Aebp2

Rattus norvegicus

Predicted to enable transcription coregulator activity. Predicted to be involved in negative regulation of transcription by RNA polymerase II. Predicted to act upstream of or within regulation of DNA-templated transcription. Predicted to be located in nucleoplasm. Predicted to be part of ESC/E(Z) complex. Orthologous to human AEBP2 (AE binding protein 2); PARTICIPATES IN histone modification pathway; INTERACTS WITH 2,3,7,8-tetrachlorodibenzodioxine; 2,4-dinitrotoluene; 3,3',5,5'-tetrabromobisphenol A.

Aebp1

Rattus norvegicus

Predicted to enable several functions, including DNA-binding transcription repressor activity, RNA polymerase II-specific; collagen binding activity; and metallocarboxypeptidase activity. Predicted to be involved in several processes, including negative regulation of transcription by RNA polymerase II; protein processing; and regulation of collagen fibril organization. Predicted to be located in extracellular region. Predicted to be active in extracellular space. Human ortholog(s) of this gene implicated in Ehlers-Danlos syndrome classic-like 2. Orthologous to human AEBP1 (AE binding protein 1); INTERACTS WITH 1,2-dimethylhydrazine; 17alpha-ethynylestradiol; 17beta-estradiol.

Slc4a1

Homo sapiens

The protein encoded by this gene is part of the anion exchanger (AE) family and is expressed in the erythrocyte plasma membrane, where it functions as a chloride/bicarbonate exchanger involved in carbon dioxide transport from tissues to lungs. The protein comprises two domains that are structurally and functionally distinct. The N-terminal 40kDa domain is located in the cytoplasm and acts as an attachment site for the red cell skeleton by binding ankyrin. The glycosylated C-terminal membrane-associated domain contains 12-14 membrane spanning segments and carries out the stilbene disulphonate-sensitive exchange transport of anions. The cytoplasmic tail at the extreme C-terminus of the membrane domain binds carbonic anhydrase II. The encoded protein associates with the red cell membrane protein glycophorin A and this association promotes the correct folding and translocation of the exchanger. This protein is predominantly dimeric but forms tetramers in the presence of ankyrin. Many mutations in this gene are known in man, and these mutations can lead to two types of disease: destabilization of red cell membrane leading to hereditary spherocytosis, and defective kidney acid secretion leading to distal renal tubular acidosis. Other mutations that do not give rise to disease result in novel blood group antigens, which form the Diego blood group system. Southeast Asian ovalocytosis (SAO, Melanesian ovalocytosis) results from the heterozygous presence of a deletion in the encoded protein and is common in areas where Plasmodium falciparum malaria is endemic. One null mutation in this gene is known, resulting in very severe anemia and nephrocalcinosis. [provided by RefSeq, Jul 2008]