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Reviewed, UniProtKB/Swiss-Prot O89106 (FHIT_MOUSE)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bis(5'-adenosyl)-triphosphatase
    EC=3.6.1.29
Alternative name(s):
    Diadenosine 5',5'''-P1,P3-triphosphate hydrolase
    Dinucleosidetriphosphatase
    AP3A hydrolase
      Short name=AP3Aase
    Fragile histidine triad protein
Gene names
Name: Fhit
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Cleaves A-5'-PPP-5'A to yield AMP and ADP.

Catalytic activity

P(1)-P(3)-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP.

Cofactor

Divalent cations. Magnesium, but manganese and to a lesser extent calcium or cobalt can be substituted; but not zinc, cadmium or nickel By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm. Ref.1

Tissue specificity

Expressed in heart, brain, lung and skeletal muscle. Particularly strong expression in liver, testis and kidney, where it is confined to the tubular epithelium. Ref.1 Ref.5

Sequence similarities

Contains 1 HIT domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
   Molecular functionHydrolase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processDNA replication

Inferred from direct assay. Source: MGI

nucleotide metabolic process

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionbis(5'-adenosyl)-triphosphatase activity

Inferred from direct assay. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 150149Bis(5'-adenosyl)-triphosphatase
PRO_0000109790

Regions

Domain2 – 109108HIT
Region82 – 9918Binding to substrate; phosphate linker By similarity
Motif94 – 985Histidine triad motif By similarity

Sites

Active site961Tele-AMP-histidine intermediate By similarity
Binding site271Substrate By similarity

Amino acid modifications

Modified residue1141Phosphotyrosine; by SRC By similarity
Modified residue1471Phosphotyrosine By similarity

Experimental info

Sequence conflict1351K → E in AAH12662. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O89106-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 27CBC57C5A4A0E2B

FASTA15017,235
        10         20         30         40         50         60 
MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFRDL HPDEVADLFQ 

        70         80         90        100        110        120 
VTQRVGTVVE KHFQGTSITF SMQDGPEAGQ TVKHVHVHVL PRKAGDFPRN DNIYDELQKH 

       130        140        150 
DREEEDSPAF WRSEKEMAAE AEALRVYFQA 

« Hide

References

« Hide 'large scale' references
[1]"The murine Fhit locus: isolation, characterization, and expression in normal and tumor cells."
Pekarsky Y., Druck T., Cotticelli M.G., Ohta M., Shou J., Mendrola J., Montgomery J.C., Buchberg A.M., Siracusa L.D., Manenti G., Fong L.Y., Dragani T.A., Croce C.M., Huebner K.
Cancer Res. 58:3401-3408(1998) [PubMed: 9699672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]Glover T.W., Hoge A., Miller D.E., Escara-Wilke J., Adam A.N., Dagenais S.L., Wilke C.M., Dierick H.A., Beer D.G.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/10J.
Tissue: Muscle.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[4]"Fragile site orthologs FHIT/FRA3B and Fhit/Fra14A2: evolutionarily conserved but highly recombinogenic."
Matsuyama A., Shiraishi T., Trapasso F., Kuroki T., Alder H., Mori M., Huebner K., Croce C.M.
Proc. Natl. Acad. Sci. U.S.A. 100:14988-14993(2003) [PubMed: 14630947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-150.
Strain: C57BL/6J.
Tissue: Kidney.
[5]"Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster and Caenorhabditis elegans."
Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y., Tillib S., Draganescu A., Wermuth P., Rothman J.H., Huebner K., Buchberg A.M., Mazo A., Brenner C., Croce C.M.
Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998) [PubMed: 9671749] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF047702, AF047700, AF047701 Genomic DNA. Translation: AAC23967.1.
AF047699 mRNA. Translation: AAC24566.1.
AF055573 mRNA. Translation: AAC24117.1.
BC012662 mRNA. Translation: AAH12662.1.
AY363103 Genomic DNA. Translation: AAR17701.1.
IPIIPI00131502.
RefSeqNP_034340.1.
UniGeneMm.397619
Mm.441926

3D structure databases

HSSPHSSP built from PDB template 4FIT based on UniProtKB P49789.
SMRO89106. Positions 1-130, 2-131.
ModBaseSearch...

PTM databases

PhosphoSiteO89106.

Proteomic databases

PRIDEO89106.

Genome annotation databases

EnsemblENSMUSG00000060579. Mus musculus. [Contig view]
GeneID14198.
KEGGmmu:14198.

Organism-specific databases

MGIMGI:1277947. Fhit.

Phylogenomic databases

HOGENOMO89106.
HOVERGENO89106.

Enzyme and pathway databases

BRENDA3.6.1.29. 244.

Gene expression databases

BgeeO89106.
CleanExMM_FHIT.

Family and domain databases

InterProIPR011151. His_triad_motif.
IPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
[Graphical view]
Gene3DG3DSA:3.30.428.10. His_triad_motif. 1 hit.
PANTHERPTHR23089. HIT. 1 hit.
PfamPF01230. HIT. 1 hit.
[Graphical view]
PROSITEPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio285422.
SOURCESearch...

Entry information

Entry nameFHIT_MOUSE
AccessionPrimary (citable) accession number: O89106
Secondary accession number(s): Q6URW5, Q91VL1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 66 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents