UniProt functional annotation for P06744



	UniProt functional annotation for P06744

UniProt code: P06744.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: In the cytoplasm, catalyzes the conversion of glucose-6- phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:3352745, PubMed:11004567). It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:3352745, PubMed:11004567). {ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:11437381, ECO:0000269|PubMed:28803808, ECO:0000269|PubMed:3352745}.

Catalytic activity: Reaction=aldehydo-D-glucose 6-phosphate = keto-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57579, ChEBI:CHEBI:57584; EC=5.3.1.9; Evidence={ECO:0000269|PubMed:28803808};

Activity regulation: Strongly inhibited by erythrose 4-phosphate. {ECO:0000269|PubMed:12054796}.

Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000269|PubMed:28803808}.

Subunit: Homodimer; in the catalytically active form (PubMed:11371164, PubMed:12054796, PubMed:12777791). Monomer in the secreted form (PubMed:11371164, PubMed:12054796, PubMed:12777791). {ECO:0000269|PubMed:11371164, ECO:0000269|PubMed:12054796, ECO:0000269|PubMed:12777791}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:11437381}. Secreted {ECO:0000269|PubMed:11437381}.

Ptm: Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway. {ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:15637053}.

Ptm: ISGylated. {ECO:0000269|PubMed:16139798}.

Disease: Hemolytic anemia, non-spherocytic, due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:613470]: A form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. {ECO:0000269|PubMed:28803808, ECO:0000269|PubMed:7989588, ECO:0000269|PubMed:8499925, ECO:0000269|PubMed:8822952, ECO:0000269|PubMed:8822954, ECO:0000269|PubMed:9446754, ECO:0000269|PubMed:9856489}. Note=The disease is caused by variants affecting the gene represented in this entry.

Similarity: Belongs to the GPI family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		In the cytoplasm, catalyzes the conversion of glucose-6- phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:3352745, PubMed:11004567). It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:3352745, PubMed:11004567). {ECO:0000269\|PubMed:11004567, ECO:0000269\|PubMed:11437381, ECO:0000269\|PubMed:28803808, ECO:0000269\|PubMed:3352745}.


Catalytic activity:		Reaction=aldehydo-D-glucose 6-phosphate = keto-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57579, ChEBI:CHEBI:57584; EC=5.3.1.9; Evidence={ECO:0000269\|PubMed:28803808};
Activity regulation:		Strongly inhibited by erythrose 4-phosphate. {ECO:0000269\|PubMed:12054796}.
Pathway:		Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000269\|PubMed:28803808}.
Subunit:		Homodimer; in the catalytically active form (PubMed:11371164, PubMed:12054796, PubMed:12777791). Monomer in the secreted form (PubMed:11371164, PubMed:12054796, PubMed:12777791). {ECO:0000269\|PubMed:11371164, ECO:0000269\|PubMed:12054796, ECO:0000269\|PubMed:12777791}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:11437381}. Secreted {ECO:0000269\|PubMed:11437381}.
Ptm:		Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway. {ECO:0000269\|PubMed:11004567, ECO:0000269\|PubMed:15637053}.
Ptm:		ISGylated. {ECO:0000269\|PubMed:16139798}.
Disease:		Hemolytic anemia, non-spherocytic, due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:613470]: A form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. {ECO:0000269\|PubMed:28803808, ECO:0000269\|PubMed:7989588, ECO:0000269\|PubMed:8499925, ECO:0000269\|PubMed:8822952, ECO:0000269\|PubMed:8822954, ECO:0000269\|PubMed:9446754, ECO:0000269\|PubMed:9856489}. Note=The disease is caused by variants affecting the gene represented in this entry.
Similarity:		Belongs to the GPI family. {ECO:0000305}.