Unknown

Dataset Information

0

1H, 13C, and 15N Backbone assignments of the human brain and acute leukemia cytoplasmic (BAALC) protein.

ABSTRACT: The brain and acute leukemia cytoplasmic (BAALC; UniProt entry Q8WXS3) is a 180-residue-long human protein having six known isoforms. BAALC is expressed in either hematopoietic or neuroectodermal cells and its specific function is still to be revealed. However, as a presumably membrane-anchored protein at the cytoplasmic side it is speculated that BAALC exerts its function at the postsynaptic densities of certain neurons and might play a role in developing cytogenetically normal acute myeloid leukemia (CN-AML) when it is highly overexpressed by myeloid or lymphoid progenitor cells. In order to better understand the physiological role of BAALC and to provide the basis for a further molecular characterization of BAALC, we report here the 1H, 13C, and 15N resonance assignments for the backbone nuclei of its longest hematopoietic isoform (isoform 1). In addition, we present a 1HN and 15NH chemical shift comparison of BAALC with its shortest, neuroectodermal isoform (isoform 6) which shows only minor changes in the 1H and 15N chemical shifts.

SUBMITTER: Lang A 

PROVIDER: S-EPMC7462906 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N Backbone assignments of the human brain and acute leukemia cytoplasmic (BAALC) protein.

Lang Andras A   Kumar Amit A   Jirschitzka Jan J   Bordusa Frank F   Ohlenschläger Oliver O   Wiedemann Christoph C  

Biomolecular NMR assignments 20200402 2

The brain and acute leukemia cytoplasmic (BAALC; UniProt entry Q8WXS3) is a 180-residue-long human protein having six known isoforms. BAALC is expressed in either hematopoietic or neuroectodermal cells and its specific function is still to be revealed. However, as a presumably membrane-anchored protein at the cytoplasmic side it is speculated that BAALC exerts its function at the postsynaptic densities of certain neurons and might play a role in developing cytogenetically normal acute myeloid le  ...[more]

Similar Datasets

Unknown <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N backbone chemical shift assignments of SARS-CoV-2 nsp3a.
| S-EPMC7819138 | biostudies-literature
Unknown <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10.
| S-EPMC7648550 | biostudies-literature
Unknown <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone resonance assignments for KPC-2, a class A serine-β-lactamase.
| S-EPMC6440833 | biostudies-literature
Unknown Backbone <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N resonance assignments of deubiquitinase A in non-phosphorylated and phosphorylated forms.
| S-EPMC6424661 | biostudies-literature
Unknown <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein).
| S-EPMC7996116 | biostudies-literature
Unknown <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone chemical shift assignments of m<sup>7</sup>GTP cap-bound Leishmania initiation factor 4E-1.
| S-EPMC7462832 | biostudies-literature
Unknown <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein.
| S-EPMC7711055 | biostudies-literature
Unknown <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7.
| S-EPMC7678775 | biostudies-literature
Unknown <sup>1</sup>H, <sup>15</sup>N, <sup>13</sup>C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-L-methionine and 3,5-dinitrocatechol.
| S-EPMC5343089 | biostudies-literature
Unknown Sequence-specific backbone (1)H, (13)C, and (15)N resonance assignments of human ribonuclease 4.
| S-EPMC4764873 | biostudies-literature