Official Symbol: RAF1provided by HGNC
Official Full Name: v-raf-1 murine leukemia viral oncogene homolog 1provided by HGNC
Primary Source: HGNC:9829
See related: Ensembl:ENSG00000132155; HPRD:01265; MIM:164760
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: NS5; CRAF; Raf-1; c-Raf; RAF1
Summary: This gene is the cellular homolog of viral raf gene (v-raf). The encoded protein is a MAP kinase kinase kinase (MAP3K), which functions downstream of the Ras family of membrane associated GTPases to which it binds directly. Once activated, the cellular RAF1 protein can phosphorylate to activate the dual specificity protein kinases MEK1 and MEK2, which in turn phosphorylate to activate the serine/threonine specific protein kinases, ERK1 and ERK2. Activated ERKs are pleiotropic effectors of cell physiology and play an important role in the control of gene expression involved in the cell division cycle, apoptosis, cell differentiation and cell migration. Mutations in this gene are associated with Noonan syndrome 5 and LEOPARD syndrome 2. [provided by RefSeq]

[Top][Help]Genomic regions, transcripts, and products

(minus strand) Go to reference sequence details Try our new Sequence Viewer

[Top][Help]Genomic context

chromosome: 3; Location: 3p25See RAF1 in MapViewer

[Top][Help]Bibliography

GeneRIFs: Gene References Into Function What's a GeneRIF?

	1.	Data show that in the presence of negative feedback, changes in the rate of Ras-c-Raf binding have little effect on ERK activation.
	2.	DC-SIGN was constitutively associated with a signalosome complex consisting of the scaffold proteins LSP1, KSR1 and CNK and the kinase Raf-1.
	3.	Raf-1 may interfere with the role of Rad24 by competing with Rad24 for binding to Cdc25 in DNA repair, bypassing the checkpoint pathway through Cdc25 activation.
	4.	Sorafenib inhibits NSCLC cell growth by targeting B-RAF in cells with wild-type KRAS and C-RAF in those with mutant KRAS.
	5.	Results identify a nuclear redistribution of Raf1 during the retinoic acid-induced differentiation of HL-60 cells.
	6.	Targeting NRAS alone or both BRAF and CRAF in combination or both BRAF and PIK3CA together showed delay in tumor growth.
	7.	loss of RKIP is a functional somatic event in carriers of C-RAF germline mutations, which contributes to the development of t-AML
	8.	GILZ1 and SGK1 provide a physical and functional link between the PI3K- and Raf-1-dependent signaling modules
	9.	Oncogenic RAF1 rearrangement and a novel BRAF mutation as alternatives to KIAA1549:BRAF fusion in activating the MAPK pathway in pilocytic astrocytoma.
	10.	Vitamin D3-triggered differentiation of human myeloid leukemia cells depends on downregulation of Akt, which dissociates from Raf1 and activates MAPK signaling.
	11.	phosphatidate promotes ERK phosphorylation in intact cells but does not activate Raf in vitro
	12.	study identified a group of melanomas with low-activity BRAF mutations (G469E- and D594G) that are reliant upon CRAF-mediated survival activity
	13.	the molecular interactions of arrestin2 and arrestin3 and their individual domains with the components of the two MAPK cascades, ASK1-MKK4-JNK3 and c-Raf-1-MEK1-ERK2
	14.	dectin-1 activates two independent signaling pathways, one through Syk and one through Raf-1, to induce immune responses.
	15.	Mutations in the RAF1 are associated with Noonan syndrome.
	16.	Alpha-adducin and Raf-1 kinase are redistributed and localized to the inclusion membrane in Chlamydia and Chlamydophila infected cells.
	17.	RAF may induce cell proliferation through hypermethylation of tumor suppressor gene p16INK4A
	18.	These data show an unexpected role of XIAP and cellular-inhibitor of apoptosis proteins in the turnover of C-RAF protein, thereby modulating the MAPK signalling pathway and cell migration.
	19.	The state of activation of components of mTOR, Ras/Raf kinase/ERK, and nuclear factor (NF)-kappaB signal transduction pathways, as well as cell cycle protein analyte correlates in gastric adenocarcinoma cases, was examined.
	20.	PAK5 is a potent regulator of Raf-1 activity and may control Raf-1 dependent signaling at mitochondria
	21.	AhR is a master regulator of c-raf and propose cross-talk between AhR and the mitogen-activated protein kinase signaling pathway.
	22.	RAS signaling in colorectal carcinomas through alteration of RAS, RAF, NF1, and/or RASSF1a.
	23.	C-RAF is the only isoform that directly binds mitochondria
	24.	Increased Raf-1 kinase is associated with glioma formation
	25.	the Rb/Raf-1 interaction has a role in cell proliferation and angiogenesis
	26.	A pathway comprising PKCs>Raf-1>MEK-1>ERK-1/-2 mediates the effect of gastrin on the CgA promoter, and strongly suggests that enhanced phosphorylation of Sp1 and CREB is crucial for CgA transactivation through the G protein-coupled CCK-B/gastrin receptor.
	27.	Loss-of-function RKIP mutants still appear to bind to Raf-1. However the stability of the complexes formed between mutants and the N-region Raf-1 phosphopeptide were drastically reduced.
	28.	GRP78 may stabilize Raf-1 to maintain mitochondrial permeability and thus protect cells from endoplasmic reticulum stress-induced apoptosis.
	29.	These results suggest that oncogenic ras-p21 induces phosphorylation of both raf-Ser259 and Ser338 and that raf-Ser 259 phosphorylation may be effected by activated JNK.
	30.	Observational study of gene-disease association. (HuGE Navigator)
	31.	These results suggest that 0.05 Gy of ionizing radiation stimulates cell proliferation through the transient activation of Raf and Akt in CCD-18 Lu cells.
	32.	Raf-1 in beta-cells led to a striking loss of Bad phosphorylation at serine 112 and an increase in the protein levels of both Bad and Bax
	33.	activated Ras, Golgi apparatus-localized Lck is needed for the full activation of Raf-1
	34.	results show overexpression of RAF-1 in mantle cell leukemia compared with tonsilar B-lymphocytes
	35.	cAMP suppresses CRAF in melanocytes. This suppresses the oncogenic potential of CRAF. When RAS is mutated in melanoma, the cells switch their signaling from BRAF to CRAF, dysregulating cAMP signaling & allowing CRAF to signal to MEK.
	36.	In contrast to C-RAF that requires farnesylated H-Ras, cytosolic B-RAF associates effectively and with significantly higher affinity with both farnesylated and nonfarnesylated H-Ras.
	37.	reveal a paradigm of spatial regulation of Raf kinase by RKTG via sequestrating Raf-1 to the Golgi apparatus and thereby inhibiting the ERK signaling pathway
	38.	Study reports that 18 of 231 individuals with Noonan syndrome and 2 of 6 individuals with LEOPARD syndrome without PTPN11 mutations have missense mutations in RAF1, which encodes a serine-threonine kinase that activates MEK1 and MEK2.
	39.	Study identified 5 mutations in RAF1 in 10 individuals with Noonan syndrome; those with mutations causing changes in the CR2 domain of RAF1 had hypertrophic cardiomyopathy, while those with mutations leading to changes in the CR3 domain did not.
	40.	These data show that Ser-259 dephosphorylation contributes to Raf-1 activation by supporting its membrane accumulation rather than by increasing the specific activity of the kinase
	41.	RAF1 promotes herpesvirus 8 infection.
	42.	Data suggest that Raf-1 may interfere with the role of Rad24 by competing with Rad24 for binding to Cdc25 or a direct phosphorylation of Cdc25, bypassing the checkpoint pathway in DNA repair through Cdc25 activation.
	43.	a functional phosphatidate binding site is necessary for Raf-1 function in embryonic development
	44.	results show that raf-1 protein induction suppresses neuroendocrine marker and hormone production in human gastrointestinal carcinoid cells via a pathway dependent on MEK activation
	45.	Raf activation increased the expression of cyclin A, cyclin D, cyclin E, and p21(Cip1), which are associated with G(1) progression
	46.	different pathogens (ie. Mycobacterium tuberculosis, M. leprae, Candida albicans, measles virus, and HIV-1) interacted with DC-SIGN to activate the Raf-1-acetylation-dependent signaling pathway to modulate signaling by different TLRs
	47.	proteomic analysis of Raf-1 signaling complexes was used to show that Raf-1 counteracts apoptosis by suppressing the activation of mammalian sterile 20-like kinase (MST2)
	48.	Results indicate that the phosphorylation of Ser(338) and Tyr(341) on Raf-1 exerts an important effect on reconfiguring the two MEK1-binding sites.
	49.	results suggest that activated JNK can, in turn, activate not only jun but also raf that, in turn, activates MEK that can then cross-activate JNK in a positive feedback loop
	50.	intracellular generation of NO* by nNOS leads to S-nitrosylation of H-Ras, which interferes with Raf-1 activation and propagation of signalling through ERK1/2
	51.	Rodent and human tumor cells containing constitutively activated Raf/Raf/MEK/ERK pathways were resistant to mda-5-induced killing.
	52.	Raf1 potentiates drug-stimulated cyclic AMP accumulation in cells expressing adenyl cyclcase 6 after activation of multiple signaling pathways.
	53.	This work provides new insight into how the cell microenvironment may influence Raf-1 expression to modulate cell-Fibronectin interactions in 3D.
	54.	Based on these findings, we speculate that Raf-1 is activated to effectively mediate Ras-dependent signals in Alzheimer's disease.
	55.	Raf-1 phosphorylation on serine 338 (S338) is a critical step in EGF aktivation of ERK that is lost in nonadherent cells.
	56.	Activation of the ras/raf-1 signal transduction pathway leads to prominent phenotypic changes that resemble differentiation of gastrointestinal carcinoid cells in vitro.
	57.	PAK1 primes MEK1 for phosphorylation by Raf-1 kinase during cross-cascade activation of the ERK pathway.
	58.	Rheb has a central role in the regulation of the Ras/B-Raf/C-Raf/MEK signaling network
	59.	PP2A ABalphaC and ABdeltaC holoenzymes function as positive regulators of Raf1-MEK1/2-ERK1/2 signaling by targeting Raf1
	60.	targeted expression inhibits juvenile myelomonocytic leukemia cell growth
	61.	a novel Ras-independent ERK1/2 activation system in which p110gamma/Raf-1/MEK1/2 and PKA/B-Raf/MEK1/2 cooperate to activate ERK1/2.
	62.	Raf1 kinase is released when it is hyperphosphorylated and activated during oxidative and other stresses
	63.	inhibition of Raf-1 using an antisense raf oligonucleotide (AS-raf-ODN) to identify downstream targets of Raf-1 using microarray gene expression analysis
	64.	These data suggest that GILZ contributes, through protein-to-protein interaction with Raf-1 and the consequent inhibition of Raf-MEK-ERK activation, to regulating the MAPK pathway and to providing a further mechanism underlying GCH immunosuppression.
	65.	c-Raf1 activation occurs without serine 338 phosphorylation
	66.	activation is regulated by CNK1
	67.	Activation of raf-1 leads to cessation of cell growth and suppression of calcitonin and chromogranin A production
	68.	Changes in flexibility upon protein-protein complex formation of H-Ras & the Ras-binding domain of C-Raf1 have been investigated using the molecular framework approach FIRST and molecular dynamics simulations of in total approximately 35 ns length.
	69.	The induction of the raf-1/MEK1 pathway blocks IGF-1-mediated intracellular neuroendocrine hormone regulation. This pathway may be a therapeutic target in gastrointestinal carcinoid tumor therapy.
	70.	These findings support a role of Slug in mediating Raf 1-induced transcriptional repression of occludin and subsequent epithelial to mesenchymal transition.
	71.	Raf1 may have a role in antineoplastic drug resistance
	72.	regulated by an N-terminal autoinhibitory domain whose actions are blocked by interaction with Ras
	73.	CD44 interaction with LARG and EGFR plays a pivotal role in Rho/Ras co-activation, PLC epsilon-Ca2+ signaling, and Raf/ERK up-regulation required for CaMKII-mediated cytoskeleton function and in head and neck squamous cell carcinoma progression
	74.	in human airway smooth muscle cells: TNF-alpha transactivation of the EGF receptor, with subsequent raf-1 kinase-mediated activation of adenylyl cyclase are two linked signaling pathways
	75.	serum stimulation of fibroblasts in floating matrices does not result in ERK translocation to the nucleus and there was decreased serum activation of upstream members of the ERK signaling pathway, MEK and Raf.
	76.	findings indicate that ligation of retinol to a specific site embedded in the regulatory domain is an important feature of c-Raf regulation in the redox pathway.
	77.	selective reduction in catalytic activity and expression of B-Raf but not Raf-1 suggest that B-Raf may be playing an important role in altered ERK signaling in brain of suicide subjects, and thus in the pathophysiology of suicide
	78.	Erbin has a regulatory role in the Ras-Raf-MEK pathway and may inhibit ERK activation by disrupting the Sur-8-Ras/Raf interaction
	79.	Despite the effects of constitutively active Raf on pro-B cell expansion in Raf transgenic mice, Raf activation is not sufficient to rescue early B cell development in IL-7 receptor-deficient mice.
	80.	Raf-1 links mitogenic signaling to Retinoblastoma Protein and that disruption of this interaction could aid in controlling proliferative disorders
	81.	data suggest that Raf-1 is the predominant Raf isoform responsible for regulating cellular growth in ovarian cancer cells and may be particularly important in high grade serous ovarian cancers
	82.	Merlin and MLK3 can interact in situ and merlin can disrupt the interactions between B-Raf and Raf-1 or those between MLK3 and either B-Raf or Raf-1.
	83.	The interaction between eEF-1A and C-Raf increases eEF-1A stability and induces a survival activity.
	84.	effects of paclitaxel on Raf-1 phosphorylation in ovarian cancer cells
	85.	together, our data suggest that the synergistic activation of Raf-1 kinase in response to PMA and H(2)O(2) occurs via mechanisms that involve an interaction of Raf-1 kinase and PKC-epsilon.
	86.	the HER2/Raf-1/AP-1 axis may promote the development of androgen insensitive prostate cancer, leading to early relapse
	87.	Coll I activates the ERK/MAP Kinase pathway in Jurkat T cells through the activation of Ras and Raf-1.
	88.	Data suggest that B-RAF activates C-RAF through a mechanism involving 14-3-3 mediated heterooligomerization and C-RAF transphosphorylation.
	89.	These findings support the thesis that Raf-1 signals cell proliferation and cell differentiation through different intermediary proteins.
	90.	mutation analysis of the conserved regions in the RAF1 gene in human colorectal adenocarcinoma
	91.	Ovarian cancers demonstrate differential sensitivity to antisense oligonucleotides targeted against Raf-1, and target expression levels.
	92.	Role for caspase-9 mediated cleavage of Raf-1 in the negative feedback regulation of hematopoietic cell apoptosis induced by growth factor withdrawal.
	93.	Raf-1 may be involved in angiogenesis by controlling the expression of angiogenesis-related factors; study provides a possible strategy for the treatment of tumor angiogenesis by targeting Raf-1
	94.	Pak1-dependent Raf-1 phosphorylation regulates its mitochondrial localization, phosphorylation of BAD, and Bcl-2 association
	95.	The 1,25(OH)(2)D3-responsive element in cystatin A gene is identical to TRE, T2 (-272 to -278). Suppression of Raf-1/MEK1/ERK1,2 signaling pathway increases cystatin A expression of normal human keratinocytes.
	96.	Raf1 and MAPK-activated protein kinase 2 are activated by L-ascorbic acid in acute myeloid leukemia cells.
	97.	findings implicate Raf-1 as a pivotal regulator of endothelial cell survival during angiogenesis
	98.	Raf-1 may mediate its anti-apoptotic function by interrupting ASK1-dependent phosphorylation of ALG-2.
	99.	findings identify MEK/ERK as a new signaling pathway activated by NPM/ALK and indicate that the pathway represents a novel therapeutic target in the ALK-induced malignancies
	100.	The Raf kinase inhibitory protein (RKIP) binds to Raf-1 interfering with binding of the MEK substrate and potentially also Raf-1 activation.
	101.	The results suggest that multiple cellular signaling pathways can reactivate the virus in a genetically homogeneous cell population. Further analysis revealed that the Raf/MEK/ERK/Ets-1 pathway mediates Ras-induced reactivation.
	102.	Hepatitis B virus X protein stimulates the mitochondrial translocation of Raf-1 via oxidative stress
	103.	Sprouty4 binds to Raf1 through its carboxy-terminal cysteine-rich domain, and this binding is necessary for the inhibitory activity of Sprouty4.
	104.	Raf is regulated through phosphorylation and N terminus-C terminus interaction
	105.	Raf-1 has a role in modulating integrin-stimulated ERK activation when bound to CAMKII
	106.	essential role of Ras-induced conformational change in mitogen-activated protein kinase kinase activation by c-Raf
	107.	phosphorylation by p21-activated kinase 1 and Src regulates Raf-1 autoinhibition
	108.	Nicotine induces cell proliferation by beta-arrestin-mediated activation of the Src and Rb-Raf-1 pathways om ;img camcer.
	109.	These studies identify XIAP as a new substrate of Raf-1.
	110.	c-Raf interacts with MEK1 and activates MEK1 by phosphorylation.

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[Top][Help]HIV-1 protein interactions

Protein	Interaction
1. Envelope surface glycoprotein gp120	Binding of HIV-1 gp120 to CD4 molecules results in the association of Lck and Raf-1, which is abolished by preincubation of the virus with soluble CD4	PubMed
2. Nef	A conserved acidic sequence motif in HIV-1 Nef at positions 174-179 binds to c-Raf1; the interaction of Nef with c-Raf1 leads to a downstream transduction of cell signaling through the c-Raf1-MAP kinase pathway in vivo	PubMed

Go to the HIV-1, Human Protein Interaction Database

[Top][Help]Interactions

Description ..........
Product	Interactant	Other Gene	Complex	Source	Pubs

NP_002871.1	NP_005154.1	AKT1		HPRD	PubMed

NP_002871.1	Androgen receptor	AR		HPRD	PubMed

NP_002871.1	BAG 1	BAG1		HPRD	PubMed

NP_002871.1	Bcl 2	BCL2		HPRD	PubMed

NP_002871.1	NP_004324.1	BRAF		HPRD	PubMed
B-RAF interacts with C-RAF. This interaction was modelled on a demonstrated interaction between human B-RAF and monkey C-RAF .
NP_002871.1	NP_004324.2	BRAF		BIND	PubMed
C-RAF interacts with CCT3.
NP_002871.1	NP_005989.2	CCT3		BIND	PubMed
RAF1 (C-Raf) interacts with CCT3 (hC87).
NP_002871.1	NP_005989.2	CCT3		BIND	PubMed

NP_002871.1	NP_001780.1	CDC25A		HPRD	PubMed

NP_002871.1	c-FLIP	CFLAR		HPRD	PubMed
C-RAF interacts with SGN3.
NP_002871.1	NP_003644.2	COPS3		BIND	PubMed
RAF1 (C-Raf) interacts with COPS3 (SGN3).
NP_002871.1	NP_003644.2	COPS3		BIND	PubMed
C-RAF interacts with CPS1.
NP_002871.1	NP_001866.2	CPS1		BIND	PubMed
RAF1 (C-Raf) interacts with CPS1.
NP_002871.1	NP_001866.2	CPS1		BIND	PubMed

NP_002871.1	Dystrophia myotonica protein kinase	DMPK		HPRD	PubMed
RAF1 (C-Raf) interacts with an unspecified isoform of EFEMP1 (FBNL).
NP_002871.1		EFEMP1		BIND	PubMed

NP_002871.1	Fyn	FYN		HPRD	PubMed

NP_002871.1	NP_005302.2	GRB10		HPRD	PubMed

NP_002871.1	NP_005334.1	HRAS		HPRD	PubMed
C-RAF interacts with Ha-Ras.
NP_002871.1	NP_005334.1	HRAS		BIND	PubMed
RAF1 (C-Raf) interacts with HRAS (Ha-Ras).
NP_002871.1	NP_005334.1	HRAS		BIND	PubMed
Raf-1 interacts with Ras.
NP_002871.1	NP_005334.1	HRAS		BIND	PubMed
Raf interacts with Ras. This interaction was modeled on a demonstrated interaction between human Raf and rat Ras.
NP_002871.1	NP_005334.1	HRAS		BIND	PubMed
Raf interacts with Ras. This interaction was modeled on a demonstrated interaction between Raf and an unspecified source and human Ras.
NP_002871.1	NP_005334.1	HRAS		BIND	PubMed
Hras interacts with Raf. This interaction was modelled on a demonstrated interaction between Hras and Raf, both from an unspecified species.
NP_002871.1		HRAS		BIND	PubMed

NP_002871.1	HSP90A	HSP90AA1		HPRD	PubMed
Raf-1 interacts with Hsp90. This interaction was modeled on a demonstrated interaction between human Raf-1 and monkey Hsp90.
NP_002871.1	NP_005339.2	HSP90AA1		BIND	PubMed

NP_002871.1	NP_000199.1	INSR		HPRD	PubMed

NP_002871.1	Janus kinase 1	JAK1		HPRD	PubMed

NP_002871.1	Janus kinase 2	JAK2		HPRD	PubMed

NP_002871.1	Lck	LCK		HPRD	PubMed

NP_002871.1	MEK1	MAP2K1		HPRD	PubMed
MEK1 interacts with and is phosphorylated by Raf-1. This interaction was modeled on a demonstrated interaction between human MEK1 and Raf-1 from an unspecified species.
NP_002871.1	NP_002746.1	MAP2K1		BIND	PubMed
Raf interacts with and phosphorylates Mek1
NP_002871.1	NP_002746.1	MAP2K1		BIND	PubMed
MEK1 interacts with c-Raf
NP_002871.1	NP_002746.1	MAP2K1		BIND	PubMed
Raf interacts with Mek2.
NP_002871.1	NP_109587.1	MAP2K2		BIND	PubMed
MEKK1 interacts with Raf-1.
NP_002871.1	Q13233	MAP3K1		BIND	PubMed

NP_002871.1	ASK1	MAP3K5		HPRD	PubMed
Raf-1 interacts with ERK2. This interaction was modelled on a demonstrated interaction between human Raf-1 and ERK2 from an unspecified species.
NP_002871.1	NP_002736.2	MAPK1		BIND	PubMed

NP_002871.1	NP_620603.1	MAPK7		HPRD	PubMed

NP_002871.1	NP_055948.1	MAPK8IP3		HPRD	PubMed

NP_002871.1	NP_055948.1	MAPK8IP3		HPRD	PubMed

NP_002871.1	MRAS	MRAS		HPRD	PubMed

NP_002871.1	NP_002458.1	MYC		HPRD	PubMed

NP_002871.1	Glucocorticoid receptor	NR3C1		HPRD	PubMed
Nras interacts with Raf. This interaction was modelled on a demonstrated interaction between Nras and Raf, both from an unspecified species.
NP_002871.1	NP_002515.1	NRAS		BIND	PubMed
RAF1 (C-Raf) interacts with NUDT14 (hA21).
NP_002871.1	NP_803877.2	NUDT14		BIND	PubMed
C-RAF interacts with OIP5.
NP_002871.1	NP_009211.1	OIP5		BIND	PubMed
RAF1 (C-Raf) interacts with OIP5 (hC73).
NP_002871.1	NP_009211.1	OIP5		BIND	PubMed

NP_002871.1	AAC24716.1	PAK1		HPRD	PubMed
RAF1 (C-Raf) interacts with PBK (TOPK).
NP_002871.1	NP_060962.2	PBK		BIND	PubMed

NP_002871.1	PDGF receptor, beta	PDGFRB		HPRD	PubMed
RKIP interacts with Raf-1. This interaction was modelled on a demonstrated interaction between RKIP from an unspecified species and Raf-1 from an unspecified species.
NP_002871.1	NP_002558.1	PEBP1		BIND	PubMed

NP_002871.1	RKIP	PEBP1		HPRD	PubMed
hPEBP4 interacts with Raf-1. This interaction was modeled on a demonstrated interaction between human hPEBP4 and mouse Raf-1.
NP_002871.1	NP_659399.1	PEBP4		BIND	PubMed

NP_002871.1	NP_057643.1	PEX5L		HPRD	PubMed

NP_002871.1	NP_002625.1	PHB		HPRD	PubMed
RAF1 (c-Raf) interacts with PHB.
NP_002871.1	NP_002625.1	PHB		BIND	PubMed
Raf-1 interacts with Pin1. This interaction was modelled on a demonstrated interaction between human Raf-1 and Pin1 from monkey and unspecified species.
NP_002871.1	NP_006212.1	PIN1		BIND	PubMed
C-RAF interacts with PyK.
NP_002871.1	NP_002645.3	PKM2		BIND	PubMed
RAF1 (C-Raf) interacts with PKM2 (PyK).
NP_002871.1	NP_002645.3	PKM2		BIND	PubMed
RAF1 (c-Raf) interact with an unspecified isoform of PPP2R2A (PP2A-A).
NP_002871.1	NP_002708.1	PPP2R2A		BIND	PubMed
RAF1 (c-Raf) interacts with an unspecified isoform of PPP2R2B (PP2A-B).
NP_002871.1		PPP2R2B		BIND	PubMed
RAF1 (c-Raf) interacts with an unspecified isoform of PPP2R2C (PP2A-C).
NP_002871.1	NP_065149.2	PPP2R2C		BIND	PubMed

NP_002871.1	Protein kinase C epsilon	PRKCE		HPRD	PubMed

NP_002871.1	Protein kinase C, zeta	PRKCZ		HPRD	PubMed

NP_002871.1	NP_002875.1	RAP1A		HPRD	PubMed

NP_002871.1	NP_002875.1	RAP1A		HPRD	PubMed

NP_002871.1	NP_002875.1	RAP1A		HPRD	PubMed
Raf-1 interacts with Rap2. This interaction was modeled on a demonstrated interaction between Raf-1 from unspecified species and human Rap2.
NP_002871.1	AAH70031.1	RAP2A		BIND	PubMed

NP_002871.1	NP_000312.1	RB1		HPRD	PubMed
Raf-1 interacts with Rb.
NP_002871.1	NP_000312.1	RB1		BIND	PubMed
Raf-1 interacts with p130.
NP_002871.1	NP_005602.2	RBL2		BIND	PubMed

NP_002871.1	Retinoblastoma like 2	RBL2		HPRD	PubMed
RAF interacts with Rheb.
NP_002871.1	NP_005605.1	RHEB		BIND	PubMed

NP_002871.1	RAS homolog enriched in brain 2	RHEB		HPRD	PubMed

NP_002871.1	MST4	RP6-213H19.1		HPRD	PubMed
RAF1 (C-Raf) interacts with RRAS2 (R-Ras).
NP_002871.1	NP_036382.2	RRAS2		BIND	PubMed

NP_002871.1	R Ras2	RRAS2		HPRD	PubMed

NP_002871.1	NP_031399.1	SHOC2		HPRD	PubMed

NP_002871.1	c-Src	SRC		HPRD	PubMed
Raf-1 interacts with MST2. This interaction was modeled on a demonstrated interaction between human Raf-1 and monkey MST2.
NP_002871.1	NP_006272.1	STK3		BIND	PubMed
C-RAF interacts with TIMM50.
NP_002871.1	NP_001001563.1	TIMM50		BIND	PubMed
RAF1 (C-Raf) interacts with TIMM50 (hC22).
NP_002871.1	NP_001001563.1	TIMM50		BIND	PubMed

NP_002871.1	GILZ	TSC22D3		HPRD	PubMed

NP_002871.1	VAV1	VAV1		HPRD	PubMed

NP_002871.1	14-3-3 Beta	YWHAB		HPRD	PubMed
C-RAF interacts with 14-3-3-beta.
NP_002871.1	NP_003395.1	YWHAB		BIND	PubMed
RAF1 (C-Raf) interacts with YWHAB (14-3-3-beta).
NP_002871.1	NP_003395.1	YWHAB		BIND	PubMed

NP_002871.1	14-3-3 epsilon	YWHAE		HPRD	PubMed
14-3-3-epsilon interacts with Raf-1.
NP_002871.1	NP_006752.1	YWHAE		BIND	PubMed

NP_002871.1	NP_036611.2	YWHAG		HPRD	PubMed

NP_002871.1	NP_003396.1	YWHAH		HPRD	PubMed

NP_002871.1	NP_003397.1	YWHAZ		HPRD	PubMed
Raf-1 interacts with 14-3-3 zeta. This interaction was modelled on a demonstrated interaction between human Raf-1 and murine 14-3-3-zeta.
NP_002871.1	NP_003397.1	YWHAZ		BIND	PubMed

NP_002871.1	GILZ			HPRD	PubMed

NP_002871.1	GNG4			HPRD	PubMed

NP_002871.1	Glucocorticoid receptor			HPRD	PubMed

NP_002871.1	Hsp90N			HPRD	PubMed

NP_002871.1	JSAP1			HPRD	PubMed

NP_002871.1	MEKK1			HPRD	PubMed

NP_002871.1	PP1C			HPRD	PubMed

NP_002871.1	PRKG1			HPRD	PubMed

NP_002871.1	Ras p21			HPRD	PubMed

NP_002871.1	Tvl-1			HPRD	PubMed
Raf-1 interacts with CASP9 dimer.
NP_002871.1				BIND	PubMed
RAF1 (RAF) interacts with GTP-HRAS (GTP-RAS).
NP_002871.1				BIND	PubMed

RAF1	AAH11604.1	CNKSR1		HPRD	PubMed

RAF1	NP_004476.1	GNG4		HPRD	PubMed

RAF1	NP_775869.2	KSR2		HPRD	PubMed

RAF1	NP_872270.1	PKM2		HPRD	PubMed

RAF1	NP_112226.2	SPRY4		HPRD	PubMed
Affinity Capture-Western; Biochemical Activity
BioGRID:111831	BioGRID:106710	AKT1		BioGRID	PubMed
Co-purification
BioGRID:111831	BioGRID:106862	AR		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:247426	Arrb2		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:107049	BAG1		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:107068	BCL2		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:107070	BCL2L1		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:106826	BIRC2		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:106827	BIRC3		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:107141	BRAF		BioGRID	PubMed
Two-hybrid
BioGRID:111831	BioGRID:113054	CCT3		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:107428	CDC25A		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:114364	CFLAR		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:115550	CNKSR1		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:116534	CNKSR2		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:109502	ERAS		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:108810	FYN		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:109045	GNB2		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:109048	GNG4		BioGRID	PubMed
Affinity Capture-Western; Co-fractionation; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:109144	GRB10		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:109501	HRAS		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:109552	HSP90AA1		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:200416	Hras1		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:109919	JAK1		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:109920	JAK2		BioGRID	PubMed
Affinity Capture-Western; Two-hybrid
BioGRID:111831	BioGRID:110043	KRAS		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:110124	LCK		BioGRID	PubMed
Two-hybrid
BioGRID:111831	BioGRID:110221	LRPAP1		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:110236	LTK		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:111590	MAP2K1		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:110378	MAP3K1		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:110381	MAP3K5		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:111580	MAPK1		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:111581	MAPK3		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:111584	MAPK7		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:116774	MAPK8IP3		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:116486	MRAS		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:110694	MYC		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:109165	NR3C1		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:110952	NRAS		BioGRID	PubMed
Two-hybrid
BioGRID:111831	BioGRID:116467	OIP5		BioGRID	PubMed
Affinity Capture-Western; Biochemical Activity; Reconstituted Complex
BioGRID:111831	BioGRID:111095	PAK1		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:111185	PDGFRB		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:111076	PEBP1		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:127592	PEBP4		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:111264	PHB		BioGRID	PubMed
Two-hybrid
BioGRID:111831	BioGRID:111274	PHKA2		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:111567	PRKCE		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:111576	PRKCZ		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:111578	PRKG1		BioGRID	PubMed
Two-hybrid
BioGRID:111831	BioGRID:117298	PRPF6		BioGRID	PubMed
Co-crystal Structure; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:111841	RAP1A		BioGRID	PubMed
Reconstituted Complex
BioGRID:111831	BioGRID:117095	RASD2		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:111860	RB1		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:111869	RBL2		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:111941	RHEB		BioGRID	PubMed
Two-hybrid
BioGRID:111831	BioGRID:119722	RP6-213H19.1		BioGRID	PubMed
Two-hybrid
BioGRID:111831	BioGRID:112151	RRAS		BioGRID	PubMed
Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:116480	RRAS2		BioGRID	PubMed
Affinity Capture-MS
BioGRID:111831	BioGRID:109072	SFN		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:113729	SHOC2		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:115547	SPRY2		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:123599	SPRY4		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:112592	SRC		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:115563	STUB1		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:108165	TSC22D3		BioGRID	PubMed
Biochemical Activity
BioGRID:111831	BioGRID:113170	UBE2D2		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:113252	VAV1		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:113259	VDAC1		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:106828	XIAP		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex; Two-hybrid
BioGRID:111831	BioGRID:113361	YWHAB		BioGRID	PubMed
Affinity Capture-Western; Two-hybrid
BioGRID:111831	BioGRID:113363	YWHAE		BioGRID	PubMed
Affinity Capture-MS; Affinity Capture-Western
BioGRID:111831	BioGRID:113364	YWHAG		BioGRID	PubMed
Affinity Capture-Western
BioGRID:111831	BioGRID:113365	YWHAH		BioGRID	PubMed
Affinity Capture-MS; Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:116168	YWHAQ		BioGRID	PubMed
Affinity Capture-Western; Reconstituted Complex
BioGRID:111831	BioGRID:113366	YWHAZ		BioGRID	PubMed

[Top][Help]General gene information

Markers

G32929(e-PCR): Links: UniSTS:117507

D3S4000(e-PCR): Links: UniSTS:8196

STS-N27641(e-PCR): Links: UniSTS:54060

GDB:181223(e-PCR): Links: UniSTS:155191

G15882(e-PCR): Links: UniSTS:44344

RH118840(e-PCR): Links: UniSTS:138822

GDB:217154(e-PCR): Links: UniSTS:156230

A009W45(e-PCR): Links: UniSTS:64891

D3S2870E(e-PCR): Links: UniSTS:81285

RAF1_478(e-PCR): Links: UniSTS:277655

PZD00074_allele_9942870(e-PCR): Links: UniSTS:513431

PZD00074_allele_9942871(e-PCR): Links: UniSTS:513431

PZD00074_allele_9942894(e-PCR): Links: UniSTS:513431

SHGC-57030(e-PCR): Links: UniSTS:24801

Phenotypes

LEOPARD syndrome 2: MIM: 611554
Noonan syndrome 5: MIM: 611553

Genotypes

See RAF1 SNP Genotype Report

See RAF1 SNP Geneview Report

Related pseudogene(s)

2 foundReview record(s) in Gene

Homology

Homologs of the RAF1 gene The RAF1 gene is conserved in chimpanzee, dog, cow, mouse, rat, chicken, and zebrafish.

Map Viewer (Mouse, Rat)

Pathways

KEGG pathway: Acute myeloid leukemia: 05221
KEGG pathway: B cell receptor signaling pathway: 04662
KEGG pathway: Bladder cancer: 05219
KEGG pathway: Chemokine signaling pathway: 04062
KEGG pathway: Chronic myeloid leukemia: 05220
KEGG pathway: Colorectal cancer: 05210
KEGG pathway: Endometrial cancer: 05213
KEGG pathway: ErbB signaling pathway: 04012
KEGG pathway: Fc epsilon RI signaling pathway: 04664
KEGG pathway: Fc gamma R-mediated phagocytosis: 04666
KEGG pathway: Focal adhesion: 04510
KEGG pathway: Gap junction: 04540
KEGG pathway: Glioma: 05214
KEGG pathway: GnRH signaling pathway: 04912
KEGG pathway: Insulin signaling pathway: 04910
KEGG pathway: Long-term depression: 04730
KEGG pathway: Long-term potentiation: 04720
KEGG pathway: MAPK signaling pathway: 04010
KEGG pathway: Melanogenesis: 04916
KEGG pathway: Melanoma: 05218
KEGG pathway: Natural killer cell mediated cytotoxicity: 04650
KEGG pathway: Neurotrophin signaling pathway: 04722
KEGG pathway: Non-small cell lung cancer: 05223
KEGG pathway: Pancreatic cancer: 05212
KEGG pathway: Pathways in cancer: 05200
KEGG pathway: Progesterone-mediated oocyte maturation: 04914
KEGG pathway: Prostate cancer: 05215
KEGG pathway: Regulation of actin cytoskeleton: 04810
KEGG pathway: Renal cell carcinoma: 05211
KEGG pathway: T cell receptor signaling pathway: 04660
KEGG pathway: VEGF signaling pathway: 04370
KEGG pathway: Vascular smooth muscle contraction: 04270
Reactome Event:Axon guidance: REACT_18266
Reactome Event:Signaling by EGFR: REACT_9417
Reactome Event:Signaling by Insulin receptor: REACT_498
Reactome Event:Signaling by PDGF: REACT_16888
Reactome Event:Signalling by NGF: REACT_11061

Gene Ontology Provided by GOA

Function	Evidence
ATP binding	IEA
metal ion binding	IEA
nucleotide binding	IEA
protein binding	IPI	PubMed
protein serine/threonine kinase activity	IEA
receptor signaling protein activity	IEA
transferase activity	IEA
zinc ion binding	IEA

Process	Evidence
Ras protein signal transduction	EXP	PubMed
apoptosis	TAS	PubMed
cell proliferation	TAS	PubMed
protein amino acid phosphorylation	TAS	PubMed

Component	Evidence
cytosol	EXP	PubMed
mitochondrial outer membrane	TAS	PubMed
plasma membrane	EXP	PubMed

[Top][Help]General protein information

Preferred Names: v-raf-1 murine leukemia viral oncogene homolog 1

Names: v-raf-1 murine leukemia viral oncogene homolog 1; Oncogene RAF1; raf proto-oncogene serine/threonine protein kinase

NP_002871.1: EC 2.7.11.1

[Top][Help]NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

Genomic

NG_007467.1 RefSeqGene

Range

4978..85578

Download

GenBank FASTA Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_002880.3 → NP_002871.1 v-raf-1 murine leukemia viral oncogene homolog 1

Source sequence(s)

BC018119,BU683389,DC342671

Consensus CDS

CCDS2612.1

UniProtKB/Swiss-Prot

P04049

Conserved Domains (4) summary

cd00029
Location:139 – 184
Blast Score: 144

C1; Protein kinase C conserved region 1 (C1) . Cysteine-rich zinc binding domain. Some members of this domain family bind phorbol esters and diacylglycerol, some are reported to bind RasGTP. May occur in tandem arrangement. Diacylglycerol (DAG) is a second...

cd00180
Location:354 – 611
Blast Score: 530

S_TKc; Serine/Threonine protein kinases, catalytic domain. Phosphotransferases of the serine or threonine-specific kinase subfamily. The enzymatic activity of these protein kinases is controlled by phosphorylation of specific residues in the activation...

cd01816
Location:57 – 131
Blast Score: 328

Raf_RBD; CR2 and CR3. CR1 has two Ras binding domains (RBD and CRD), CR2 is a serine/threonine rich domain and CR3 is the catalytic kinase domain. The RBD of Raf is structurally similar to ubiquitin with little of no sequence similarity.The Raf signalling...

pfam00069
Location:354 – 605
Blast Score: 648

Pkinase; Protein kinase domain

RefSeqs of Annotated Genomes: Build 37.1

The following sections contain reference sequences that belong to a specific genome build. Explain

Genome Reference Consortium Human Build 37 (GRCh37), Primary_Assembly

Genomic

NC_000003.11

Range

12625099..12705699, complement

Download

GenBank FASTA Sequence Viewer (Graphics)
NT_022517.18

Range

12565099..12645699, complement

Download

GenBank FASTA Sequence Viewer (Graphics)

Alternate assembly (Celera)

Genomic

AC_000046.1

Range

12563425..12643993, complement

Download

GenBank FASTA Sequence Viewer (Graphics)
NW_921651.1

Range

12563425..12643993, complement

Download

GenBank FASTA Sequence Viewer (Graphics)

Alternate assembly (HuRef)

Genomic

AC_000135.1

Range

12559317..12640382

Download

GenBank FASTA Sequence Viewer (Graphics)
NW_001838877.2

Range

53627279..53708344

Download

GenBank FASTA Sequence Viewer (Graphics)

[Top][Help]Related Sequences

Nucleotide		Protein
genomic	AC018500.4 (125370..150809)	None
genomic	AC026170.5 (34768..89898)	None
genomic	AY271661.1	AAP03432.1
genomic	CH471055.1	EAW64134.1
		EAW64135.1
genomic	EU332868.1	ABY87557.1
genomic	L00212.1	AAA60247.1
mRNA	AK226028.1	None
mRNA	AK303561.1	BAG64584.1
mRNA	AK303920.1	BAG64848.1
mRNA	AK312248.1	BAG35180.1
mRNA	BC018119.2	AAH18119.1
mRNA	BQ221862.1	None
mRNA	BU683389.1	None
mRNA	CR598160.1	None
mRNA	CR608506.1	None
mRNA	CR609564.1	None
mRNA	CR616511.1	None
mRNA	CR617502.1	None
mRNA	DC342671.1	None
mRNA	X03484.1	CAA27204.1