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Sequence of IPMK_HUMAN

EC Number:2.7.1.140

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
inositol-tetrakisphosphate 5-kinase
Q8NFU5
Homo sapiens
416
47222
Reaction
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
Other sequences found for EC No. 2.7.1.140

EC Number:2.7.1.151

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
inositol-polyphosphate multikinase
Q8NFU5
Homo sapiens
416
47222
Reaction
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
Other sequences found for EC No. 2.7.1.151

EC Number:2.7.1.153

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
phosphatidylinositol-4,5-bisphosphate 3-kinase
Q8NFU5
Homo sapiens
416
47222
Reaction
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Other sequences found for EC No. 2.7.1.153

General information:

Sequence
show sequence in fasta format
  0 MATEPPSPLR VEAPGPPEMR TSPAIESTPE GTPQPAGGRL RFLNGCVPLS HQVAGHMYGK
 60 DKVGILQHPD GTVLKQLQPP PRGPRELEFY NMVYAADCFD GVLLELRKYL PKYYGIWSPP
120 TAPNDLYLKL EDVTHKFNKP CIMDVKIGQK SYDPFASSEK IQQQVSKYPL MEEIGFLVLG
180 MRVYHVHSDS YETENQHYGR SLTKETIKDG VSRFFHNGYC LRKDAVAASI QKIEKILQWF
240 ENQKQLNFYA SSLLFVYEGS SQPTTTKLND RTLAEKFLSK GQLSDTEVLE YNNNFHVLSS
300 TANGKIESSV GKSLSKMYAR HRKIYTKKHH SQTSLKVENL EQDNGWKSMS QEHLNGNVLS
360 QLEKVFYHLP TGCQEIAEVE VRMIDFAHVF PSNTIDEGYV YGLKHLISVL RSILDN
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
686447
Nalaskowski M.M.,Deschermeier C.,Fanick W.,Mayr G.W.
The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization.
Biochem. J.
366
549-556
2002
686448
Chang S.-C.,Miller A.L.,Feng Y.,Wente S.R.,Majerus P.W.
The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase.
J. Biol. Chem.
277
43836-43843
2002
686449
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
686450
Daub H.,Olsen J.V.,Bairlein M.,Gnad F.,Oppermann F.S.,Korner R.,Greff Z.,Keri G.,Stemmann O.,Mann M.
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
Mol. Cell
31
438-448
2008
686451
Oppermann F.S.,Gnad F.,Olsen J.V.,Hornberger R.,Greff Z.,Keri G.,Mann M.,Daub H.
Large-scale proteomics analysis of the human kinome.
Mol. Cell. Proteomics
8
1751-1764
2009
686452
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
686453
Dovey C.M.,Diep J.,Clarke B.P.,Hale A.T.,McNamara D.E.,Guo H.,Brown N.W. Jr.,Cao J.Y.,Grace C.R.,Gough P.J.,Bertin J.,Dixon S.J.,Fiedler D.,Mocarski E.S.,Kaiser W.J.,Moldoveanu T.,York J.D.,Carette J.E.
MLKL requires the inositol phosphate code to execute necroptosis.
Mol. Cell
70
936-948
2018
686454
Wang H.,Shears S.B.
Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities.
J. Biol. Chem.
292
18192-18202
2017
686455
Seacrist C.D.,Blind R.D.
Crystallographic and kinetic analyses of human IPMK reveal disordered domains modulate ATP binding and kinase activity.
Sci. Rep.
8
16672-16672
2018
686456
Gu C.,Stashko M.A.,Puhl-Rubio A.C.,Chakraborty M.,Chakraborty A.,Frye S.V.,Pearce K.H.,Wang X.,Shears S.B.,Wang H.
Inhibition of Inositol Polyphosphate Kinases by Quercetin and Related Flavonoids: A Structure-Activity Analysis.
J. Med. Chem.
62
1443-1454
2019