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Literature summary for 2.7.12.1 extracted from

  • Heizmann, B; Reth, M.; Infantino, S.
    Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor (2010), Proc. Natl. Acad. Sci. USA, 107, 18563-18568.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + a protein Homo sapiens
-
ADP + a phosphoprotein
-
?
ATP + adaptor protein SH2 domain-containing leukocyte protein Homo sapiens phosphorylation of SLP-65 on several tyrosines ADP + phospho-[adaptor protein SH2 domain-containing leukocyte protein]
-
?
ATP + immunglobulin-alpha Homo sapiens the inhibitory residue of Ig-alpha S197 is phosphorylated in activated B cells by Syk ADP + phospho-[immunglobulin-alpha]
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P43405 cf. EC 2.7.10.2
-

Source Tissue

Source Tissue Comment Organism Textmining
B-lymphocyte
-
Homo sapiens
-
spleen
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + a protein
-
Homo sapiens ADP + a phosphoprotein
-
?
ATP + a protein enzyme Syk phosphoryles serine and tyrosine residues Homo sapiens ADP + a phosphoprotein
-
?
ATP + adaptor protein SH2 domain-containing leukocyte protein
-
Homo sapiens ADP + phospho-[adaptor protein SH2 domain-containing leukocyte protein]
-
?
ATP + adaptor protein SH2 domain-containing leukocyte protein phosphorylation of SLP-65 on several tyrosines Homo sapiens ADP + phospho-[adaptor protein SH2 domain-containing leukocyte protein]
-
?
ATP + immunglobulin-alpha the inhibitory residue of Ig-alpha S197 is phosphorylated in activated B cells by Syk Homo sapiens ADP + phospho-[immunglobulin-alpha]
-
?
ATP + immunglobulin-alpha phosphorylation of tyrosines of Ig-alpha and Ig-beta and on Ser197, immunohistochemic determination of phosphorylation site Ser197 Homo sapiens ADP + phospho-[immunglobulin-alpha]
-
?
additional information autophosphorylation of Syk at Tyr630 Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Spleen tyrosine kinase
-
Homo sapiens
Syk cf. EC 2.7.10.2 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens

General Information

General Information Comment Organism
additional information rebuilding of the BCR receptor complex in S2 Drodophila melanogster system and phosphorylation and analysis with Syk overview Homo sapiens
physiological function Syk is a dual-specificity kinase, phosphorylating serine and tyrosine residues, that self-regulates the signal output from the B-cell antigen receptor. The B-cell antigen receptor (BCR) comprises the membrane-bound Ig molecule and the Ig-alpha/Ig-beta heterodimer, which function as the ligand-binding and signaling subunits, respectively. The cytoplasmic tails of Ig-alpha and Ig-beta contain an immunoreceptor tyrosine-based activation motif. The ITAM tyrosines of Ig-alpha and Ig-beta are phosphorylated by Syk. And enzyme Syk (spleen tyrosine kinase) phosphorylates S197 on Ig-alpha, not only activating but also inhibiting signaling from the B-cell antigen receptor. Phosphorylation of S197 in the Ig-alpha cytoplasmic tail plays a negative role in B-cell antigen receptor (BCR) activation Homo sapiens