BCL2-related protein A1

BCL2A1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2VM6, 3I1H, 3MQP, 4ZEQ

Identifiers

Aliases

BCL2A1, ACC-1, ACC-2, ACC1, ACC2, BCL2L5, BFL1, GRS, HBPA1, BCL2 related protein A1

External IDs

OMIM: 601056 MGI: 1278325 HomoloGene: 2988 GeneCards: BCL2A1

Gene location (Human)

Chr.	Chromosome 15 (human)^[1]

Band	15q25.1	Start	79,960,892 bp^[1]
Band	15q25.1	End	79,971,196 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 9 (mouse)^[2]

Band	9\|9 E3.1	Start	88,605,338 bp^[2]
Band	9\|9 E3.1	End	88,613,967 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

periodontal fiber

monocyte

bone marrow

right lung

bone marrow cells

spleen

appendix

upper lobe of left lung

blood

lymph node

Top expressed in

membranous bone

human mandible

spleen

maxilla

thymus

right lung

left lung

ileum

jejunum

pancreas

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding channel activity protein homodimerization activity protein heterodimerization activity BH domain binding
Cellular component	cytoplasm mitochondrial outer membrane
Biological process	apoptotic process regulation of apoptotic process negative regulation of apoptotic process release of cytochrome c from mitochondria mitochondrial fusion intrinsic apoptotic signaling pathway in response to DNA damage positive regulation of apoptotic process transmembrane transport extrinsic apoptotic signaling pathway in absence of ligand human ageing cerebral cortex development negative regulation of intrinsic apoptotic signaling pathway
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


597


12047

Ensembl


ENSG00000140379


ENSMUSG00000099974

UniProt


Q16548


O55179

RefSeq (mRNA)


NM_004049 NM_001114735


NM_007536

RefSeq (protein)


NP_001108207 NP_004040


NP_031562

Location (UCSC)

Chr 15: 79.96 – 79.97 Mb

Chr 9: 88.61 – 88.61 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Bcl-2-related protein A1 is a protein in humans which is encoded by the BCL2A1 gene.^[5]^[6]^[7]

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Transcription

Function

This gene encodes a member of the bcl2 protein family. The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators that are involved in a wide variety of cellular activities such as embryonic development, homeostasis, and tumorigenesis. The protein encoded by this gene can reduce the release of pro-apoptotic cytochrome c from mitochondria and block caspase activation. This gene is a direct transcription target of NF-kappa B in response to inflammatory mediators and is up-regulated by different extracellular signals, such as granulocyte-macrophage colony-stimulating factor (GM-CSF), CD40, phorbol ester, and inflammatory cytokine TNF and IL-1, which suggests a cytoprotective function that is essential for lymphocyte activation as well as cell survival.^[7]

In melanocytic cells BCL2A1 gene expression may be regulated by MITF.^[8]

Interactions

BCL2-related protein A1 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000140379 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000099974 – 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.
^ Savitsky K, Sfez S, Tagle DA, Ziv Y, Sartiel A, Collins FS, Shiloh Y, Rotman G (March 1996). "The complete sequence of the coding region of the ATM gene reveals similarity to cell cycle regulators in different species". Hum Mol Genet. 4 (11): 2025–32. doi:10.1093/hmg/4.11.2025. PMID 8589678.
^ Akatsuka Y, Nishida T, Kondo E, Miyazaki M, Taji H, Iida H, Tsujimura K, Yazaki M, Naoe T, Morishima Y, Kodera Y, Kuzushima K, Takahashi T (June 2003). "Identification of a polymorphic gene, BCL2A1, encoding two novel hematopoietic lineage-specific minor histocompatibility antigens". J Exp Med. 197 (11): 1489–500. doi:10.1084/jem.20021925. PMC 2193899. PMID 12771180.
^ ^a ^b "Entrez Gene: BCL2A1 BCL2-related protein A1".
^ Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
^ Sedlak TW, Oltvai ZN, Yang E, Wang K, Boise LH, Thompson CB, Korsmeyer SJ (Aug 15, 1995). "Multiple Bcl-2 family members demonstrate selective dimerizations with Bax". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7834–8. Bibcode:1995PNAS...92.7834S. doi:10.1073/pnas.92.17.7834. PMC 41240. PMID 7644501.
^ Zhang H, Cowan-Jacob SW, Simonen M, Greenhalf W, Heim J, Meyhack B (2000). "Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells". J. Biol. Chem. 275 (15): 11092–9. doi:10.1074/jbc.275.15.11092. PMID 10753914.
^ Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ (2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30. doi:10.1023/A:1011319901057. PMID 11483855. S2CID 23119757.
^ Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.

External links

Human BCL2A1 genome location and BCL2A1 gene details page in the UCSC Genome Browser.

Choi SS, Park IC, Yun JW, et al. (1995). "A novel Bcl-2 related gene, Bfl-1, is overexpressed in stomach cancer and preferentially expressed in bone marrow". Oncogene. 11 (9): 1693–8. PMID 7478596.
Lin EY, Orlofsky A, Berger MS, Prystowsky MB (1993). "Characterization of A1, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2". J. Immunol. 151 (4): 1979–88. doi:10.4049/jimmunol.151.4.1979. PMID 8345191. S2CID 22930599.
Karsan A, Yee E, Kaushansky K, Harlan JM (1996). "Cloning of human Bcl-2 homologue: inflammatory cytokines induce human A1 in cultured endothelial cells". Blood. 87 (8): 3089–96. doi:10.1182/blood.V87.8.3089.bloodjournal8783089. PMID 8605321.
Karsan A, Yee E, Harlan JM (1996). "Endothelial cell death induced by tumor necrosis factor-alpha is inhibited by the Bcl-2 family member, A1". J. Biol. Chem. 271 (44): 27201–4. doi:10.1074/jbc.271.44.27201. PMID 8910286.
Carrió R, López-Hoyos M, Jimeno J, et al. (1997). "A1 demonstrates restricted tissue distribution during embryonic development and functions to protect against cell death". Am. J. Pathol. 149 (6): 2133–42. PMC 1865360. PMID 8952545.
Kenny JJ, Knobloch TJ, Augustus M, et al. (1997). "GRS, a novel member of the Bcl-2 gene family, is highly expressed in multiple cancer cell lines and in normal leukocytes". Oncogene. 14 (8): 997–1001. doi:10.1038/sj.onc.1200898. PMID 9050999. S2CID 365249.
Choi SS, Park SH, Kim UJ, Shin HS (1997). "Bfl-1, a Bcl-2-related gene, is the human homolog of the murine A1, and maps to chromosome 15q24.3". Mamm. Genome. 8 (10): 781–2. doi:10.1007/s003359900567. PMID 9321477. S2CID 8472273.
Hsu SY, Kaipia A, McGee E, et al. (1997). "Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members". Proc. Natl. Acad. Sci. U.S.A. 94 (23): 12401–6. Bibcode:1997PNAS...9412401H. doi:10.1073/pnas.94.23.12401. PMC 24966. PMID 9356461.
Takemoto Y, Furuta M, Sato M, et al. (1998). "Growth factor receptor-bound protein 2 (Grb2) association with hemopoietic specific protein 1: linkage between Lck and Grb2". J. Immunol. 161 (2): 625–30. doi:10.4049/jimmunol.161.2.625. PMID 9670936. S2CID 11576096.
Zong WX, Edelstein LC, Chen C, et al. (1999). "The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis". Genes Dev. 13 (4): 382–7. doi:10.1101/gad.13.4.382. PMC 316475. PMID 10049353.
Holmgreen SP, Huang DC, Adams JM, Cory S (1999). "Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members". Cell Death Differ. 6 (6): 525–32. doi:10.1038/sj.cdd.4400519. PMID 10381646.
Lee HH, Dadgostar H, Cheng Q, et al. (1999). "NF-kappaB-mediated up-regulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signaling in B lymphocytes". Proc. Natl. Acad. Sci. U.S.A. 96 (16): 9136–41. Bibcode:1999PNAS...96.9136L. doi:10.1073/pnas.96.16.9136. PMC 17745. PMID 10430908.
Wang CY, Guttridge DC, Mayo MW, Baldwin AS (1999). "NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis". Mol. Cell. Biol. 19 (9): 5923–9. doi:10.1128/MCB.19.9.5923. PMC 84448. PMID 10454539.
Tomayko MM, Punt JA, Bolcavage JM, et al. (1999). "Expression of the Bcl-2 family member A1 is developmentally regulated in T cells". Int. Immunol. 11 (11): 1753–61. doi:10.1093/intimm/11.11.1753. PMID 10545479.
Zhang H, Cowan-Jacob SW, Simonen M, et al. (2000). "Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells". J. Biol. Chem. 275 (15): 11092–9. doi:10.1074/jbc.275.15.11092. PMID 10753914.
Duriez PJ, Wong F, Dorovini-Zis K, et al. (2000). "A1 functions at the mitochondria to delay endothelial apoptosis in response to tumor necrosis factor". J. Biol. Chem. 275 (24): 18099–107. doi:10.1074/jbc.M908925199. PMID 10849436.
Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. doi:10.1038/88107. PMID 11329013. S2CID 25064683.
Bae J, Hsu SY, Leo CP, et al. (2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30. doi:10.1023/A:1011319901057. PMID 11483855. S2CID 23119757.
Akari H, Bour S, Kao S, et al. (2001). "The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factors". J. Exp. Med. 194 (9): 1299–311. doi:10.1084/jem.194.9.1299. PMC 2195969. PMID 11696595.

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This page was last edited on 23 December 2023, at 15:45

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