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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Glucokinase

UniprotKB/SwissProt ID: HXK4_HUMAN (P35557)

Gene Name: GCK

Organism: Homo sapiens (Human).

Function: Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization:

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Protein disease:
Disease database Database Entry Disease information
HPRD00680Diabetes mellitus, gestational
HPRD00680Diabetes mellitus, noninsulin-dependent, late-onset
HPRD00680Diabetes mellitus, permanent neonatal
HPRD00680Hyperinsulinemic hypoglycemia, familial, 3
HPRD00680Maturity-onset diabetes of the young, type II
Network with metabolic pathway:
Kegg map ID Pathway Link
map00010Glycolysis / Gluconeogenesis
map00052Galactose metabolism
map00500Starch and sucrose metabolism
map00520Amino sugar and nucleotide sugar metabolism
map00524Butirosin and neomycin biosynthesis
map04930Type II diabetes mellitus
map04950Maturity onset diabetes of the young
map04910Insulin signaling pathway
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR001312

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1GLK Model - A1-465Link
1V4S X-ray 2.30 A A16-465Link
1V4T X-ray 3.40 A A16-465Link
3A0I X-ray 2.20 A X16-465Link
3F9M X-ray 1.50 A A12-465Link
3FGU X-ray 2.15 A A12-465Link
3FR0 X-ray 2.70 A A16-465Link
3GOI X-ray 2.52 A A16-465Link
3H1V X-ray 2.11 A X16-465Link
3ID8 X-ray 2.40 A A12-465Link
3IDH X-ray 2.14 A A12-465Link
3IMX X-ray 2.00 A A16-465Link
3QIC X-ray 2.20 A A12-465Link
3S41 X-ray 2.18 A A12-465Link
3VEV X-ray 1.80 A A12-465Link
3VEY X-ray 2.25 A A16-465Link
3VF6 X-ray 1.86 A A12-465Link
4DCH X-ray 1.79 A A1-465Link
4DHY X-ray 2.38 A A12-465Link
4ISE X-ray 1.78 A A16-465Link
4ISF X-ray 2.09 A A16-465Link
4ISG X-ray 2.64 A A16-465Link
4IWV X-ray 2.10 A A16-465Link
4IXC X-ray 2.00 A A16-465Link
4L3Q X-ray 2.70 A A16-465Link
4LC9 X-ray 3.40 A B3-465Link
4MLE X-ray 2.60 A A16-465Link
4MLH X-ray 2.90 A A16-465Link

The S-nitrosylation sites of HXK4_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1371TTDCDIVRRA C ESVSTRAAHM HHHHHHHHHH H HHHHHHHHHH 3.67%HC0922178444-
2371TTDCDIVRRA C ESVSTRAAHM HHHHHHHHHH H HHHHHHHHHH 3.67%HC0912707306-
3371TTDCDIVRRA C ESVSTRAAHM HHHHHHHHHH H HHHHHHHHHH 3.67%HC0915688001-