KRAS encodes a membrane-associated Ras-family small GTPase that functions as a GDP/GTP molecular switch in receptor-driven signal transduction. In the GTP-bound state KRAS recruits effectors including RAF-family kinases and PI3Kalpha to activate downstream MAPK and PI3K-AKT-mTOR signaling; intrinsic and GAP-stimulated GTP hydrolysis return KRAS to the GDP-bound inactive state. KRAS4A and KRAS4B differ in their C-terminal hypervariable regions and membrane-targeting mechanisms, but both depend on lipid modification and membrane localization for signaling. Oncogenic and rasopathy variants alter nucleotide cycling, GAP responsiveness, effector interactions, or localization, producing context-dependent effects on proliferation, survival, senescence, and gene expression.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: IBA annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md Both isoforms are farnesylated at the CAAX cysteine and further processed (RCE1 cleavage and ICMT methylation) in the ER, enabling membrane association. KRAS4B lacks palmitoylatable cysteines and instead uses a lysine-rich polybasic HVR (reported net charge +8) to electrostatically stabilize plasma membrane association with anionic lipids. |
| GO:0007265 Ras protein signal transduction | IBA GO_REF:0000033 | ACCEPT | Summary: IBA annotation for Ras protein signal transduction. KRAS participates directly in Ras signaling through SOS-mediated activation and effector engagement. Reason: This process annotation is appropriate for KRAS, whose active GTP-bound form transmits receptor inputs to downstream pathways including RAF-MEK-ERK and PI3K-AKT-mTOR. Supporting Evidence: PMID:38188543 SOS1 facilitates the exchange of GDP to GTP thereby leading to activation of KRAS Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active file:human/KRAS/KRAS-deep-research-falcon.md Primary structural evidence for Ras activation by SOS comes from the crystal structure of Ras in complex with the SOS catalytic region, indicating SOS stabilizes Ras in a nucleotide-free state, a mechanistic basis for GEF-driven exchange. |
| GO:0008284 positive regulation of cell population proliferation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: KRAS signaling can promote cell proliferation through MAPK and PI3K effector pathways, but proliferation is a downstream cellular outcome rather than the molecular core function. Reason: The annotation is biologically plausible and supported by pathway literature, but it should not be treated as the core activity of KRAS. Supporting Evidence: Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active PMID:39788953 Their interaction plays a crucial role in activating PI3KΞ± and amplifying the PI3K-AKT-mTOR pathway |
| GO:0003924 GTPase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA annotation for KRAS GTPase activity. KRAS is a Ras-family small GTPase with intrinsic GTP hydrolysis activity and GAP-stimulated hydrolysis. Reason: This is the core molecular activity of KRAS. The UniProt record, Reactome intrinsic GTPase reaction, and biochemical KRAS mutant studies all support GTP hydrolysis as the central catalytic activity. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Ras proteins bind GDP/GTP and possess intrinsic GTPase activity Reactome:R-HSA-9649736 RAS proteins have weak intrinsic GTPase activity in the absence of other effectors file:human/KRAS/KRAS-deep-research-falcon.md **KRAS is a Ras-family small GTPase** that functions as a GDP/GTP-regulated switch. GTP binding induces conformational changes in **switch I/II** regions enabling effector recognition, while GTP hydrolysis returns KRAS to the GDP-bound state. |
| GO:0000165 MAPK cascade | IEA GO_REF:0000117 | ACCEPT | Summary: KRAS participates in the RAF/MAP kinase cascade by recruiting and activating RAF-family kinases when GTP-bound. Reason: Reactome and structural work support active KRAS as an upstream activator of the RAF-MEK-ERK MAPK cascade. Supporting Evidence: Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active |
| GO:0003924 GTPase activity | IEA GO_REF:0000002 | ACCEPT | Summary: IEA annotation for KRAS GTPase activity. KRAS is a Ras-family small GTPase with intrinsic GTP hydrolysis activity and GAP-stimulated hydrolysis. Reason: This is the core molecular activity of KRAS. The UniProt record, Reactome intrinsic GTPase reaction, and biochemical KRAS mutant studies all support GTP hydrolysis as the central catalytic activity. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Ras proteins bind GDP/GTP and possess intrinsic GTPase activity Reactome:R-HSA-9649736 RAS proteins have weak intrinsic GTPase activity in the absence of other effectors file:human/KRAS/KRAS-deep-research-falcon.md **KRAS is a Ras-family small GTPase** that functions as a GDP/GTP-regulated switch. GTP binding induces conformational changes in **switch I/II** regions enabling effector recognition, while GTP hydrolysis returns KRAS to the GDP-bound state. |
| GO:0003925 G protein activity | IEA GO_REF:0000003 | MODIFY | Summary: KRAS functions as a small monomeric G protein that switches between GDP-bound inactive and GTP-bound active states. Reason: The integrated falcon DR guidance explicitly recommends the more specific GTPase activity term (GO:0003924) over the generic G protein activity term for KRAS. GO:0003924 is already separately annotated for KRAS with IBA, IEA, EXP, TAS, and IMP evidence (all ACCEPT), so MODIFY replaces this generic IEA term with the established specific term. Proposed replacements: GTPase activity Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Alternates between an inactive form bound to GDP and an active form bound to GTP file:human/KRAS/KRAS-deep-research-falcon.md Use "GTPase activity," not broad "G protein activity"; mutant-impaired hydrolysis should not redefine WT function. Prefer specific MF terms (GTP binding, GDP binding, GTPase activity) over generic "G protein activity/protein binding." |
| GO:0005525 GTP binding | IEA GO_REF:0000002 | ACCEPT | Summary: KRAS binds GTP as the active nucleotide state of the Ras molecular switch. Reason: GTP binding is essential to KRAS activation and downstream effector recruitment. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Alternates between an inactive form bound to GDP and an active form bound to GTP file:human/KRAS/KRAS-deep-research-falcon.md KRAS is a Ras-family small GTPase that functions as a GDP/GTP-regulated switch. GTP binding induces conformational changes in switch I/II regions enabling effector recognition, while GTP hydrolysis returns KRAS to the GDP-bound state. A primary structural and functional demonstration of Ras effector engagement is the RasβPI3KΞ³ complex: PI3KΞ³ is directly activated by GTP-loaded Ras, and the structure shows Ras uses switch I/II to bind the PI3KΞ³ Ras-binding domain. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: IEA annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | MODIFY | Summary: The generic signal transduction annotation reflects KRAS signaling but is less informative than Ras-specific signaling terms. Reason: KRAS should be annotated to Ras protein signal transduction rather than broad signal transduction when the domain and pathway evidence are Ras-specific. Proposed replacements: Ras protein signal transduction Supporting Evidence: PMID:38188543 SOS1 facilitates the exchange of GDP to GTP thereby leading to activation of KRAS |
| GO:0012505 endomembrane system | IEA GO_REF:0000044 | ACCEPT | Summary: KRAS, especially K-Ras4a under SIRT2-regulated lysine defatty-acylation, can localize to endomembrane compartments. Reason: Endomembrane localization is supported by K-Ras4a acylation experiments and by UniProt subcellular-location curation. Supporting Evidence: PMID:29239724 SIRT2-mediated lysine defatty-acylation promotes endomembrane localization of K-Ras4a file:human/KRAS/KRAS-deep-research-falcon.md KRAS4A contains a palmitoylation site (Cys180) enabling reversible palmitoylation-dependent Golgi trafficking. Expert synthesis notes that farnesylation + palmitoylation can increase membrane affinity by >100-fold and acts as a Golgi "affinity trap" promoting vesicular delivery to the plasma membrane. |
| GO:0016020 membrane | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: The generic membrane annotation is directionally correct for lipid-anchored KRAS but lacks the useful subcellular specificity available from curated evidence. Reason: KRAS has more specific and better-supported plasma membrane, cytoplasmic-side-of-plasma-membrane, endomembrane, and cytosolic localization annotations. Generic membrane should not be used as an informative KRAS localization. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor |
| GO:0005515 protein binding | IPI PMID:12732644 RASSF2 is a novel K-Ras-specific effector and potential tumo... | REMOVE | Summary: This protein binding annotation records a physical interaction, but GO:0005515 is too generic to describe KRAS function. Reason: Protein binding is specifically uninformative for KRAS. Specific effector/regulator interactions should support Ras signaling, MAPK cascade, PI3K signaling, or localization annotations rather than a generic protein binding MF term. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: This protein binding annotation records a physical interaction, but GO:0005515 is too generic to describe KRAS function. Reason: Protein binding is specifically uninformative for KRAS. Specific effector/regulator interactions should support Ras signaling, MAPK cascade, PI3K signaling, or localization annotations rather than a generic protein binding MF term. |
| GO:0005515 protein binding | IPI PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apo... | REMOVE | Summary: This protein binding annotation records a physical interaction, but GO:0005515 is too generic to describe KRAS function. Reason: Protein binding is specifically uninformative for KRAS. Specific effector/regulator interactions should support Ras signaling, MAPK cascade, PI3K signaling, or localization annotations rather than a generic protein binding MF term. |
| GO:0005515 protein binding | IPI PMID:30194290 Interrogating the protein interactomes of RAS isoforms ident... | REMOVE | Summary: This protein binding annotation records a physical interaction, but GO:0005515 is too generic to describe KRAS function. Reason: Protein binding is specifically uninformative for KRAS. Specific effector/regulator interactions should support Ras signaling, MAPK cascade, PI3K signaling, or localization annotations rather than a generic protein binding MF term. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: This protein binding annotation records a physical interaction, but GO:0005515 is too generic to describe KRAS function. Reason: Protein binding is specifically uninformative for KRAS. Specific effector/regulator interactions should support Ras signaling, MAPK cascade, PI3K signaling, or localization annotations rather than a generic protein binding MF term. |
| GO:0001889 liver development | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The liver development annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0007249 canonical NF-kappaB signal transduction | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The canonical NF-kappaB signal transduction annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0007565 female pregnancy | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The female pregnancy annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0009629 response to gravity | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The response to gravity annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0019002 GMP binding | IEA GO_REF:0000107 | MODIFY | Summary: This orthology-transferred GMP binding annotation does not match the established KRAS nucleotide cycle, which is GDP/GTP based. Reason: KRAS is characterized as a GDP/GTP-binding small GTPase. GMP binding is not the physiologically informative ligand state for KRAS and should be replaced by the specific GDP and GTP binding terms. Proposed replacements: GTP binding GDP binding Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Ras proteins bind GDP/GTP and possess intrinsic GTPase activity |
| GO:0019003 GDP binding | IEA GO_REF:0000107 | ACCEPT | Summary: KRAS binds GDP as the inactive nucleotide state of the Ras molecular switch. Reason: GDP binding is a normal part of the KRAS regulatory cycle and is supported by the UniProt activity-regulation statement. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Alternates between an inactive form bound to GDP and an active form bound to GTP |
| GO:0019221 cytokine-mediated signaling pathway | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The cytokine-mediated signaling pathway annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0030275 LRR domain binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: KRAS can interact with LRR-containing SHOC2 in the SHOC2-PP1C-RAS regulatory system, but LRR domain binding is not the core KRAS molecular function. Reason: The orthology-transferred MF term overemphasizes one regulator interaction. The functional consequence is better represented by Ras/MAPK signaling annotations. Supporting Evidence: PMID:36175670 The canonical RAS family members HRAS, KRAS, and NRAS (H/K/NRAS) also bind SHOC2 |
| GO:0035900 response to isolation stress | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The response to isolation stress annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0051384 response to glucocorticoid | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The response to glucocorticoid annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0051385 response to mineralocorticoid | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The response to mineralocorticoid annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0051450 myoblast proliferation | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The myoblast proliferation annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:0060038 cardiac muscle cell proliferation | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The cardiac muscle cell proliferation annotation is an orthology-transferred high-level biological-process term and is not directly supported as a specific human KRAS function in the reviewed evidence. Reason: These developmental, stress, hormone, cytokine, or cell-type proliferation terms are likely indirect consequences of Ras pathway perturbation or non-human phenotype propagation. They overstate the direct functional role of KRAS. |
| GO:2000774 positive regulation of cellular senescence | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: RAS pathway activation can be associated with cellular senescence in oncogene-stress contexts, but this is a context-dependent downstream outcome. Reason: The term should not be considered core for KRAS; it reflects a cellular response to signaling intensity and context rather than the conserved molecular role. |
| GO:0005515 protein binding | IPI PMID:23524970 Desmoglein-1/Erbin interaction suppresses ERK activation to ... | REMOVE | Summary: This protein binding annotation records a physical interaction, but GO:0005515 is too generic to describe KRAS function. Reason: Protein binding is specifically uninformative for KRAS. Specific effector/regulator interactions should support Ras signaling, MAPK cascade, PI3K signaling, or localization annotations rather than a generic protein binding MF term. |
| GO:0005737 cytoplasm | IDA PMID:23524970 Desmoglein-1/Erbin interaction suppresses ERK activation to ... | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0005886 plasma membrane | IDA PMID:23524970 Desmoglein-1/Erbin interaction suppresses ERK activation to ... | ACCEPT | Summary: IDA annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0007265 Ras protein signal transduction | IDA PMID:38188543 Studying early structural changes in SOS1 mediated KRAS acti... | ACCEPT | Summary: IDA annotation for Ras protein signal transduction. KRAS participates directly in Ras signaling through SOS-mediated activation and effector engagement. Reason: This process annotation is appropriate for KRAS, whose active GTP-bound form transmits receptor inputs to downstream pathways including RAF-MEK-ERK and PI3K-AKT-mTOR. Supporting Evidence: PMID:38188543 SOS1 facilitates the exchange of GDP to GTP thereby leading to activation of KRAS Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active file:human/KRAS/KRAS-deep-research-falcon.md Primary structural evidence for Ras activation by SOS comes from the crystal structure of Ras in complex with the SOS catalytic region, indicating SOS stabilizes Ras in a nucleotide-free state, a mechanistic basis for GEF-driven exchange. |
| GO:0032008 positive regulation of TOR signaling | NAS PMID:39788953 Structural insights into isoform-specific RAS-PI3KΞ± interact... | KEEP AS NON CORE | Summary: RAS-PI3Kalpha interaction can amplify PI3K-AKT-mTOR signaling, placing KRAS upstream of TOR pathway activation in some contexts. Reason: This is a supported effector branch but not the primary core function; KRAS is best represented first as a membrane-associated small GTPase in Ras/MAPK signaling. Supporting Evidence: PMID:39788953 Their interaction plays a crucial role in activating PI3KΞ± and amplifying the PI3K-AKT-mTOR pathway |
| GO:0042127 regulation of cell population proliferation | NAS PMID:38188543 Studying early structural changes in SOS1 mediated KRAS acti... | KEEP AS NON CORE | Summary: KRAS signaling can promote cell proliferation through MAPK and PI3K effector pathways, but proliferation is a downstream cellular outcome rather than the molecular core function. Reason: The annotation is biologically plausible and supported by pathway literature, but it should not be treated as the core activity of KRAS. Supporting Evidence: Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active PMID:39788953 Their interaction plays a crucial role in activating PI3KΞ± and amplifying the PI3K-AKT-mTOR pathway |
| GO:0043069 negative regulation of programmed cell death | NAS PMID:39788953 Structural insights into isoform-specific RAS-PI3KΞ± interact... | MARK AS OVER ANNOTATED | Summary: Negative regulation of programmed cell death can occur downstream of RAS effector pathways, especially through PI3K-AKT survival signaling, but the annotation is broad. Reason: The cited PI3Kalpha structural work supports RAS-PI3K pathway activation, not a direct KRAS role in the general programmed cell death process. Supporting Evidence: PMID:39788953 Their interaction plays a crucial role in activating PI3KΞ± and amplifying the PI3K-AKT-mTOR pathway |
| GO:0043410 positive regulation of MAPK cascade | NAS PMID:33608534 KRAS interaction with RAF1 RAS-binding domain and cysteine-r... | ACCEPT | Summary: KRAS positively regulates the MAPK cascade through direct active-RAS interaction with RAF-family kinases. Reason: This is an accurate pathway-level annotation for the canonical KRAS effector branch. Supporting Evidence: Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active |
| GO:1902554 serine/threonine protein kinase complex | IPI PMID:33608534 KRAS interaction with RAF1 RAS-binding domain and cysteine-r... | MARK AS OVER ANNOTATED | Summary: The cited RAF1 structural work supports KRAS binding to RAF regulatory domains during RAF activation, not stable membership in a serine/threonine protein kinase complex. Reason: KRAS is an upstream small GTPase effector-binding partner for RAF; representing it as part of a kinase complex overstates a transient signaling interaction. Supporting Evidence: Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active |
| GO:1905360 GTPase complex | IPI PMID:39043660 Allosteric nanobodies to study the interactions between SOS1... | MARK AS OVER ANNOTATED | Summary: The GTPase complex annotation is based on a structural interaction context rather than evidence that KRAS is a stable component of a native cellular complex. Reason: KRAS forms transient complexes with GEFs, GAPs, effectors, inhibitors, and structural binders. A generic GTPase complex cellular-component term is not informative as a gene-level KRAS annotation. |
| GO:0000164 protein phosphatase type 1 complex | IPI PMID:36175670 Structure of the SHOC2-MRAS-PP1C complex provides insights i... | MARK AS OVER ANNOTATED | Summary: SHOC2-MRAS-PP1C studies show that canonical RAS proteins, including KRAS, can bind this regulatory phosphatase system with lower affinity than MRAS. Reason: The core complex is SHOC2-MRAS-PP1C. Assigning KRAS as part of a protein phosphatase type 1 complex overstates a non-core, weaker regulatory interaction. Supporting Evidence: PMID:36175670 The canonical RAS family members HRAS, KRAS, and NRAS (H/K/NRAS) also bind SHOC2 |
| GO:0046579 positive regulation of Ras protein signal transduction | NAS PMID:35831509 Structure-function analysis of the SHOC2-MRAS-PP1C holophosp... | MODIFY | Summary: This annotation captures KRAS-dependent positive signaling but frames the role as regulation of Ras signaling rather than direct participation in the Ras/MAPK pathway. Reason: The evidence is better represented by KRAS involvement in Ras protein signal transduction and positive regulation of the MAPK cascade. Proposed replacements: Ras protein signal transduction positive regulation of MAPK cascade Supporting Evidence: PMID:36175670 The canonical RAS family members HRAS, KRAS, and NRAS (H/K/NRAS) also bind SHOC2 Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active |
| GO:0000165 MAPK cascade | TAS Reactome:R-HSA-5673001 | ACCEPT | Summary: KRAS participates in the RAF/MAP kinase cascade by recruiting and activating RAF-family kinases when GTP-bound. Reason: Reactome and structural work support active KRAS as an upstream activator of the RAF-MEK-ERK MAPK cascade. Supporting Evidence: Reactome:R-HSA-5673001 GTP-bound RAS recruits RAF (the MAPK kinase kinase), and promotes its dimerization and activation PMID:33608534 Active RAS recruits RAF to the membrane where RAF dimerizes and becomes active |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0003924 GTPase activity | EXP PMID:20949621 Germline KRAS mutations cause aberrant biochemical and physi... | ACCEPT | Summary: EXP annotation for KRAS GTPase activity. KRAS is a Ras-family small GTPase with intrinsic GTP hydrolysis activity and GAP-stimulated hydrolysis. Reason: This is the core molecular activity of KRAS. The UniProt record, Reactome intrinsic GTPase reaction, and biochemical KRAS mutant studies all support GTP hydrolysis as the central catalytic activity. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Ras proteins bind GDP/GTP and possess intrinsic GTPase activity Reactome:R-HSA-9649736 RAS proteins have weak intrinsic GTPase activity in the absence of other effectors file:human/KRAS/KRAS-deep-research-falcon.md A widely cited expert synthesis reports Ras intrinsic hydrolysis is slow (kcat β 2Γ10β4 sβ1), but it is a real enzymatic activity central to the molecular switch. GAPs accelerate Ras hydrolysis (reported up to ~10^5-fold in expert synthesis) and do so by complementing the active site, including an external arginine ("arginine finger") concept. |
| GO:0005886 plasma membrane | EXP PMID:29239724 SIRT2 and lysine fatty acylation regulate the transforming a... | ACCEPT | Summary: EXP annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0012505 endomembrane system | EXP PMID:29239724 SIRT2 and lysine fatty acylation regulate the transforming a... | ACCEPT | Summary: KRAS, especially K-Ras4a under SIRT2-regulated lysine defatty-acylation, can localize to endomembrane compartments. Reason: Endomembrane localization is supported by K-Ras4a acylation experiments and by UniProt subcellular-location curation. Supporting Evidence: PMID:29239724 SIRT2-mediated lysine defatty-acylation promotes endomembrane localization of K-Ras4a file:human/KRAS/KRAS-deep-research-falcon.md KRAS4A contains a palmitoylation site (Cys180) enabling reversible palmitoylation-dependent Golgi trafficking. Expert synthesis notes that farnesylation + palmitoylation can increase membrane affinity by >100-fold and acts as a Golgi "affinity trap" promoting vesicular delivery to the plasma membrane. |
| GO:0003924 GTPase activity | TAS Reactome:R-HSA-9649736 | ACCEPT | Summary: TAS annotation for KRAS GTPase activity. KRAS is a Ras-family small GTPase with intrinsic GTP hydrolysis activity and GAP-stimulated hydrolysis. Reason: This is the core molecular activity of KRAS. The UniProt record, Reactome intrinsic GTPase reaction, and biochemical KRAS mutant studies all support GTP hydrolysis as the central catalytic activity. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Ras proteins bind GDP/GTP and possess intrinsic GTPase activity Reactome:R-HSA-9649736 RAS proteins have weak intrinsic GTPase activity in the absence of other effectors file:human/KRAS/KRAS-deep-research-falcon.md **KRAS is a Ras-family small GTPase** that functions as a GDP/GTP-regulated switch. GTP binding induces conformational changes in **switch I/II** regions enabling effector recognition, while GTP hydrolysis returns KRAS to the GDP-bound state. |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:23698361 Small molecule inhibition of the KRAS-PDEΞ΄ interaction impai... | ACCEPT | Summary: KRAS localizes to the cytoplasmic side of the plasma membrane through C-terminal lipid modification and membrane-targeting motifs. Reason: This is the most precise cellular-component annotation for signaling-competent membrane-associated KRAS. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0003924 GTPase activity | IMP PMID:26037647 Biochemical and Structural Analysis of Common Cancer-Associa... | ACCEPT | Summary: IMP annotation for KRAS GTPase activity. KRAS is a Ras-family small GTPase with intrinsic GTP hydrolysis activity and GAP-stimulated hydrolysis. Reason: This is the core molecular activity of KRAS. The UniProt record, Reactome intrinsic GTPase reaction, and biochemical KRAS mutant studies all support GTP hydrolysis as the central catalytic activity. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Ras proteins bind GDP/GTP and possess intrinsic GTPase activity Reactome:R-HSA-9649736 RAS proteins have weak intrinsic GTPase activity in the absence of other effectors file:human/KRAS/KRAS-deep-research-falcon.md **KRAS is a Ras-family small GTPase** that functions as a GDP/GTP-regulated switch. GTP binding induces conformational changes in **switch I/II** regions enabling effector recognition, while GTP hydrolysis returns KRAS to the GDP-bound state. |
| GO:0005515 protein binding | IPI PMID:24415755 The chaperone protein SmgGDS interacts with small GTPases en... | REMOVE | Summary: This protein binding annotation records a physical interaction, but GO:0005515 is too generic to describe KRAS function. Reason: Protein binding is specifically uninformative for KRAS. Specific effector/regulator interactions should support Ras signaling, MAPK cascade, PI3K signaling, or localization annotations rather than a generic protein binding MF term. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9674816 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9654521 | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9654523 | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9654525 | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9654533 | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9653592 | KEEP AS NON CORE | Summary: Reactome places phosphorylated KRAS4B at the mitochondrial outer membrane in a regulated trafficking/signaling context. Reason: This is context-specific and isoform/modification-state dependent, so it should be kept as non-core rather than treated as a general KRAS localization. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-9653595 | KEEP AS NON CORE | Summary: Reactome places phosphorylated KRAS4B at the mitochondrial outer membrane in a regulated trafficking/signaling context. Reason: This is context-specific and isoform/modification-state dependent, so it should be kept as non-core rather than treated as a general KRAS localization. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9653503 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9653592 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9651280 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802834 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802908 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802918 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802922 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802924 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802925 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802926 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802937 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802941 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802942 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802943 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6803233 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6803234 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6803240 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8936731 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9647977 | KEEP AS NON CORE | Summary: ER membrane annotations reflect CAAX processing and maturation reactions for farnesylated RAS proteins in Reactome. Reason: The ER membrane is relevant to RAS processing but is not the primary location of signaling-competent KRAS. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9647978 | KEEP AS NON CORE | Summary: ER membrane annotations reflect CAAX processing and maturation reactions for farnesylated RAS proteins in Reactome. Reason: The ER membrane is relevant to RAS processing but is not the primary location of signaling-competent KRAS. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9647999 | KEEP AS NON CORE | Summary: ER membrane annotations reflect CAAX processing and maturation reactions for farnesylated RAS proteins in Reactome. Reason: The ER membrane is relevant to RAS processing but is not the primary location of signaling-competent KRAS. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9649732 | KEEP AS NON CORE | Summary: ER membrane annotations reflect CAAX processing and maturation reactions for farnesylated RAS proteins in Reactome. Reason: The ER membrane is relevant to RAS processing but is not the primary location of signaling-competent KRAS. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9647978 | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-9647980 | KEEP AS NON CORE | Summary: Golgi membrane localization is relevant to RAS membrane trafficking and palmitoylation cycles, especially for the K-Ras4A isoform. Reason: This is a plausible trafficking/maturation localization but not the primary signaling location for KRAS. Supporting Evidence: Reactome:R-HSA-9647980 mature RAS proteins translocate to the plasma membrane file:human/KRAS/KRAS-deep-research-falcon.md KRAS4A contains a palmitoylation site (Cys180) enabling reversible palmitoylation-dependent Golgi trafficking. Expert synthesis notes that farnesylation + palmitoylation can increase membrane affinity by >100-fold and acts as a Golgi "affinity trap" promoting vesicular delivery to the plasma membrane. |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-9647982 | KEEP AS NON CORE | Summary: Golgi membrane localization is relevant to RAS membrane trafficking and palmitoylation cycles, especially for the K-Ras4A isoform. Reason: This is a plausible trafficking/maturation localization but not the primary signaling location for KRAS. Supporting Evidence: Reactome:R-HSA-9647980 mature RAS proteins translocate to the plasma membrane file:human/KRAS/KRAS-deep-research-falcon.md KRAS4A contains a palmitoylation site (Cys180) enabling reversible palmitoylation-dependent Golgi trafficking. Expert synthesis notes that farnesylation + palmitoylation can increase membrane affinity by >100-fold and acts as a Golgi "affinity trap" promoting vesicular delivery to the plasma membrane. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1168636 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225951 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225957 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250383 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306972 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1433471 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-170986 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177938 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177945 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-186834 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-210977 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2179407 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2424477 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-392054 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5218845 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5621573 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5624486 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5624492 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5624494 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637806 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637808 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654392 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654402 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654413 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654426 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654600 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654618 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654647 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5654663 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655241 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655277 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655326 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5655347 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5658231 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5658435 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672950 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672965 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672966 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672969 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672972 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672973 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672978 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672980 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5674018 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5674022 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5675417 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5675431 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5675433 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802837 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8851827 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8851877 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8851899 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8941613 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8941618 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8941623 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8941628 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8981353 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8981355 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9607304 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9632906 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9632918 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9634418 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9647980 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9647994 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9649733 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9649735 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9649736 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9653108 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9656209 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9656211 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9656212 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9656213 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9656214 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9656215 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9657599 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9657603 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9657606 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9657608 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9658253 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664991 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665009 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665404 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665408 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665700 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665707 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9670436 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9672163 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9672170 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9695853 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9703441 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9647982 | KEEP AS NON CORE | Summary: ER membrane annotations reflect CAAX processing and maturation reactions for farnesylated RAS proteins in Reactome. Reason: The ER membrane is relevant to RAS processing but is not the primary location of signaling-competent KRAS. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9649732 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9653585 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9654521 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9654533 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0044877 protein-containing complex binding | IDA PMID:23209302 KIF14 negatively regulates Rap1a-Radil signaling during brea... | REMOVE | Summary: The protein-containing complex binding annotation is broad and the cited paper is not KRAS-centered; it does not clarify KRAS molecular function. Reason: This generic binding term is not useful for KRAS and appears to come from a broad complex-binding assertion rather than evidence for a specific KRAS activity. |
| GO:0005737 cytoplasm | IDA PMID:23698361 Small molecule inhibition of the KRAS-PDEΞ΄ interaction impai... | ACCEPT | Summary: KRAS has a cytoplasmic/cytosolic pool during its membrane-trafficking cycle, including PDEdelta-mediated solubilization of farnesylated KRAS. Reason: Although signaling-competent KRAS is membrane-associated, cytosolic localization is supported as part of its trafficking and recycling cycle. Supporting Evidence: PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ file:human/KRAS/KRAS-deep-research-falcon.md KRAS4B (and depalmitoylated prenylated cargo) can bind PDE6D to shield its prenyl group and support trafficking between endomembranes and plasma membrane. Quantitatively summarized evidence indicates that loss of KRAS4B carboxymethylation reduces PDE6D affinity by >35-fold, and a Ser181 phosphomimic (S181E) reduces affinity by >6-fold. |
| GO:0005925 focal adhesion | HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome... | MARK AS OVER ANNOTATED | Summary: The focal adhesion annotation comes from high-throughput proteomic detection rather than targeted KRAS localization evidence. Reason: Focal adhesion is not a supported core or well-established localization for KRAS in the reviewed evidence. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | MARK AS OVER ANNOTATED | Summary: The generic membrane annotation is directionally correct for lipid-anchored KRAS but lacks the useful subcellular specificity available from curated evidence. Reason: KRAS has more specific and better-supported plasma membrane, cytoplasmic-side-of-plasma-membrane, endomembrane, and cytosolic localization annotations. Generic membrane should not be used as an informative KRAS localization. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802914 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802915 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802916 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802919 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6802921 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6803230 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8936676 | ACCEPT | Summary: TAS annotation for plasma membrane localization. KRAS is lipid-anchored and functions at the cytoplasmic face of the plasma membrane. Reason: Plasma membrane localization is well supported by UniProt, PDEdelta localization work, K-Ras4a acylation work, and many Reactome RAS pathway events. Supporting Evidence: file:human/KRAS/KRAS-uniprot.txt Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor PMID:23698361 Correct localization and signalling by farnesylated KRAS is regulated by the prenyl-binding protein PDEΞ΄ |
| GO:0010628 positive regulation of gene expression | IMP PMID:22065586 Oncogenic Ras and B-Raf proteins positively regulate death r... | MARK AS OVER ANNOTATED | Summary: Oncogenic Ras can increase expression of specific genes such as DR5 through ERK/JNK-dependent transcription factor activation. Reason: The evidence concerns oncogenic Ras/B-Raf regulation of a specific death receptor transcriptional response. The broad gene expression term is a downstream, mutant/context-dependent outcome rather than a general KRAS function. |
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Download this section (compressed HTML)Q: Which KRAS4A and KRAS4B functions should be represented as isoform-specific GO annotations rather than gene-level annotations?
Q: Should SHOC2-PP1C complex annotations be restricted to MRAS, or should weak H/K/NRAS interactions support non-core annotations?
Q: Can KRAS mitochondrial outer membrane localization be curated as a modification- or isoform-specific function rather than a general localization?
Q: Should pathway-level proliferation, senescence, and programmed cell death annotations be retained for KRAS or replaced by more direct Ras/MAPK and PI3K pathway terms?
Experiment: Endogenous isoform-specific tagging or proteomics to quantify KRAS4A and KRAS4B localization across plasma membrane, Golgi, ER, endomembrane, cytosol, and mitochondria.
Hypothesis: Gene-level KRAS localization annotations conflate distinct KRAS4A and KRAS4B trafficking mechanisms.
Experiment: Compare endogenous KRAS, NRAS, HRAS, and MRAS binding to SHOC2-PP1C under matched nucleotide-loading and membrane conditions.
Hypothesis: Canonical RAS isoforms bind SHOC2-PP1C weakly relative to MRAS and should not receive core phosphatase-complex component annotations.
Experiment: Use pathway-resolved KRAS perturbation with rescue by GTPase, effector-binding, and localization mutants to separate direct MAPK/PI3K signaling from downstream proliferation and gene-expression outcomes.
Hypothesis: Most broad biological-process annotations for KRAS are downstream consequences of Ras effector signaling rather than direct gene-level functions.
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