The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Transferase(Phosphotransferase) domain 1
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 79449: Insulin receptor

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 44 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
3 P06213 (/IPI) P15127 (/IPI) P15208 (/IPI)
Protein tyrosine kinase activity GO:0004713
Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
2 P06213 (/IDA) P15127 (/IDA)
Insulin-activated receptor activity GO:0005009
Combining with insulin and transmitting the signal across the plasma membrane to initiate a change in cell activity.
2 P06213 (/IDA) P15127 (/IDA)
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
2 P06213 (/IPI) P15127 (/IPI)
Insulin binding GO:0043559
Interacting selectively and non-covalently with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
2 P06213 (/IDA) P15127 (/IDA)
Protein kinase activity GO:0004672
Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
1 P15127 (/IDA)
Protein tyrosine kinase activity GO:0004713
Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
1 P06213 (/IMP)
Protein tyrosine kinase activity GO:0004713
Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
1 P15208 (/ISO)
Signal transducer, downstream of receptor, with protein tyrosine kinase activity GO:0004716
Conveys a signal from an upstream receptor or intracellular signal transducer by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate.
1 P06213 (/IDA)
Signal transducer, downstream of receptor, with protein tyrosine kinase activity GO:0004716
Conveys a signal from an upstream receptor or intracellular signal transducer by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate.
1 P15208 (/ISO)
Insulin-activated receptor activity GO:0005009
Combining with insulin and transmitting the signal across the plasma membrane to initiate a change in cell activity.
1 P15127 (/IMP)
Insulin-activated receptor activity GO:0005009
Combining with insulin and transmitting the signal across the plasma membrane to initiate a change in cell activity.
1 P15208 (/ISO)
Insulin-activated receptor activity GO:0005009
Combining with insulin and transmitting the signal across the plasma membrane to initiate a change in cell activity.
1 P15208 (/ISS)
Insulin-like growth factor receptor binding GO:0005159
Interacting selectively and non-covalently with the insulin-like growth factor receptor.
1 P06213 (/IDA)
Insulin-like growth factor receptor binding GO:0005159
Interacting selectively and non-covalently with the insulin-like growth factor receptor.
1 P15208 (/ISO)
Insulin-like growth factor binding GO:0005520
Interacting selectively and non-covalently with an insulin-like growth factor, any member of a group of polypeptides that are structurally homologous to insulin and share many of its biological activities, but are immunologically distinct from it.
1 G5ARX9 (/ISS)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 P06213 (/IDA)
ATP binding GO:0005524
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
1 P15208 (/ISO)
GTP binding GO:0005525
Interacting selectively and non-covalently with GTP, guanosine triphosphate.
1 P06213 (/IDA)
GTP binding GO:0005525
Interacting selectively and non-covalently with GTP, guanosine triphosphate.
1 P15208 (/ISO)
Protein kinase binding GO:0019901
Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
1 P15127 (/IPI)
Protein phosphatase binding GO:0019903
Interacting selectively and non-covalently with any protein phosphatase.
1 P15127 (/IMP)
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
1 P15208 (/ISO)
Lipoic acid binding GO:0031405
Interacting selectively and non-covalently with lipoic acid, 1,2-dithiolane-3-pentanoic acid.
1 P15127 (/IPI)
Insulin-like growth factor I binding GO:0031994
Interacting selectively and non-covalently with insulin-like growth factor I.
1 P06213 (/IPI)
Insulin-like growth factor I binding GO:0031994
Interacting selectively and non-covalently with insulin-like growth factor I.
1 P15208 (/ISO)
Insulin-like growth factor II binding GO:0031995
Interacting selectively and non-covalently with insulin-like growth factor II.
1 P06213 (/IPI)
Insulin-like growth factor II binding GO:0031995
Interacting selectively and non-covalently with insulin-like growth factor II.
1 P15208 (/ISO)
Protein complex binding GO:0032403
Interacting selectively and non-covalently with any protein complex (a complex of two or more proteins that may include other nonprotein molecules).
1 P15127 (/IDA)
3-phosphoinositide-dependent protein kinase binding GO:0043423
Interacting selectively and non-covalently with a 3-phosphoinositide-dependent protein kinase.
1 P15127 (/IDA)
Phosphatidylinositol 3-kinase binding GO:0043548
Interacting selectively and non-covalently with a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.
1 P06213 (/IPI)
Phosphatidylinositol 3-kinase binding GO:0043548
Interacting selectively and non-covalently with a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.
1 P15208 (/ISO)
Phosphatidylinositol 3-kinase binding GO:0043548
Interacting selectively and non-covalently with a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.
1 P15208 (/ISS)
Insulin binding GO:0043559
Interacting selectively and non-covalently with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
1 P15127 (/IMP)
Insulin binding GO:0043559
Interacting selectively and non-covalently with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
1 P06213 (/IPI)
Insulin binding GO:0043559
Interacting selectively and non-covalently with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
1 P15208 (/ISO)
Insulin binding GO:0043559
Interacting selectively and non-covalently with insulin, a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
1 P15208 (/ISS)
Insulin receptor substrate binding GO:0043560
Interacting selectively and non-covalently with any of the insulin receptor substrate (IRS) proteins, adaptor proteins that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex.
1 P15127 (/IMP)
Insulin receptor substrate binding GO:0043560
Interacting selectively and non-covalently with any of the insulin receptor substrate (IRS) proteins, adaptor proteins that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex.
1 P06213 (/IPI)
Insulin receptor substrate binding GO:0043560
Interacting selectively and non-covalently with any of the insulin receptor substrate (IRS) proteins, adaptor proteins that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex.
1 P15208 (/ISO)
Insulin receptor substrate binding GO:0043560
Interacting selectively and non-covalently with any of the insulin receptor substrate (IRS) proteins, adaptor proteins that bind to the transphosphorylated insulin and insulin-like growth factor receptors, are themselves phosphorylated and in turn recruit SH2 domain-containing signaling molecules to form a productive signaling complex.
1 P15208 (/ISS)
PTB domain binding GO:0051425
Interacting selectively and non-covalently with a phosphotyrosine-binding (PTB) domain of a protein.
1 P06213 (/IPI)
PTB domain binding GO:0051425
Interacting selectively and non-covalently with a phosphotyrosine-binding (PTB) domain of a protein.
1 P15208 (/ISO)
PTB domain binding GO:0051425
Interacting selectively and non-covalently with a phosphotyrosine-binding (PTB) domain of a protein.
1 P15208 (/ISS)

There are 98 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Insulin receptor signaling pathway GO:0008286
The series of molecular signals generated as a consequence of the insulin receptor binding to insulin.
2 P06213 (/IDA) P15127 (/IDA)
Insulin receptor signaling pathway GO:0008286
The series of molecular signals generated as a consequence of the insulin receptor binding to insulin.
2 P15127 (/IMP) P15208 (/IMP)
Positive regulation of mitotic nuclear division GO:0045840
Any process that activates or increases the frequency, rate or extent of mitosis.
2 P06213 (/IMP) P15208 (/IMP)
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
2 P06213 (/IDA) P15127 (/IDA)
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
2 P06213 (/IMP) P15127 (/IMP)
Protein heterotetramerization GO:0051290
The formation of a protein heterotetramer, a macromolecular structure consisting of four noncovalently associated subunits, of which not all are identical.
2 P06213 (/IDA) P15127 (/IDA)
Activation of MAPK activity GO:0000187
The initiation of the activity of the inactive enzyme MAP kinase (MAPK).
1 P06213 (/IMP)
Activation of MAPK activity GO:0000187
The initiation of the activity of the inactive enzyme MAP kinase (MAPK).
1 P15208 (/ISO)
Negative regulation of protein phosphorylation GO:0001933
Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein.
1 P15127 (/IMP)
Positive regulation of protein phosphorylation GO:0001934
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.
1 P06213 (/IDA)
Positive regulation of protein phosphorylation GO:0001934
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.
1 P15208 (/ISO)
Heart morphogenesis GO:0003007
The developmental process in which the heart is generated and organized. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
1 P06213 (/IMP)
Heart morphogenesis GO:0003007
The developmental process in which the heart is generated and organized. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
1 P15208 (/ISO)
Regulation of transcription, DNA-templated GO:0006355
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
1 P06213 (/IMP)
Regulation of transcription, DNA-templated GO:0006355
Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
1 P15208 (/ISO)
Protein phosphorylation GO:0006468
The process of introducing a phosphate group on to a protein.
1 P15127 (/IDA)
G-protein coupled receptor signaling pathway GO:0007186
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription. The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
1 P06213 (/IDA)
G-protein coupled receptor signaling pathway GO:0007186
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription. The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
1 P15208 (/ISO)
Positive regulation of cell proliferation GO:0008284
Any process that activates or increases the rate or extent of cell proliferation.
1 P06213 (/IC)
Positive regulation of cell proliferation GO:0008284
Any process that activates or increases the rate or extent of cell proliferation.
1 P06213 (/IDA)
Positive regulation of cell proliferation GO:0008284
Any process that activates or increases the rate or extent of cell proliferation.
1 P15208 (/ISO)
Insulin receptor signaling pathway GO:0008286
The series of molecular signals generated as a consequence of the insulin receptor binding to insulin.
1 P15208 (/ISO)
Insulin receptor signaling pathway GO:0008286
The series of molecular signals generated as a consequence of the insulin receptor binding to insulin.
1 P06213 (/TAS)
Epidermis development GO:0008544
The process whose specific outcome is the progression of the epidermis over time, from its formation to the mature structure. The epidermis is the outer epithelial layer of an animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
1 P15208 (/IMP)
Male gonad development GO:0008584
The process whose specific outcome is the progression of the male gonad over time, from its formation to the mature structure.
1 P15208 (/IGI)
Response to hormone GO:0009725
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hormone stimulus.
1 P15127 (/IEP)
Response to glucose GO:0009749
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucose stimulus.
1 P15127 (/IEP)
Animal organ morphogenesis GO:0009887
Morphogenesis of an animal organ. An organ is defined as a tissue or set of tissues that work together to perform a specific function or functions. Morphogenesis is the process in which anatomical structures are generated and organized. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions.
1 P15208 (/IMP)
Response to manganese ion GO:0010042
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a manganese ion stimulus.
1 P15127 (/IEP)
Regulation of hydrogen peroxide metabolic process GO:0010310
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving hydrogen peroxide.
1 P15127 (/IDA)
Positive regulation of glycoprotein biosynthetic process GO:0010560
Any process that increases the rate, frequency, or extent of the chemical reactions and pathways resulting in the formation of glycoproteins, any protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
1 P15127 (/IMP)
Negative regulation of gene expression GO:0010629
Any process that decreases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
1 P15127 (/IMP)
Response to activity GO:0014823
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an activity stimulus.
1 P15127 (/IEP)
Peptidyl-tyrosine phosphorylation GO:0018108
The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
1 P06213 (/IDA)
Peptidyl-tyrosine phosphorylation GO:0018108
The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
1 P15127 (/IMP)
Peptidyl-tyrosine phosphorylation GO:0018108
The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
1 P15208 (/ISO)
Transformation of host cell by virus GO:0019087
Any virus-induced change in the morphological, biochemical, or growth parameters of a cell.
1 P06213 (/IMP)
Transformation of host cell by virus GO:0019087
Any virus-induced change in the morphological, biochemical, or growth parameters of a cell.
1 P15208 (/ISO)
Cerebellum development GO:0021549
The process whose specific outcome is the progression of the cerebellum over time, from its formation to the mature structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. In mice, the cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
1 P15127 (/IEP)
Hippocampus development GO:0021766
The progression of the hippocampus over time from its initial formation until its mature state.
1 P15127 (/IEP)
Male sex determination GO:0030238
The specification of male sex of an individual organism.
1 P15208 (/IMP)
Adrenal gland development GO:0030325
The process whose specific outcome is the progression of the adrenal gland over time, from its formation to the mature structure. This gland can either be a discrete structure located bilaterally above each kidney, or a cluster of cells in the head kidney that perform the functions of the adrenal gland. In either case, this organ consists of two cells types, aminergic chromaffin cells and steroidogenic cortical cells.
1 P15208 (/IGI)
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
1 P06213 (/IMP)
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
1 P15208 (/ISO)
Exocrine pancreas development GO:0031017
The process whose specific outcome is the progression of the exocrine pancreas over time, from its formation to the mature structure. The exocrine pancreas produces and store zymogens of digestive enzymes, such as chymotrypsinogen and trypsinogen in the acinar cells.
1 P15208 (/IMP)
Response to nutrient levels GO:0031667
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients.
1 P15127 (/IEP)
Activation of protein kinase activity GO:0032147
Any process that initiates the activity of an inactive protein kinase.
1 P06213 (/IMP)
Activation of protein kinase activity GO:0032147
Any process that initiates the activity of an inactive protein kinase.
1 P15208 (/ISO)
Activation of protein kinase B activity GO:0032148
Any process that initiates the activity of the inactive enzyme protein kinase B.
1 P06213 (/IDA)
Activation of protein kinase B activity GO:0032148
Any process that initiates the activity of the inactive enzyme protein kinase B.
1 P15208 (/ISO)
Response to estradiol GO:0032355
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of stimulus by estradiol, a C18 steroid hormone hydroxylated at C3 and C17 that acts as a potent estrogen.
1 P15127 (/IEP)
Negative regulation of transporter activity GO:0032410
Any process that stops or reduces the activity of a transporter.
1 P15127 (/IMP)
Response to insulin GO:0032868
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
1 P15127 (/IEP)
Cellular response to insulin stimulus GO:0032869
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
1 P06213 (/IDA)
Cellular response to insulin stimulus GO:0032869
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
1 P15208 (/ISO)
Response to vitamin D GO:0033280
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin D stimulus.
1 P15127 (/IEP)
Response to testosterone GO:0033574
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a testosterone stimulus.
1 P15127 (/IEP)
Response to tumor necrosis factor GO:0034612
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus.
1 P15127 (/IMP)
Peptidyl-tyrosine autophosphorylation GO:0038083
The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein.
1 P15208 (/IDA)
Positive regulation of phosphorylation GO:0042327
Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to a molecule.
1 P15127 (/IDA)
Glucose homeostasis GO:0042593
Any process involved in the maintenance of an internal steady state of glucose within an organism or cell.
1 P15127 (/IDA)
Glucose homeostasis GO:0042593
Any process involved in the maintenance of an internal steady state of glucose within an organism or cell.
1 P06213 (/IMP)
Glucose homeostasis GO:0042593
Any process involved in the maintenance of an internal steady state of glucose within an organism or cell.
1 P15208 (/ISO)
Positive regulation of MAPK cascade GO:0043410
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade.
1 P06213 (/IDA)
Positive regulation of MAPK cascade GO:0043410
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade.
1 P06213 (/IMP)
Positive regulation of MAPK cascade GO:0043410
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade.
1 P15208 (/ISO)
Positive regulation of nitric oxide biosynthetic process GO:0045429
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nitric oxide.
1 P06213 (/IMP)
Positive regulation of nitric oxide biosynthetic process GO:0045429
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nitric oxide.
1 P15208 (/ISO)
Fat cell differentiation GO:0045444
The process in which a relatively unspecialized cell acquires specialized features of an adipocyte, an animal connective tissue cell specialized for the synthesis and storage of fat.
1 P15127 (/IEP)
Response to ethanol GO:0045471
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethanol stimulus.
1 P15127 (/IEP)
Positive regulation of glycogen biosynthetic process GO:0045725
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glycogen.
1 P06213 (/IDA)
Positive regulation of glycogen biosynthetic process GO:0045725
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glycogen.
1 P15208 (/IMP)
Positive regulation of glycogen biosynthetic process GO:0045725
Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of glycogen.
1 P15208 (/ISO)
Positive regulation of DNA replication GO:0045740
Any process that activates or increases the frequency, rate or extent of DNA replication.
1 P06213 (/IMP)
Positive regulation of DNA replication GO:0045740
Any process that activates or increases the frequency, rate or extent of DNA replication.
1 P15208 (/ISO)
Positive regulation of glycolytic process GO:0045821
Any process that activates or increases the frequency, rate or extent of glycolysis.
1 P06213 (/IMP)
Positive regulation of glycolytic process GO:0045821
Any process that activates or increases the frequency, rate or extent of glycolysis.
1 P15208 (/ISO)
Positive regulation of mitotic nuclear division GO:0045840
Any process that activates or increases the frequency, rate or extent of mitosis.
1 P15208 (/ISO)
Positive regulation of transcription, DNA-templated GO:0045893
Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
1 P15208 (/IGI)
Regulation of embryonic development GO:0045995
Any process that modulates the frequency, rate or extent of embryonic development.
1 P06213 (/IMP)
Regulation of embryonic development GO:0045995
Any process that modulates the frequency, rate or extent of embryonic development.
1 P15208 (/ISO)
Positive regulation of glucose import GO:0046326
Any process that activates or increases the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle.
1 P06213 (/IDA)
Positive regulation of glucose import GO:0046326
Any process that activates or increases the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle.
1 P15208 (/ISO)
Positive regulation of glucose import GO:0046326
Any process that activates or increases the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle.
1 P06213 (/NAS)
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
1 P15208 (/ISO)
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
1 P15208 (/ISS)
Positive regulation of developmental growth GO:0048639
Any process that activates, maintains or increases the rate of developmental growth.
1 P06213 (/IMP)
Positive regulation of developmental growth GO:0048639
Any process that activates, maintains or increases the rate of developmental growth.
1 P15208 (/ISO)
Protein heterotetramerization GO:0051290
The formation of a protein heterotetramer, a macromolecular structure consisting of four noncovalently associated subunits, of which not all are identical.
1 P15208 (/ISO)
Protein heterotetramerization GO:0051290
The formation of a protein heterotetramer, a macromolecular structure consisting of four noncovalently associated subunits, of which not all are identical.
1 P15208 (/ISS)
Response to glucocorticoid GO:0051384
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucocorticoid stimulus. Glucocorticoids are hormonal C21 corticosteroids synthesized from cholesterol with the ability to bind with the cortisol receptor and trigger similar effects. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects.
1 P15127 (/IEP)
Positive regulation of meiotic cell cycle GO:0051446
Any process that activates or increases the frequency, rate or extent of progression through the meiotic cell cycle.
1 P15208 (/IGI)
Positive regulation of protein kinase B signaling GO:0051897
Any process that activates or increases the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
1 P06213 (/IMP)
Positive regulation of protein kinase B signaling GO:0051897
Any process that activates or increases the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
1 P15208 (/ISO)
Positive regulation of respiratory burst GO:0060267
Any process that increases the rate frequency or extent of a phase of elevated metabolic activity, during which oxygen consumption increases; this leads to the production, by an NADH dependent system, of hydrogen peroxide (H2O2), superoxide anions and hydroxyl radicals.
1 P06213 (/IDA)
Positive regulation of respiratory burst GO:0060267
Any process that increases the rate frequency or extent of a phase of elevated metabolic activity, during which oxygen consumption increases; this leads to the production, by an NADH dependent system, of hydrogen peroxide (H2O2), superoxide anions and hydroxyl radicals.
1 P15208 (/ISO)
Cellular response to growth factor stimulus GO:0071363
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus.
1 P15208 (/IDA)
Regulation of female gonad development GO:2000194
Any process that modulates the frequency, rate or extent of female gonad development.
1 P15208 (/IGI)

There are 23 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
2 P15127 (/IDA) P15208 (/IDA)
Caveola GO:0005901
A membrane raft that forms small pit, depression, or invagination that communicates with the outside of a cell and extends inward, indenting the cytoplasm and the cell membrane. Examples include flask-shaped invaginations of the plasma membrane in adipocytes associated with caveolin proteins, and minute pits or incuppings of the cell membrane formed during pinocytosis. Caveolae may be pinched off to form free vesicles within the cytoplasm.
2 P06213 (/IDA) P15208 (/IDA)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
2 P06213 (/IDA) P15208 (/IDA)
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
1 P15127 (/IDA)
Endosome GO:0005768
A vacuole to which materials ingested by endocytosis are delivered.
1 P15127 (/IDA)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 P15127 (/IDA)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
1 P06213 (/IC)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
1 G5ARX9 (/ISS)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
1 P06213 (/TAS)
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
1 P06213 (/IDA)
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
1 P15208 (/ISO)
Insulin receptor complex GO:0005899
A disulfide-bonded, heterotetrameric receptor complex. The alpha chains are entirely extracellular, while each beta chain has one transmembrane domain. The ligand binds to the alpha subunit extracellular domain and the kinase is associated with the beta subunit intracellular domain.
1 P06213 (/IMP)
Insulin receptor complex GO:0005899
A disulfide-bonded, heterotetrameric receptor complex. The alpha chains are entirely extracellular, while each beta chain has one transmembrane domain. The ligand binds to the alpha subunit extracellular domain and the kinase is associated with the beta subunit intracellular domain.
1 P15208 (/ISO)
Caveola GO:0005901
A membrane raft that forms small pit, depression, or invagination that communicates with the outside of a cell and extends inward, indenting the cytoplasm and the cell membrane. Examples include flask-shaped invaginations of the plasma membrane in adipocytes associated with caveolin proteins, and minute pits or incuppings of the cell membrane formed during pinocytosis. Caveolae may be pinched off to form free vesicles within the cytoplasm.
1 P15208 (/ISO)
Endosome membrane GO:0010008
The lipid bilayer surrounding an endosome.
1 P06213 (/TAS)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 P15208 (/ISO)
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
1 P15127 (/IDA)
Intracellular membrane-bounded organelle GO:0043231
Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
1 P15127 (/IDA)
Receptor complex GO:0043235
Any protein complex that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
1 P06213 (/IDA)
Receptor complex GO:0043235
Any protein complex that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
1 P15208 (/ISO)
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
1 P15127 (/IDA)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
1 P06213 (/IDA)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
1 P15208 (/ISO)