Harmonizome 3.0

DIS3 exosome endoribonuclease and 3'-5' exoribonuclease

Enables 3'-5'-RNA exonuclease activity; endonuclease activity; and guanyl-nucleotide exchange factor activity. Involved in CUT catabolic process; RNA processing; and rRNA catabolic process. Located in cytosol and nucleoplasm. Part of nuclear exosome (RNase complex). [provided by Alliance of Genome Resources, Mar 2025]

RNA component of mitochondrial RNA processing endoribonuclease

This gene encodes the RNA component of mitochondrial RNA processing endoribonuclease, which cleaves mitochondrial RNA at a priming site of mitochondrial DNA replication. This RNA also interacts with the telomerase reverse transcriptase catalytic subunit to form a distinct ribonucleoprotein complex that has RNA-dependent RNA polymerase activity and produces double-stranded RNAs that can be processed into small interfering RNA. Mutations in this gene are associated with cartilage-hair hypoplasia.[provided by RefSeq, Mar 2010]

SWT1 RNA endoribonuclease homolog (S. cerevisiae)

Predicted to be active in nucleus. [provided by Alliance of Genome Resources, Mar 2025]

phosphoglycerate mutase 1 (brain) pseudogene

This gene has characteristics of a retrotransposed pseudogene derived from the PGAM1 gene. [provided by RefSeq, Jul 2008]

phosphoglycerate mutase family member 5 pseudogene 1

phosphoglycerate mutase family member 4 pseudogene 1

phosphoglycerate mutase family member 4 pseudogene 2

phosphoglycerate mutase 1 pseudogene 5

phosphoglycerate mutase 1 pseudogene 4

phosphoglycerate mutase 1 pseudogene 9

phosphoglycerate mutase 3, pseudogene

methylmalonyl CoA mutase

This gene encodes the mitochondrial enzyme methylmalonyl Coenzyme A mutase. In humans, the product of this gene is a vitamin B12-dependent enzyme which catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, while in other species this enzyme may have different functions. Mutations in this gene may lead to various types of methylmalonic aciduria. [provided by RefSeq, Jul 2008]

phosphoglycerate mutase 1 (brain) pseudogene

This gene has characteristics of a retrotransposed pseudogene derived from the PGAM1 gene. [provided by RefSeq, Jul 2008]

phosphoglycerate mutase family member 5 pseudogene

phosphoglycerate mutase 1 pseudogene 7

phosphoglycerate mutase 1 pseudogene 1

phosphoglycerate mutase 1 pseudogene 3

phosphoglycerate mutase 1 pseudogene 2

phosphoglycerate mutase 1 pseudogene 8

phosphoglycerate mutase 1 (brain)

The protein encoded by this gene is a mutase that catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015]

phosphoglycerate mutase family member 4

This intronless gene appears to have arisen from a retrotransposition event, yet it is thought to be an expressed, protein-coding gene. The encoded protein is a member of the phosphoglycerate mutase family, a set of enzymes that catalyze the transfer of a phosphate group from 3-phosphoglycerate to 2-phosphoglycerate. [provided by RefSeq, May 2010]

phosphoglycerate mutase family member 5

Enables GTPase activator activity and protein serine/threonine phosphatase activity. Involved in necroptotic process. Located in mitochondrial inner membrane. [provided by Alliance of Genome Resources, Mar 2025]

phosphoglycerate mutase 2 (muscle)

Phosphoglycerate mutase (PGAM) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. The PGAM is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). This gene encodes muscle-specific PGAM subunit. Mutations in this gene cause muscle phosphoglycerate mutase eficiency, also known as glycogen storage disease X. [provided by RefSeq, Sep 2009]

2,3-bisphosphoglycerate mutase

2,3-diphosphoglycerate (2,3-DPG) is a small molecule found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. This gene encodes a multifunctional enzyme that catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. The enzyme also has phosphoglycerate phosphomutase activity. Deficiency of this enzyme increases the affinity of cells for oxygen. Mutations in this gene result in hemolytic anemia. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Sep 2009]

phosphoglycerate mutase 1 pseudogene 6

phosphoglycerate mutase 1 pseudogene 11

phosphoglycerate mutase 1 pseudogene 10

phosphoglycerate mutase 1 pseudogene 13

phosphoglycerate mutase 1 pseudogene 12

methylmalonyl-CoA mutase

This gene encodes the mitochondrial enzyme methylmalonyl Coenzyme A mutase. In humans, the product of this gene is a vitamin B12-dependent enzyme which catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, while in other species this enzyme may have different functions. Mutations in this gene may lead to various types of methylmalonic aciduria. [provided by RefSeq, Jul 2008]

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Endoribonuclease L-PSP/chorismate mutase-like protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Methylmalonic Aciduria due to Methylmalonyl-CoA Mutase Deficiency from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease BISPHOSPHOGLYCERATE MUTASE DEFICIENCY from the curated CTD Gene-Disease Associations dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term mutase in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Molecular Function Annotations 2015

genes performing the bisphosphoglycerate mutase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphoglycerate mutase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphoacetylglucosamine mutase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the methylmalonyl-coa mutase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From HPO Gene-Disease Associations

genes associated with the decreased methylmalonyl-coa mutase activity phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Methylmalonyl-CoA mutase, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphoglycerate/bisphosphoglycerate mutase, active site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphoglycerate mutase 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosphoacetylglucosamine mutase protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Methylmalonyl-CoA mutase, alpha/beta chain, catalytic protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Methylmalonyl-CoA mutase, alpha chain, catalytic protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From OMIM Gene-Disease Associations

genes associated with the erythrocytosis due to bisphosphoglycerate mutase deficiency phenotype from the curated OMIM Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Deficiency Of Bisphosphoglycerate Mutase in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Methylmalonyl-Coenzyme A Mutase Deficiency in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Decreased Methylmalonyl-Coa Mutase Activity in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From GO Molecular Function Annotations 2023

genes performing the phosphoacetylglucosamine mutase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the bisphosphoglycerate mutase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the phosphoglycerate mutase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the methylmalonyl-CoA mutase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2025

genes performing the phosphoacetylglucosamine mutase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the bisphosphoglycerate mutase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the phosphoglycerate mutase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the methylmalonyl-CoA mutase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores 2025

genes co-occuring with the disease Methylmalonic aciduria due to methylmalonyl-CoA mutase deficiency in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Methylmalonic aciduria due to methylmalonyl-CoA mutase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Methylmalonic aciduria due to complete methylmalonyl-CoA mutase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the endoribonuclease complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the endoribonuclease complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term endoribonuclease in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of endoribonuclease activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of endoribonuclease activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the endoribonuclease complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the endoribonuclease activity, cleaving mirna-paired mrna molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the endoribonuclease activity, producing 3'-phosphomonoesters molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the endoribonuclease activity, cleaving sirna-paired mrna molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the endoribonuclease activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the endoribonuclease inhibitor activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the endoribonuclease activity, producing 5'-phosphomonoesters molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Endoribonuclease YbeY, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Endoribonuclease YbeY protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Endoribonuclease XendoU protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of endoribonuclease activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of endoribonuclease activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of endoribonuclease activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the endoribonuclease complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the endoribonuclease inhibitor activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the endoribonuclease activity, cleaving miRNA-paired mRNA molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the endoribonuclease activity, cleaving siRNA-paired mRNA molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the 3'-tRNA processing endoribonuclease activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of endoribonuclease activity biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of endoribonuclease activity biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of endoribonuclease activity biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the endoribonuclease complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the endoribonuclease inhibitor activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the endoribonuclease activity, cleaving miRNA-paired mRNA molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the endoribonuclease activity, cleaving siRNA-paired mRNA molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the 3'-tRNA processing endoribonuclease activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Endoribonuclease complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Endoribonuclease complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.