dom
IPR015919 Cadherin-like_sf
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR014868 Cadherin_pro_dom
IPR027397 Catenin_binding_dom_sf
IPR030051 CDH2

The PANTHER Classification System

More...PANTHERi		PTHR24027 PTHR24027, 1 hit
PTHR24027:SF79 PTHR24027:SF79, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF08758 Cadherin_pro, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00205 CADHERIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00112 CA, 5 hits
SM01055 Cadherin_pro, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49313 SSF49313, 6 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 5 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P15116-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MCRIAGAPRT LLPLLAALLQ ASVEASGEIA LCKTGFPEDV YSAVLPKDVH 
        60         70         80         90        100
EGQPLLNVKF SNCNRKRKVQ YESSEPADFK VDEDGTVYAV RSFPLTAEQA 
       110        120        130        140        150
KFLIYAQDKE TQEKWQVAVN LSREPTLTEE PMKEPHEIEE IVFPRQLAKH 
       160        170        180        190        200
SGALQRQKRD WVIPPINLPE NSRGPFPQEL VRIRSDRDKN LSLRYSVTGP 
       210        220        230        240        250
GADQPPTGIF IINPISGQLS VTKPLDRELI ARFHLRAHAV DINGNQVENP 
       260        270        280        290        300
IDIVINVIDM NDNRPEFLHQ VWNGSVPEGS KPGTYVMTVT AIDADDPNAL 
       310        320        330        340        350
NGMLRYRILS QAPSTPSPNM FTINNETGDI ITVAAGLDRE KVQQYTLIIQ 
       360        370        380        390        400
ATDMEGNPTY GLSNTATAVI TVTDVNDNPP EFTAMTFYGE VPENRVDVIV 
       410        420        430        440        450
ANLTVTDKDQ PHTPAWNAAY RISGGDPTGR FAILTDPNSN DGLVTVVKPI 
       460        470        480        490        500
DFETNRMFVL TVAAENQVPL AKGIQHPPQS TATVSVTVID VNENPYFAPN 
       510        520        530        540        550
PKIIRQEEGL HAGTMLTTLT AQDPDRYMQQ NIRYTKLSDP ANWLKIDPVN 
       560        570        580        590        600
GQITTIAVLD RESPNVKNNI YNATFLASDN GIPPMSGTGT LQIYLLDIND 
       610        620        630        640        650
NAPQVLPQEA ETCETPEPNS INITALDYDI DPNAGPFAFD LPLSPVTIKR 
       660        670        680        690        700
NWTINRLNGD FAQLNLKIKF LEAGIYEVPI IITDSGNPPK SNISILRVKV 
       710        720        730        740        750
CQCDSNGDCT DVDRIVGAGL GTGAIIAILL CIIILLILVL MFVVWMKRRD 
       760        770        780        790        800
KERQAKQLLI DPEDDVRDNI LKYDEEGGGE EDQDYDLSQL QQPDTVEPDA 
       810        820        830        840        850
IKPVGIRRLD ERPIHAEPQY PVRSAAPHPG DIGDFINEGL KAADNDPTAP 
       860        870        880        890        900
PYDSLLVFDY EGSGSTAGSL SSLNSSSSGG DQDYDYLNDW GPRFKKLADM 

YGGGDD
Length:906
Mass (Da):99,796
Last modified:July 27, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBDAB8063A23E1F13
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3YYT0D3YYT0_MOUSE
Cadherin-2
Cdh2
849Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti7 – 9APR → GRG in AAA37353 (PubMed:2762814).Curated3
Sequence conflicti565 – 567NVK → YVQ in AAA37353 (PubMed:2762814).Curated3
Sequence conflicti624T → A in AAA37353 (PubMed:2762814).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS29076.1

Protein sequence database of the Protein Information Resource

More...PIRi		A32759 IJMSCN

NCBI Reference Sequences

More...RefSeqi		NP_031690.3, NM_007664.5

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.257437

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000025166; ENSMUSP00000025166; ENSMUSG00000024304

Database of genes from NCBI RefSeq genomes

More...GeneIDi		12558

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:12558

UCSC genome browser

More...UCSCi		uc008edx.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_007664.5
UniGeneiMm.257437

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
4NUMX-ray3.30A/B/C/D160-374[»]
4NUPX-ray2.70A/B/C162-374[»]
4NUQX-ray2.12A160-374[»]
ProteinModelPortaliP15116
SMRiP15116
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198637, 26 interactors
CORUMiP15116
DIPiDIP-31564N
IntActiP15116, 18 interactors
MINTiP15116
STRINGi10090.ENSMUSP00000025166

PTM databases

iPTMnetiP15116
PhosphoSitePlusiP15116

Proteomic databases

MaxQBiP15116
PaxDbiP15116
PeptideAtlasiP15116
PRIDEiP15116

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1000
MGIiMGI:88355 Cdh2

Phylogenomic databases

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
GeneTreeiENSGT00940000155981
HOGENOMiHOG000231254
HOVERGENiHBG106438
InParanoidiP15116
KOiK06736
OrthoDBiEOG091G01FV
TreeFamiTF316817

Enzyme and pathway databases

ReactomeiR-MMU-375170 CDO in myogenesis
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-418990 Adherens junctions interactions
R-MMU-8957275 Post-translational protein phosphorylation

Miscellaneous databases

EvolutionaryTraceiP15116

Protein Ontology

More...PROi		PR:P15116

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000024304 Expressed in 398 organ(s), highest expression level in cardiac ventricle
CleanExiMM_CDH2
ExpressionAtlasiP15116 baseline and differential
GenevisibleiP15116 MM

Family and domain databases

Gene3Di4.10.900.10, 1 hit
InterProiView protein in InterPro
IPR039808 Cadherin
IPR002126 Cadherin-like_dom
IPR015919 Cadherin-like_sf
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR014868 Cadherin_pro_dom
IPR027397 Catenin_binding_dom_sf
IPR030051 CDH2
PANTHERiPTHR24027 PTHR24027, 1 hit
PTHR24027:SF79 PTHR24027:SF79, 1 hit
PfamiView protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF08758 Cadherin_pro, 1 hit
PRINTSiPR00205 CADHERIN
SMARTiView protein in SMART
SM00112 CA, 5 hits
SM01055 Cadherin_pro, 1 hit
SUPFAMiSSF49313 SSF49313, 6 hits
PROSITEiView protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 5 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCADH2_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15116
Secondary accession number(s): Q64260, Q6GU11
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: December 5, 2018
This is version 187 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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