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Protein

Bis(5'-adenosyl)-triphosphatase

Gene

Fhit

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Functions as tumor suppressor (By similarity).By similarity

Catalytic activityi

P(1)-P(3)-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81SubstrateBy similarity
Binding sitei27 – 271SubstrateBy similarity
Binding sitei83 – 831SubstrateBy similarity
Active sitei96 – 961Tele-AMP-histidine intermediateBy similarity
Binding sitei98 – 981SubstrateBy similarity
Sitei114 – 1141Important for induction of apoptosisBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi89 – 924SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

Magnesium, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620448. Fhit.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 150150Bis(5'-adenosyl)-triphosphatasePRO_0000288473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141PhosphotyrosineBy similarity
Modified residuei147 – 1471PhosphotyrosineBy similarity

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.
PhosphoSiteiQ9JIX3.

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. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 109108HITPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi94 – 985Histidine triad motifPROSITE-ProRule annotation

Sequence similaritiesi

Contains 1 HIT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3379. Eukaryota.
COG0537. LUCA.
HOGENOMiHOG000164170.
HOVERGENiHBG051614.
InParanoidiQ9JIX3.
KOiK01522.
PhylomeDBiQ9JIX3.

Family and domain databases

Gene3Di3.30.428.10. 1 hit.
InterProiIPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
[Graphical view]
PANTHERiPTHR23089. PTHR23089. 1 hit.
PfamiPF01230. HIT. 1 hit.
[Graphical view]
SUPFAMiSSF54197. SSF54197. 1 hit.
PROSITEiPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ9JIX3.
SMRiQ9JIX3. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009393.

PTM databases

iPTMnetiQ9JIX3.
PhosphoSiteiQ9JIX3.

Proteomic databases

PaxDbiQ9JIX3.
PRIDEiQ9JIX3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi60398.
KEGGirno:60398.

Organism-specific databases

CTDi2272.
RGDi620448. Fhit.

Phylogenomic databases

eggNOGiKOG3379. Eukaryota.
COG0537. LUCA.
HOGENOMiHOG000164170.
HOVERGENiHBG051614.
InParanoidiQ9JIX3.
KOiK01522.
PhylomeDBiQ9JIX3.

Miscellaneous databases

PROiQ9JIX3.

Family and domain databases

Gene3Di3.30.428.10. 1 hit.
InterProiIPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
[Graphical view]
PANTHERiPTHR23089. PTHR23089. 1 hit.
PfamiPF01230. HIT. 1 hit.
[Graphical view]
SUPFAMiSSF54197. SSF54197. 1 hit.
PROSITEiPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFHIT_RAT
AccessioniPrimary (citable) accession number: Q9JIX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.