Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Automatic Gene Ontology annotation based on Rhea mapping

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

14-3-3Gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells.

JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway.

Hepatitis C virus core protein interacts with 14-3-3 protein and activates the kinase Raf-1.

Functional conservation of 14-3-3 isoforms in inhibiting bad-induced apoptosis.

Identification of interaction between MEK2 and A-Raf-1.

Di-Ras, a distinct subgroup of ras family GTPases with unique biochemical properties.

Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis.

Dynamic changes in C-Raf phosphorylation and 14-3-3 protein binding in response to growth factor stimulation: differential roles of 14-3-3 protein binding sites.

Raf kinase activation of adenylyl cyclases: isoform-selective regulation.

Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer.

Raf-1 is a binding partner of DSCR1.

Second nature: biological functions of the Raf-1 "kinase".

CAPRI and RASAL impose different modes of information processing on Ras due to contrasting temporal filtering of Ca2+.

Positive regulation of Raf1-MEK1/2-ERK1/2 signaling by protein serine/threonine phosphatase 2A holoenzymes.

14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK.

Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones.

Raf-1 kinase associates with Hepatitis C virus NS5A and regulates viral replication.

Back to the roots: the remarkable RAF oncogene story.

A dimeric kinase assembly underlying autophosphorylation in the p21 activated kinases.

Regulation of RKIP binding to the N-region of the Raf-1 kinase.

DYRK1A autophosphorylation on serine residue 520 modulates its kinase activity via 14-3-3 binding.

Gain-of-function RAF1 mutations cause Noonan and LEOPARD syndromes with hypertrophic cardiomyopathy.

Spatial regulation of Raf kinase signaling by RKTG.

A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes.

GRP78 and Raf-1 cooperatively confer resistance to endoplasmic reticulum stress-induced apoptosis.

Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf.

A novel switch region regulates H-ras membrane orientation and signal output.

Endothelial nitric oxide synthase regulates N-Ras activation on the Golgi complex of antigen-stimulated T cells.

Regulation of RAF activity by 14-3-3 proteins: RAF kinases associate functionally with both homo- and heterodimeric forms of 14-3-3 proteins.

Regulation of growth and survival of activated T cells by cell-transducing inhibitors of Ras.

Identification of small-molecule inducers of pancreatic beta-cell expansion.

Regulation of human myoblast differentiation by PEBP4.

Reassessment of the role of FKBP38 in the Rheb/mTORC1 pathway.

The C-terminus of Raf-1 acts as a 14-3-3-dependent activation switch.

Identification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylation.

Nucleocytoplasmic transport of Alp7/TACC organizes spatiotemporal microtubule formation in fission yeast.

Molecular and clinical analysis of RAF1 in Noonan syndrome and related disorders: dephosphorylation of serine 259 as the essential mechanism for mutant activation.

Ras membrane orientation and nanodomain localization generate isoform diversity.

RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth.

Allosteric gating of Son of sevenless activity by the histone domain.

Kinase-dead BRAF and oncogenic RAS cooperate to drive tumor progression through CRAF.

Genetic and functional characterization of putative Ras/Raf interaction inhibitors in C. elegans and mammalian cells.

Active Mek2 as a regulatory scaffold that promotes Pin1 binding to BPGAP1 to suppress BPGAP1-induced acute Erk activation and cell migration.

The prolyl isomerase Pin1 enhances HER-2 expression and cellular transformation via its interaction with mitogen-activated protein kinase/extracellular signal-regulated kinase kinase 1.

Impaired binding of 14-3-3 to C-RAF in Noonan syndrome suggests new approaches in diseases with increased Ras signaling.

K-Ras4B phosphorylation at Ser181 is inhibited by calmodulin and modulates K-Ras activity and function.

Rb-Raf-1 interaction disruptor RRD-251 induces apoptosis in metastatic melanoma cells and synergizes with dacarbazine.

The membrane localization of Ras2p and the association between Cdc25p and Ras2-GTP are regulated by protein kinase A (PKA) in the yeast Saccharomyces cerevisiae.

ERK and PDE4 cooperate to induce RAF isoform switching in melanoma.

The Ras signaling inhibitor LOX-PP interacts with Hsp70 and c-Raf to reduce Erk activation and transformed phenotype of breast cancer cells.

Raf family kinases: old dogs have learned new tricks.

15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells.

Toward an understanding of the protein interaction network of the human liver.

Nilotinib and MEK inhibitors induce synthetic lethality through paradoxical activation of RAF in drug-resistant chronic myeloid leukemia.

Distinct requirement for an intact dimer interface in wild-type, V600E and kinase-dead B-Raf signalling.

FAM83B mediates EGFR- and RAS-driven oncogenic transformation.

FAM83A confers EGFR-TKI resistance in breast cancer cells and in mice.

Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition.

MASL1 induces erythroid differentiation in human erythropoietin-dependent CD34+ cells through the Raf/MEK/ERK pathway.

Phosphodiesterase-8A binds to and regulates Raf-1 kinase.

RAF inhibitors activate the MAPK pathway by relieving inhibitory autophosphorylation.

Mechanism of MEK inhibition determines efficacy in mutant KRAS- versus BRAF-driven cancers.

Structure homology and interaction redundancy for discovering virus-host protein interactions.

Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms.

Protein interaction network of the mammalian Hippo pathway reveals mechanisms of kinase-phosphatase interactions.

Nuclear Raf-1 kinase regulates the CXCR5 promoter by associating with NFATc3 to drive retinoic acid-induced leukemic cell differentiation.

The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells.

Conserved oncogenic behavior of the FAM83 family regulates MAPK signaling in human cancer.

Disruption of CRAF-mediated MEK activation is required for effective MEK inhibition in KRAS mutant tumors.

Protein interaction switches coordinate Raf-1 and MST2/Hippo signalling.

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

A Novel SHOC2 Variant in Rasopathy.

Structure of the BRAF-MEK complex reveals a kinase activity independent role for BRAF in MAPK signaling.

Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.

Allosteric effects of the oncogenic RasQ61L mutant on Raf-RBD.

Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy.

RAF inhibitors that evade paradoxical MAPK pathway activation.

A human interactome in three quantitative dimensions organized by stoichiometries and abundances.

Architecture of the human interactome defines protein communities and disease networks.

Interrogating the protein interactomes of RAS isoforms identifies PIP5K1A as a KRAS-specific vulnerability.

A YWHAZ Variant Associated With Cardiofaciocutaneous Syndrome Activates the RAF-ERK Pathway.

Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).

A reference map of the human binary protein interactome.

Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.

Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.

KRAS interaction with RAF1 RAS-binding domain and cysteine-rich domain provides insights into RAS-mediated RAF activation.

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

A protein interaction landscape of breast cancer.

A protein network map of head and neck cancer reveals PIK3CA mutant drug sensitivity.

Proteome-scale mapping of binding sites in the unstructured regions of the human proteome.

OpenCell: Endogenous tagging for the cartography of human cellular organization.

Systematic discovery of mutation-directed neo-protein-protein interactions in cancer.

A Proteomic Approach Identifies Isoform-Specific and Nucleotide-Dependent RAS Interactions.

Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF activation and Noonan syndrome.

HERC2 deficiency activates C-RAF/MKK3/p38 signalling pathway altering the cellular response to oxidative stress.

A central chaperone-like role for 14-3-3 proteins in human cells.

Interactome dynamics of RAF1-BRAF kinase monomers and dimers.

Systematic identification of post-transcriptional regulatory modules.

Multimodal cell maps as a foundation for structural and functional genomics.

14-3-3 proteins associate with cdc25 phosphatases.

14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner.

The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue.

Regulation of Raf-1 kinase activity by the 14-3-3 family of proteins.

Activation of Raf-1 by 14-3-3 proteins.

Interaction of the protein kinase Raf-1 with 14-3-3 proteins.

Signaling through transforming G protein-coupled receptors in NIH 3T3 cells involves c-Raf activation. Evidence for a protein kinase C-independent pathway.

Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation.

Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1.

Interleukin-8 regulation of the Ras/Raf/mitogen-activated protein kinase pathway in human neutrophils.

Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine.

Identification of a novel Rac1-interacting protein involved in membrane ruffling.

Ras/Rap effector specificity determined by charge reversal.

Bcl-2 targets the protein kinase Raf-1 to mitochondria.

14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner.

Protein binding and signaling properties of RIN1 suggest a unique effector function.

Interferon gamma activation of Raf-1 is Jak1-dependent and p21ras-independent.

Binding of c-Raf1 kinase to a conserved acidic sequence within the carboxyl-terminal region of the HIV-1 Nef protein.

Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling.

RAF1:SGK:TSC22D3:WPP ubiquitinates SCNN channels

Rap1 sequesters Raf1 to inhibit ERK cascade

c-Src binds Raf1

14-3-3-zeta binds Raf1

SFKs phosphorylates RAF1 on Y340,Y341

PAK phosphorylates p21 RAF1 on S338

RAF1 binds p21 RAS:GTP

Inactive RAFs bind YWHAB

YWHAB dimer dissociates from dephosphorylated RAF

PP2A dephosphorylates inactive RAFs

RAS:GTP:'activator' RAF homo/heterodimerizes with other RAF monomers

Phosphorylation of RAF

MAP2Ks and MAPKs bind to the activated RAF complex

MAP2Ks phosphorylate MAPKs

RAF phosphorylates MAP2K dimer

Dissociation of RAS:RAF complex

MAP2Ks and MAPKs are phosphorylated at the endosome membrane

WDR83:LAMTOR2:LAMTOR3 binds MAPK components

PAQR3 binds inactive RAFs

Activated MAPK phosphorylates RAF1

PEBP1 binds activated RAF1

PP2A dephosphorylates RAF1

PP5 dephosphorylates RAF1 S338

RAS mutants bind inactive RAF

RAS:GTP:moderate kinase activity p-RAF complexes bind MAP2Ks and MAPKs

RAF is phosphorylated downstream of moderate kinase activity BRAF mutants

Activated MAP2Ks phosphorylate MAPKs downstream of inactive BRAF mutants

RAS:GTP:moderate kinase activity p-RAF complexes phosphorylate MAP2Ks

Activated MAP2Ks phosphorylate MAPKs downstream of moderate kinase activity BRAF mutants

Activated MAP2Ks phosphorylate MAPKs downstream of oncogenic RAS

RAF is phosphorylated downstream of oncogenic RAS

Mutant RAS:p-RAF complexes bind MAP2Ks and MAPKs

Mutant RAS:p-RAF complexes phosphorylate MAP2Ks

RAF is paradoxically phosphorylated downstream of kinase-inactive RAF

RAS:GTP:p-RAF complexes paradoxically bind MAP2Ks and MAPKs

RAS:GTP:inactive p-RAF complexes phosphorylate MAP2Ks

Dissociation of moderate activity BRAF complexes

Dissociation of oncogenic RAS:RAF complex

Dissociation of paradoxically activated RAS:BRAF complexes

Homo- or heterodimerization of RAF downstream of mutant RAS

Interferon gamma signaling

Moderate kinase activity BRAF mutants:RAS:GTP homo/heterodimerize

Inactive BRAF mutants:mutant RAS:GTP bind RAF1

Raf dimer inhibitors bind RAF heterodimers

CR2 RAF1 mutants don't bind YWHAB

Dissociation of RAS:RAF1 mutant complex

MAP2Ks and MAPKs bind to the activated mutant RAF1 complex

Phosphorylation of RAF1 mutants

RAF1 mutants show enhanced heterodimerization with BRAF

MAP2Ks phosphorylate MAPKs downstream of RAF1 mutants

RAF1 mutant complexes phosphorylate MAP2K dimer

Dual mechanism MAP2K inhibitors bind MAP2Ks

Dual mechanism MAPK inhibitors bind MAPKs

Single mechanism MAP2K inhibitors bind phosphorylated MAP2Ks

Single mechanism MAPK inhibitors bind phosphorylated MAPK

MRAS:SHOC2:PPP1CC dephosphorylates inactive RAFs

SHOC2 M173I disrupts the SHOC2:MRAS:PP1 complex

Mutant MRAS:SHOC2:PPP1CC complexes dephosphorylate inactive RAFs

Activated JAK1 binds RAF1

JAK1-mediated phosphorylation of RAF1

JAK1-activated RAF1 phosphorylates MAPKs

UniProt record for human RAF1 (P04049)

Falcon deep research report for human RAF1