Barrier-to-autointegration factor (BANF1)
The protein contains 89 amino acids for an estimated molecular weight of 10059 Da.
Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging.', '(Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.', '(Microbial infection) In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication. (updated: Jan. 31, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| NGPS |
Biological Process
Chromosome condensation
Chromosome segregation
DNA integration
Establishment of integrated proviral latency
Mitotic cell cycle
Mitotic nuclear membrane disassembly
Mitotic nuclear membrane reassembly
Negative regulation of viral genome replication
Nuclear transport
Response to virus
Viral process
Cellular Component
Chromosome
Condensed chromosome
Cytoplasm
Cytosol
Extracellular exosome
Nuclear envelope
Nucleoplasm
Nucleus
The reference OMIM entry for this protein is 603811
Barrier-to-autointegration factor 1; banf1
Barrier-to-autointegration factor; baf
CLONING
Lee and Craigie (1998) purified a host cell protein, which they termed BAF, that protects viral DNA from autointegration (integration into itself, rather than into the host genome). By sequence analysis and RACE using mRNA from NIH 3T3 fibroblasts, the authors obtained a full-length cDNA encoding BAF. The deduced 89-amino acid BAF protein has a calculated molecular mass of 10.1 kD and likely exists as a dimer. Expression of the BAF gene resulted in a protein that was active in an autointegration barrier assay.BIOCHEMICAL FEATURES
- Crystal Structure Umland et al. (2000) determined the crystal structure of homodimeric BAF to 1.9-angstrom resolution. They identified a helix-hairpin-helix motif that mediates nonspecific DNA binding. Binding occurs through interactions between amide groups of the peptide chain and phosphate groups of the DNA backbone.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the BANF1 gene to chromosome 11 (TMAP WI-8432). Lynch et al. (1998) mapped a BANF1 pseudogene, which they called BCRP1, to chromosome 14q24.1-q24.2 (see BCRP2; 603812).GENE FUNCTION
Zheng et al. (2000) demonstrated that BAF can bridge double-stranded DNA into a highly ordered nucleoprotein complex. Whereas BAF alone was a dimer in solution, upon binding DNA, BAF formed a dodecamer with DNA bound at multiple discrete sites in the complex. The interactions between BAF and DNA were entirely nonspecific with respect to DNA sequence. By RNA interference, Zheng et al. (2000) demonstrated a role of BAF in mitosis in C. elegans. Embryo development in worms injected with double-stranded BAF RNA arrested at an early stage, and chromosomes showed a defect in chromatin segregation during mitosis. Lee et al. (2001) determined that BAF binds the N-terminal LEM domain of emerin (300384). Haraguchi et al. (2001) visualized colocalization between emerin and BAF at the 'core' region of chromosomes during telophase in HeLa cells. An emerin mutant defective in BAF binding in vitro failed to localize at the core in vivo and subsequently failed to localize at the reformed nuclear envelope. In HeLa cells expressing a BAF mutant that did not show core localization, endogenous emerin failed to localize at the core region during telophase and did not assemble into the nuclear envelope during the subsequent interphase. This BAF mutant also dominantly dislocalized LAP2-beta (188380) and lamin A (150330) from the nuclear envelope. Haraguchi et al. (2001) concluded that BAF is required for the assembly of emerin and A-type lamins at the reforming nuclear envelope during telophase and may mediate their stability in the subsequent interphase. Jacque and Stevenson (2006) examined susceptibility of primary macrophages to human immunodeficiency virus (HIV)-1 infection following short interfering RNA (siRNA)-mediated silencing of nuclear lamins and several lamin-associated proteins. They found that silencing of emerin and BAF prevented infection with HIV-1, but not murine leukemia virus, by preventing integration of the virus into host DNA. Chromatin immunoprecipitation analysis identified emerin and BAF as cooperative cofactors of HIV-1, and mutation analysis showed that viral cDNA did not associate with BAF defective in emerin binding or with emerin lacking the LEM domain. Jacque and Stevenson (2006) concluded that HIV-1 cDNA, upon entering the nucleus, must interact with emerin to contact chromatin, and t ... More on the omim web site
Feb. 5, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603811 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed