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O89106 (FHIT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Fhit
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processDNA replication

Inferred from direct assay. Source: MGI

nucleotide metabolic process

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular functionbis(5'-adenosyl)-triphosphatase activity

Inferred from direct assay. Source: UniProtKB

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 [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

EMBL
GenBank
DDBJ
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. NM_010210.2.
UniGeneMm.397619.
Mm.441926.

3D structure databases

ProteinModelPortalO89106.
SMRO89106. Positions 2-149.
ModBaseSearch...

Protein-protein interaction databases

STRINGO89106.

PTM databases

PhosphoSiteO89106.

Proteomic databases

PRIDEO89106.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000161302; ENSMUSP00000123874; ENSMUSG00000060579.
ENSMUST00000162278; ENSMUSP00000124073; ENSMUSG00000060579.
GeneID14198.
KEGGmmu:14198.
UCSCuc007sfj.1. mouse.

Organism-specific databases

CTD2272.
MGIMGI:1277947. Fhit.

Phylogenomic databases

eggNOGroNOG10442.
HOGENOMHBG396802.
HOVERGENHBG051614.
InParanoidO89106.
OrthoDBEOG4GQQ68.

Gene expression databases

BgeeO89106.
CleanExMM_FHIT.
GenevestigatorO89106.

Family and domain databases

InterProIPR011146. His_triad-like_motif.
IPR011151. His_triad_motif.
IPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
[Graphical view]
Gene3DG3DSA:3.30.428.10. His_triad_motif. 1 hit.
KOK01522.
PANTHERPTHR23089. HIT. 1 hit.
PfamPF01230. HIT. 1 hit.
[Graphical view]
SUPFAMSSF54197. His_triad-like_motif. 1 hit.
PROSITEPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

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: November 16, 2011
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families