Annexin A11

Annexin A11 is a protein that in humans is encoded by the ANXA11 gene.[5][6][7]

ANXA11
Identifiers
Aliases	ANXA11, ANX11, CAP50, annexin A11, CAP-50, ALS23
External IDs	OMIM: 602572 MGI: 108481 HomoloGene: 22759 GeneCards: ANXA11
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10q22.3 Start 80,150,889 bp[1] End 80,205,572 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14 A3|14 15.06 cM Start 25,842,156 bp[2] End 25,886,804 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium ion binding • S100 protein binding • calcium-dependent protein binding • phosphatidylethanolamine binding • GO:0001948 protein binding • MHC class II protein complex binding • calcium-dependent phospholipid binding • RNA binding Cellular component • cytoplasm • nuclear envelope • membrane • melanosome • spindle • nucleoplasm • midbody • azurophil granule • specific granule • phagocytic vesicle • extracellular exosome • cytoskeleton • cell nucleus • cytosol • collagen-containing extracellular matrix Biological process • cell division • response to calcium ion • phagocytosis • cell cycle • cytokinetic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	311	11744
Ensembl	ENSG00000122359	ENSMUSG00000021866
UniProt	P50995	P97384
RefSeq (mRNA)	NM_001157 NM_001278407 NM_001278408 NM_001278409 NM_145868 NM_145869	NM_013469
RefSeq (protein)	NP_001148 NP_001265336 NP_001265337 NP_001265338 NP_665875 NP_665876	NP_038497
Location (UCSC)	Chr 10: 80.15 – 80.21 Mb	Chr 14: 25.84 – 25.89 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of the annexin family, a group of calcium-dependent phospholipid-binding proteins. Annexins have unique N-terminal domains and conserved C-terminal domains, which contain the calcium-dependent phospholipid-binding sites. The encoded protein is a 56-kD antigen recognized by sera from patients with various autoimmune diseases. Transcript variants encoding the same isoform have been identified.[7]

Interactions

ANXA11 has been shown to interact with PDCD6[8] and ALG2.[9]

Clinical significance

It is shown that over-expression of the ANXA11 is involved in apoptotic alterations in schizophrenia and contribute to pathomechanisms of this disorder.[10]

References

1. GRCh38: Ensembl release 89: ENSG00000122359 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021866 - 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.
5. Misaki Y, Pruijn GJ, van der Kemp AW, van Venrooij WJ (Feb 1994). "The 56K autoantigen is identical to human annexin XI". The Journal of Biological Chemistry. 269 (6): 4240–6. PMID 7508441.
6. Morgan RO, Bell DW, Testa JR, Fernandez MP (Feb 1998). "Genomic locations of ANX11 and ANX13 and the evolutionary genetics of human annexins". Genomics. 48 (1): 100–10. doi:10.1006/geno.1997.5148. PMID 9503022.
7. "Entrez Gene: ANXA11 annexin A11".
8. Satoh H, Shibata H, Nakano Y, Kitaura Y, Maki M (Mar 2002). "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner". Biochemical and Biophysical Research Communications. 291 (5): 1166–72. doi:10.1006/bbrc.2002.6600. PMID 11883939.
9. Satoh H, Nakano Y, Shibata H, Maki M (Nov 2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460.
10. Ghazaryan H (Jul 2013). "Annexin 11 expression pattern in schizophrenia". Electronic Journal of Natural Sciences. 21 (2): 74–76.

External links

• Human ANXA11 genome location and ANXA11 gene details page in the UCSC Genome Browser.

Further reading

• Minami H, Tokumitsu H, Mizutani A, Watanabe Y, Watanabe M, Hidaka H (Jul 1992). "Specific binding of CAP-50 to calcyclin". FEBS Letters. 305 (3): 217–9. doi:10.1016/0014-5793(92)80671-3. PMID 1299619.
• Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Sjölin C, Dahlgren C (Jun 1996). "Isolation by calcium-dependent translation to neutrophil-specific granules of a 42-kD cytosolic protein, identified as being a fragment of annexin XI". Blood. 87 (11): 4817–23. doi:10.1182/blood.V87.11.4817.bloodjournal87114817. PMID 8639854.
• Brownawell AM, Creutz CE (Aug 1997). "Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII)". The Journal of Biological Chemistry. 272 (35): 22182–90. doi:10.1074/jbc.272.35.22182. PMID 9268363.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Sudo T, Hidaka H (Feb 1999). "Characterization of the calcyclin (S100A6) binding site of annexin XI-A by site-directed mutagenesis". FEBS Letters. 444 (1): 11–4. doi:10.1016/S0014-5793(99)00014-9. PMID 10037139.
• Bances P, Fernandez MR, Rodriguez-Garcia MI, Morgan RO, Fernandez MP (Oct 2000). "Annexin A11 (ANXA11) gene structure as the progenitor of paralogous annexins and source of orthologous cDNA isoforms". Genomics. 69 (1): 95–103. doi:10.1006/geno.2000.6309. PMID 11013079.
• Satoh H, Shibata H, Nakano Y, Kitaura Y, Maki M (Mar 2002). "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner". Biochemical and Biophysical Research Communications. 291 (5): 1166–72. doi:10.1006/bbrc.2002.6600. PMID 11883939.
• Satoh H, Nakano Y, Shibata H, Maki M (Nov 2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460.
• Breen EC, Tang K (Mar 2003). "Calcyclin (S100A6) regulates pulmonary fibroblast proliferation, morphology, and cytoskeletal organization in vitro". Journal of Cellular Biochemistry. 88 (4): 848–54. doi:10.1002/jcb.10398. PMID 12577318.
• Tomas A, Moss SE (May 2003). "Calcium- and cell cycle-dependent association of annexin 11 with the nuclear envelope". The Journal of Biological Chemistry. 278 (22): 20210–6. doi:10.1074/jbc.M212669200. PMID 12601007.
• Farnaes L, Ditzel HJ (Aug 2003). "Dissecting the cellular functions of annexin XI using recombinant human annexin XI-specific autoantibodies cloned by phage display". The Journal of Biological Chemistry. 278 (35): 33120–6. doi:10.1074/jbc.M210852200. PMID 12805373.
• Tomas A, Futter C, Moss SE (Jun 2004). "Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis". The Journal of Cell Biology. 165 (6): 813–22. doi:10.1083/jcb.200311054. PMC 2172404. PMID 15197175.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.