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P49789

- FHIT_HUMAN

UniProt

P49789 - FHIT_HUMAN

Protein

Bis(5'-adenosyl)-triphosphatase

Gene

FHIT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca2+ transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.7 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei8 – 81Substrate
    Binding sitei27 – 271Substrate
    Binding sitei83 – 831Substrate
    Active sitei96 – 961Tele-AMP-histidine intermediate2 Publications
    Binding sitei98 – 981Substrate
    Sitei114 – 1141Important for induction of apoptosis

    Regions

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

    GO - Molecular functioni

    1. bis(5'-adenosyl)-triphosphatase activity Source: UniProtKB
    2. catalytic activity Source: ProtInc
    3. hydrolase activity Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. nucleotide binding Source: UniProtKB-KW
    6. protein binding Source: IntAct
    7. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. DNA replication Source: Ensembl
    2. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    3. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    4. nucleotide metabolic process Source: ProtInc
    5. purine nucleotide metabolic process Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB-KW
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation

    Keywords - Ligandi

    Manganese, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP49789.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3701. FHIT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrion Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    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.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101I → W: Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-25. 1 Publication
    Mutagenesisi25 – 251L → W: Reduces affinity for substrates and impairs apoptosis. Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-10. 1 Publication
    Mutagenesisi35 – 351H → N: 50% decrease in catalytic activity. No loss in substrate binding. 1 Publication
    Mutagenesisi94 – 941H → N: 75% decrease in catalytic activity. No loss in substrate binding. 1 Publication
    Mutagenesisi96 – 961H → D: Loss of catalytic activity. 4 Publications
    Mutagenesisi96 – 961H → G: Total loss of catalytic activity. Rescuable with free imidazole. 4 Publications
    Mutagenesisi96 – 961H → N: Total loss of catalytic activity. No loss in substrate binding. 4 Publications
    Mutagenesisi98 – 981H → N: 98% decrease in catalytic activity. 1 Publication
    Mutagenesisi114 – 1141Y → A: Impairs induction of apoptosis. Strongly reduced affinity for substrates. 2 Publications
    Mutagenesisi114 – 1141Y → D: Impairs induction of apoptosis. Reduces affinity for substrates. 2 Publications
    Mutagenesisi114 – 1141Y → F: Loss of phosphorylation by SRC. Impairs induction of apoptosis. 2 Publications
    Mutagenesisi145 – 1451Y → F: No effect on phosphorylation by SRC. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    Orphaneti151. Familial renal cell carcinoma.
    PharmGKBiPA28140.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 147147Bis(5'-adenosyl)-triphosphatasePRO_0000109789Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei114 – 1141Phosphotyrosine; by SRC1 Publication
    Modified residuei145 – 1451Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylation at Tyr-114 by SRC is required for induction of apoptosis.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49789.
    PaxDbiP49789.
    PeptideAtlasiP49789.
    PRIDEiP49789.

    PTM databases

    PhosphoSiteiP49789.

    Expressioni

    Tissue specificityi

    Low levels expressed in all tissues tested. Phospho-FHIT observed in liver and kidney, but not in brain and lung. Phospho-FHIT undetected in all tested human tumor cell lines.

    Gene expression databases

    ArrayExpressiP49789.
    BgeeiP49789.
    CleanExiHS_FHIT.
    GenevestigatoriP49789.

    Organism-specific databases

    HPAiCAB002684.
    HPA018840.
    HPA018909.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with UBE2I. Interacts with MDM2. Interacts with CTNNB1. Identified in a complex with CTNNB1 and LEF1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-741760,EBI-741760
    FDXRP225704EBI-741760,EBI-1751533
    HSPD1P108095EBI-741760,EBI-352528
    HSPE1P616044EBI-741760,EBI-711483

    Protein-protein interaction databases

    BioGridi108563. 7 interactions.
    DIPiDIP-29947N.
    IntActiP49789. 8 interactions.
    MINTiMINT-150697.
    STRINGi9606.ENSP00000342087.

    Structurei

    Secondary structure

    1
    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi8 – 103
    Helixi12 – 143
    Beta strandi15 – 184
    Beta strandi20 – 267
    Beta strandi36 – 427
    Helixi47 – 493
    Helixi52 – 7221
    Beta strandi76 – 827
    Helixi86 – 883
    Beta strandi92 – 943
    Beta strandi97 – 1026
    Helixi132 – 14413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FHIX-ray3.10A1-147[»]
    1FITX-ray1.85A1-147[»]
    2FHIX-ray2.60A1-147[»]
    2FITX-ray1.90A1-147[»]
    3FITX-ray2.40A1-147[»]
    4FITX-ray2.50A1-147[»]
    5FITX-ray2.30A1-147[»]
    6FITX-ray2.60A1-147[»]
    ProteinModelPortaliP49789.
    SMRiP49789. Positions 2-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49789.

    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 motif

    Sequence similaritiesi

    Contains 1 HIT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0537.
    HOGENOMiHOG000164170.
    HOVERGENiHBG051614.
    InParanoidiP49789.
    KOiK01522.
    OMAiDKWRTEE.
    PhylomeDBiP49789.
    TreeFamiTF105432.

    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.

    P49789-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL    50
    RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL 100
    PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQ 147
    Length:147
    Mass (Da):16,858
    Last modified:January 23, 2007 - v3
    Checksum:i14D85961A19ECF3E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461F → S in BAF82513. (PubMed:14702039)Curated

    Mass spectrometryi

    Molecular mass is 16733 Da from positions 2 - 147. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46922 mRNA. Translation: AAA99013.1.
    U76271
    , U76267, U76268, U76269, U76270 Genomic DNA. Translation: AAB52539.1.
    KJ534835 mRNA. Translation: AHW56475.1.
    AY625256 Genomic DNA. Translation: AAT37530.1.
    DQ120721 mRNA. Translation: AAZ23623.1.
    EF186677 Genomic DNA. Translation: ABM65879.1.
    EF183457 Genomic DNA. Translation: ABM66086.1.
    EF183458 Genomic DNA. Translation: ABM66087.1.
    EF183459 Genomic DNA. Translation: ABM66088.1.
    EF183461 Genomic DNA. Translation: ABM66090.1.
    EF183464 Genomic DNA. Translation: ABM66093.1.
    AK289824 mRNA. Translation: BAF82513.1.
    CH471055 Genomic DNA. Translation: EAW65393.1.
    BC032336 mRNA. Translation: AAH32336.1.
    CCDSiCCDS2894.1.
    PIRiA58802.
    RefSeqiNP_001159715.1. NM_001166243.1.
    NP_002003.1. NM_002012.2.
    XP_005265009.1. XM_005264952.2.
    XP_005265010.1. XM_005264953.2.
    XP_006713090.1. XM_006713027.1.
    UniGeneiHs.655995.

    Genome annotation databases

    EnsembliENST00000341848; ENSP00000342087; ENSG00000189283.
    ENST00000468189; ENSP00000417480; ENSG00000189283.
    ENST00000476844; ENSP00000417557; ENSG00000189283.
    ENST00000492590; ENSP00000418582; ENSG00000189283.
    GeneIDi2272.
    KEGGihsa:2272.
    UCSCiuc003dkx.4. human.

    Polymorphism databases

    DMDMi1706794.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46922 mRNA. Translation: AAA99013.1 .
    U76271
    , U76267 , U76268 , U76269 , U76270 Genomic DNA. Translation: AAB52539.1 .
    KJ534835 mRNA. Translation: AHW56475.1 .
    AY625256 Genomic DNA. Translation: AAT37530.1 .
    DQ120721 mRNA. Translation: AAZ23623.1 .
    EF186677 Genomic DNA. Translation: ABM65879.1 .
    EF183457 Genomic DNA. Translation: ABM66086.1 .
    EF183458 Genomic DNA. Translation: ABM66087.1 .
    EF183459 Genomic DNA. Translation: ABM66088.1 .
    EF183461 Genomic DNA. Translation: ABM66090.1 .
    EF183464 Genomic DNA. Translation: ABM66093.1 .
    AK289824 mRNA. Translation: BAF82513.1 .
    CH471055 Genomic DNA. Translation: EAW65393.1 .
    BC032336 mRNA. Translation: AAH32336.1 .
    CCDSi CCDS2894.1.
    PIRi A58802.
    RefSeqi NP_001159715.1. NM_001166243.1.
    NP_002003.1. NM_002012.2.
    XP_005265009.1. XM_005264952.2.
    XP_005265010.1. XM_005264953.2.
    XP_006713090.1. XM_006713027.1.
    UniGenei Hs.655995.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FHI X-ray 3.10 A 1-147 [» ]
    1FIT X-ray 1.85 A 1-147 [» ]
    2FHI X-ray 2.60 A 1-147 [» ]
    2FIT X-ray 1.90 A 1-147 [» ]
    3FIT X-ray 2.40 A 1-147 [» ]
    4FIT X-ray 2.50 A 1-147 [» ]
    5FIT X-ray 2.30 A 1-147 [» ]
    6FIT X-ray 2.60 A 1-147 [» ]
    ProteinModelPortali P49789.
    SMRi P49789. Positions 2-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108563. 7 interactions.
    DIPi DIP-29947N.
    IntActi P49789. 8 interactions.
    MINTi MINT-150697.
    STRINGi 9606.ENSP00000342087.

    Chemistry

    BindingDBi P49789.
    ChEMBLi CHEMBL1795151.

    PTM databases

    PhosphoSitei P49789.

    Polymorphism databases

    DMDMi 1706794.

    Proteomic databases

    MaxQBi P49789.
    PaxDbi P49789.
    PeptideAtlasi P49789.
    PRIDEi P49789.

    Protocols and materials databases

    DNASUi 2272.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341848 ; ENSP00000342087 ; ENSG00000189283 .
    ENST00000468189 ; ENSP00000417480 ; ENSG00000189283 .
    ENST00000476844 ; ENSP00000417557 ; ENSG00000189283 .
    ENST00000492590 ; ENSP00000418582 ; ENSG00000189283 .
    GeneIDi 2272.
    KEGGi hsa:2272.
    UCSCi uc003dkx.4. human.

    Organism-specific databases

    CTDi 2272.
    GeneCardsi GC03M059712.
    HGNCi HGNC:3701. FHIT.
    HPAi CAB002684.
    HPA018840.
    HPA018909.
    MIMi 601153. gene.
    neXtProti NX_P49789.
    Orphaneti 151. Familial renal cell carcinoma.
    PharmGKBi PA28140.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0537.
    HOGENOMi HOG000164170.
    HOVERGENi HBG051614.
    InParanoidi P49789.
    KOi K01522.
    OMAi DKWRTEE.
    PhylomeDBi P49789.
    TreeFami TF105432.

    Enzyme and pathway databases

    SABIO-RK P49789.

    Miscellaneous databases

    ChiTaRSi FHIT. human.
    EvolutionaryTracei P49789.
    GeneWikii FHIT.
    GenomeRNAii 2272.
    NextBioi 35461054.
    PROi P49789.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49789.
    Bgeei P49789.
    CleanExi HS_FHIT.
    Genevestigatori P49789.

    Family and domain databases

    Gene3Di 3.30.428.10. 1 hit.
    InterProi IPR019808. Histidine_triad_CS.
    IPR001310. Histidine_triad_HIT.
    IPR011146. HIT-like.
    [Graphical view ]
    PANTHERi PTHR23089. PTHR23089. 1 hit.
    Pfami PF01230. HIT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54197. SSF54197. 1 hit.
    PROSITEi PS00892. HIT_1. 1 hit.
    PS51084. HIT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The FHIT gene, spanning the chromosome 3p14.2 fragile site and renal carcinoma-associated t(3;8) breakpoint, is abnormal in digestive tract cancers."
      Ohta M., Inoue H., Cotticelli M.G., Kastury K., Baffa R., Palazzo J., Siprashvili Z., Mori M., McCue P., Druck T., Croce C.M., Huebner K.
      Cell 84:587-597(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Structure and expression of the human FHIT gene in normal and tumor cells."
      Druck T., Hadaczek P., Fu T.B., Ohta M., Siprashvili Z., Baffa R., Negrini M., Kastury K., Veronese M.L., Rosen D., Rothstein J., McCue P., Cotticelli M.G., Inoue H., Croce C.M., Huebner K.
      Cancer Res. 57:504-512(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
      Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
      , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
      Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Mutational analysis of FHIT gene."
      Naqvi S.R.A., Malik A., Kukreti H., Chaudhary A., Anand R., Deo S.S., Shukla N.K., Husain S.A., Pasha S.T.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-146.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    8. "Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5''-P1,P3-triphosphate hydrolase."
      Barnes L.D., Garrison P.N., Siprashvili Z., Guranowski A., Robinson A.K., Ingram S.W., Croce C.M., Ohta M., Huebner K.
      Biochemistry 35:11529-11535(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-35; HIS-94; HIS-96 AND HIS-98.
    9. "The hereditary renal cell carcinoma 3;8 translocation fuses FHIT to a patched-related gene, TRC8."
      Gemmill R.M., West J.D., Boldog F., Tanaka N., Robinson L.J., Smith D.I., Li F., Drabkin H.A.
      Proc. Natl. Acad. Sci. U.S.A. 95:9572-9577(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH RNF139.
    10. "Association of FHIT (fragile histidine triad), a candidate tumour suppressor gene, with the ubiquitin-conjugating enzyme hUBC9."
      Shi Y., Zou M., Farid N.R., Paterson M.C.
      Biochem. J. 352:443-448(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2I.
    11. "Designed FHIT alleles establish that Fhit-induced apoptosis in cancer cells is limited by substrate binding."
      Trapasso F., Krakowiak A., Cesari R., Arkles J., Yendamuri S., Ishii H., Vecchione A., Kuroki T., Bieganowski P., Pace H.C., Huebner K., Croce C.M., Brenner C.
      Proc. Natl. Acad. Sci. U.S.A. 100:1592-1597(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-10; LEU-25 AND HIS-96.
    12. "The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit."
      Huang K., Arabshahi A., Wei Y., Frey P.A.
      Biochemistry 43:7637-7642(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-96.
    13. "Synergistic tumor suppression by coexpression of FHIT and p53 coincides with FHIT-mediated MDM2 inactivation and p53 stabilization in human non-small cell lung cancer cells."
      Nishizaki M., Sasaki J., Fang B., Atkinson E.N., Minna J.D., Roth J.A., Ji L.
      Cancer Res. 64:5745-5752(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MDM2.
    14. Cited for: PHOSPHORYLATION BY SRC, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, DISEASE, PHOSPHORYLATION AT TYR-114 AND TYR-145, MUTAGENESIS OF TYR-114 AND TYR-145.
    15. "Fhit modulation of the Akt-survivin pathway in lung cancer cells: Fhit-tyrosine 114 (Y114) is essential."
      Semba S., Trapasso F., Fabbri M., McCorkell K.A., Volinia S., Druck T., Iliopoulos D., Pekarsky Y., Ishii H., Garrison P.N., Barnes L.D., Croce C.M., Huebner K.
      Oncogene 25:2860-2872(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-114, FUNCTION.
    16. "The tumor suppressor Fhit acts as a repressor of beta-catenin transcriptional activity."
      Weiske J., Albring K.F., Huber O.
      Proc. Natl. Acad. Sci. U.S.A. 104:20344-20349(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTNNB1, IDENTIFICATION IN A COMPLEX WITH CTNNB1 AND LEF1, FUNCTION.
    17. "Intramitochondrial calcium regulation by the FHIT gene product sensitizes to apoptosis."
      Rimessi A., Marchi S., Fotino C., Romagnoli A., Huebner K., Croce C.M., Pinton P., Rizzuto R.
      Proc. Natl. Acad. Sci. U.S.A. 106:12753-12758(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION IN APOPTOSIS.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family."
      Lima C.D., D'Amico K.L., Naday I., Rosenbaum G., Westbrook E.M., Hendrickson W.A.
      Structure 5:763-774(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    20. "Structure-based analysis of catalysis and substrate definition in the HIT protein family."
      Lima C.D., Klein M.G., Hendrickson W.A.
      Science 278:286-290(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, ACTIVE SITE, ABSENCE OF METAL COFACTOR.
    21. "Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit."
      Pace H.C., Garrison P.N., Robinson A.K., Barnes L.D., Draganescu A., Roesler A., Blackburn G.M., Siprashvili Z., Croce C.M., Huebner K., Brenner C.
      Proc. Natl. Acad. Sci. U.S.A. 95:5484-5489(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF HIS-96.

    Entry informationi

    Entry nameiFHIT_HUMAN
    AccessioniPrimary (citable) accession number: P49789
    Secondary accession number(s): A2IAS9
    , A2IAT0, A2IAT6, A8K1A9, Q45QG9, Q6IU12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3