- Annexin A2
Annexin A2 is a
pleiotropic protein , meaning that its function is dependent on place and time in the body.PBB_Summary
section_title =
summary_text = This gene encodes 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. This gene 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.cite web | title = Entrez Gene: ANXA2 annexin A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=302| accessdate = ]Annexin A2 has been proposed to function inside the cell in sorting of
endosomes and outside the cell inanticoagulant reactions.ee also
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Annexin References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Kwon M, MacLeod TJ, Zhang Y, Waisman DM |title=S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors. |journal=Front. Biosci. |volume=10 |issue= |pages= 300–25 |year= 2006 |pmid= 15574370 |doi=
*cite journal | author=Babiychuk EB, Draeger A |title=Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement? |journal=Biochem. Soc. Trans. |volume=34 |issue= Pt 3 |pages= 374–6 |year= 2006 |pmid= 16709165 |doi= 10.1042/BST0340374
*cite journal | author=Bohn E, Gerke V, Kresse H, "et al." |title=Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase. |journal=FEBS Lett. |volume=296 |issue= 3 |pages= 237–40 |year= 1992 |pmid= 1531641 |doi=
*cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=
*cite journal | author=Jindal HK, Chaney WG, Anderson CW, "et al." |title=The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha. |journal=J. Biol. Chem. |volume=266 |issue= 8 |pages= 5169–76 |year= 1991 |pmid= 1825830 |doi=
*cite journal | author=Filipek A, Gerke V, Weber K, Kuźnicki J |title=Characterization of the cell-cycle-regulated protein calcyclin from Ehrlich ascites tumor cells. Identification of two binding proteins obtained by Ca2(+)-dependent affinity chromatography. |journal=Eur. J. Biochem. |volume=195 |issue= 3 |pages= 795–800 |year= 1991 |pmid= 1999197 |doi=
*cite journal | author=Becker T, Weber K, Johnsson N |title=Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11. |journal=EMBO J. |volume=9 |issue= 13 |pages= 4207–13 |year= 1991 |pmid= 2148288 |doi=
*cite journal | author=Spano F, Raugei G, Palla E, "et al." |title=Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication. |journal=Gene |volume=95 |issue= 2 |pages= 243–51 |year= 1991 |pmid= 2174397 |doi=
*cite journal | author=Johnsson N, Johnsson K, Weber K |title=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. |journal=FEBS Lett. |volume=236 |issue= 1 |pages= 201–4 |year= 1988 |pmid= 2456953 |doi=
*cite journal | author=Gould KL, Woodgett JR, Isacke CM, Hunter T |title=The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo. |journal=Mol. Cell. Biol. |volume=6 |issue= 7 |pages= 2738–44 |year= 1987 |pmid= 2946940 |doi=
*cite journal | author=Huebner K, Cannizzaro LA, Frey AZ, "et al." |title=Chromosomal localization of the human genes for lipocortin I and lipocortin II. |journal=Oncogene Res. |volume=2 |issue= 4 |pages= 299–310 |year= 1988 |pmid= 2969496 |doi=
*cite journal | author=Huang KS, Wallner BP, Mattaliano RJ, "et al." |title=Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase. |journal=Cell |volume=46 |issue= 2 |pages= 191–9 |year= 1986 |pmid= 3013422 |doi=
*cite journal | author=Buday L, Egan SE, Rodriguez Viciana P, "et al." |title=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. |journal=J. Biol. Chem. |volume=269 |issue= 12 |pages= 9019–23 |year= 1994 |pmid= 7510700 |doi=
*cite journal | author=Chung CY, Erickson HP |title=Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. |journal=J. Cell Biol. |volume=126 |issue= 2 |pages= 539–48 |year= 1994 |pmid= 7518469 |doi=
*cite journal | author=Kato S, Sekine S, Oh SW, "et al." |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243–50 |year= 1995 |pmid= 7821789 |doi=
*cite journal | author=Richard I, Broux O, Chiannilkulchai N, "et al." |title=Regional localization of human chromosome 15 loci. |journal=Genomics |volume=23 |issue= 3 |pages= 619–27 |year= 1995 |pmid= 7851890 |doi=
*cite journal | author=Takahashi S, Reddy SV, Chirgwin JM, "et al." |title=Cloning and identification of annexin II as an autocrine/paracrine factor that increases osteoclast formation and bone resorption. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 28696–701 |year= 1994 |pmid= 7961821 |doi=
*cite journal | author=Hyatt SL, Liao L, Chapline C, Jaken S |title=Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells. |journal=Biochemistry |volume=33 |issue= 5 |pages= 1223–8 |year= 1994 |pmid= 8110754 |doi=
*cite journal | author=Wright JF, Kurosky A, Wasi S |title=An endothelial cell-surface form of annexin II binds human cytomegalovirus. |journal=Biochem. Biophys. Res. Commun. |volume=198 |issue= 3 |pages= 983–9 |year= 1994 |pmid= 8117306 |doi= 10.1006/bbrc.1994.1140
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=External links
*MeshName|Annexin+A2
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