Annexin A3: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Annexin A3''' is a [[protein]] that in humans is encoded by the ''ANXA3'' [[gene]].<ref name="pmid1830024">{{cite journal |vauthors=Tait JF, Frankenberry DA, Miao CH, Killary AM, Adler DA, Disteche CM | title = Chromosomal localization of the human annexin III (ANX3) gene | journal = Genomics | volume = 10 | issue = 2 | pages = 441–8 |date=Aug 1991 | pmid = 1830024 | pmc =  | doi =10.1016/0888-7543(91)90330-H  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ANXA3 annexin A3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=306| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
It is abnormally expressed in fetuses of both [[in vitro fertilization|IVF]] and [[intracytoplasmic sperm injection|ICSI]], which may contribute to the increase risk of birth defects in these [[assisted reproductive technology|ART]].<ref name=zhang>{{cite journal |vauthors=Zhang Y, Zhang YL, Feng C |title=Comparative proteomic analysis of human placenta derived from assisted reproductive technology |journal=Proteomics |volume= 8|issue= 20|pages= 4344–56|date=September 2008 |pmid=18792929 |doi=10.1002/pmic.200800294 |url=|display-authors=etal}}</ref>
{{GNF_Protein_box
| image = PBB_Protein_ANXA3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aii.
| PDB = {{PDB2|1aii}}, {{PDB2|1axn}}
| Name = Annexin A3
| HGNCid = 541
| Symbol = ANXA3
| AltSymbols =; ANX3
| OMIM = 106490
| ECnumber =
| Homologene = 68445
| MGIid = 1201378
| GeneAtlas_image1 = PBB_GE_ANXA3_209369_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005544 |text = calcium-dependent phospholipid binding}} {{GNF_GO|id=GO:0008486 |text = diphosphoinositol-polyphosphate diphosphatase activity}} {{GNF_GO|id=GO:0019834 |text = phospholipase A2 inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 306
    | Hs_Ensembl = ENSG00000138772
    | Hs_RefseqProtein = NP_005130
    | Hs_RefseqmRNA = NM_005139
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 79694613
    | Hs_GenLoc_end = 79750606
    | Hs_Uniprot = P12429
    | Mm_EntrezGene = 11745
    | Mm_Ensembl = ENSMUSG00000029484
    | Mm_RefseqmRNA = XM_977289
    | Mm_RefseqProtein = XP_982383
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 97042796
    | Mm_GenLoc_end = 97086270
    | Mm_Uniprot = Q3TFK4
  }}
}}
'''Annexin A3''', also known as '''ANXA3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ANXA3 annexin A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=306| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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 phopholipase A2 and cleavage of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. This protein may also play a role in anti-coagulation.<ref name="entrez">{{cite web | title = Entrez Gene: ANXA3 annexin A3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=306| accessdate = }}</ref>
| 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.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ANXA3}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| 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  |vauthors=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=10.1172/JCI114537  | pmc=296536 }}
*{{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  |vauthors=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=10.1126/science.2159184 }}
*{{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  |vauthors=Pepinsky RB, Tizard R, Mattaliano RJ |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=  |display-authors=etal}}
*{{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  |vauthors=Tait JF, Sakata M, McMullen BA |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=10.1021/bi00417a011 |display-authors=etal}}
*{{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  |vauthors=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=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  |vauthors=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=10.1074/jbc.271.14.8295 }}
*{{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  |vauthors=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=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  |vauthors=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=10.1101/gr.6.9.791 }}
*{{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  |vauthors=Cargill M, Altshuler D, Ireland J |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 |display-authors=etal}}
*{{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  |vauthors=Bödeker H, Keim V, Fiedler F |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 |display-authors=etal}}
*{{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  |vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |display-authors=etal}}
*{{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  |vauthors=Gevaert K, Goethals M, Martens L |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 |display-authors=etal}}
*{{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  |vauthors=Gerhard DS, Wagner L, Feingold EA |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 | pmc=528928 |display-authors=etal}}
*{{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  |vauthors=Bruneel A, Labas V, Mailloux A |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 |display-authors=etal}}
*{{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  |vauthors=Stelzl U, Worm U, Lalowski M |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 |display-authors=etal}}
*{{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  |vauthors=Park JE, Lee DH, Lee JA |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 |display-authors=etal}}
*{{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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=306}}
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{{protein-stub}}
{{gene-4-stub}}

Latest revision as of 23:47, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Annexin A3 is a protein that in humans is encoded by the ANXA3 gene.[1][2]

It is abnormally expressed in fetuses of both IVF and ICSI, which may contribute to the increase risk of birth defects in these ART.[3]

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.[2]

References

  1. ↑ Tait JF, Frankenberry DA, Miao CH, Killary AM, Adler DA, Disteche CM (Aug 1991). "Chromosomal localization of the human annexin III (ANX3) gene". Genomics. 10 (2): 441–8. doi:10.1016/0888-7543(91)90330-H. PMID 1830024.
  2. ↑ 2.0 2.1 "Entrez Gene: ANXA3 annexin A3".
  3. ↑ Zhang Y, Zhang YL, Feng C, et al. (September 2008). "Comparative proteomic analysis of human placenta derived from assisted reproductive technology". Proteomics. 8 (20): 4344–56. doi:10.1002/pmic.200800294. PMID 18792929.

External links

Further reading



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