[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/annexin-a2-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/annexin-a2-wikipedia\/","headline":"Annexin A2 – Wikipedia","name":"Annexin A2 – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens ANXA2 Identifiers Aliases ANXA2, ANX2, ANX2L4,","datePublished":"2014-12-02","dateModified":"2014-12-02","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/0\/09\/Protein_ANXA2_PDB_1w7b.png\/250px-Protein_ANXA2_PDB_1w7b.png","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/0\/09\/Protein_ANXA2_PDB_1w7b.png\/250px-Protein_ANXA2_PDB_1w7b.png","height":"163","width":"250"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/annexin-a2-wikipedia\/","wordCount":9432,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensANXA2IdentifiersAliasesANXA2, ANX2, ANX2L4, CAL1H, HEL-S-270, LIP2, LPC2, LPC2D, P36, PAP-IV, annexin A2External IDsOMIM: 151740 MGI: 88246 HomoloGene: 20857 GeneCards: ANXA2 WikidataAnnexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2 gene.[5]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Annexin 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.[6]Table of Contents       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Function[edit]Interactions[edit]See also[edit]References[edit]Further reading[edit]External links[edit]Function[edit]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.[6] Epigenetic regulation of Annexin A2 has been identified as a key determinant of mesenchymal transformation in brain tumors.[7]  Maternal deficiency of the ANXA2 gene contributes to shallow decidual invasion by placental cytotrophoblast cells. These findings highlight the maternal contribution to the pathogenesis of severe preeclampsia.[8]Annexin A2 has been proposed to function inside the cell in sorting of endosomes and outside the cell in anticoagulant reactions.Interactions[edit]Annexin A2 has been shown to interact with Prohibitin,[9]CEACAM1,[10]S100A10,[11][12]PCNA,[13] complement Factor H,[14] and a number of viral factors including the HPV16 minor capsid protein L2.[15][16]See also[edit]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000182718 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032231 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ 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”. The Journal of Biological Chemistry. 269 (46): 28696\u201328701. doi:10.1016\/S0021-9258(19)61961-7. PMID\u00a07961821.^ a b “Entrez Gene: ANXA2 annexin A2”.^ Kling T, Ferrarese R, \u00d3 hAil\u00edn D, Johansson P, Heiland DH, Dai F,  et\u00a0al. (October 2016). “Integrative Modeling Reveals Annexin A2-mediated Epigenetic Control of Mesenchymal Glioblastoma”. EBioMedicine. 12: 72\u201385. doi:10.1016\/j.ebiom.2016.08.050. PMC\u00a05078587. PMID\u00a027667176.^ Ng SW, Norwitz GA, Pavlicev M, Tilburgs T, Sim\u00f3n C, Norwitz ER (June 2020). “Endometrial Decidualization: The Primary Driver of Pregnancy Health”. International Journal of Molecular Sciences. 21 (11): 4092. doi:10.3390\/ijms21114092. PMC\u00a07312091. PMID\u00a032521725.^ Bacher S, Achatz G, Schmitz ML, Lamers MC (December 2002). “Prohibitin and prohibitone are contained in high-molecular weight complexes and interact with alpha-actinin and annexin A2”. Biochimie. 84 (12): 1207\u20131220. doi:10.1016\/S0300-9084(02)00027-5. PMID\u00a012628297.^ Kirshner J, Schumann D, Shively JE (December 2003). “CEACAM1, a cell-cell adhesion molecule, directly associates with annexin II in a three-dimensional model of mammary morphogenesis”. The Journal of Biological Chemistry. 278 (50): 50338\u201350345. doi:10.1074\/jbc.M309115200. PMID\u00a014522961.^ R\u00e9ty S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S,  et\u00a0al. (January 1999). “The crystal structure of a complex of p11 with the annexin II N-terminal peptide”. Nature Structural Biology. 6 (1): 89\u201395. doi:10.1038\/4965. PMID\u00a09886297. S2CID\u00a026400923.^ He KL, Deora AB, Xiong H, Ling Q, Weksler BB, Niesvizky R, Hajjar KA (July 2008). “Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10\/p11”. The Journal of Biological Chemistry. 283 (28): 19192\u201319200. doi:10.1074\/jbc.M800100200. PMC\u00a02443646. PMID\u00a018434302.^ Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (October 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”. The Journal of Biological Chemistry. 277 (43): 40362\u201340367. doi:10.1074\/jbc.M206194200. PMID\u00a012171929.^ Leffler J, Herbert AP, Norstr\u00f6m E, Schmidt CQ, Barlow PN, Blom AM, Martin M (February 2010). “Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells”. The Journal of Biological Chemistry. 285 (6): 3766\u20133776. doi:10.1074\/jbc.M109.045427. PMC\u00a02823518. PMID\u00a019951950.^ Woodham AW, Da Silva DM, Skeate JG, Raff AB, Ambroso MR, Brand HE,  et\u00a0al. (2012). “The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection”. PLOS ONE. 7 (8): e43519. Bibcode:2012PLoSO…743519W. doi:10.1371\/journal.pone.0043519. PMC\u00a03425544. PMID\u00a022927980.^ Woodham AW, Raff AB, Raff LM, Da Silva DM, Yan L, Skeate JG,  et\u00a0al. (May 2014). “Inhibition of Langerhans cell maturation by human papillomavirus type 16: a novel role for the annexin A2 heterotetramer in immune suppression”. Journal of Immunology. 192 (10): 4748\u20134757. doi:10.4049\/jimmunol.1303190. PMC\u00a04019435. PMID\u00a024719459.Further reading[edit]Kwon M, MacLeod TJ, Zhang Y, Waisman DM (January 2005). “S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors”. Frontiers in Bioscience. 10 (1\u20133): 300\u2013325. doi:10.2741\/1529. PMID\u00a015574370.Babiychuk EB, Draeger A (June 2006). “Regulation of ecto-5′-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?”. Biochemical Society Transactions. 34 (Pt 3): 374\u2013376. doi:10.1042\/BST0340374. PMID\u00a016709165.Bohn E, Gerke V, Kresse H, L\u00f6ffler BM, Kunze H (January 1992). “Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase”. FEBS Letters. 296 (3): 237\u2013240. doi:10.1016\/0014-5793(92)80294-Q. PMID\u00a01531641. S2CID\u00a019633878.Dawson SJ, White LA (May 1992). “Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin”. The Journal of Infection. 24 (3): 317\u2013320. doi:10.1016\/S0163-4453(05)80037-4. PMID\u00a01602151.Jindal HK, Chaney WG, Anderson CW, Davis RG, Vishwanatha JK (March 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”. The Journal of Biological Chemistry. 266 (8): 5169\u20135176. doi:10.1016\/S0021-9258(19)67770-7. PMID\u00a01825830.Filipek A, Gerke V, Weber K, Ku\u017anicki J (February 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”. European Journal of Biochemistry. 195 (3): 795\u2013800. doi:10.1111\/j.1432-1033.1991.tb15768.x. PMID\u00a01999197.Becker T, Weber K, Johnsson N (December 1990). “Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11”. The EMBO Journal. 9 (13): 4207\u20134213. doi:10.1002\/j.1460-2075.1990.tb07868.x. PMC\u00a0552202. PMID\u00a02148288.Spano F, Raugei G, Palla E, Colella C, Melli M (November 1990). “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\u2013251. doi:10.1016\/0378-1119(90)90367-Z. PMID\u00a02174397.Johnsson N, Johnsson K, Weber K (August 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 Letters. 236 (1): 201\u2013204. doi:10.1016\/0014-5793(88)80314-4. PMID\u00a02456953.Gould KL, Woodgett JR, Isacke CM, Hunter T (July 1986). “The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo”. Molecular and Cellular Biology. 6 (7): 2738\u20132744. doi:10.1128\/mcb.6.7.2738. PMC\u00a0367834. PMID\u00a02946940.Huebner K, Cannizzaro LA, Frey AZ, Hecht BK, Hecht F, Croce CM, Wallner BP (May 1988). “Chromosomal localization of the human genes for lipocortin I and lipocortin II”. Oncogene Research. 2 (4): 299\u2013310. PMID\u00a02969496.Huang KS, Wallner BP, Mattaliano RJ, Tizard R, Burne C, Frey A,  et\u00a0al. (July 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\u2013199. doi:10.1016\/0092-8674(86)90736-1. PMID\u00a03013422. S2CID\u00a024557024.Buday L, Egan SE, Rodriguez Viciana P, Cantrell DA, Downward J (March 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”. The Journal of Biological Chemistry. 269 (12): 9019\u20139023. doi:10.1016\/S0021-9258(17)37070-9. PMID\u00a07510700.Chung CY, Erickson HP (July 1994). “Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C”. The Journal of Cell Biology. 126 (2): 539\u2013548. doi:10.1083\/jcb.126.2.539. PMC\u00a02200039. PMID\u00a07518469.Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N,  et\u00a0al. (December 1994). “Construction of a human full-length cDNA bank”. Gene. 150 (2): 243\u2013250. doi:10.1016\/0378-1119(94)90433-2. PMID\u00a07821789.Richard I, Broux O, Chiannilkulchai N, Fougerousse F, Allamand V, Bourg N,  et\u00a0al. (October 1994). “Regional localization of human chromosome 15 loci”. Genomics. 23 (3): 619\u2013627. doi:10.1006\/geno.1994.1550. PMID\u00a07851890.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”. The Journal of Biological Chemistry. 269 (46): 28696\u201328701. doi:10.1016\/S0021-9258(19)61961-7. PMID\u00a07961821.Hyatt SL, Liao L, Chapline C, Jaken S (February 1994). “Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells”. Biochemistry. 33 (5): 1223\u20131228. doi:10.1021\/bi00171a023. PMID\u00a08110754.Wright JF, Kurosky A, Wasi S (February 1994). “An endothelial cell-surface form of annexin II binds human cytomegalovirus”. Biochemical and Biophysical Research Communications. 198 (3): 983\u2013989. doi:10.1006\/bbrc.1994.1140. PMID\u00a08117306.Maruyama K, Sugano S (January 1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1\u20132): 171\u2013174. doi:10.1016\/0378-1119(94)90802-8. PMID\u00a08125298.External links[edit]PDB gallery1w7b: ANNEXIN A2: DOES IT INDUCE MEMBRANE AGGREGATION BY A NEW MULTIMERIC STATE OF THE PROTEIN.1xjl: Structure of human annexin A2 in the presence of calcium ions2hyu: Human Annexin A2 with heparin tetrasaccharide bound2hyv: Human Annexin A2 with heparin hexasaccharide bound2hyw: Human Annexin A2 with Calcium bound       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/annexin-a2-wikipedia\/#breadcrumbitem","name":"Annexin A2 – Wikipedia"}}]}]