Harmonizome 3.0

fat storage-inducing transmembrane protein 2

Enables coenzyme A diphosphatase activity. Involved in several processes, including fatty-acyl-CoA catabolic process; lipid droplet formation; and lipid homeostasis. Predicted to be located in endoplasmic reticulum and membrane. Predicted to be active in endoplasmic reticulum membrane. Implicated in Siddiqi syndrome. [provided by Alliance of Genome Resources, Mar 2025]

fat storage-inducing transmembrane protein 1

Predicted to enable diacylglycerol binding activity and triglyceride binding activity. Predicted to be involved in lipid droplet formation; phospholipid biosynthetic process; and positive regulation of sequestering of triglyceride. Predicted to be located in endoplasmic reticulum and membrane. Predicted to be active in endoplasmic reticulum membrane. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) subunit, beta type, 9

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. This gene is located in the class II region of the MHC (major histocompatibility complex). Expression of this gene is induced by gamma interferon and this gene product replaces catalytic subunit 1 (proteasome beta 6 subunit) in the immunoproteasome. Proteolytic processing is required to generate a mature subunit. [provided by RefSeq, Mar 2010]

proteasome (prosome, macropain) subunit, beta type, 8

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. This gene is located in the class II region of the MHC (major histocompatibility complex). Expression of this gene is induced by gamma interferon and this gene product replaces catalytic subunit 3 (proteasome beta 5 subunit) in the immunoproteasome. Proteolytic processing is required to generate a mature subunit. Two alternative transcripts encoding two isoforms have been identified; both isoforms are processed to yield the same mature subunit. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) subunit, beta type, 7

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. The encoded protein is a member of the proteasome B-type family, also known as the T1B family, and is a 20S core beta subunit in the proteasome. Expression of this catalytic subunit is downregulated by gamma interferon, and proteolytic processing is required to generate a mature subunit. A pseudogene of this gene is located on the long arm of chromosome 14. [provided by RefSeq, Jul 2012]

proteasome (prosome, macropain) subunit, beta type, 6

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. The encoded protein is a member of the proteasome B-type family, also known as the T1B family, and is a 20S core beta subunit in the proteasome. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jul 2012]

proteasome (prosome, macropain) subunit, beta type, 5

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit in the proteasome. This catalytic subunit is not present in the immunoproteasome and is replaced by catalytic subunit 3i (proteasome beta 8 subunit). Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2009]

proteasome (prosome, macropain) subunit, beta type, 4

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) subunit, beta type, 3

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. The 26 S proteasome may be involved in trinucleotide repeat expansion, a phenomenon which is associated with many hereditary neurological diseases. Pseudogenes have been identified on chromosomes 2 and 12. Alternative splicing results in multiple transcript variants [provided by RefSeq, Sep 2013]

proteasome (prosome, macropain) subunit, beta type, 2

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Dec 2010]

proteasome (prosome, macropain) subunit, beta type, 1

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. This gene is tightly linked to the TBP (TATA-binding protein) gene in human and in mouse, and is transcribed in the opposite orientation in both species. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 14

This gene encodes a component of the 26S proteasome. The 26S proteasome is a large multiprotein complex that catalyzes the degradation of ubiquitinated intracellular proteins. The encoded protein is a component of the 19S regulatory cap complex of the 26S proteasome and mediates substrate deubiquitination. A pseudogene of this gene is also located on the long arm of chromosome 2. [provided by RefSeq, Feb 2012]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 11

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a member of the proteasome subunit S9 family that functions as a non-ATPase subunit of the 19S regulator and is phosphorylated by AMP-activated protein kinase. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, Jul 2012]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 10

This gene encodes a subunit of the PA700/19S complex, which is the regulatory component of the 26S proteasome. The 26S proteosome complex is required for ubiquitin-dependent protein degradation. This protein is a non-ATPase subunit that may be involved in protein-protein interactions. Aberrant expression of this gene may paly a role in tumorigenesis. Two transcripts encoding different isoforms have been described. Pseudogenes have been identified on chromosomes 3 and 20.[provided by RefSeq, Mar 2011]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 13

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. Two transcripts encoding different isoforms have been described. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 12

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 3. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2015]

proteasome (prosome, macropain) subunit, beta type, 3 pseudogene

proteasome activator subunit 2 pseudogene 6

proteasome activator subunit 2 pseudogene 4

proteasome activator subunit 2 pseudogene 3

proteasome (prosome, macropain) assembly chaperone 4

Predicted to be involved in proteasome assembly. Predicted to be part of protein-containing complex. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) assembly chaperone 1

Enables molecular adaptor activity. Involved in chaperone-mediated protein complex assembly. Located in several cellular components, including Golgi apparatus; endoplasmic reticulum; and nucleoplasm. Part of protein folding chaperone complex. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) assembly chaperone 2

Enables molecular adaptor activity. Involved in chaperone-mediated protein complex assembly. Located in nucleus. Part of protein folding chaperone complex. Implicated in proteosome-associated autoinflammatory syndrome 4. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) assembly chaperone 3

Enables molecular adaptor activity. Involved in chaperone-mediated protein complex assembly. Predicted to be part of protein-containing complex. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) subunit, alpha type, 2 pseudogene 3

proteasome (prosome, macropain) subunit, alpha type, 2 pseudogene 1

proteasome (prosome, macropain) subunit, alpha type, 2 pseudogene 2

proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 pseudogene

proteasome 26S subunit, non-ATPase, 10 pseudogene 3

proteasome 26S subunit, non-ATPase, 10 pseudogene 2

proteasome 26S subunit, non-ATPase, 10 pseudogene 1

proteasome (prosome, macropain) 26S subunit, non-ATPase, 8

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 1. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 5

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a non-ATPase subunit of the 19S regulator base that functions as a chaperone protein during 26S proteasome assembly. [provided by RefSeq, Jul 2012]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 4

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the non-ATPase subunits of the 19S regulator lid. Pseudogenes have been identified on chromosomes 10 and 21. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 7

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 17. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 6

This gene encodes a member of the protease subunit S10 family. The encoded protein is a subunit of the 26S proteasome which colocalizes with DNA damage foci and is involved in the ATP-dependent degradation of ubiquinated proteins. Alternative splicing results in multiple transcript variants [provided by RefSeq, Nov 2012]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 1

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes the largest non-ATPase subunit of the 19S regulator lid, which is responsible for substrate recognition and binding. There is evidence that this proteasome and its subunits interact with viral proteins, including those of coronaviruses. Alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Aug 2020]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 3

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a member of the proteasome subunit S3 family that functions as one of the non-ATPase subunits of the 19S regulator lid. Single nucleotide polymorphisms in this gene are associated with neutrophil count. [provided by RefSeq, Jul 2012]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 2

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the non-ATPase subunits of the 19S regulator lid. In addition to participation in proteasome function, this subunit may also participate in the TNF signalling pathway since it interacts with the tumor necrosis factor type 1 receptor. A pseudogene has been identified on chromosome 1. Alternative splicing results in multiple transcript variants of this gene. [provided by RefSeq, Jul 2013]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 4 pseudogene 1

proteasome (prosome, macropain) subunit, alpha type, 3

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. Two alternative transcripts encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) subunit, beta type, 11

Proteasomes generate peptides that are presented by major histocompatibility complex (MHC) I molecules to other cells of the immune system. Proteolysis is conducted by 20S proteasomes, complexes of 28 subunits arranged as a cylinder in 4 heteroheptameric rings: alpha-1 to -7, beta-1 to -7, beta-1 to -7, and alpha-1 to -7. The catalytic subunits are beta-1 (PSMB6; MIM 600307), beta-2 (PSMB7; MIM 604030), and beta-5 (PSMB5; MIM 600306). Three additional subunits, beta-1i (PSMB9; MIM 177045), beta-2i (PSMB10; MIM 176847), and beta-5i (PSMB8; MIM 177046), are induced by gamma-interferon (IFNG; MIM 147570) and are preferentially incorporated into proteasomes to make immunoproteasomes. PSMB11, or beta-5t, is a catalytic subunit expressed exclusively in cortical thymic epithelial cells (Murata et al., 2007 [PubMed 17540904]).[supplied by OMIM, Mar 2008]

proteasome (prosome, macropain) subunit, beta type, 10

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. Proteolytic processing is required to generate a mature subunit. Expression of this gene is induced by gamma interferon, and this gene product replaces catalytic subunit 2 (proteasome beta 7 subunit) in the immunoproteasome. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 12 pseudogene

proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 pseudogene

proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 pseudogene

proteasome (prosome, macropain) subunit, alpha type, 2

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) subunit, alpha type, 1

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Jan 2009]

proteasome (prosome, macropain) subunit, alpha type, 7

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a member of the peptidase T1A family that functions as a 20S core alpha subunit. The encoded protein interacts with the hepatitis B virus X protein and plays a role in regulating hepatitis C virus internal ribosome entry site (IRES) activity, an activity essential for viral replication. The encoded protein also plays a role in the cellular stress response by regulating hypoxia-inducible factor-1alpha. A pseudogene of this gene is located on the long arm of chromosome 9. [provided by RefSeq, Jul 2012]

proteasome (prosome, macropain) subunit, alpha type, 4

This gene encodes a core alpha subunit of the 20S proteosome, which is a highly ordered ring-shaped structure composed of four rings of 28 non-identical subunits. Proteasomes cleave peptides in an ATP- and ubiquitin-dependent manner. [provided by RefSeq, Aug 2016]

proteasome (prosome, macropain) subunit, alpha type, 5

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. Multiple alternatively spliced transcript variants encoding two distinct isoforms have been found for this gene. [provided by RefSeq, Dec 2010]

proteasome (prosome, macropain) subunit, alpha type, 8

Predicted to be involved in meiotic cell cycle and proteasome-mediated ubiquitin-dependent protein catabolic process. Located in extracellular exosome and nucleus. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) 26S subunit, non-ATPase, 9

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, May 2012]

proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki) pseudogene

proteasome (prosome, macropain) 26S subunit, non-ATPase, 14 pseudogene

proteasome (prosome, macropain) inhibitor subunit 1 (PI31)

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a protein that inhibits the activation of the proteasome by the 11S and 19S regulators. Alternative transcript variants have been identified for this gene. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) subunit, beta type, 5 pseudogene

proteasome (prosome, macropain) subunit, alpha type, 3 pseudogene

proteasome (prosome, macropain) subunit, alpha type, 1 pseudogene

proteasome (prosome, macropain) subunit, alpha type, 3 pseudogene

proteasome (prosome, macropain) subunit, beta type, 1 pseudogene

proteasome 26S subunit, non-ATPase, 2 pseudogene 1

proteasome activator subunit 2 pseudogene 2

proteasome activator subunit 2 pseudogene 1

proteasome (prosome, macropain) 26S subunit, ATPase, 2 pseudogene

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 9

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 8

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 2

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 1

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 7

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 6

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 4

proteasome (prosome, macropain) 26S subunit, ATPase, 5 pseudogene

proteasome (prosome, macropain) subunit, alpha type, 6 pseudogene 3

proteasome (prosome, macropain) 26S subunit, ATPase, 3 pseudogene

proteasome (prosome, macropain) 26S subunit, ATPase, 1

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. This subunit and a 20S core alpha subunit interact specifically with the hepatitis B virus X protein, a protein critical to viral replication. This subunit also interacts with the adenovirus E1A protein and this interaction alters the activity of the proteasome. Finally, this subunit interacts with ataxin-7, suggesting a role for the proteasome in the development of spinocerebellar ataxia type 7, a progressive neurodegenerative disorder. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) 26S subunit, ATPase, 2

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. This subunit has been shown to interact with several of the basal transcription factors so, in addition to participation in proteasome functions, this subunit may participate in the regulation of transcription. This subunit may also compete with PSMC3 for binding to the HIV tat protein to regulate the interaction between the viral protein and the transcription complex. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Mar 2011]

proteasome (prosome, macropain) 26S subunit, ATPase, 3

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases that have chaperone-like activity. This subunit may compete with PSMC2 for binding to the HIV tat protein to regulate the interaction between the viral protein and the transcription complex. A pseudogene has been identified on chromosome 9. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) 26S subunit, ATPase, 4

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a member of the triple-A family of ATPases that is a component of the 19S regulatory subunit and plays a role in 26S proteasome assembly. The encoded protein interacts with gankyrin, a liver oncoprotein, and may also play a role in Parkinson's disease through interactions with synphilin-1. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jul 2012]

proteasome (prosome, macropain) 26S subunit, ATPase, 5

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been shown to interact with the thyroid hormone receptor and retinoid X receptor-alpha. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]

proteasome (prosome, macropain) 26S subunit, ATPase, 6

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. Pseudogenes have been identified on chromosomes 8 and 12. [provided by RefSeq, Jul 2008]

proteasome 26S subunit, non-ATPase, 8 pseudogene 1

proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 pseudogene 1

proteasome activator subunit 2 pseudogene 5

proteasome (prosome, macropain) 26S subunit, non-ATPase, 8 pseudogene

proteasome 26S subunit, ATPase, 6 pseudogene 1

proteasome 26S subunit, ATPase, 6 pseudogene 2

proteasome 26S subunit, ATPase, 6 pseudogene 3

proteasome maturation protein pseudogene

proteasome (prosome, macropain) subunit, alpha type, 6

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. Multiple transcript variants encoding several different isoforms have been found for this gene. A pseudogene has been identified on the Y chromosome. [provided by RefSeq, Aug 2013]

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 13

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 12

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 11

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 10

proteasome (prosome, macropain) 26S subunit, ATPase, 1 pseudogene 3

proteasome maturation protein

The protein encoded by this gene is a molecular chaperone that binds 20S preproteasome components and is essential for 20S proteasome formation. The 20S proteasome is the proteolytically active component of the 26S proteasome complex. The encoded protein is degraded before the maturation of the 20S proteasome is complete. A variant in the 5' UTR of this gene has been associated with KLICK syndrome, a rare skin disorder.[provided by RefSeq, Aug 2010]

proteasome 26S subunit, non-ATPase, 12 pseudogene

proteasome (prosome, macropain) activator subunit 4

Predicted to enable lysine-acetylated histone binding activity; peptidase activator activity; and proteasome binding activity. Predicted to be involved in DNA repair; proteasomal ubiquitin-independent protein catabolic process; and sperm DNA condensation. Located in nucleoplasm. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) activator subunit 2 (PA28 beta)

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the beta subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three beta and three alpha subunits combine to form a heterohexameric ring. Six pseudogenes have been identified on chromosomes 4, 5, 8, 10 and 13. [provided by RefSeq, Jul 2008]

proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Alternate splicing results in multiple transcript variants. [provided by RefSeq, May 2012]

proteasome (prosome, macropain) activator subunit 1 (PA28 alpha)

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the alpha subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three alpha and three beta subunits combine to form a heterohexameric ring. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013]

proteasome (prosome, macropain) 26S subunit, ATPase, 2 pseudogene

proteasome (prosome, macropain) subunit, alpha type, 6 pseudogene 4

proteasome (prosome, macropain) subunit, alpha type, 6 pseudogene 2

proteasome (prosome, macropain) subunit, alpha type, 6 pseudogene 1

proteasome (prosome, macropain) subunit, beta type, 3 pseudogene 2

PITH (C-terminal proteasome-interacting domain of thioredoxin-like) domain containing 1

Involved in positive regulation of DNA-templated transcription and positive regulation of megakaryocyte differentiation. Located in cytoplasm. [provided by Alliance of Genome Resources, Mar 2025]

proteasome (prosome, macropain) subunit, alpha type, 7 pseudogene

Ecm29 proteasome adaptor and scaffold

Enables proteasome binding activity. Involved in ERAD pathway. Located in several cellular components, including centrosome; cytoplasmic vesicle; and nucleoplasm. [provided by Alliance of Genome Resources, Mar 2025]

proteasome activator subunit 3 interacting protein 1

Involved in negative regulation of proteasomal protein catabolic process. Located in nucleoplasm. [provided by Alliance of Genome Resources, Mar 2025]

SEM1 26S proteasome subunit

The product of this gene has been localized within the split hand/split foot malformation locus SHFM1 at chromosome 7. It has been proposed to be a candidate gene for the autosomal dominant form of the heterogeneous limb developmental disorder split hand/split foot malformation type 1. In addition, it has been shown to directly interact with BRCA2. It also may play a role in the completion of the cell cycle. [provided by RefSeq, Jul 2008]

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Proteasome storage granule 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 Proteasome storage granule cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From GO Biological Process Annotations 2015

genes participating in the cerebellar purkinje cell-granule cell precursor cell signaling involved in regulation of granule cell precursor cell proliferation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2023

genes participating in the cerebellar Purkinje cell-granule cell precursor cell signaling involved in regulation of granule cell precursor cell proliferation biological process from the curated GO Biological Process Annotations 2023 dataset.

From Biocarta Pathways

proteins participating in the proteasome complex pathway from the Biocarta Pathways dataset.

From Biocarta Pathways

proteins participating in the degradation of the rar and rxr by the proteasome pathway from the Biocarta Pathways dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

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

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the proteasome regulatory particle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the proteasome core complex, alpha-subunit complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the proteasome regulatory particle, base subcomplex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

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

From COMPARTMENTS Curated Protein Localization Evidence Scores

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

From COMPARTMENTS Curated Protein Localization Evidence Scores

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

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the proteasome regulatory particle, lid subcomplex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

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

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the nuclear proteasome 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 cytosolic proteasome complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From CORUM Protein Complexes

proteins in the PA28-20S proteasome protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the Ubiquilin-proteasome complex protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the PA28gamma-20S proteasome protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the 26S proteasome protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the 20S proteasome protein complex from the CORUM Protein Complexes dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term proteasome 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 proteasome assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the proteasome regulatory particle assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the proteasome-mediated ubiquitin-dependent protein catabolic process biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the proteasome core complex assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

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

From GO Cellular Component Annotations 2015

proteins localized to the proteasome regulatory particle cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the proteasome core complex, alpha-subunit complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the proteasome regulatory particle, base subcomplex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

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

From GO Cellular Component Annotations 2015

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

From GO Cellular Component Annotations 2015

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

From GO Cellular Component Annotations 2015

proteins localized to the proteasome regulatory particle, lid subcomplex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

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

From GO Cellular Component Annotations 2015

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

From GO Molecular Function Annotations 2015

genes performing the proteasome binding molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome component ECM29/Translational activator GCN1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome B-type subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 26S proteasome, regulatory subunit Rpn7 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 26S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 26S proteasome non-ATPase regulatory subunit 5 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome subunit Rpn10 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome stabiliser ECM29 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome beta-type subunit, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 26S proteasome subunit P45 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome component (PCI) domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome assembly chaperone 2, eukaryotic protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome beta subunit, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 26S proteasome regulatory subunit, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome/cyclosome repeat protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 26S proteasome non-ATPase regulatory subunit Rpn12 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome, subunit alpha/beta protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome maturation factor UMP1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome alpha-subunit, N-terminal domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome activator pa28, C-terminal domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidase T1A, proteasome beta-subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome assembly chaperone 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome assembly chaperone 3 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome assembly chaperone 2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome activator pa28, N-terminal domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome endopeptidase complex, beta subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 26S proteasome complex ubiquitin receptor, subunit Rpn13 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the PI31 proteasome regulator protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the 26S proteasome regulatory complex, non-ATPase subcomplex, Rpn2/Psmd1 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome activator pa28 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Proteasome A-type subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From KEGG Pathways

proteins participating in the proteasome pathway from the KEGG Pathways dataset.

From PANTHER Pathways

proteins participating in the Ubiquitin proteasome pathway pathway from the PANTHER Pathways dataset.

From Phosphosite Textmining Biological Term Annotations

proteins co-occuring with the biological term proteasome-endopeptidase-complex in abstracts of publications describing phosphosites from the Phosphosite Textmining Biological Term Annotations dataset.

From Reactome Pathways 2014

proteins participating in the Degradation of GLI2 by the proteasome pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Regulation of activated PAK-2p34 by proteasome mediated degradation pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the GLI3 is processed to GLI3R by the proteasome pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the phosphorylation site mutants of CTNNB1 are not targeted to the proteasome by the destruction complex pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Antigen processing: Ubiquitination & Proteasome degradation pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the Degradation of GLI1 by the proteasome pathway from the Reactome Pathways dataset.

From WikiPathways Pathways 2014

proteins participating in the Proteasome Degradation(Homo sapiens) pathway from the WikiPathways Pathways 2014 dataset.

From WikiPathways Pathways 2014

proteins participating in the Proteasome Degradation(Mus musculus) pathway from the WikiPathways Pathways 2014 dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Proteasome-Associated Autoinflammatory Syndrome in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From GO Biological Process Annotations 2023

genes participating in the proteasome-mediated ubiquitin-dependent protein catabolic process biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the proteasome assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the proteasome regulatory particle assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein localization to cytosolic proteasome complex involved in ERAD pathway biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the nuclear protein quality control by the ubiquitin-proteasome system biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the cytoplasm protein quality control by the ubiquitin-proteasome system biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the proteasome core complex assembly biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protein localization to cytosolic proteasome complex biological process from the curated GO Biological Process Annotations 2023 dataset.

From WikiPathways Pathways 2024

proteins participating in the Proteasome degradation pathway from the WikiPathways Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Antigen processing: Ubiquitination & Proteasome degradation pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Degradation of GLI1 by the proteasome pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Degradation of GLI2 by the proteasome pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the GLI3 is processed to GLI3R by the proteasome pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Proteasome assembly pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Regulation of activated PAK-2p34 by proteasome mediated degradation pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

genes participating in the proteasome-mediated ubiquitin-dependent protein catabolic process biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the proteasome assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the proteasome regulatory particle assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the cytoplasm protein quality control by the ubiquitin-proteasome system biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the nuclear protein quality control by the ubiquitin-proteasome system biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protein localization to cytosolic proteasome complex biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

genes participating in the proteasome core complex assembly biological process from the curated GO Biological Process Annotations 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease proteasome-associated autoinflammatory syndrome 1 from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

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

genes co-occuring with the disease proteasome-associated autoinflammatory syndrome 1 in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease proteasome-associated autoinflammatory syndrome 3 in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Proteasome regulatory particle cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Proteasome core complex, alpha-subunit complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Proteasome core complex, beta-subunit complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Proteasome regulatory particle, lid subcomplex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Proteasome regulatory particle, base subcomplex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Cytosolic proteasome 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 Proteasome activator complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Proteasome regulatory particle, lid subcomplex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Proteasome regulatory particle, base subcomplex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Proteasome-associated autoinflammatory syndrome phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Protein quality control and ubiquitin-proteasome system regulation assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Proteasome-associated machinery assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Ubiquitin-proteasome complex assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Proteasome complex assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising Proteasome assembly and regulation assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.

From KEGG Pathways 2026

proteins participating in the Proteasome pathway from the KEGG Pathways 2026 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the PROTEASOME INHIBITOR drug from theDGIdb Drug Targets 2026 dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease type IXa1 phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease IV, congenital neuromuscular phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Myopathy, myosin storage phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Phytanic acid storage disease phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Triglyceride storage disease with ichthyosis phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease type II, infantile phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease 0, muscle phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease type X phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease IXa2 phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Cholestanol storage disease phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease IIIa phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease type 13 phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease type 1A phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Neutral lipid storage disease with myopathy phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease, type VII phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease XV phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease IXb phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease IXc phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease, type VI phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease, type II phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease IIIc phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease IIIb phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Sialic acid storage disease, severe infantile type phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the GLYCOGEN STORAGE DISEASE II, ADULT FORM phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease type III phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease IXd phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Glycogen storage disease, type V phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the monolayer-surrounded lipid storage body cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the protein storage vacuole membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From CTD Gene-Disease Associations

genes/proteins associated with the disease Cholesterol Ester Storage Disease from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease 0, Liver from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease 0, Muscle from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease Type IV from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease IXB from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease, Type IXD from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease GLYCOGEN STORAGE DISEASE IXa1 from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease XII from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Hepatorenal form of glycogen storage disease from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Neutral Lipid Storage Disease with Myopathy from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease Type III from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease Type II from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease XIII from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease Type VII from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease IXC from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease Type VI from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease IB from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease Type IIb from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Sialic Acid Storage Disease from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Myopathy, Myosin Storage from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Triglyceride storage disease with impaired long-chain fatty acid oxidation from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease GLYCOGEN STORAGE DISEASE XV from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease Type I from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease of Heart, Lethal Congenital from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease IC from the curated CTD Gene-Disease Associations dataset.

From CTD Gene-Disease Associations

genes/proteins associated with the disease Glycogen Storage Disease Type V from the curated CTD Gene-Disease Associations dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease glycogen storage disease from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease glycogen storage disease vii from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease cholesterol ester storage disease from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease glycogen storage disease i from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease glycogen storage disease v from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease lysosomal storage disease from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease lipid storage disease from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease neutral lipid storage disease from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease glycogen storage disease iv from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease glycogen storage disease ii from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores

genes involed in the disease glycogen storage disease vi from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Experimental Gene-Disease Association Evidence Scores

genes associated with the disease lipid storage disease in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Experimental Gene-Disease Association Evidence Scores

genes associated with the disease lysosomal storage disease in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease xv in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease cholesterol ester storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease viii in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease iv in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease vi in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease iii in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease lipid storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease platelet storage pool deficiency in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease vii in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease i in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease v in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease lysosomal storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease ix in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease glycogen storage disease ii in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From DISEASES Text-mining Gene-Disease Association Evidence Scores

genes co-occuring with the disease neutral lipid storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease type ii; heart diseases in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease type v in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease type i in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease type ii in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease acid lipase deficiency and cholesterol ester storage disease in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease anemia, sickle cell; glycogen storage disease type i; sickle cell anemia in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease type iii in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease type i; malaria, falciparum in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease late-onset glycogen storage disease type ii in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease type i; hemolysis; malaria, falciparum in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease glycogen storage disease type iiia in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease lysosomal storage disorders in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GAD Gene-Disease Associations

genes associated with the disease cholesteryl ester storage disease in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term storage 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 positive regulation of lipid storage biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cholesterol storage biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the nitric oxide storage biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

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

From GO Biological Process Annotations 2015

genes participating in the lipid storage biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of cholesterol storage biological process from the curated GO Biological Process Annotations 2015 dataset.

From GWASdb SNP-Disease Associations

genes associated with the disease cholesterol ester storage disease in GWAS and other genetic association datasets from the GWASdb SNP-Disease Associations dataset.

From GWASdb SNP-Disease Associations

genes associated with the disease lipid storage disease in GWAS and other genetic association datasets from the GWASdb SNP-Disease Associations dataset.

From GWASdb SNP-Disease Associations

genes associated with the disease lysosomal storage disease in GWAS and other genetic association datasets from the GWASdb SNP-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the intraaxonal accumulation of curvilinear autofluorescent lipopigment storage material phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the intracellular accumulation of autofluorescent lipopigment storage material phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the curvilinear intracellular accumulation of autofluorescent lipopigment storage material phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the fingerprint intracellular accumulation of autofluorescent lipopigment storage material phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HPO Gene-Disease Associations

genes associated with the rectilinear intracellular accumulation of autofluorescent lipopigment storage material phenotype by mapping known disease genes to disease phenotypes from the HPO Gene-Disease Associations dataset.

From HuGE Navigator Gene-Phenotype Associations

genes associated with the Cholesterol Ester Storage Disease phenotype by text-mining GWAS publications from the HuGE Navigator Gene-Phenotype Associations dataset.

From HuGE Navigator Gene-Phenotype Associations

genes associated with the Glycogen Storage Disease Type II phenotype by text-mining GWAS publications from the HuGE Navigator Gene-Phenotype Associations dataset.

From HuGE Navigator Gene-Phenotype Associations

genes associated with the Glycogen Storage Disease phenotype by text-mining GWAS publications from the HuGE Navigator Gene-Phenotype Associations dataset.

From HuGE Navigator Gene-Phenotype Associations

genes associated with the Glycogen Storage Disease Type III phenotype by text-mining GWAS publications from the HuGE Navigator Gene-Phenotype Associations dataset.

From HuGE Navigator Gene-Phenotype Associations

genes associated with the Glycogen Storage Disease Type V phenotype by text-mining GWAS publications from the HuGE Navigator Gene-Phenotype Associations dataset.

From HuGE Navigator Gene-Phenotype Associations

genes associated with the Glycogen Storage Disease Type I phenotype by text-mining GWAS publications from the HuGE Navigator Gene-Phenotype Associations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Fat storage-inducing transmembrane protein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the decreased mast cell protease storage phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the decreased mast cell histamine storage phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease iiia phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease iiib phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease 0, muscle phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease ixc phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the myopathy, myosin storage phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease of heart, lethal congenital phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the neutral lipid storage disease with myopathy phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease 0, liver phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease xii phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the ?glycogen storage disease xiii phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease iv phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease ia phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease ic phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease ib phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease ii phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease, type ixa2 phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease, type ixa1 phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease vi phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the ?glycogen storage disease xv phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease x phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease xi phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the sialic acid storage disorder, infantile phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the glycogen storage disease vii phenotype from the curated OMIM Gene-Disease Associations dataset.

From OMIM Gene-Disease Associations

genes associated with the cholesteryl ester storage disease phenotype from the curated OMIM Gene-Disease Associations dataset.

From Reactome Pathways 2014

proteins participating in the Glycogen storage diseases pathway from the Reactome Pathways dataset.

From TISSUES Text-mining Tissue Protein Expression Evidence Scores

proteins co-occuring with the tissue storage tissue in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Triglyceride Storage Disease With Ichthyosis in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Cholesterol Ester Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Glycogen Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Platelet Storage Pool Deficiency in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Neutral Lipid Storage Disease With Myopathy in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Generalized Glycogen Storage Disease Of Infants in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Sialic Acid Storage Disease, Finnish Type (Disorder) in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Lipid Storage Myopathy Due To Flavin Adenine Dinucleotide Synthetase Deficiency in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Adult Glycogen Storage Disease Type Ii in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Infantile Sialic Acid Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Glycoprotein Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease N-Acetylneuraminic Acid Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Free Sialic Acid Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Infantile Free Sialic Acid Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Sialic Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Curvilinear Intracellular Accumulation Of Autofluorescent Lipopigment Storage Material in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Fingerprint Intracellular Accumulation Of Autofluorescent Lipopigment Storage Material in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Rectilinear Intracellular Accumulation Of Autofluorescent Lipopigment Storage Material in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Glycogen Storage Disease in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Intraaxonal Accumulation Of Curvilinear Autofluorescent Lipopigment Storage Material in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From DisGeNET Gene-Phenotype Associations

genes associated with the phenotype Hepatic Glycogen Storage in GWAS and other genetic association datasets from the DisGeNET Gene-Phenotype Associations dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the lipid transport involved in lipid storage biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the cholesterol storage biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From GO Biological Process Annotations 2023

genes participating in the cholesterol transport involved in cholesterol storage biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

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

From MGI Mouse Phenotype Associations 2023

gene mutations causing the decreased mast cell histamine storage phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the decreased mast cell protease storage phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From Reactome Pathways 2024

proteins participating in the Glycogen storage disease type 0 (liver GYS2) pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glycogen storage disease type 0 (muscle GYS1) pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glycogen storage disease type II (GAA) pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glycogen storage disease type IV (GBE1) pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glycogen storage disease type Ia (G6PC) pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glycogen storage disease type Ib (SLC37A4) pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glycogen storage disease type XV (GYG1) pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Glycogen storage diseases pathway from the Reactome Pathways 2024 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

genes participating in the lipid transport involved in lipid storage biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

genes participating in the cholesterol storage biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

genes participating in the cholesterol transport involved in cholesterol storage biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

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

From GO Biological Process Annotations 2025

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

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Lysosomal storage disease from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Lipid storage disease from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glycogen storage disease from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glycogen storage disease VI from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glycogen storage disease I from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glycogen storage disease V from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glycogen storage disease VII from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glycogen storage disease IV from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glycogen storage disease II from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Curated Gene-Disease Association Evidence Scores 2025

genes involed in the disease Glycogen storage disease III from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.

From DISEASES Experimental Gene-Disease Association Evidence Scores 2025

genes associated with the disease Lysosomal storage disease in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.

From DISEASES Experimental Gene-Disease Association Evidence Scores 2025

genes associated with the disease Lipid storage disease in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Lysosomal storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Lipid storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease II in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease V in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease VII in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease IXc in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease IXa in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Cholesterol ester storage disease in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease XV in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease III in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease IV in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease I in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease Ia in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease IX in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Lethal congenital glycogen storage disease of heart in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease VI in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease IXd in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease IXb in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease VIII in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Glycogen storage disease Ib in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

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

genes co-occuring with the disease Platelet storage pool deficiency in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.

From TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025

proteins co-occuring with the tissue Storage root in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 dataset.

From TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025

proteins co-occuring with the tissue Storage tissue in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the monolayer-surrounded lipid storage body cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Lytic vacuole within protein storage vacuole cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Cholesteryl ester storage disease phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease IIIa phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease IIIb phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to glycogen branching enzyme deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to acid maltase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Cholestanol storage disease phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Sialic acid storage disease phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Lethal congenital glycogen storage disease of heart phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Phytanic acid storage disease phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease IXd phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to phosphoglycerate kinase 1 deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease IXa phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to glucose-6-phosphatase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease IXb phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease IXc phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Myosin storage myopathy phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disorder due to hepatic glycogen synthase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to muscle beta-enolase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Neutral lipid storage myopathy phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to SLC37A4 mutation phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to muscle and heart glycogen synthase deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Triglyceride storage disease phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to lactate dehydrogenase M-subunit deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycogen storage disease due to lactate dehydrogenase H-subunit deficiency phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Storage pool disease of platelets phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From ClinVar Gene-Phenotype Associations 2025

genes associated with the Glycoprotein storage disease phenotype from the curated ClinVar Gene-Phenotype Associations 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the hemolysis of donated blood (cold-storage) phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in granule cell layer of the DG relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Dentate gyrus, granule cell layer relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles

genes with high or low expression in Main olfactory bulb, granule layer relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.

From ClinVar Gene-Phenotype Associations

genes associated with the Birbeck granule deficiency phenotype from the curated ClinVar Gene-Phenotype Associations dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the chromaffin granule lumen cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the cortical granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the ribonucleoprotein granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the glycogen granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the cytoplasmic ribonucleoprotein granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the platelet alpha granule membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the p granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the secretory granule lumen cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the platelet dense granule membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the azurophil granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the platelet alpha granule lumen cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the zymogen granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the pigment granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the specific granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the secretory granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the dense core granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the mast cell granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the cytoplasmic stress granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the chromaffin granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the azurophil granule lumen cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the zymogen granule membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the dense core granule membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the nuclear stress granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the tertiary granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the tertiary granule membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the secretory granule membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the platelet alpha granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the platelet dense granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the neuronal ribonucleoprotein granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the chromaffin granule membrane cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the cytolytic granule cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the platelet alpha granule membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the platelet dense granule membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the dense core granule membrane cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

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

From CTD Gene-Disease Associations

genes/proteins associated with the disease Specific Granule Deficiency from the curated CTD Gene-Disease Associations dataset.

From GeneRIF Biological Term Annotations

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

From GEO Signatures of Differentially Expressed Genes for Gene Perturbations

genes differentially expressed following the CSTB_KO_GDS5089_486_mouse_Cerebellum and granule neurons gene perturbation from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.

From GEO Signatures of Differentially Expressed Genes for Gene Perturbations

genes differentially expressed following the CSTB_KO_GDS5091_23_mouse_cerebellar granule gene perturbation from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.

From GEO Signatures of Differentially Expressed Genes for Gene Perturbations

genes differentially expressed following the CSTB_KO_GSE47516_18_mouse_brain (P7 cerebellum, P30 cerebellum, cerebellar granule cells) gene perturbation from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.

From GEO Signatures of Differentially Expressed Genes for Gene Perturbations

genes differentially expressed following the CSTB_KO_GDS5089_565_mouse_cerebellum and granule neurons gene perturbation from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.

From GEO Signatures of Differentially Expressed Genes for Gene Perturbations

genes differentially expressed following the CSTB_KO_GDS5090_200_mouse_Cerebellar granule cells gene perturbation from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of cerebellar granule cell precursor proliferation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the secretory granule organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the eye pigment granule organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the endosome to pigment granule transport biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the pigment granule maturation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the stress granule assembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of dense core granule biogenesis biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the secretory granule localization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cell proliferation in external granule layer biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of dense core granule biogenesis biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cerebellar granule cell precursor tangential migration biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the maintenance of protease location in mast cell secretory granule biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the pigment granule transport biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the maintenance of granzyme b location in t cell secretory granule biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the zymogen granule exocytosis biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the dense core granule maturation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the mast cell secretory granule organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the maintenance of protein location in t cell secretory granule biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the t cell secretory granule organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of cerebellar granule cell precursor proliferation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the p granule organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the establishment of pigment granule localization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the maintenance of protease location in t cell secretory granule biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the platelet dense granule organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cerebellar granule cell precursor proliferation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the stress granule disassembly biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the radial glia guided migration of cerebellar granule cell biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of cerebellar granule cell precursor proliferation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the platelet alpha granule organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the cerebellar granule cell differentiation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the pigment granule aggregation in cell center biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the pigment granule organization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the maintenance of protein location in mast cell secretory granule biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the golgi to secretory granule transport biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of dense core granule biogenesis biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the pigment granule localization biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the chromaffin granule lumen cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the cortical granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the ribonucleoprotein granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the glycogen granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the platelet alpha granule lumen cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the cytoplasmic ribonucleoprotein granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the platelet alpha granule membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the p granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the specific granule membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the keratohyalin granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the secretory granule lumen cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the platelet dense granule membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the azurophil granule membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the azurophil granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the zymogen granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the pigment granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the specific granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the secretory granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the dense core granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the mast cell granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the dense core granule membrane cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the mucin granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the cytoplasmic stress granule cellular component from the curated GO Cellular Component Annotations 2015 dataset.