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Sequence of FHIT_HUMAN

EC Number:2.7.7.51

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
adenylylsulfate-ammonia adenylyltransferase
P49789
Homo sapiens
147
16858
Reaction
adenylyl sulfate + NH3 = adenosine 5'-phosphoramidate + sulfate
Other sequences found for EC No. 2.7.7.51

General information:

Sequence
show sequence in fasta format
  0 MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL RPDEVADLFQ
 60 TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH
120 DKEDFPASWR SEEEMAAEAA ALRVYFQ
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
671410
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.
The FHIT gene, spanning the chromosome 3p14.2 fragile site and renal carcinoma-associated t(3;8) breakpoint, is abnormal in digestive tract cancers.
Cell
84
587-597
1996
671411
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.
Structure and expression of the human FHIT gene in normal and tumor cells.
Cancer Res.
57
504-512
1997
671412
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.
Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism.
Nat. Commun.
5
3650-3650
2014
671414
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.
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet.
36
40-45
2004
671416
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
671417
Barnes L.D.,Garrison P.N.,Siprashvili Z.,Guranowski A.,Robinson A.K.,Ingram S.W.,Croce C.M.,Ohta M.,Huebner K.
Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5''-P1,P3-triphosphate hydrolase.
Biochemistry
35
11529-11535
1996
671418
Brenner C.,Pace H.C.,Garrison P.N.,Robinson A.K.,Rosler A.,Liu X.H.,Blackburn G.M.,Croce C.M.,Huebner K.,Barnes L.D.
Purification and crystallization of complexes modeling the active state of the fragile histidine triad protein.
Protein Eng.
10
1461-1463
1997
671419
Gemmill R.M.,West J.D.,Boldog F.,Tanaka N.,Robinson L.J.,Smith D.I.,Li F.,Drabkin H.A.
The hereditary renal cell carcinoma 3;8 translocation fuses FHIT to a patched-related gene, TRC8.
Proc. Natl. Acad. Sci. U.S.A.
95
9572-9577
1998
671420
Shi Y.,Zou M.,Farid N.R.,Paterson M.C.
Association of FHIT (fragile histidine triad), a candidate tumour suppressor gene, with the ubiquitin-conjugating enzyme hUBC9.
Biochem. J.
352
443-448
2000
671421
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.
Designed FHIT alleles establish that Fhit-induced apoptosis in cancer cells is limited by substrate binding.
Proc. Natl. Acad. Sci. U.S.A.
100
1592-1597
2003
671422
Huang K.,Arabshahi A.,Wei Y.,Frey P.A.
The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit.
Biochemistry
43
7637-7642
2004
671423
Nishizaki M.,Sasaki J.,Fang B.,Atkinson E.N.,Minna J.D.,Roth J.A.,Ji L.
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.
Cancer Res.
64
5745-5752
2004
671424
Pekarsky Y.,Garrison P.N.,Palamarchuk A.,Zanesi N.,Aqeilan R.I.,Huebner K.,Barnes L.D.,Croce C.M.
Fhit is a physiological target of the protein kinase Src.
Proc. Natl. Acad. Sci. U.S.A.
101
3775-3779
2004
671425
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.
Fhit modulation of the Akt-survivin pathway in lung cancer cells: Fhit-tyrosine 114 (Y114) is essential.
Oncogene
25
2860-2872
2006
671426
Weiske J.,Albring K.F.,Huber O.
The tumor suppressor Fhit acts as a repressor of beta-catenin transcriptional activity.
Proc. Natl. Acad. Sci. U.S.A.
104
20344-20349
2007
671427
Guranowski A.,Wojdyla A.M.,Pietrowska-Borek M.,Bieganowski P.,Khurs E.N.,Cliff M.J.,Blackburn G.M.,Blaziak D.,Stec W.J.
Fhit proteins can also recognize substrates other than dinucleoside polyphosphates.
FEBS Lett.
582
3152-3158
2008
671428
Rimessi A.,Marchi S.,Fotino C.,Romagnoli A.,Huebner K.,Croce C.M.,Pinton P.,Rizzuto R.
Intramitochondrial calcium regulation by the FHIT gene product sensitizes to apoptosis.
Proc. Natl. Acad. Sci. U.S.A.
106
12753-12758
2009
671429
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
671430
Wojdyla-Mamon A.M.,Guranowski A.
Adenylylsulfate-ammonia adenylyltransferase activity is another inherent property of Fhit proteins.
Biosci. Rep.
35
0-0
2015
671431
Lima C.D.,D'Amico K.L.,Naday I.,Rosenbaum G.,Westbrook E.M.,Hendrickson W.A.
MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family.
Structure
5
763-774
1997
671432
Lima C.D.,Klein M.G.,Hendrickson W.A.
Structure-based analysis of catalysis and substrate definition in the HIT protein family.
Science
278
286-290
1997
671433
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.
Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit.
Proc. Natl. Acad. Sci. U.S.A.
95
5484-5489
1998