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Sequence of NIT2_MOUSE

EC Number:3.5.1.3

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
omega-amidase
Q9JHW2
Mus musculus
276
30502
Reaction
a monoamide of a dicarboxylate + H2O = a dicarboxylate + NH3
Other sequences found for EC No. 3.5.1.3

General information:

Sequence
show sequence in fasta format
  0 MSTFRLALIQ LQVSSIKSDN LTRACSLVRE AAKQGANIVS LPECFNSPYG TTYFPDYAEK
 60 IPGESTQKLS EVAKESSIYL IGGSIPEEDA GKLYNTCSVF GPDGSLLVKH RKIHLFDIDV
120 PGKITFQESK TLSPGDSFST FDTPYCKVGL GICYDMRFAE LAQIYAQRGC QLLVYPGAFN
180 LTTGPAHWEL LQRARAVDNQ VYVATASPAR DDKASYVAWG HSTVVDPWGQ VLTKAGTEET
240 ILYSDIDLKK LAEIRQQIPI LKQKRADLYT VESKKP
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1220599
Pace H.C.,Hodawadekar S.C.,Draganescu A.,Huang J.,Bieganowski P.,Pekarsky Y.,Croce C.M.,Brenner C.
Crystal structure of the worm NitFhit Rosetta stone protein reveals a Nit tetramer binding two Fhit dimers.
Curr. Biol.
10
907-917
2000
1220600
Carninci P.,Kasukawa T.,Katayama S.,Gough J.,Frith M.C.,Maeda N.,Oyama R.,Ravasi T.,Lenhard B.,Wells C.,Kodzius R.,Shimokawa K.,Bajic V.B.,Brenner S.E.,Batalov S.,Forrest A.R.,Zavolan M.,Davis M.J.,Wilming L.G.,Aidinis V.,Allen J.E.,Ambesi-Impiombato A.,Apweiler R.,Aturaliya R.N.,Bailey T.L.,Bansal M.,Baxter L.,Beisel K.W.,Bersano T.,Bono H.,Chalk A.M.,Chiu K.P.,Choudhary V.,Christoffels A.,Clutterbuck D.R.,Crowe M.L.,Dalla E.,Dalrymple B.P.,de Bono B.,Della Gatta G.,di Bernardo D.,Down T.,Engstrom P.,Fagiolini M.,Faulkner G.,Fletcher C.F.,Fukushima T.,Furuno M.,Futaki S.,Gariboldi M.,Georgii-Hemming P.,Gingeras T.R.,Gojobori T.,Green R.E.,Gustincich S.,Harbers M.,Hayashi Y.,Hensch T.K.,Hirokawa N.,Hill D.,Huminiecki L.,Iacono M.,Ikeo K.,Iwama A.,Ishikawa T.,Jakt M.,Kanapin A.,Katoh M.,Kawasawa Y.,Kelso J.,Kitamura H.,Kitano H.,Kollias G.,Krishnan S.P.,Kruger A.,Kummerfeld S.K.,Kurochkin I.V.,Lareau L.F.,Lazarevic D.,Lipovich L.,Liu J.,Liuni S.,McWilliam S.,Madan Babu M.,Madera M.,Marchionni L.,Matsuda H.,Matsuzawa S.,Miki H.,Mignone F.,Miyake S.,Morris K.,Mottagui-Tabar S.,Mulder N.,Nakano N.,Nakauchi H.,Ng P.,Nilsson R.,Nishiguchi S.,Nishikawa S.,Nori F.,Ohara O.,Okazaki Y.,Orlando V.,Pang K.C.,Pavan W.J.,Pavesi G.,Pesole G.,Petrovsky N.,Piazza S.,Reed J.,Reid J.F.,Ring B.Z.,Ringwald M.,Rost B.,Ruan Y.,Salzberg S.L.,Sandelin A.,Schneider C.,Schoenbach C.,Sekiguchi K.,Semple C.A.,Seno S.,Sessa L.,Sheng Y.,Shibata Y.,Shimada H.,Shimada K.,Silva D.,Sinclair B.,Sperling S.,Stupka E.,Sugiura K.,Sultana R.,Takenaka Y.,Taki K.,Tammoja K.,Tan S.L.,Tang S.,Taylor M.S.,Tegner J.,Teichmann S.A.,Ueda H.R.,van Nimwegen E.,Verardo R.,Wei C.L.,Yagi K.,Yamanishi H.,Zabarovsky E.,Zhu S.,Zimmer A.,Hide W.,Bult C.,Grimmond S.M.,Teasdale R.D.,Liu E.T.,Brusic V.,Quackenbush J.,Wahlestedt C.,Mattick J.S.,Hume D.A.,Kai C.,Sasaki D.,Tomaru Y.,Fukuda S.,Kanamori-Katayama M.,Suzuki M.,Aoki J.,Arakawa T.,Iida J.,Imamura K.,Itoh M.,Kato T.,Kawaji H.,Kawagashira N.,Kawashima T.,Kojima M.,Kondo S.,Konno H.,Nakano K.,Ninomiya N.,Nishio T.,Okada M.,Plessy C.,Shibata K.,Shiraki T.,Suzuki S.,Tagami M.,Waki K.,Watahiki A.,Okamura-Oho Y.,Suzuki H.,Kawai J.,Hayashizaki Y.
The transcriptional landscape of the mammalian genome.
Science
309
1559-1563
2005
1220601
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
1220602
Jaisson S.,Veiga-da-Cunha M.,Van Schaftingen E.
Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2.
Biochimie
91
1066-1071
2009
1220603
Krasnikov B.F.,Chien C.-H.,Nostramo R.,Pinto J.T.,Nieves E.,Callaway M.,Sun J.,Huebner K.,Cooper A.J.L.
Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination.
Biochimie
91
1072-1080
2009
1220604
Huttlin E.L.,Jedrychowski M.P.,Elias J.E.,Goswami T.,Rad R.,Beausoleil S.A.,Villen J.,Haas W.,Sowa M.E.,Gygi S.P.
A tissue-specific atlas of mouse protein phosphorylation and expression.
Cell
143
1174-1189
2010
1220605
Park J.,Chen Y.,Tishkoff D.X.,Peng C.,Tan M.,Dai L.,Xie Z.,Zhang Y.,Zwaans B.M.,Skinner M.E.,Lombard D.B.,Zhao Y.
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.
Mol. Cell
50
919-930
2013
1220606
Rardin M.J.,Newman J.C.,Held J.M.,Cusack M.P.,Sorensen D.J.,Li B.,Schilling B.,Mooney S.D.,Kahn C.R.,Verdin E.,Gibson B.W.
Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Proc. Natl. Acad. Sci. U.S.A.
110
6601-6606
2013
1220607
Peracchi A.,Veiga-da-Cunha M.,Kuhara T.,Ellens K.W.,Paczia N.,Stroobant V.,Seliga A.K.,Marlaire S.,Jaisson S.,Bommer G.T.,Sun J.,Huebner K.,Linster C.L.,Cooper A.J.L.,Van Schaftingen E.
Nit1 is a metabolite repair enzyme that hydrolyzes deaminated glutathione.
Proc. Natl. Acad. Sci. U.S.A.
114
0-0
2017
1220608
Barglow K.T.,Saikatendu K.S.,Bracey M.H.,Huey R.,Morris G.M.,Olson A.J.,Stevens R.C.,Cravatt B.F.
Functional proteomic and structural insights into molecular recognition in the nitrilase family enzymes.
Biochemistry
47
13514-13523
2008