Annexin A2

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Annexin A2
Protein ANXA2 PDB 1w7b.png
PDB rendering based on 1w7b.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols ANXA2 ; ANX2; ANX2L4; CAL1H; HEL-S-270; LIP2; LPC2; LPC2D; P36; PAP-IV
External IDs OMIM151740 MGI88246 HomoloGene20857 ChEMBL: 1764938 GeneCards: ANXA2 Gene
RNA expression pattern
PBB GE ANXA2 201590 x at tn.png
PBB GE ANXA2 208816 x at tn.png
PBB GE ANXA2 210427 x at tn.png
More reference expression data
Species Human Mouse
Entrez 302 12306
Ensembl ENSG00000182718 ENSMUSG00000032231
UniProt P07355 P07356
RefSeq (mRNA) NM_001002857 NM_007585
RefSeq (protein) NP_001002857 NP_031611
Location (UCSC) Chr 15:
60.64 – 60.7 Mb
Chr 9:
69.45 – 69.49 Mb
PubMed search [1] [2]

Annexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2 gene.[1]

Annexin 2 is involved in diverse cellular processes such as cell motility (especially that of the epithelial cells), linkage of membrane-associated protein complexes to the actin cytoskeleton, endocytosis, fibrinolysis, ion channel formation, and cell matrix interactions. It is a calcium-dependent phospholipid-binding protein whose function is to help organize exocytosis of intracellular proteins to the extracellular domain. Annexin II is a pleiotropic protein meaning that its function is dependent on place and time in the body.


The ANXA2 gene, located at 15q22.2, has three pseudogenes located on chromosomes 4, 9 and 10, respectively. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.[2]


This protein is a member of the annexin family. Members of this calcium-dependent phospholipid-binding protein family play a role in the regulation of cellular growth and in signal transduction pathways. This protein functions as an autocrine factor which heightens osteoclast formation and bone resorption.[2]

Annexin A2 has been proposed to function inside the cell in sorting of endosomes and outside the cell in anticoagulant reactions.


Annexin A2 has been shown to interact with Prohibitin,[3] CEACAM1,[4] S100A10,[5][6] PCNA[7] and complement Factor H [8]

See also[edit]


  1. ^ Takahashi S, Reddy SV, Chirgwin JM, Devlin R, Haipek C, Anderson J, Roodman GD (November 1994). "Cloning and identification of annexin II as an autocrine/paracrine factor that increases osteoclast formation and bone resorption". J. Biol. Chem. 269 (46): 28696–701. PMID 7961821. 
  2. ^ a b "Entrez Gene: ANXA2 annexin A2". 
  3. ^ Bacher, Susanne; Achatz Gernot; Schmitz M L; Lamers Marinus C (Dec 2002). "Prohibitin and prohibitone are contained in high-molecular weight complexes and interact with alpha-actinin and annexin A2". Biochimie (France) 84 (12): 1207–20. doi:10.1016/S0300-9084(02)00027-5. ISSN 0300-9084. PMID 12628297. 
  4. ^ Kirshner, Julia; Schumann Detlef; Shively John E (Dec 2003). "CEACAM1, a cell-cell adhesion molecule, directly associates with annexin II in a three-dimensional model of mammary morphogenesis". J. Biol. Chem. (United States) 278 (50): 50338–45. doi:10.1074/jbc.M309115200. ISSN 0021-9258. PMID 14522961. 
  5. ^ Réty, S; Sopkova J; Renouard M; Osterloh D; Gerke V; Tabaries S; Russo-Marie F; Lewit-Bentley A (Jan 1999). "The crystal structure of a complex of p11 with the annexin II N-terminal peptide". Nat. Struct. Biol. (UNITED STATES) 6 (1): 89–95. doi:10.1038/4965. ISSN 1072-8368. PMID 9886297. 
  6. ^ He, Kai-Li; Deora Arunkumar B; Xiong Huabao; Ling Qi; Weksler Babette B; Niesvizky Ruben; Hajjar Katherine A (Jul 2008). "Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11". J. Biol. Chem. (United States) 283 (28): 19192–200. doi:10.1074/jbc.M800100200. ISSN 0021-9258. PMC 2443646. PMID 18434302. 
  7. ^ Ohta, Satoshi; Shiomi Yasushi; Sugimoto Katsunori; Obuse Chikashi; Tsurimoto Toshiki (Oct 2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". J. Biol. Chem. (United States) 277 (43): 40362–7. doi:10.1074/jbc.M206194200. ISSN 0021-9258. PMID 12171929. 
  8. ^ Leffler, Jonatan; Andrew P. Herbert; Eva Norstrom; Christoph Q. Schmidt; Paul N. Barlow; Anna M. Blom; Myriam Martin (Feb 2010). "Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells.". J. Biol. Chem. (United States) 285 (6): 3766–76. doi:10.1074/jbc.M109.045427. PMC 2823518. PMID 19951950. 

Further reading[edit]

  • Kwon M, MacLeod TJ, Zhang Y, Waisman DM (2006). "S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors.". Front. Biosci. 10 (1-3): 300–25. doi:10.2741/1529. PMID 15574370. 
  • Babiychuk EB, Draeger A (2006). "Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?". Biochem. Soc. Trans. 34 (Pt 3): 374–6. doi:10.1042/BST0340374. PMID 16709165. 
  • Bohn E, Gerke V, Kresse H et al. (1992). "Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase.". FEBS Lett. 296 (3): 237–40. doi:10.1016/0014-5793(92)80294-Q. PMID 1531641. 
  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151. 
  • Jindal HK, Chaney WG, Anderson CW et al. (1991). "The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha.". J. Biol. Chem. 266 (8): 5169–76. PMID 1825830. 
  • Filipek A, Gerke V, Weber K, Kuźnicki J (1991). "Characterization of the cell-cycle-regulated protein calcyclin from Ehrlich ascites tumor cells. Identification of two binding proteins obtained by Ca2(+)-dependent affinity chromatography.". Eur. J. Biochem. 195 (3): 795–800. doi:10.1111/j.1432-1033.1991.tb15768.x. PMID 1999197. 
  • Becker T, Weber K, Johnsson N (1991). "Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11.". EMBO J. 9 (13): 4207–13. PMC 552202. PMID 2148288. 
  • Spano F, Raugei G, Palla E et al. (1991). "Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication.". Gene 95 (2): 243–51. doi:10.1016/0378-1119(90)90367-Z. PMID 2174397. 
  • Johnsson N, Johnsson K, Weber K (1988). "A discontinuous epitope on p36, the major substrate of src tyrosine-protein-kinase, brings the phosphorylation site into the neighbourhood of a consensus sequence for Ca2+/lipid-binding proteins.". FEBS Lett. 236 (1): 201–4. doi:10.1016/0014-5793(88)80314-4. PMID 2456953. 
  • Gould KL, Woodgett JR, Isacke CM, Hunter T (1987). "The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo.". Mol. Cell. Biol. 6 (7): 2738–44. PMC 367834. PMID 2946940. 
  • Huebner K, Cannizzaro LA, Frey AZ et al. (1988). "Chromosomal localization of the human genes for lipocortin I and lipocortin II.". Oncogene Res. 2 (4): 299–310. PMID 2969496. 
  • Huang KS, Wallner BP, Mattaliano RJ et al. (1986). "Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase.". Cell 46 (2): 191–9. doi:10.1016/0092-8674(86)90736-1. PMID 3013422. 
  • Buday L, Egan SE, Rodriguez Viciana P et al. (1994). "A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells.". J. Biol. Chem. 269 (12): 9019–23. PMID 7510700. 
  • Chung CY, Erickson HP (1994). "Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.". J. Cell Biol. 126 (2): 539–48. doi:10.1083/jcb.126.2.539. PMC 2200039. PMID 7518469. 
  • Kato S, Sekine S, Oh SW et al. (1995). "Construction of a human full-length cDNA bank.". Gene 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789. 
  • Richard I, Broux O, Chiannilkulchai N et al. (1995). "Regional localization of human chromosome 15 loci.". Genomics 23 (3): 619–27. doi:10.1006/geno.1994.1550. PMID 7851890. 
  • Takahashi S, Reddy SV, Chirgwin JM et al. (1994). "Cloning and identification of annexin II as an autocrine/paracrine factor that increases osteoclast formation and bone resorption.". J. Biol. Chem. 269 (46): 28696–701. PMID 7961821. 
  • Hyatt SL, Liao L, Chapline C, Jaken S (1994). "Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells.". Biochemistry 33 (5): 1223–8. doi:10.1021/bi00171a023. PMID 8110754. 
  • Wright JF, Kurosky A, Wasi S (1994). "An endothelial cell-surface form of annexin II binds human cytomegalovirus.". Biochem. Biophys. Res. Commun. 198 (3): 983–9. doi:10.1006/bbrc.1994.1140. PMID 8117306. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 

External links[edit]