Annexin A9: Difference between revisions

ANXA9
Identifiers
Aliases	ANXA9, ANX31, annexin A9
External IDs	OMIM: 603319; MGI: 1923711; HomoloGene: 2643; GeneCards: ANXA9; OMA:ANXA9 - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	150,995,634 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	95,214,487 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; right lobe of liver; ; skin of leg; ; skin of abdomen; ; pancreatic ductal cell; ; testicle; ; amniotic fluid; ; C1 segment; ; left lobe of thyroid gland; ; right lobe of thyroid gland;
	Top expressed in
	esophagus; ; lip; ; seminal vesicula; ; skin of back; ; skin of external ear; ; epidermis; ; hair follicle; ; renal pelvis; ; conjunctival fornix; ; vestibular membrane of cochlear duct;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	calcium-dependent phospholipid binding; calcium ion binding; acetylcholine receptor activity; phosphatidylserine binding; protein binding; phospholipid binding; protein homodimerization activity;
Cellular component	cell surface; cytosol;
Biological process	signal transduction; cell-cell adhesion;
	Sources:Amigo / QuickGO
Orthologs
	8416
	71790
	ENSG00000143412
	ENSMUSG00000015702
	O76027
	Q9JHQ0
	NM_003568
	NM_001085383; NM_023628; NM_001379545; NM_001379546
	NP_003559
	NP_001078852; NP_076117; NP_001366474; NP_001366475
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 15:13, 3 December 2023

Annexin A9 is a protein that in humans is encoded by the ANXA9 gene.^[5]^[6]^[7]

Function

The annexins are a family of calcium-dependent phospholipid-binding proteins. Members of the annexin family contain 4 internal repeat domains, each of which includes a type II calcium-binding site. The calcium-binding sites are required for annexins to aggregate and cooperatively bind anionic phospholipids and extracellular matrix proteins. This gene encodes a divergent member of the annexin protein family in which all four homologous type II calcium-binding sites in the conserved tetrad core contain amino acid substitutions that ablate their function. However, structural analysis suggests that the conserved putative ion channel formed by the tetrad core is intact.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000143412 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000015702 – 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.
^ Morgan RO, Fernandez MP (Sep 1998). "Expression profile and structural divergence of novel human annexin 31". FEBS Letters. 434 (3): 300–4. doi:10.1016/S0014-5793(98)00997-1. PMID 9742942. S2CID 13751169.
^ Morgan RO, Bell DW, Testa JR, Fernandez MP (Feb 1999). "Human annexin 31 genetic mapping and origin". Gene. 227 (1): 33–8. doi:10.1016/S0378-1119(98)00597-6. PMID 9931420.
^ ^a ^b "Entrez Gene: ANXA9 annexin A9".

External links

Human ANXA9 genome location and ANXA9 gene details page in the UCSC Genome Browser.

Benz J, Hofmann A (1997). "Annexins: from structure to function". Biological Chemistry. 378 (3–4): 177–83. PMID 9165068.
Nguyen VT, Ndoye A, Grando SA (Sep 2000). "Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine". The Journal of Biological Chemistry. 275 (38): 29466–76. doi:10.1074/jbc.M003174200. PMID 10899159.
Goebeler V, Ruhe D, Gerke V, Rescher U (Jul 2003). "Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca(2+) and lipid binding proteins". FEBS Letters. 546 (2–3): 359–64. doi:10.1016/S0014-5793(03)00634-3. PMID 12832069. S2CID 13433731.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000143412 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000015702 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9742942-5] Morgan RO, Fernandez MP (Sep 1998). "Expression profile and structural divergence of novel human annexin 31". FEBS Letters. 434 (3): 300–4. doi:10.1016/S0014-5793(98)00997-1. PMID 9742942. S2CID 13751169.

[pmid9931420-6] Morgan RO, Bell DW, Testa JR, Fernandez MP (Feb 1999). "Human annexin 31 genetic mapping and origin". Gene. 227 (1): 33–8. doi:10.1016/S0378-1119(98)00597-6. PMID 9931420.

[entrez-7] "Entrez Gene: ANXA9 annexin A9".

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@@ Line 1: / Line 1: @@
+{{Short description|Protein-coding gene in the species Homo sapiens}}
-{{PBB|geneid=8416}}
+{{Infobox_gene}}
-'''Annexin A9''' is a [[protein]] that in humans is encoded by the ''ANXA9'' [[gene]].<ref name="pmid9742942">{{cite journal | author = Morgan RO, Fernandez MP | title = Expression profile and structural divergence of novel human annexin 31 | journal = FEBS Lett | volume = 434 | issue = 3 | pages = 300–4 | year = 1998 | month = Oct | pmid = 9742942 | pmc =  | doi =  }}</ref><ref name="pmid9931420">{{cite journal | author = Morgan RO, Bell DW, Testa JR, Fernandez MP | title = Human annexin 31 genetic mapping and origin | journal = Gene | volume = 227 | issue = 1 | pages = 33–8 | year = 1999 | month = Apr | pmid = 9931420 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ANXA9 annexin A9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8416| accessdate = }}</ref>
+'''Annexin A9''' is a [[protein]] that in humans is encoded by the ''ANXA9'' [[gene]].<ref name="pmid9742942">{{cite journal | vauthors = Morgan RO, Fernandez MP | title = Expression profile and structural divergence of novel human annexin 31 | journal = FEBS Letters | volume = 434 | issue = 3 | pages = 300–4 | date = Sep 1998 | pmid = 9742942 | doi = 10.1016/S0014-5793(98)00997-1 | s2cid = 13751169 | doi-access = free }}</ref><ref name="pmid9931420">{{cite journal | vauthors = Morgan RO, Bell DW, Testa JR, Fernandez MP | title = Human annexin 31 genetic mapping and origin | journal = Gene | volume = 227 | issue = 1 | pages = 33–8 | date = Feb 1999 | pmid = 9931420 | doi = 10.1016/S0378-1119(98)00597-6 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ANXA9 annexin A9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8416}}</ref>
+== Function ==
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| section_title =
-| summary_text = The annexins are a family of calcium-dependent phospholipid-binding proteins. Members of the annexin family contain 4 internal repeat domains, each of which includes a type II calcium-binding site. The calcium-binding sites are required for annexins to aggregate and cooperatively bind anionic phospholipids and extracellular matrix proteins. This gene encodes a divergent member of the annexin protein family in which all four homologous type II calcium-binding sites in the conserved tetrad core contain amino acid substitutions that ablate their function. However, structural analysis suggests that the conserved putative ion channel formed by the tetrad core is intact.<ref name="entrez">{{cite web | title = Entrez Gene: ANXA9 annexin A9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8416| accessdate = }}</ref>
-}}
+The [[annexin]]s are a family of calcium-dependent [[phospholipid]]-binding proteins. Members of the annexin family contain 4 internal repeat domains, each of which includes a type II calcium-binding site. The calcium-binding sites are required for annexins to aggregate and cooperatively bind anionic phospholipids and [[extracellular matrix]] proteins. This gene encodes a divergent member of the annexin protein family in which all four homologous type II calcium-binding sites in the conserved tetrad core contain amino acid substitutions that ablate their function. However, structural analysis suggests that the conserved putative ion channel formed by the tetrad core is intact.<ref name="entrez" />
-==References==
+== References ==
 {{reflist}}
-==Further reading==
+==External links==
+* {{UCSC gene info|ANXA9}}
+== Further reading ==
 {{refbegin | 2}}
+* {{cite journal | vauthors = Benz J, Hofmann A | title = Annexins: from structure to function | journal = Biological Chemistry | volume = 378 | issue = 3–4 | pages = 177–83 | year = 1997 | pmid = 9165068 }}
-{{PBB_Further_reading
+* {{cite journal | vauthors = Nguyen VT, Ndoye A, Grando SA | title = Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine | journal = The Journal of Biological Chemistry | volume = 275 | issue = 38 | pages = 29466–76 | date = Sep 2000 | pmid = 10899159 | doi = 10.1074/jbc.M003174200 | doi-access = free }}
-| citations =
-*{{cite journal  | author=Benz J, Hofmann A |title=Annexins: from structure to function. |journal=Biol. Chem. |volume=378 |issue= 3-4 |pages= 177–83 |year= 1997 |pmid= 9165068 |doi=  }}
+* {{cite journal | vauthors = Goebeler V, Ruhe D, Gerke V, Rescher U | title = Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca(2+) and lipid binding proteins | journal = FEBS Letters | volume = 546 | issue = 2–3 | pages = 359–64 | date = Jul 2003 | pmid = 12832069 | doi = 10.1016/S0014-5793(03)00634-3 | s2cid = 13433731 | doi-access = free }}
+* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 | bibcode = 2004PNAS..10112130B | doi-access = free }}
-*{{cite journal  | author=Nguyen VT, Ndoye A, Grando SA |title=Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29466–76 |year= 2000 |pmid= 10899159 |doi= 10.1074/jbc.M003174200 }}
-*{{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=Goebeler V, Ruhe D, Gerke V, Rescher U |title=Atypical properties displayed by annexin A9, a novel member of the annexin family of Ca(2+) and lipid binding proteins. |journal=FEBS Lett. |volume=546 |issue= 2-3 |pages= 359–64 |year= 2003 |pmid= 12832069 |doi=10.1016/S0014-5793(03)00634-3  }}
-*{{cite journal  | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
-*{{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=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
-}}
 {{refend}}
-{{gene-1-stub}}
+{{gene-1-stub}}
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