FHIT blocking peptide

FHIT Blocking Peptide (N-Term)

• Gene Names: FHIT; FRA3B; AP3Aase
• Synonyms: FHIT; FHIT Blocking Peptide (N-Term); Bis(5'-adenosyl)-triphosphatase; AP3A hydrolase; AP3Aase; Diadenosine 5';5'''-P1;P3-triphosphate hydrolase; Dinucleosidetriphosphatase; Fragile histidine triad protein; FHIT blocking peptide

• Specificity: The synthetic peptide sequence is selected from aa 39-54 of HUMAN FHIT
• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 147

• Cellular Location: Cytoplasm. Mitochondrion. Nucleus.
• Tissue Location: Low levels expressed in all tissues tested. Phospho-FHIT observed in liver and kidney, but not in brain and lung. Phospho-FHIT undetected in all tested human tumor cell lines
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for FHIT blocking peptide

Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'- adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low- affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.

NCBI and Uniprot Product Information

• NCBI GI #: 1706794
• NCBI GeneID: 2272
• UniProt Accession #: P49789; Q45QG9; Q6IU12; A2IAS9; A2IAT0; A2IAT6; A8K1A9
• Molecular Weight: 16,858 Da
• NCBI Official Full Name: Bis(5'-adenosyl)-triphosphatase
• NCBI Official Synonym Full Names: fragile histidine triad
• NCBI Official Symbol: FHIT
• NCBI Official Synonym Symbols: FRA3B; AP3Aase
• NCBI Protein Information: bis(5'-adenosyl)-triphosphatase
• UniProt Protein Name: Bis(5'-adenosyl)-triphosphatase
• Protein Family: Bis(5'-adenosyl)-triphosphatase
• UniProt Gene Name: FHIT
• UniProt Synonym Gene Names: AP3Aase
• UniProt Entry Name: FHIT_HUMAN

NCBI Description

This gene, a member of the histidine triad gene family, encodes a diadenosine 5',5'''-P1,P3-triphosphate hydrolase involved in purine metabolism. The gene encompasses the common fragile site FRA3B on chromosome 3, where carcinogen-induced damage can lead to translocations and aberrant transcripts of this gene. In fact, aberrant transcripts from this gene have been found in about half of all esophageal, stomach, and colon carcinomas. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Oct 2009]

Uniprot Description

FHIT: a member of the histidine triad gene family. A diadenosine 5',5'''-P1,P3-triphosphate hydrolase involved in purine metabolism. Its gene encompasses the common fragile site FRA3B on chromosome 3, where carcinogen-induced damage can lead to translocations and aberrant transcripts of this gene. A possible tumor suppressor in specific tissues. Phospho-FHIT observed in liver and kidney, but not in brain and lung. Phospho-FHIT undetected in all tested human tumor cell lines. Aberrant transcripts from this gene have been found in about half of all esophageal, stomach, and colon carcinomas.

Protein type: EC 3.6.1.29; Hydrolase; Motility/polarity/chemotaxis; DNA replication; Nucleotide Metabolism - purine; Tumor suppressor

Chromosomal Location of Human Ortholog: 3p14.2

Cellular Component: cytoplasm; cytosol

Molecular Function: bis(5'-adenosyl)-triphosphatase activity; catalytic activity; hydrolase activity; identical protein binding; protein binding; ubiquitin protein ligase binding

Biological Process: negative regulation of proteasomal ubiquitin-dependent protein catabolic process; nucleotide metabolic process; purine nucleotide metabolic process