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Cadherin 11, type 2, OB-cadherin (osteoblast)
Protein CDH11 PDB 2a4c.png
PDB rendering based on 2a4c.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CDH11 ; CAD11; CDHOB; OB; OSF-4
External IDs OMIM600023 MGI99217 HomoloGene1361 GeneCards: CDH11 Gene
RNA expression pattern
PBB GE CDH11 207172 s at tn.png
PBB GE CDH11 207173 x at tn.png
More reference expression data
Species Human Mouse
Entrez 1009 12552
Ensembl ENSG00000140937 ENSMUSG00000031673
UniProt P55287 P55288
RefSeq (mRNA) NM_001308392 NM_009866
RefSeq (protein) NP_001295321 NP_033996
Location (UCSC) Chr 16:
64.94 – 65.13 Mb
Chr 8:
102.63 – 102.79 Mb
PubMed search [1] [2]

Cadherin-11 is a protein that in humans is encoded by the CDH11 gene.[1][2]


This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Mature cadherin proteins are composed of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small, highly conserved C-terminal cytoplasmic domain. Type II (atypical) cadherins are defined based on their lack of a HAV cell adhesion recognition sequence specific to type I cadherins. Expression of this particular cadherin in osteoblastic cell lines, and its upregulation during differentiation, suggests a specific function in bone development and maintenance.[2] The mammalian CDH-11 homologues are termed calsyntenin.[3]

Relevance to cancer[edit]

CDH11 is overexpressed in 15% of breast cancers and seems essential to tumour progression in some other cancer types.[4][5]

Drug interactions[edit]

Arthritis drug celecoxib binds to CDH11.[4][5]


CDH11 has been shown to interact with CDH2.[6]


  1. ^ Kremmidiotis G, Baker E, Crawford J, Eyre HJ, Nahmias J, Callen DF (Aug 1998). "Localization of human cadherin genes to chromosome regions exhibiting cancer-related loss of heterozygosity". Genomics 49 (3): 467–71. doi:10.1006/geno.1998.5281. PMID 9615235. 
  2. ^ a b "Entrez Gene: CDH11 cadherin 11, type 2, OB-cadherin (osteoblast)". 
  3. ^ Vogt L, Schrimpf SP, Meskenaite V, Frischknecht R, Kinter J, Leone DP, Ziegler U, Sonderegger P (2001). "Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain". Mol. Cell. Neurosci. 17 (1): 151–66. doi:10.1006/mcne.2000.0937. PMID 11161476. 
  4. ^ a b "New Therapeutic Approach Could Target Both Cancer and Arthritis". 15 Nov 2013. 
  5. ^ a b Assefnia S, Dakshanamurthy S, Guidry Auvil JM, Hampel C, Anastasiadis PZ, Kallakury B, Uren A, Foley DW, Brown ML, Shapiro L, Brenner M, Haigh D, Byers SW (Mar 2014). "Cadherin-11 in poor prognosis malignancies and rheumatoid arthritis: common target, common therapies.". Oncotarget 5 (6): 1458–74. PMID 24681547. 
  6. ^ Straub BK, Boda J, Kuhn C, Schnoelzer M, Korf U, Kempf T, Spring H, Hatzfeld M, Franke WW (Dec 2003). "A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells". J. Cell. Sci. 116 (Pt 24): 4985–95. doi:10.1242/jcs.00815. PMID 14625392. 

Further reading[edit]

External links[edit]