Search by BoMiProt ID - Bomi6409


Primary Information

BoMiProt ID Bomi6409
Protein Name Inositol-tetrakisphosphate 1-kinase / Inositol 1,3,4-trisphosphate 5/6-kinase
Organism Bos taurus
Uniprot IDP0C0T1
Milk FractionWhey
Ref Sequence ID NP_001179418.1
Aminoacid Length 419
Molecular Weight 45842
FASTA Sequence Download
Gene Name ITPK1
Gene ID 518488
Protein Existence Status reviewed

Secondary Information

Protein Function ITPK1 is the rate limiting enzyme in the pathway leading to formation of the highly phosphorylated inositol phosphates including IP6 and the inositol pyrophosphates.It is a kinase that phosphorylates inositol polyphosphates such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. It forms Ins(1,3,4,5,6)P5 from Ins(3,4,5,6)P4 by phosphorylation at position 1.
Biochemical Properties 1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H+.Binds 2 magnesium ions per subunit as cofactor.KM=80 nM for Ins(1,3,4)P3 and Vmax=60 nmol/min/mg enzyme with Ins(1,3,4)P3 as substrate.
PTMs Acetylation and Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P0C0T1|ITPK1_BOVIN Inositol-tetrakisphosphate 1-kinase OS=Bos taurus OX=9913 GN=ITPK1 PE=1 SV=1 MQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGIEVVQLNLSRPIEEQGPLDVIIHKL TDVILEADQNDSQALELVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYM KDDRICSPPFMELTSLCGDDTMRLLEENGLAFPFICKTRVAHGTNSHEMAIVFNQEGLSA IQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVSKPES SSVLTALDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFP GYEGVSEFFTDLLNHIASVLQGQSSGVAGAGDVAPLKHSRLLAEQAGGLAAERTCSASPG CCSSMMGQEPPWTPEADMGGVGAGSTAKLPHQRLGCTAGVS*401PSFQQHCVASLATKASSQ
Predicted Disorder Regions (330-334), (358-391), (414-419)
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Acetylation by EP300 and CREBBP destabilizes ITPK1, and down-regulates enzymatic activity. Deacetylated by SIRT1
Bibliography Wilson, M. P., & Majerus, P. W. (1996). Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning and expression of the recombinant enzyme. The Journal of biological chemistry, 271(20), 11904–11910. https://doi.org/10.1074/jbc.271.20.11904