Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P49789 (FHIT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.11 Ref.13 Ref.15 Ref.16 Ref.17 Ref.20

Catalytic activity

P(1)-P(3)-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP. Ref.8 Ref.11 Ref.12 Ref.20 Ref.21

Subunit structure

Homodimer. Interacts with UBE2I. Interacts with MDM2. Interacts with CTNNB1. Identified in a complex with CTNNB1 and LEF1. Ref.10 Ref.13 Ref.14 Ref.16 Ref.20 Ref.21

Subcellular location

Cytoplasm. Mitochondrion. Nucleus Ref.13 Ref.14 Ref.17.

Tissue specificity

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.

Post-translational modification

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

Involvement in disease

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. Ref.14

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. Ref.14

Sequence similarities

Contains 1 HIT domain.

Mass spectrometry

Molecular mass is 16733 Da from positions 2 - 147. Determined by MALDI. Ref.14

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityChromosomal rearrangement
   DiseaseTumor suppressor
   LigandManganese
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from mutant phenotype Ref.13. Source: UniProtKB

negative regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

nucleotide metabolic process

Traceable author statement Ref.8. Source: ProtInc

purine nucleotide metabolic process

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

cytosol

Inferred from direct assay Ref.13. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbis(5'-adenosyl)-triphosphatase activity

Inferred from direct assay Ref.8Ref.20. Source: UniProtKB

catalytic activity

Traceable author statement Ref.1. Source: ProtInc

hydrolase activity

Inferred from direct assay Ref.8. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16189514Ref.19Ref.21. Source: IntAct

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 18319262. Source: IntAct

ubiquitin protein ligase binding

Inferred from physical interaction Ref.13. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 147147Bis(5'-adenosyl)-triphosphatase
PRO_0000109789

Regions

Domain2 – 109108HIT
Nucleotide binding89 – 924Substrate
Motif94 – 985Histidine triad motif

Sites

Active site961Tele-AMP-histidine intermediate Ref.12 Ref.20
Binding site81Substrate
Binding site271Substrate
Binding site831Substrate
Binding site981Substrate
Site1141Important for induction of apoptosis

Amino acid modifications

Modified residue1141Phosphotyrosine; by SRC Ref.14
Modified residue1451Phosphotyrosine Ref.14

Experimental info

Mutagenesis101I → W: Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-25. Ref.11
Mutagenesis251L → W: Reduces affinity for substrates and impairs apoptosis. Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-10. Ref.11
Mutagenesis351H → N: 50% decrease in catalytic activity. No loss in substrate binding. Ref.8
Mutagenesis941H → N: 75% decrease in catalytic activity. No loss in substrate binding. Ref.8
Mutagenesis961H → D: Loss of catalytic activity. Ref.8 Ref.11 Ref.12 Ref.21
Mutagenesis961H → G: Total loss of catalytic activity. Rescuable with free imidazole. Ref.8 Ref.11 Ref.12 Ref.21
Mutagenesis961H → N: Total loss of catalytic activity. No loss in substrate binding. Ref.8 Ref.11 Ref.12 Ref.21
Mutagenesis981H → N: 98% decrease in catalytic activity. Ref.8
Mutagenesis1141Y → A: Impairs induction of apoptosis. Strongly reduced affinity for substrates. Ref.14 Ref.15
Mutagenesis1141Y → D: Impairs induction of apoptosis. Reduces affinity for substrates. Ref.14 Ref.15
Mutagenesis1141Y → F: Loss of phosphorylation by SRC. Impairs induction of apoptosis. Ref.14 Ref.15
Mutagenesis1451Y → F: No effect on phosphorylation by SRC. Ref.14
Sequence conflict1461F → S in BAF82513. Ref.5

Secondary structure

.......................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49789 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 14D85961A19ECF3E

FASTA14716,858
        10         20         30         40         50         60 
MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL RPDEVADLFQ 

        70         80         90        100        110        120 
TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH 

       130        140 
DKEDFPASWR SEEEMAAEAA ALRVYFQ 

« Hide

References

« Hide 'large scale' references
[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., Trigg S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Fhit is a physiological target of the protein kinase Src."
Pekarsky Y., Garrison P.N., Palamarchuk A., Zanesi N., Aqeilan R.I., Huebner K., Barnes L.D., Croce C.M.
Proc. Natl. Acad. Sci. U.S.A. 101:3775-3779(2004) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46922 mRNA. Translation: AAA99013.1.
U76271 expand/collapse EMBL AC list , 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.
CCDSCCDS2894.1.
PIRA58802.
RefSeqNP_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.
UniGeneHs.655995.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP49789.
SMRP49789. Positions 2-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108563. 6 interactions.
DIPDIP-29947N.
IntActP49789. 8 interactions.
MINTMINT-150697.
STRING9606.ENSP00000342087.

Chemistry

BindingDBP49789.
ChEMBLCHEMBL1795151.

PTM databases

PhosphoSiteP49789.

Polymorphism databases

DMDM1706794.

Proteomic databases

MaxQBP49789.
PaxDbP49789.
PeptideAtlasP49789.
PRIDEP49789.

Protocols and materials databases

DNASU2272.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341848; ENSP00000342087; ENSG00000189283.
ENST00000468189; ENSP00000417480; ENSG00000189283.
ENST00000476844; ENSP00000417557; ENSG00000189283.
ENST00000492590; ENSP00000418582; ENSG00000189283.
ENST00000571334; ENSP00000458888; ENSG00000262683.
ENST00000571653; ENSP00000460853; ENSG00000262683.
ENST00000573237; ENSP00000461165; ENSG00000262683.
GeneID2272.
KEGGhsa:2272.
UCSCuc003dkx.4. human.

Organism-specific databases

CTD2272.
GeneCardsGC03M059712.
HGNCHGNC:3701. FHIT.
HPACAB002684.
HPA018840.
HPA018909.
MIM601153. gene.
neXtProtNX_P49789.
Orphanet151. Familial renal cell carcinoma.
PharmGKBPA28140.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0537.
HOGENOMHOG000164170.
HOVERGENHBG051614.
InParanoidP49789.
KOK01522.
OMADKWRTEE.
PhylomeDBP49789.
TreeFamTF105432.

Enzyme and pathway databases

SABIO-RKP49789.

Gene expression databases

ArrayExpressP49789.
BgeeP49789.
CleanExHS_FHIT.
GenevestigatorP49789.

Family and domain databases

Gene3D3.30.428.10. 1 hit.
InterProIPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
[Graphical view]
PANTHERPTHR23089. PTHR23089. 1 hit.
PfamPF01230. HIT. 1 hit.
[Graphical view]
SUPFAMSSF54197. SSF54197. 1 hit.
PROSITEPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFHIT. human.
EvolutionaryTraceP49789.
GeneWikiFHIT.
GenomeRNAi2272.
NextBio35461054.
PROP49789.
SOURCESearch...

Entry information

Entry nameFHIT_HUMAN
AccessionPrimary (citable) accession number: P49789
Secondary accession number(s): A2IAS9 expand/collapse secondary AC list , A2IAT0, A2IAT6, A8K1A9, Q45QG9, Q6IU12
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM