![Fig. 2. BAL predicted aa sequence and homologies to additional proteins. / (A) BAL predicted aa sequence. The predicted initiation methionine, which is bolded, is surrounded by a classic Kozak consensus sequence. The BAL aa sequence (aa 17-51), which is included in the minor (BALLong[L]) form and is spliced out of the major (BALs) form, is underlined. A single proline-rich putative SH3 binding site is also indicated (aa 781-786). (B) Schematic representation of BAL cDNA and aa sequence. The BAL N-terminal region contains a duplicated domain of unknown function(http://pfam.wustl.edu; BAL aa 160-288 [22% identity, 42% homology, PSI-BLAST] and aa 319-485 [26% identity, 48% homology, PSI-BLAST]) which is found in the nonhistone region of histone macroH2A.17 Secondary structure analysis of the proximal C-terminal region of BAL predicts an alpha-helical region. The distal BAL C-terminus also has limited partial homology with the C-terminal region of the recently described TRF-1 interacting ankrin repeat ADP-ribose polymerase (Tankyrase)33 and a related hypothetical protein, AL 080156 (BAL aa 667-820, 27% identity, 48% homology [with AL080156], PSI-BLAST). Although the Tankyrase C-terminus encodes a poly ADP-ribose polymerase (PARP) domain, several amino acid residues required for PARP activity33 are not conserved in the BAL C-terminal sequence and BAL lacks PARP activity (data not shown). (C) Predicted BAL secondary structure and partial homology with KIAA1268. The predicted BAL C-terminal alpha-helical region includes 2 putative short coiled-coil domains (BAL aa 586-617 and aa 746-758) with 4-heptad (BAL aa 586-617) and 2-heptad (BAL aa 746-758) repeats. The BAL aa sequence also displays extended partial homology with a recently described human protein of unknown function, KIAA126821 (BAL aa 85-487, 31% identity, 50% homology and BAL aa 160-616, 25% identity, 46% homology, PSI-BLAST). Whereas BAL contains a duplicated N-terminal domain homologous to the nonhistone region of histone macroH2A, the KIAA1268 N-terminus contains 3 repeats of this region. The KIAA1268 C-terminus is also predicted to include an unrelated alpha-helical region with 2 short coiled-coils. (D) Alignment of homologous N-terminal domains of BAL, KIAA1268, and the nonhistone region of histone macroH2A. Identical residues are shown in black and similar residues are shown in gray.](https://ash.silverchair-cdn.com/ash/content_public/journal/blood/96/13/10.1182_blood.v96.13.4328/5/h82400510002.jpeg?Expires=1726826057&Signature=HBS6RTYnmoQVeIajAj8E9v2aC2T0SSYgFG0J9ucGpJkBEYMgbE0yo8vUfnSxi1K~qOluemZ1xUpAi4bvH96Wu4DNP~OolHxT~2gCPHrjGGDzWqhaxd0CP-B4LUm7nQxK8nbh9hq-Oq61qkujEEVlhH6GYF7sW5gwRvtrSI5AD95H~dFRKgfPAfCbhGmZuX3OcNE3-qkTZCPQCq4JCulQy7uBZRXO8q0DItdFS9fjYoEGToEyPkBoBrfgYRwfBA9bTaEHEWzQbMf7z0Bd2Ak2jY3EaB9TBT~2slUy8X8Oe0GJ4Sruz0XbmIFH2igEanmi9EnMQzVibs7SjUF9xNdYRQ__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA)
BAL predicted aa sequence and homologies to additional proteins.
(A) BAL predicted aa sequence. The predicted initiation methionine, which is bolded, is surrounded by a classic Kozak consensus sequence. The BAL aa sequence (aa 17-51), which is included in the minor (BALLong[L]) form and is spliced out of the major (BALs) form, is underlined. A single proline-rich putative SH3 binding site is also indicated (aa 781-786). (B) Schematic representation of BAL cDNA and aa sequence. The BAL N-terminal region contains a duplicated domain of unknown function(http://pfam.wustl.edu; BAL aa 160-288 [22% identity, 42% homology, PSI-BLAST] and aa 319-485 [26% identity, 48% homology, PSI-BLAST]) which is found in the nonhistone region of histone macroH2A.17 Secondary structure analysis of the proximal C-terminal region of BAL predicts an alpha-helical region. The distal BAL C-terminus also has limited partial homology with the C-terminal region of the recently described TRF-1 interacting ankrin repeat ADP-ribose polymerase (Tankyrase)33 and a related hypothetical protein, AL 080156 (BAL aa 667-820, 27% identity, 48% homology [with AL080156], PSI-BLAST). Although the Tankyrase C-terminus encodes a poly ADP-ribose polymerase (PARP) domain, several amino acid residues required for PARP activity33 are not conserved in the BAL C-terminal sequence and BAL lacks PARP activity (data not shown). (C) Predicted BAL secondary structure and partial homology with KIAA1268. The predicted BAL C-terminal alpha-helical region includes 2 putative short coiled-coil domains (BAL aa 586-617 and aa 746-758) with 4-heptad (BAL aa 586-617) and 2-heptad (BAL aa 746-758) repeats. The BAL aa sequence also displays extended partial homology with a recently described human protein of unknown function, KIAA126821 (BAL aa 85-487, 31% identity, 50% homology and BAL aa 160-616, 25% identity, 46% homology, PSI-BLAST). Whereas BAL contains a duplicated N-terminal domain homologous to the nonhistone region of histone macroH2A, the KIAA1268 N-terminus contains 3 repeats of this region. The KIAA1268 C-terminus is also predicted to include an unrelated alpha-helical region with 2 short coiled-coils. (D) Alignment of homologous N-terminal domains of BAL, KIAA1268, and the nonhistone region of histone macroH2A. Identical residues are shown in black and similar residues are shown in gray.
