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:
60.35 – 60.4 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. 

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