Annexin A3

Annexin A3

Annexin A3, also known as ANXA3, is a human gene.cite web | title = Entrez Gene: ANXA3 annexin A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=306| accessdate = ]

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 in the inhibition of phospholipase A2 and cleavage of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. This protein may also play a role in anti-coagulation.cite web | title = Entrez Gene: ANXA3 annexin A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=306| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Tait JF, Frankenberry DA, Miao CH, "et al." |title=Chromosomal localization of the human annexin III (ANX3) gene. |journal=Genomics |volume=10 |issue= 2 |pages= 441–8 |year= 1991 |pmid= 1830024 |doi=
*cite journal | author=Ernst JD, Hoye E, Blackwood RA, Jaye D |title=Purification and characterization of an abundant cytosolic protein from human neutrophils that promotes Ca2(+)-dependent aggregation of isolated specific granules. |journal=J. Clin. Invest. |volume=85 |issue= 4 |pages= 1065–71 |year= 1990 |pmid= 2138632 |doi=
*cite journal | author=Ross TS, Tait JF, Majerus PW |title=Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with lipocortin III. |journal=Science |volume=248 |issue= 4955 |pages= 605–7 |year= 1990 |pmid= 2159184 |doi=
*cite journal | author=Pepinsky RB, Tizard R, Mattaliano RJ, "et al." |title=Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. |journal=J. Biol. Chem. |volume=263 |issue= 22 |pages= 10799–811 |year= 1988 |pmid= 2968983 |doi=
*cite journal | author=Tait JF, Sakata M, McMullen BA, "et al." |title=Placental anticoagulant proteins: isolation and comparative characterization four members of the lipocortin family. |journal=Biochemistry |volume=27 |issue= 17 |pages= 6268–76 |year= 1989 |pmid= 2975506 |doi=
*cite journal | author=Tait JF, Smith C, Xu L, Cookson BT |title=Structure and polymorphisms of the human annexin III (ANX3) gene. |journal=Genomics |volume=18 |issue= 1 |pages= 79–86 |year= 1994 |pmid= 8276419 |doi= 10.1006/geno.1993.1428
*cite journal | author=Sekar MC, Sambandam V, Grizzle WE, McDonald JM |title=Dissociation of cyclic inositol phosphohydrolase activity from annexin III. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8295–9 |year= 1996 |pmid= 8626524 |doi=
*cite journal | author=Favier-Perron B, Lewit-Bentley A, Russo-Marie F |title=The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. |journal=Biochemistry |volume=35 |issue= 6 |pages= 1740–4 |year= 1996 |pmid= 8639653 |doi= 10.1021/bi952092o
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Cargill M, Altshuler D, Ireland J, "et al." |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231–8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290
*cite journal | author=Bödeker H, Keim V, Fiedler F, "et al." |title=PAP I interacts with itself, PAP II, PAP III, and lithostathine/regIalpha. |journal=Mol. Cell Biol. Res. Commun. |volume=2 |issue= 3 |pages= 150–4 |year= 2000 |pmid= 10662590 |doi= 10.1006/mcbr.1999.0166
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gevaert K, Goethals M, Martens L, "et al." |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Bruneel A, Labas V, Mailloux A, "et al." |title=Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. |journal=Proteomics |volume=5 |issue= 15 |pages= 3876–84 |year= 2006 |pmid= 16130169 |doi= 10.1002/pmic.200401239
*cite journal | author=Stelzl U, Worm U, Lalowski M, "et al." |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029
*cite journal | author=Park JE, Lee DH, Lee JA, "et al." |title=Annexin A3 is a potential angiogenic mediator. |journal=Biochem. Biophys. Res. Commun. |volume=337 |issue= 4 |pages= 1283–7 |year= 2005 |pmid= 16236264 |doi= 10.1016/j.bbrc.2005.10.004

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужна курсовая?

Look at other dictionaries:

  • Annexin A5 — (or annexin V) is a cellular protein in the annexin group. The function of the protein is unknown, however annexin A5 has been proposed to play a role in the inhibition of blood coagulation by competing for phosphatidylserine binding sites with… …   Wikipedia

  • Annexin A1 — (or Lipocortin I) is a human protein encoded by the ANXA1 gene. PBB Summary section title = summary text = Annexin I belongs to a family of Ca(2+) dependent phospholipid binding proteins that have a molecular weight of approximately 35,000 to… …   Wikipedia

  • 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… …   Wikipedia

  • Annexin V — is the cause of a syndrome called the antiphospholipid antibody syndrome with abnormal blood clotting. The annexins are a family of proteins first described in 1990. All of the annexin proteins share the property of binding calcium and… …   Medical dictionary

  • Annexin 2 — is a protein shown to be 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… …   Wikipedia

  • Annexin — Pfam box Symbol = Annexin Name = width = 220 caption = Structure of human annexin III. Pfam= PF00191 InterPro= IPR001464 SMART= PROSITE= PDOC00195 SCOP = 2ran TCDB = 1.A.31 OPM family= 43 OPM protein= 1w3w PDB=PDB3|1n00A:14 79 PDB3|1dk5B:15 80… …   Wikipedia

  • Annexin II — Structure cristallographique modélisée de l annexine II Annexine II (autres noms : Annexin II, Annexin A2, Annexin 2, Lipocortin II, Calpactin I heavy chain, Chromobindin 8, p. 36, Placental anticoagulant protein IV). UniProtKB/Swiss… …   Wikipédia en Français

  • Annexin A5 affinity assay — Annexin A5 is a protein that binds in a calcium dependent manner to phosphatidylserine containing membrane surfaces. Cell surface expression of phosphatidylserine during cell deathApoptosis is a form of programmed cell death which is used by the… …   Wikipedia

  • annexin — noun Any of a group of cellular proteins found in all kingdoms (animal, plant and fungi) with the exception of the bacteria …   Wiktionary

  • annexin — an·nex·in (ə nekґsin) any of a family of Ca2+ dependent phospholipid binding proteins, which share a common primary structure in the C terminal region, four or eight repeats of an approximately 70 amino acid sequence. Proposed functions… …   Medical dictionary

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”