FHIT
entrez
2272
canonical
uniprot
P49789
canonical
ensembl
ENSG00000189283
resolver
ensp
ENSP00000417480
resolver
ensp
ENSP00000417557
resolver
ensp
ENSP00000418582
resolver
enst
ENST00000468189
resolver
enst
ENST00000476844
resolver
enst
ENST00000492590
resolver
genesymbol
FHIT
resolver
hgnc
HGNC:3701
resolver
uniprot
A2IAS9
resolver
uniprot
A2IAT0
resolver
uniprot
A2IAT6
resolver
uniprot
A8K1A9
resolver
uniprot
Q45QG9
resolver
uniprot
Q6IU12
resolver
uniprot_entry
FHIT_HUMAN
resolver
uniprot_sec
A2IAS9
resolver
uniprot_sec
A2IAT0
resolver
uniprot_sec
A2IAT6
resolver
uniprot_sec
A8K1A9
resolver
uniprot_sec
Q45QG9
resolver
uniprot_sec
Q6IU12
resolver
amino_acid_sequence
MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKHDKEDFPASWRSEEEMAAEAAALRVYFQ
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving FHIT has been found in a lymphoblastoid cell line established from a family with renal cell carcinoma and thyroid carcinoma. Translocation t(3;8)(p14.2;q24.1) with RNF139. Although the 3p14.2 breakpoint has been shown to interrupt FHIT in its 5-prime non-coding region, it is unlikely that FHIT is causally related to renal or other malignancies. {ECO:0000269|PubMed:15007172}.; DISEASE: Note=Associated with digestive tract cancers. Numerous tumor types are found to have aberrant forms of FHIT protein due to deletions in a coding region of chromosome 3p14.2 including the fragile site locus FRA3B. {ECO:0000269|PubMed:15007172}.
uniprot
proteins
ec_number
2.7.7.51
uniprot
proteins
ec_number
3.6.1.29
uniprot
proteins
ec_number
3.6.2.1
uniprot
proteins
ec_number
3.9.1.-
uniprot
proteins
function
FUNCTION: Possesses dinucleoside triphosphate hydrolase activity (PubMed:12574506, PubMed:15182206, PubMed:8794732, PubMed:9323207, PubMed:9543008, PubMed:9576908). Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP (PubMed:12574506, PubMed:15182206, PubMed:8794732, PubMed:9323207, PubMed:9543008, PubMed:9576908). Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP (PubMed:8794732). Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate (PubMed:18694747). Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:18694747). Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate (PubMed:26181368). Also catalyzes the ammonolysis of adenosine 5-phosphorofluoridate and diadenosine triphosphate (PubMed:26181368). 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 (PubMed:18077326). Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways (PubMed:16407838). Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis (PubMed:15313915). 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 (PubMed:12574506, PubMed:19622739). Functions as a tumor suppressor (By similarity). {ECO:0000250|UniProtKB:O89106, ECO:0000269|PubMed:12574506, ECO:0000269|PubMed:15313915, ECO:0000269|PubMed:16407838, ECO:0000269|PubMed:18077326, ECO:0000269|PubMed:18694747, ECO:0000269|PubMed:19622739, ECO:0000269|PubMed:26181368, ECO:0000269|PubMed:8794732, ECO:0000269|PubMed:9323207, ECO:0000269|PubMed:9543008}.
uniprot
proteins
mass_dalton
16858
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="I->W: Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-25."; /evidence="ECO:0000269|PubMed:12574506"; MUTAGEN 25; /note="L->W: Reduces affinity for substrates and impairs apoptosis. Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-10."; /evidence="ECO:0000269|PubMed:12574506"; MUTAGEN 35; /note="H->N: 50% decrease in catalytic activity. No loss in substrate binding."; /evidence="ECO:0000269|PubMed:8794732"; MUTAGEN 94; /note="H->N: 75% decrease in catalytic activity. No loss in substrate binding."; /evidence="ECO:0000269|PubMed:8794732"; MUTAGEN 96; /note="H->D: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:12574506, ECO:0000269|PubMed:15182206, ECO:0000269|PubMed:8794732, ECO:0000269|PubMed:9576908"; MUTAGEN 96; /note="H->G: Total loss of catalytic activity. Rescuable with free imidazole."; /evidence="ECO:0000269|PubMed:12574506, ECO:0000269|PubMed:15182206, ECO:0000269|PubMed:8794732, ECO:0000269|PubMed:9576908"; MUTAGEN 96; /note="H->N: Total loss of catalytic activity. No loss in substrate binding."; /evidence="ECO:0000269|PubMed:12574506, ECO:0000269|PubMed:15182206, ECO:0000269|PubMed:8794732, ECO:0000269|PubMed:9576908"; MUTAGEN 98; /note="H->N: 98% decrease in catalytic activity."; /evidence="ECO:0000269|PubMed:8794732"; MUTAGEN 114; /note="Y->A: Impairs induction of apoptosis. Strongly reduced affinity for substrates."; /evidence="ECO:0000269|PubMed:15007172, ECO:0000269|PubMed:16407838"; MUTAGEN 114; /note="Y->D: Impairs induction of apoptosis. Reduces affinity for substrates."; /evidence="ECO:0000269|PubMed:15007172, ECO:0000269|PubMed:16407838"; MUTAGEN 114; /note="Y->F: Loss of phosphorylation by SRC. Impairs induction of apoptosis."; /evidence="ECO:0000269|PubMed:15007172, ECO:0000269|PubMed:16407838"; MUTAGEN 145; /note="Y->F: No effect on phosphorylation by SRC."; /evidence="ECO:0000269|PubMed:15007172
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Tyr-114 by SRC is required for induction of apoptosis. {ECO:0000269|PubMed:15007172}.
uniprot
proteins
pubmed
11085938
uniprot
proteins
pubmed
12574506
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15007172
uniprot
proteins
pubmed
15182206
uniprot
proteins
pubmed
15313915
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16407838
uniprot
proteins
pubmed
18077326
uniprot
proteins
pubmed
18694747
uniprot
proteins
pubmed
19622739
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24722188
uniprot
proteins
pubmed
26181368
uniprot
proteins
pubmed
8598045
uniprot
proteins
pubmed
8794732
uniprot
proteins
pubmed
9012482
uniprot
proteins
pubmed
9261067
uniprot
proteins
pubmed
9323207
uniprot
proteins
pubmed
9543008
uniprot
proteins
pubmed
9576908
uniprot
proteins
pubmed
9689122
uniprot
proteins
sequence_length
147
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15007172, ECO:0000269|PubMed:15313915}. Mitochondrion {ECO:0000269|PubMed:19622739}. Nucleus {ECO:0000269|PubMed:15313915}.
uniprot
proteins