Anti-ATIC Antibody Picoband® Fluoro647 Conjugated

Bifunctional purine biosynthesis protein PURH is a protein that in humans is encoded by the ATIC gene. This gene encodes a bifunctional protein that catalyzes the last two steps of the de novo purine biosynthetic pathway. The N-terminal domain has phosphoribosylaminoimidazolecarboxamide formyltransferase activity, and the C-terminal domain has IMP cyclohydrolase activity. A mutation in this gene results in AICA-ribosiduria.

Cell Type Marker, Developmental Families, Domain Families, Epigenetics and Nuclear Signaling, Neurogenesis, Neurology Process, Neuroscience, Transcription

Multifunctional transcription factor with different regions mediating its different effects. Acts by binding (via its C-terminal domain) to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Regulates the expression of specific genes involved in differentiation and survival within a subset of neuronal lineages. It has been shown that activation of some of these genes requires its N-terminal domain, maybe through a neuronal-specific cofactor. Ativates BCL2 expression and protects neuronal cells from apoptosis (via the N-terminal domain) . Induces neuronal process outgrowth and the coordinate expression of genes encoding synaptic proteins. Exerts its major developmental effects in somatosensory neurons and in brainstem nuclei involved in motor control. Stimulates the binding affinity of the nuclear estrogene receptor ESR1 to DNA estrogen response element (ERE), and hence modulates ESR1-induced transcriptional activity. May positively regulate POU4F2 and POU4F3. Regulates dorsal root ganglion sensory neuron specification and axonal projection into the spinal cord. Plays a role in TNFSF11-mediated terminal osteoclast differentiation. Negatively regulates its own expression interacting ly with a highly conserved autoregulatory domain surrounding the transcription initiation site.

1. Baresova, V., Skopova, V., Sikora, J., Patterson, D., Sovova, J., Zikanova, M., Kmoch, S. Mutations of ATIC and ADSL affect purinosome assembly in cultured skin fibroblasts from patients with AICA-ribosiduria and ADSL deficiency. Hum. Molec. Genet. 21: 1534-1543, 2012. 2. Greasley, S. E., Horton, P., Ramcharan, J., Beardsley, G. P., Benkovic, S. J., Wilson, I. A. Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis. Nature Struct. Biol. 8: 402-406, 2001. 3. Marie, S., Heron, B., Bitoun, P., Timmerman, T., Van den Berghe, G., Vincent, M.-F. AICA-ribosiduria: a novel, neurologically devastating inborn error of purine biosynthesis caused by mutation of ATIC. Am. J. Hum. Genet. 74: 1276-1281, 2004.