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Protein

Bis(5'-adenosyl)-triphosphatase

Gene

Fhit

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cleaves P1-P3-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P1-P4-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 P1-P3-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity. Functions as tumor suppressor (By similarity).By similarity

Catalytic activityi

P1-P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP.

Cofactori

Mg2+By similarity, Mn2+By similarity, Ca2+By similarity, Co2+By similarityNote: Divalent metal cations. Mg2+, but Mn2+ and to a lesser extent Ca2+ or Co2+ can be substituted; but not Zn2+, Cd2+ or Ni2+.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8SubstrateBy similarity1
Binding sitei27SubstrateBy similarity1
Binding sitei83SubstrateBy similarity1
Active sitei96Tele-AMP-histidine intermediateBy similarity1
Binding sitei98SubstrateBy similarity1
Sitei114Important for induction of apoptosisBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi89 – 92SubstrateBy similarity4

GO - Molecular functioni

  • bis(5'-adenosyl)-triphosphatase activity Source: RGD
  • nickel cation binding Source: RGD
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processApoptosis, Transcription, Transcription regulation
LigandMagnesium, Manganese, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bis(5'-adenosyl)-triphosphatase (EC:3.6.1.29)
Alternative name(s):
AP3A hydrolase
Short name:
AP3Aase
Diadenosine 5',5'''-P1,P3-triphosphate hydrolase
Dinucleosidetriphosphatase
Fragile histidine triad protein
Gene namesi
Name:Fhit
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620448 Fhit

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002884731 – 150Bis(5'-adenosyl)-triphosphataseAdd BLAST150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei114PhosphotyrosineBy similarity1
Modified residuei147PhosphotyrosineBy similarity1

Post-translational modificationi

Phosphorylation at Tyr-114 by SRC is required for induction of apoptosis.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9JIX3
PRIDEiQ9JIX3

PTM databases

iPTMnetiQ9JIX3
PhosphoSitePlusiQ9JIX3

Interactioni

Subunit structurei

Homodimer. Interacts with UBE2I. Interacts with MDM2. Interacts with CTNNB1. Identified in a complex with CTNNB1 and LEF1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009393

Structurei

3D structure databases

ProteinModelPortaliQ9JIX3
SMRiQ9JIX3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 109HITPROSITE-ProRule annotationAdd BLAST108

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi94 – 98Histidine triad motifPROSITE-ProRule annotation5

Phylogenomic databases

eggNOGiKOG3379 Eukaryota
COG0537 LUCA
HOGENOMiHOG000164170
HOVERGENiHBG051614
InParanoidiQ9JIX3
KOiK01522
PhylomeDBiQ9JIX3

Family and domain databases

Gene3Di3.30.428.10, 1 hit
InterProiView protein in InterPro
IPR019808 Histidine_triad_CS
IPR001310 Histidine_triad_HIT
IPR011146 HIT-like
IPR036265 HIT-like_sf
PANTHERiPTHR23089 PTHR23089, 1 hit
PfamiView protein in Pfam
PF01230 HIT, 1 hit
SUPFAMiSSF54197 SSF54197, 1 hit
PROSITEiView protein in PROSITE
PS00892 HIT_1, 1 hit
PS51084 HIT_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9JIX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFKFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLMCP LRPVERFRDL
60 70 80 90 100
RPDEVADLFQ VTQRVGTVVE KHFQGTSITF SMQDGPEAGQ TVKHVHVHIL
110 120 130 140 150
PRKSGDFRRN DNIYDELQKH DREEEDSPAF WRSEEEMAAE AEVLRAYFQA
Length:150
Mass (Da):17,348
Last modified:October 1, 2000 - v1
Checksum:iE0C466FB045EE714
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170064 mRNA Translation: AAF89328.1
RefSeqiNP_068542.1, NM_021774.1
UniGeneiRn.45598

Genome annotation databases

GeneIDi60398
KEGGirno:60398

Similar proteinsi

Entry informationi

Entry nameiFHIT_RAT
AccessioniPrimary (citable) accession number: Q9JIX3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2000
Last modified: May 23, 2018
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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