| Primary Identifier | IPR046408 | Type | Domain |
| Short Name | CIAPIN1 |
| description | This entry represents the C-terminal domain of anamorsin and its homologues which contains two highly conserved cysteine rich motifs that bind Fe-S clusters [].Anamorsin (also named CIAPIN1 for cytokine-induced anti-apoptosis inhibitor 1), is the humanhomologue of yeast Dre2, a conserved soluble eukaryotic Fe-S cluster protein, that functions in cytosolic Fe-S protein biogenesis [, , , ]. It is found in both the cytoplasm and in the mitochondrial intermembrane space (IMS) []. Anamorsin is found to be up-regulated in hepatocellular cancer, is considered to be a downstream effector of the receptor tyrosine kinase-Ras signalling pathway, and is essential in mouse definitive haematopoiesis []. In addition, it mediates the anti-apoptotic effects of various cytokines []. These proteins consist of a well-folded N-terminal domain with an overall typical S-adenosylmethionine methyltransferase fold and a more flexible C-terminal domain. |
