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Reviewed, UniProtKB/Swiss-Prot P19022 (CADH2_HUMAN)

Last modified June 16, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cadherin-2
Alternative name(s):
    Neural cadherin
      Short name=N-cadherin
    CDw325
    CD_antigen=CD325
Gene names
Name: CDH2
Synonyms: CDHN, NCAD
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. CDH2 may be involved in neuronal recognition mechanism.

Subunit structure

Interacts with CDCP1. Ref.8

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Sequence similarities

Contains 5 cadherin domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
   LigandCalcium
   PTMCleavage on pair of basic residues
Glycoprotein
Phosphoprotein
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 159134
PRO_0000003731
Chain160 – 906747Cadherin-2
PRO_0000003732

Regions

Topological domain160 – 724565Extracellular Potential
Transmembrane725 – 74521 Potential
Topological domain746 – 906161Cytoplasmic Potential
Domain160 – 267108Cadherin 1
Domain268 – 382115Cadherin 2
Domain383 – 497115Cadherin 3
Domain498 – 603106Cadherin 4
Domain604 – 714111Cadherin 5
Compositional bias863 – 87816Ser-rich

Amino acid modifications

Modified residue7851Phosphotyrosine Ref.7
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...)
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...)
Glycosylation5721N-linked (GlcNAc...)
Glycosylation6511N-linked (GlcNAc...) Potential
Glycosylation6921N-linked (GlcNAc...)

Natural variations

Natural variant211A → T: dbSNP rs17495042.
VAR_028254
Natural variant1181A → T: dbSNP rs17445840.
VAR_028255
Natural variant1961S → T: dbSNP rs1041970. Ref.1
VAR_028256
Natural variant2121I → L: dbSNP rs1041972. Ref.5
VAR_028257
Natural variant4541T → A: dbSNP rs17857112. Ref.4
VAR_048503
Natural variant8451N → S: dbSNP rs2289664.
VAR_028258

Experimental info

Sequence conflict121Missing in AAB22854. Ref.3
Sequence conflict161A → L in CAA38213. Ref.1
Sequence conflict1641P → S in AAH36470. Ref.4
Sequence conflict3571N → I in CAA38213. Ref.1
Sequence conflict4371P → Q in AAH36470. Ref.4
Sequence conflict4841V → M in AAH36470. Ref.4
Sequence conflict6291D → G in AAH36470. Ref.4
Sequence conflict8671A → L in AAB22854. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P19022-1 [UniParc].

Last modified October 17, 2006. Version 4.
Checksum: 7267E2A00489DF94

FASTA90699,809
        10         20         30         40         50         60 
MCRIAGALRT LLPLLAALLQ ASVEASGEIA LCKTGFPEDV YSAVLSKDVH EGQPLLNVKF 

        70         80         90        100        110        120 
SNCNGKRKVQ YESSEPADFK VDEDGMVYAV RSFPLSSEHA KFLIYAQDKE TQEKWQVAVK 

       130        140        150        160        170        180 
LSLKPTLTEE SVKESAEVEE IVFPRQFSKH SGHLQRQKRD WVIPPINLPE NSRGPFPQEL 

       190        200        210        220        230        240 
VRIRSDRDKN LSLRYSVTGP GADQPPTGIF IINPISGQLS VTKPLDREQI ARFHLRAHAV 

       250        260        270        280        290        300 
DINGNQVENP IDIVINVIDM NDNRPEFLHQ VWNGTVPEGS KPGTYVMTVT AIDADDPNAL 

       310        320        330        340        350        360 
NGMLRYRIVS QAPSTPSPNM FTINNETGDI ITVAAGLDRE KVQQYTLIIQ ATDMEGNPTY 

       370        380        390        400        410        420 
GLSNTATAVI TVTDVNDNPP EFTAMTFYGE VPENRVDIIV ANLTVTDKDQ PHTPAWNAVY 

       430        440        450        460        470        480 
RISGGDPTGR FAIQTDPNSN DGLVTVVKPI DFETNRMFVL TVAAENQVPL AKGIQHPPQS 

       490        500        510        520        530        540 
TATVSVTVID VNENPYFAPN PKIIRQEEGL HAGTMLTTFT AQDPDRYMQQ NIRYTKLSDP 

       550        560        570        580        590        600 
ANWLKIDPVN GQITTIAVLD RESPNVKNNI YNATFLASDN GIPPMSGTGT LQIYLLDIND 

       610        620        630        640        650        660 
NAPQVLPQEA ETCETPDPNS INITALDYDI DPNAGPFAFD LPLSPVTIKR NWTITRLNGD 

       670        680        690        700        710        720 
FAQLNLKIKF LEAGIYEVPI IITDSGNPPK SNISILRVKV CQCDSNGDCT DVDRIVGAGL 

       730        740        750        760        770        780 
GTGAIIAILL CIIILLILVL MFVVWMKRRD KERQAKQLLI DPEDDVRDNI LKYDEEGGGE 

       790        800        810        820        830        840 
EDQDYDLSQL QQPDTVEPDA IKPVGIRRMD ERPIHAEPQY PVRSAAPHPG DIGDFINEGL 

       850        860        870        880        890        900 
KAADNDPTAP PYDSLLVFDY EGSGSTAGSL SSLNSSSSGG EQDYDYLNDW GPRFKKLADM 


YGGGDD 

« Hide

References

« Hide 'large scale' references
[1]"Human N-cadherin: nucleotide and deduced amino acid sequence."
Reid R.A., Hemperly J.J.
Nucleic Acids Res. 18:5896-5896(1990) [PubMed: 2216790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-196.
[2]Reid R.A.
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 341; 699 AND 705.
[3]"Extrajunctional distribution of N-cadherin in cultured human endothelial cells."
Salomon D., Ayalon O., Patel-King R., Hynes R.O., Geiger B.
J. Cell Sci. 102:7-17(1992) [PubMed: 1500442] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-454.
Tissue: Brain.
[5]"N-cadherin gene maps to human chromosome 18 and is not linked to the E-cadherin gene."
Walsh F.S., Barton C.H., Putt W., Moore S.E., Kelsell D., Spurr N., Goodfellow P.N.
J. Neurochem. 55:805-812(1990) [PubMed: 2384753] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 160-906, VARIANT LEU-212.
[6]"Structure of the human N-cadherin gene: YAC analysis and fine chromosomal mapping to 18q11.2."
Wallis J.A., Fox M., Walsh F.S.
Genomics 22:172-179(1994) [PubMed: 7959764] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[7]"Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)."
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.
J. Proteome Res. 4:1661-1671(2005) [PubMed: 16212419] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-785, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Adhesion signaling by a novel mitotic substrate of src kinases."
Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.
Oncogene 24:5333-5343(2005) [PubMed: 16007225] [Abstract]
Cited for: INTERACTION WITH CDCP1.
[9]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-273; ASN-402; ASN-572 AND ASN-692, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

X54315 mRNA. Translation: CAA38213.1.
S42303 mRNA. Translation: AAB22854.1.
BC036470 mRNA. Translation: AAH36470.1.
M34064 mRNA. Translation: AAA03236.1.
X57548 mRNA. Translation: CAA40773.1.
Z27420 Genomic DNA. Translation: CAA81799.1.
IPIIPI00290085.
PIRIJHUCN. A38870.
RefSeqNP_001783.2.
UniGeneHs.464829
Hs.606106

3D structure databases

HSSPHSSP built from PDB template 1NCJ based on UniProtKB P15116.
SMRP19022. Positions 24-159, 161-373, 836-901.
ModBaseSearch...

Protein-protein interaction databases

IntActP19022. 11 interactions.

PTM databases

PhosphoSiteP19022.

Proteomic databases

PeptideAtlasP19022.
PRIDEP19022.

Genome annotation databases

EnsemblENSG00000170558. Homo sapiens. [Contig view]
GeneID1000.
KEGGhsa:1000.

Organism-specific databases

GeneCardsGC18M023784.
HGNCHGNC:1759. CDH2.
HPACAB000141.
MIM114020. gene.
PharmGKBPA26293.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP19022.
HOVERGENP19022.
OMAP19022. DPNSINI.

Enzyme and pathway databases

Pathway_Interaction_DBfgf_pathway. FGF signaling pathway.
ptp1bpathway. Signaling events mediated by PTP1B.

Gene expression databases

ArrayExpressP19022.
BgeeP19022.
CleanExHS_CDH2.
GermOnlineENSG00000170558. Homo sapiens.

Family and domain databases

InterProIPR002126. Cadherin.
IPR000233. Cadherin_C_term.
IPR014868. Cadherin_pro.
IPR009124. Desmocollin.
[Graphical view]
Gene3DG3DSA:2.60.40.60. Cadherin. 4 hits.
PfamPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
PR01820. DESMOCOLLIN.
SMARTSM00112. CA. 5 hits.
[Graphical view]
PROSITEPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio4204.
PMAP-CutDBP19022.
SOURCESearch...

Entry information

Entry nameCADH2_HUMAN
AccessionPrimary (citable) accession number: P19022
Secondary accession number(s): Q14923, Q8N173
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 93 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents