Catenin (cadherin-associated protein), alpha 1

Catenin (cadherin-associated protein), alpha 1, 102kDa

PDB rendering based on 1dov.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsCTNNA1 ; CAP102
External IDsOMIM: 116805 MGI: 88274 HomoloGene: 1433 GeneCards: CTNNA1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez149512385
EnsemblENSG00000044115ENSMUSG00000037815
UniProtP35221P26231
RefSeq (mRNA)NM_001290307NM_009818
RefSeq (protein)NP_001277236NP_033948
Location (UCSC)Chr 5:
137.95 – 138.27 Mb		Chr 18:
35.12 – 35.25 Mb
PubMed search

Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene.[1][2]

Interactions

Catenin (cadherin-associated protein), alpha 1 has been shown to interact with:

See also

References

  1. ↑ Herrenknecht K, Ozawa M, Eckerskorn C, Lottspeich F, Lenter M, Kemler R (November 1991). "The uvomorulin-anchorage protein alpha catenin is a vinculin homologue". Proc Natl Acad Sci U S A 88 (20): 9156–60. doi:10.1073/pnas.88.20.9156. PMC 52671. PMID 1924379.
  2. ↑ "Entrez Gene: CTNNA1 catenin (cadherin-associated protein), alpha 1, 102kDa".
  3. ↑ Su LK, Vogelstein B, Kinzler KW (December 1993). "Association of the APC tumor suppressor protein with catenins". Science 262 (5140): 1734–7. doi:10.1126/science.8259519. PMID 8259519.
  4. ↑ Daniel JM, Reynolds AB (September 1995). "The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". Mol. Cell. Biol. 15 (9): 4819–24. PMC 230726. PMID 7651399.
  5. ↑ Oyama T, Kanai Y, Ochiai A, Akimoto S, Oda T, Yanagihara K et al. (December 1994). "A truncated beta-catenin disrupts the interaction between E-cadherin and alpha-catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines". Cancer Res. 54 (23): 6282–7. PMID 7954478.
  6. ↑ 6.0 6.1 Roe S, Koslov ER, Rimm DL (June 1998). "A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and beta-catenin binding activity". Cell Adhes. Commun. 5 (4): 283–96. doi:10.3109/15419069809040298. PMID 9762469.
  7. ↑ Piedra J, Miravet S, Castaño J, Pálmer HG, Heisterkamp N, García de Herreros A et al. (April 2003). "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction". Mol. Cell. Biol. 23 (7): 2287–97. doi:10.1128/mcb.23.7.2287-2297.2003. PMC 150740. PMID 12640114. Vancouver style error (help)
  8. ↑ Aberle H, Butz S, Stappert J, Weissig H, Kemler R, Hoschuetzky H (December 1994). "Assembly of the cadherin-catenin complex in vitro with recombinant proteins". J. Cell. Sci. 107 (12): 3655–63. PMID 7706414.
  9. ↑ Reuver SM, Garner CC (April 1998). "E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton". J. Cell. Sci. 111 (8): 1071–80. PMID 9512503.
  10. ↑ Kinch MS, Clark GJ, Der CJ, Burridge K (July 1995). "Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia". J. Cell Biol. 130 (2): 461–71. doi:10.1083/jcb.130.2.461. PMC 2199929. PMID 7542250.
  11. ↑ Oneyama C, Nakano H, Sharma SV (March 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug". Oncogene 21 (13): 2037–50. doi:10.1038/sj.onc.1205271. PMID 11960376.
  12. ↑ Navarro P, Lozano E, Cano A (August 1993). "Expression of E- or P-cadherin is not sufficient to modify the morphology and the tumorigenic behavior of murine spindle carcinoma cells. Possible involvement of plakoglobin". J. Cell. Sci. 105 (4): 923–34. PMID 8227214.
  13. ↑ Takahashi K, Suzuki K, Tsukatani Y (July 1997). "Induction of tyrosine phosphorylation and association of beta-catenin with EGF receptor upon tryptic digestion of quiescent cells at confluence". Oncogene 15 (1): 71–8. doi:10.1038/sj.onc.1201160. PMID 9233779.
  14. ↑ 14.0 14.1 Schmeiser K, Grand RJ (April 1999). "The fate of E- and P-cadherin during the early stages of apoptosis". Cell Death Differ. 6 (4): 377–86. doi:10.1038/sj.cdd.4400504. PMID 10381631.
  15. ↑ Straub BK, Boda J, Kuhn C, Schnoelzer M, Korf U, Kempf T et al. (December 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.
  16. ↑ Wahl JK, Kim YJ, Cullen JM, Johnson KR, Wheelock MJ (May 2003). "N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane". J. Biol. Chem. 278 (19): 17269–76. doi:10.1074/jbc.M211452200. PMID 12604612.
  17. ↑ Klingelhöfer J, Troyanovsky RB, Laur OY, Troyanovsky S (August 2000). "Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions". J. Cell. Sci. 113 (16): 2829–36. PMID 10910767. Vancouver style error (help)
  18. ↑ Sacco PA, McGranahan TM, Wheelock MJ, Johnson KR (August 1995). "Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin". J. Biol. Chem. 270 (34): 20201–6. doi:10.1074/jbc.270.34.20201. PMID 7650039.
  19. ↑ Obama H, Ozawa M (April 1997). "Identification of the domain of alpha-catenin involved in its association with beta-catenin and plakoglobin (gamma-catenin)". J. Biol. Chem. 272 (17): 11017–20. doi:10.1074/jbc.272.17.11017. PMID 9110993.
  20. ↑ Lewalle JM, Bajou K, Desreux J, Mareel M, Dejana E, Noël A et al. (December 1997). "Alteration of interendothelial adherens junctions following tumor cell-endothelial cell interaction in vitro". Exp. Cell Res. 237 (2): 347–56. doi:10.1006/excr.1997.3799. PMID 9434630. Vancouver style error (help)
  21. ↑ Shasby DM, Ries DR, Shasby SS, Winter MC (June 2002). "Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin". Am. J. Physiol. Lung Cell Mol. Physiol. 282 (6): L1330–8. doi:10.1152/ajplung.00329.2001. PMID 12003790.

Further reading