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P49789

- FHIT_HUMAN

UniProt

P49789 - FHIT_HUMAN

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Protein

Bis(5'-adenosyl)-triphosphatase

Gene

FHIT

Organism
Homo sapiens (Human)
Status
Reviewed - 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, 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. 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
Complete GO annotation...

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-KW
  5. nucleus Source: UniProtKB-KW
Complete GO annotation...

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

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

BgeeiP49789.
CleanExiHS_FHIT.
ExpressionAtlasiP49789. baseline and differential.
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. 9 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 – 53Combined sources
Beta strandi8 – 103Combined sources
Helixi12 – 143Combined sources
Beta strandi15 – 184Combined sources
Beta strandi20 – 267Combined sources
Beta strandi36 – 427Combined sources
Helixi47 – 493Combined sources
Helixi52 – 7221Combined sources
Beta strandi76 – 827Combined sources
Helixi86 – 883Combined sources
Beta strandi92 – 943Combined sources
Beta strandi97 – 1026Combined sources
Helixi132 – 14413Combined sources

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.
GeneTreeiENSGT00510000047967.
HOGENOMiHOG000164170.
HOVERGENiHBG051614.
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

        10         20         30         40         50
MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL
60 70 80 90 100
RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL
110 120 130 140
PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQ
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

EnsembliENST00000468189; 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. 9 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

PaxDbi P49789.
PeptideAtlasi P49789.
PRIDEi P49789.

Protocols and materials databases

DNASUi 2272.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli 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.
GeneTreei ENSGT00510000047967.
HOGENOMi HOG000164170.
HOVERGENi HBG051614.
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

Bgeei P49789.
CleanExi HS_FHIT.
ExpressionAtlasi P49789. baseline and differential.
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

« Hide 'large scale' publications
  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. 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 29, 2014
This is version 142 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