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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: Pyruvate kinase PKM

UniprotKB/SwissProt ID: KPYM_HUMAN (P14618)

Gene Name: PKM

Synonyms: OIP3, PK2, PK3, PKM2

Organism: Homo sapiens (Human).

Function: Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus. Note=Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity.

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

Network with metabolic pathway:
Kegg map ID Pathway Link
map00010Glycolysis / Gluconeogenesis
map00230Purine metabolism
map00620Pyruvate metabolism
map04930Type II diabetes mellitus
map05203Viral carcinogenesis
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR001697
IPR011037
IPR015793
IPR015794
IPR015795
IPR015813

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1T5A X-ray 2.80 A A/B/C/D1-531Link
1ZJH X-ray 2.20 A A3-530Link
3BJF X-ray 2.03 A A/B/C/D14-531Link
3BJT X-ray 2.50 A A/B/C/D2-531Link
3G2G X-ray 2.00 A A/B/C/D1-531Link
3GQY X-ray 1.85 A A/B/C/D1-531Link
3GR4 X-ray 1.60 A A/B/C/D1-531Link
3H6O X-ray 2.00 A A/B/C/D1-531Link
3ME3 X-ray 1.95 A A/B/C/D1-531Link
3SRD X-ray 2.90 A A/B/C/D1-531Link
3SRF X-ray 2.84 A A/B/C/D/E/F/G/H1-531Link
3SRH X-ray 2.60 A A/B/C/D1-531Link
3U2Z X-ray 2.10 A A/B/C/D1-531Link
4B2D X-ray 2.30 A A/B/C/D2-531Link
4FXF X-ray 2.55 A A/B/C/D1-531Link
4FXJ X-ray 2.90 A A/B/C/D1-531Link
4G1N X-ray 2.30 A A/B/C/D14-531Link
4JPG X-ray 2.33 A A/B/C/D1-531Link

The S-nitrosylation sites of KPYM_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1152ITLDNAYMEK C DENILWLDYK EEECHHHCCC C CCCEEEECCC 5.17%HC0219483679in vivo
2326RCNRAGKPVI C ATQMLESMIK HHHHHCCCEE E EEHHHHHHHC 3.23%HC1125040305in vivo
3423AVGAVEASFK C CSGAIIVLTK HHHHHHHHHH C CCCEEEEEEC 1.79%HC0219483679in vivo
4424VGAVEASFKC C SGAIIVLTKS HHHHHHHHHC C CCEEEEEECC 4.30%HC0919483679in vivo
5474HLYRGIFPVL C KDPVQEAWAE CEEECEEEEE E CCCCCCCCHH 4.84%HC1119483679in vivo