Search results for PKM

Showing 11 results out of 14

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Species

Types

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Reaction types

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Protein (6 results from a total of 9)

PKM

Identifier: R-HSA-6801387
Species: Homo sapiens
Compartment: ficolin-1-rich granule lumen
Primary external reference: UniProt: PKM: P14618

PKM

Identifier: R-HSA-6806491
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: PKM: P14618

PKM

Identifier: R-HSA-6801401
Species: Homo sapiens
Compartment: secretory granule lumen
Primary external reference: UniProt: PKM: P14618
Identifier: R-HSA-450658
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PKM: P14618
Identifier: R-HSA-71667
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PKM: P14618
Identifier: R-HSA-9861692
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PKM: P14618

Reaction (2 results from a total of 2)

Identifier: R-HSA-71670
Species: Homo sapiens
Compartment: cytosol
Cytosolic pyruvate kinase catalyzes the transfer of a high-energy phosphate from phosphoenolpyruvate to ADP, forming pyruvate and ATP. This reaction, an instance of substrate-level phosphorylation, is essentially irreversible under physiological conditions.

Four isozymes of human pyruvate kinase have been described, L, R, M1 and M2. Isozymes L and R are encoded by alternatively spliced transcripts of the PKLR gene; isozymes M1 and M2 are encoded by alternatively spliced transcripts of PKM2. In the body, L pyruvate kinase is found in liver (Tani et al. 1988), R in red blood cells (Kanno et al. 1991), M1 in muscle, heart and brain (Takenaka et al. 1991), and M2 in early fetal tissues and tumors (e.g., Lee et al. 2008). In all cases, the active form of the enzyme is a homotetramer, activated by fructose 1,6-bisphosphate (Valentini et al. 2002; Dombrauckas et al. 2005). Mutations in PKLR have been associated with hemolytic anemias (e.g., Zanella et al. 2005).

Identifier: R-HSA-9861640
Species: Homo sapiens
Compartment: cytosol
CTLH E3 ligase complex transfers multiple ubiquitin (Ub) units onto PKM-1 (PKM2), inhibiting pyruvate kinase activity. Which E2 enzyme and which ubiquitin linkage type are involved in these ubiquitination events remain an open question (Maitland et al., 2021). The CTLH complex consists of the proteins ARMC8, GID4, Muskelin, GID8, RANBP9, WDR26, and the catalytic subunits RMND5A or RMND5B and MAEA (Lampert et al., 2018; Maitland et al., 2019).

Interactor (1 results from a total of 1)

Identifier: Q99640-2
Species: Homo sapiens
Primary external reference: UniProt: Q99640-2

Pathway (1 results from a total of 1)

Identifier: R-HSA-3214841
Species: Homo sapiens
Lysine methyltransferases (KMTs) and arginine methyltransferases (RMTs) have a common mechanism of catalysis. Both families transfer a methyl group from a common donor, S-adenosyl-L-methionine (SAM), to the nitrogen atom on the epsilon-amino group of lysine or arginine (Smith & Denu 2009) using a bimolecular nucleophillic substitution (SN2) methyl transfer mechanism (Smith & Denu 2009, Zhang & Bruice 2008). All human KMTs except DOT1L (KMT4) (Feng et al. 2002, van Leeuwen et al. 2002, Lacoste et al. 2002) have a ~130 amino acid catalytic domain referred to as the SET domain (Del Rizzo & Trievel 2011, Dillon et al. 2005, Herz et al. 2013).

Some KMTs selectively methylate a particular lysine residue on a specific histone type. The extent of this methylation (mono-, di- or tri-methylation) also can be stringent (Herz et al. 2013, Copeland et al. 2009). Many KMTs also have non-histone substrates (Herz et al 2013), which are not discussed in this module.

The coordinates of post-translational modifications represented and described here follow UniProt standard practice whereby coordinates refer to the translated protein before any processing. Histone literature typically refers to specific residues by numbers which are determined after the initiating methionine has been removed. Therefore the coordinates of post-translated residues in the Reactome database and described here are frequently +1 when compared to the histone literature.

SET domain-containing proteins are classified in one of 7 families (Dillon et al. 2005). First to be discovered were the SUV39 family named after founding member SUV39H1 (KMT1A), which selectively methylates lysine-10 of histone H3 (H3K9) (Rea et al. 2000). Family member EHMT2 (KMT1C, G9A) is the predominant H3K9 methyltransferase in mammals (Tachibana et al. 2002). SETDB1 (KMT1E, ESET) also predominantly methylates H3K9, most effectively when complexed with ATF7IP (MCAF, hAM) (Wang et al. 2003).

SETD2 (KMT3A, HYPB), a member of the SET2 family, specifically methylates histone H3 lysine-37 (H3K36) (Sun et al. 2005). WHSC1 (KMT3G, NSD2, MMSET) a member of the same family, targets H3K36 when provided with nucleosome substrates but also can methylate histone H4 lysine-45 when octameric native or recombinant nucleosome substrates are provided (Li et al. 2009); dimethylation of histone H3 at lysine-37 (H3K36me2) is thought to be the principal chromatin-regulatory activity of WHSC1 (Kuo et al. 2011). Relatives NSD1 (KMT3B) and WHSC1L1 (KMT3F, NSD3) also methylate nucleosomal H3K36. NSD1 is active on unmethylated or a mimetic monomethylated H3K36, but not di- or trimethylated H3K36 mimetics (Li et al. 2009). Human SETD7 (KMT7, SET7/9), not classified within the 7 SET-domain containing families, mono-methylates lysine-5 of histone H3 (H3K4) (Xiao et al. 2003).

Icon (1 results from a total of 1)

Species: Homo sapiens
Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
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