The gene HAP1 (huntingtin-associated protein 1) encodes a nuclear enzyme that is mainly expressed in neurons. It is the human homolog of exonuclease III protein from E. coli. The gene is mapped to human chromosome 17q21.2-q21.3.
Immunogen
Peptide with sequence C-RYDFRYSEDREQ from the internal region of the protein sequence according to NP_003940.2; NP_817084.1.
Biochem/physiol Actions
The gene HAP1 (huntingtin-associated protein 1) is a bifunctional enzyme that functions as a DNA repair enzyme as well as in redox activation of transcription factors. It binds to the Huntington′s disease (HD) protein huntingtin in a polyglutamine length-dependent manner. It associates with huntingtin via the cytoskeletal proteins dynactin and pericentriolar autoantigen protein 1 forming coiled-coils. It plays a role in vesicle trafficking by facilitating interactions among cytoskeletal, vesicular and motor proteins. It is an apurinic/apyrimidinic (AP) site-specific DNA repair endonuclease that removes the AP sites produced naturally or by cytotoxic drugs and radiation. It also has RNAse H activity and controls the redox state of certain proto-oncogene products, such as the transcription factor c-Jun. The HAP1 protein is a candidate for pathology associated with HD.
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Physical form
Supplied at 0.5 mg/mL in Tris saline with 0.02% sodium azide and 0.5% bovine serum albumin.
Assignment of the huntingtin (Hdh) gene, the huntingtin associated protein (Hap1) gene, and the huntingtin interacting protein (Hip1) gene to rat chromosomes 14, 10, and 12 by radiation hybrid mapping and fluorescent in situ hybridization.
Zimdahl H
Cytogenetics and Cell Genetics, 94, 101-104 (2001)
Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued subunit of dynactin.
Engelender S
Human Molecular Genetics, 6, 2205-2212 (1997)
A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging agents and hypoxic stress.
Molecular and cellular biology, 13(9), 5370-5376 (1993-09-01)
The DNA binding activity of the c-jun proto-oncogene product is inhibited by oxidation of a specific cysteine residue (Cys-252) in the DNA binding domain. Jun protein inactivated by oxidation of this residue can be efficiently reactivated by a factor from
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