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RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)

 RAF1_MOUSE              Reviewed;         648 AA.
Q99N57; Q3UR68; Q58E75; Q91WH1; Q99N58; Q9QUU8;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 2.
18-JUL-2018, entry version 171.
RecName: Full=RAF proto-oncogene serine/threonine-protein kinase;
EC=2.7.11.1;
AltName: Full=Proto-oncogene c-RAF;
Short=cRaf;
AltName: Full=Raf-1;
Name=Raf1; Synonyms=Craf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=11597136; DOI=10.1006/geno.2001.6627;
Gray T.A., Azama K., Whitmore K., Min A., Abe S., Nicholls R.D.;
"Phylogenetic conservation of the makorin-2 gene, encoding a multiple
zinc-finger protein, antisense to the raf1 proto-oncogene.";
Genomics 77:119-126(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND
TISSUE SPECIFICITY.
PubMed=1886707;
Dozier C., Ansieau S., Ferreira E., Coll J., Stehelin D.;
"An alternatively spliced c-mil/raf mRNA is predominantly expressed in
chicken muscular tissues and conserved among vertebrate species.";
Oncogene 6:1307-1311(1991).
[5]
FUNCTION, AND INTERACTION WITH ROCK2.
PubMed=15753127; DOI=10.1083/jcb.200409162;
Ehrenreiter K., Piazzolla D., Velamoor V., Sobczak I., Small J.V.,
Takeda J., Leung T., Baccarini M.;
"Raf-1 regulates Rho signaling and cell migration.";
J. Cell Biol. 168:955-964(2005).
[6]
PHOSPHORYLATION AT SER-29; SER-43; SER-259; SER-289; SER-296; SER-301;
SER-338; SER-621 AND SER-642, ENZYME REGULATION, AND INTERACTION WITH
PIN1; PPP2CA AND PPP2R1B.
PubMed=15664191; DOI=10.1016/j.molcel.2004.11.055;
Dougherty M.K., Muller J., Ritt D.A., Zhou M., Zhou X.Z.,
Copeland T.D., Conrads T.P., Veenstra T.D., Lu K.P., Morrison D.K.;
"Regulation of Raf-1 by direct feedback phosphorylation.";
Mol. Cell 17:215-224(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
SUBCELLULAR LOCATION.
PubMed=19298812; DOI=10.1016/j.yexcr.2009.03.004;
Smith J., Bunaciu R.P., Reiterer G., Coder D., George T., Asaly M.,
Yen A.;
"Retinoic acid induces nuclear accumulation of Raf1 during
differentiation of HL-60 cells.";
Exp. Cell Res. 315:2241-2248(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-301 AND
SER-642, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Serine/threonine-protein kinase that acts as a
regulatory link between the membrane-associated Ras GTPases and
the MAPK/ERK cascade, and this critical regulatory link functions
as a switch determining cell fate decisions including
proliferation, differentiation, apoptosis, survival and oncogenic
transformation. RAF1 activation initiates a mitogen-activated
protein kinase (MAPK) cascade that comprises a sequential
phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and
MAP2K2/MEK2) and the extracellular signal-regulated kinases
(MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on
residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-
antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl
cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation.
Phosphorylates PPP1R12A resulting in inhibition of the phosphatase
activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can
promote NF-kB activation and inhibit signal transducers involved
in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2),
proliferation and angiogenesis (RB1). Can protect cells from
apoptosis also by translocating to the mitochondria where it binds
BCL2 and displaces BAD/Bcl2-antagonist of cell death. Plays a role
in the oncogenic transformation of epithelial cells via repression
of the TJ protein, occludin (OCLN) by inducing the up-regulation
of a transcriptional repressor SNAI2/SLUG, which induces down-
regulation of OCLN. Restricts caspase activation in response to
selected stimuli, notably Fas stimulation, pathogen-mediated
macrophage apoptosis, and erythroid differentiation (By
similarity). Regulates Rho signaling and migration, and is
required for normal wound healing. {ECO:0000250,
ECO:0000269|PubMed:15753127}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Regulation is a highly complex process
involving membrane recruitment, protein-protein interactions,
dimerization, and phosphorylation/dephosphorylation events. Ras-
GTP recruits RAF1 to the membrane, thereby promoting its
activation. The inactive conformation of RAF1 is maintained by
autoinhibitory interactions occurring between the N-terminal
regulatory and the C-terminal catalytic domains and by the binding
of a 14-3-3 protein that contacts two phosphorylation sites, Ser-
259 and Ser-621. Upon mitogenic stimulation, Ras and PPP2R1A
cooperate to release autoinhibition and the subsequent
phosphorylation of activating sites: Ser-338, Tyr-341, Thr-491,
and Ser-494, yields a fully active kinase. Through a negative
feedback mechanism involving MAPK1/ERK2, RAF1 is phosphorylated on
Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by
MAPK1/ERK2, which yields an inactive, desensitized kinase. The
signaling-competent conformation of RAF1 is finally re-established
by the coordinated action of PIN1, a prolyl isomerase that
converts pSer and pThr residues from the cis to the trans
conformation, which is preferentially recognized and
dephosphorylated by PPP2R1A. Activated by homodimerization and
heterodimerization (with BRAF). Also regulated through association
with other proteins such as KSR2, CNKSR1/CNK1, PEBP1/RKIP,
PHB/prohibitin and SPRY4. PEBP1/RKIP acts by dissociating RAF1
from its substrates MAP2K1/MEK1 and MAP2K2/MEK2. PHB/prohibitin
facilitates the displacement of 14-3-3 from RAF1 by activated Ras,
thereby promoting cell membrane localization and phosphorylation
of RAF1 at the activating Ser-338. SPRY4 inhibits Ras-independent,
but not Ras-dependent, activation of RAF1. CNKSR1/CNK1 regulates
Src-mediated RAF1 activation (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer (By similarity). Homodimer (By similarity).
Heterodimerizes with BRAF and this heterodimer possesses a highly
increased kinase activity compared to the respective homodimers or
monomers (By similarity). Heterodimerization is mitogen-regulated
and enhanced by 14-3-3 proteins (By similarity). MAPK1/ERK2
activation can induce a negative feedback that promotes the
dissociation of the heterodimer (By similarity). Forms a
multiprotein complex with Ras (M-Ras/MRAS), SHOC2 and protein
phosphatase 1 (PPP1CA, PPP1CB and PPP1CC) (By similarity).
Interacts with Ras proteins; the interaction is antagonized by
RIN1 (By similarity). Weakly interacts with RIT1 (By similarity).
Interacts (via N-terminus) with RGS14 (via RBD domains); the
interaction mediates the formation of a ternary complex with BRAF,
a ternary complex inhibited by GNAI1 (By similarity). Probably
forms a complex composed of chaperones HSP90 and HSP70, co-
chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT,
RAF1 and NR3C1; this complex does not contain co-chaperones
STIP1/HOP and PTGES3/p23 (By similarity). Interacts with
STK3/MST2; the interaction inhibits its pro-apoptotic activity (By
similarity). Interacts (when phosphorylated at Ser-259) with YWHAZ
(unphosphorylated at 'Thr-232') (By similarity). Interacts with
MAP2K1/MEK1 and MAP2K2/MEK2 (By similarity). Interacts with
MAP3K5/ASF1 (via N-terminus) and this interaction inhibits the
proapoptotic function of MAP3K5/ASK1 (By similarity). Interacts
with PAK1 (via kinase domain) (By similarity). The Ser-338 and
Ser-339 phosphorylated form (by PAK1) interacts with BCL2 (By
similarity). Interacts with PEBP1/RKIP and this interaction is
enhanced if RAF1 is phosphorylated on residues Ser-338, Ser-339,
Tyr-340 and Tyr-341 (By similarity). Interacts with ADCY2, ADCY5,
ADCY6, DGKH, RCAN1/DSCR1, PPP1R12A, PKB/AKT1, SPRY2, SPRY4,
CNKSR1/CNK1, KSR2 and PHB/prohibitin (By similarity). The
phosphorylated form interacts with PIN1 (PubMed:15664191).
Interacts with PPP2CA, PPP2R1B and ROCK2 (PubMed:15753127,
PubMed:15664191). In its active form, interacts with PRMT5 (By
similarity). Interacts with FAM83B; displaces 14-3-3 proteins from
RAF1 and activates RAF1 (By similarity). Interacts with PDE8A; the
interaction promotes RAF1 activity (By similarity). Interacts with
MFHAS1 (By similarity). {ECO:0000250|UniProtKB:P04049,
ECO:0000250|UniProtKB:P11345, ECO:0000269|PubMed:15664191,
ECO:0000269|PubMed:15753127}.
-!- INTERACTION:
P15056:BRAF (xeno); NbExp=3; IntAct=EBI-397757, EBI-365980;
P28028:Braf; NbExp=2; IntAct=EBI-397757, EBI-2584830;
P32883-2:Kras; NbExp=3; IntAct=EBI-397757, EBI-644285;
Q8CFI0:Nedd4l; NbExp=2; IntAct=EBI-397757, EBI-8046183;
P01111:NRAS (xeno); NbExp=2; IntAct=EBI-397757, EBI-721993;
Q9WVC6:Sgk1; NbExp=2; IntAct=EBI-397757, EBI-15591730;
Q9Z2S7-3:Tsc22d3; NbExp=2; IntAct=EBI-397757, EBI-15771036;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:19298812}. Note=Colocalizes with RGS14 and
BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-
259 impairs its membrane accumulation. Recruited to the cell
membrane by the active Ras protein. Phosphorylation at Ser-338 and
Ser-339 by PAK1 is required for its mitochondrial localization (By
similarity). Retinoic acid-induced Ser-621 phosphorylated form of
RAF1 is predominantly localized at the nucleus. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=6C;
IsoId=Q99N57-1; Sequence=Displayed;
Name=2; Synonyms=1A;
IsoId=Q99N57-2; Sequence=VSP_034629;
-!- TISSUE SPECIFICITY: Present in all tissues tested: testis, ovary,
small intestine, colon, peripheral blood leukocytes, fetal liver,
bone marrow, thymus, lymph node and spleen, and the cell lines
melanoma G-361, lung carcinoma A-549, colorectal adenocarcinoma
SW480, Burkitt's lymphoma Raji and lymphoblastic leukemia MOLT-4.
In skeletal muscle, isoform 1 is more abundant than isoform 2.
{ECO:0000269|PubMed:11597136, ECO:0000269|PubMed:1886707}.
-!- PTM: Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and
Ser-494 results in its activation. Phosphorylation at Ser-29, Ser-
43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in
its inactivation. Phosphorylation at Ser-259 induces the
interaction with YWHAZ and inactivates kinase activity.
Dephosphorylation of Ser-259 by the complex containing protein
phosphatase 1, SHOC2 and M-Ras/MRAS relieves inactivation, leading
to stimulate RAF1 activity. Phosphorylation at Ser-338 by PAK1 and
PAK5 and Ser-339 by PAK1 is required for its mitochondrial
localization (By similarity). Phosphorylation at Ser-621 in
response to growth factor treatment stabilizes the protein,
possibly by preventing proteasomal degradation. Phosphorylation at
Ser-289, Ser-296, Ser-301, Ser-338 and Ser-621 are somehow linked
to the methylation potential of cells. Treatment of cells with HGF
in the presence of the methylation inhibitor 5'-
methylthioadenosine (MTA) results in increased phosphorylation at
Ser-338 and Ser-621 and decreased phosphorylation at Ser-296, Ser-
301 and Ser-338. Dephosphorylation at SER-338 by PPP5C results in
a decreased of activity (By similarity). {ECO:0000250}.
-!- PTM: Methylated at Arg-563 in response to EGF treatment. This
modification leads to destabilization of the protein, possibly
through proteasomal degradation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. RAF subfamily. {ECO:0000305}.
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EMBL; AB057655; BAB39748.1; -; mRNA.
EMBL; AB057663; BAB39743.2; -; mRNA.
EMBL; AK141745; BAE24820.1; -; mRNA.
EMBL; BC015273; AAH15273.1; -; mRNA.
EMBL; BC092040; AAH92040.1; -; mRNA.
EMBL; X55432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS20441.1; -. [Q99N57-1]
RefSeq; NP_084056.1; NM_029780.3. [Q99N57-1]
RefSeq; XP_006505426.1; XM_006505363.3.
RefSeq; XP_006505427.1; XM_006505364.2. [Q99N57-2]
RefSeq; XP_006505428.1; XM_006505365.2.
UniGene; Mm.184163; -.
ProteinModelPortal; Q99N57; -.
SMR; Q99N57; -.
BioGrid; 225343; 16.
CORUM; Q99N57; -.
DIP; DIP-31555N; -.
IntAct; Q99N57; 17.
MINT; Q99N57; -.
STRING; 10090.ENSMUSP00000000451; -.
BindingDB; Q99N57; -.
ChEMBL; CHEMBL3804748; -.
iPTMnet; Q99N57; -.
PhosphoSitePlus; Q99N57; -.
PaxDb; Q99N57; -.
PeptideAtlas; Q99N57; -.
PRIDE; Q99N57; -.
Ensembl; ENSMUST00000000451; ENSMUSP00000000451; ENSMUSG00000000441. [Q99N57-1]
Ensembl; ENSMUST00000112949; ENSMUSP00000108571; ENSMUSG00000000441. [Q99N57-1]
GeneID; 110157; -.
KEGG; mmu:110157; -.
UCSC; uc009dix.1; mouse. [Q99N57-1]
CTD; 5894; -.
MGI; MGI:97847; Raf1.
eggNOG; KOG0193; Eukaryota.
eggNOG; ENOG410Y4UP; LUCA.
GeneTree; ENSGT00900000140880; -.
HOGENOM; HOG000252972; -.
HOVERGEN; HBG001886; -.
InParanoid; Q99N57; -.
KO; K04366; -.
OMA; HQFIRKT; -.
OrthoDB; EOG091G09SB; -.
PhylomeDB; Q99N57; -.
TreeFam; TF317006; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
Reactome; R-MMU-392517; Rap1 signalling.
Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
Reactome; R-MMU-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-5673000; RAF activation.
Reactome; R-MMU-5674135; MAP2K and MAPK activation.
Reactome; R-MMU-5674499; Negative feedback regulation of MAPK pathway.
Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
ChiTaRS; Raf1; mouse.
PRO; PR:Q99N57; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000000441; -.
CleanEx; MM_RAF1; -.
ExpressionAtlas; Q99N57; baseline and differential.
Genevisible; Q99N57; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0031143; C:pseudopodium; IDA:UniProtKB.
GO; GO:0010856; F:adenylate cyclase activator activity; ISO:MGI.
GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004709; F:MAP kinase kinase kinase activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; TAS:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0017016; F:Ras GTPase binding; IPI:MGI.
GO; GO:0007190; P:activation of adenylate cyclase activity; ISO:MGI.
GO; GO:0000186; P:activation of MAPKK activity; ISO:MGI.
GO; GO:0030154; P:cell differentiation; IGI:MGI.
GO; GO:0001678; P:cellular glucose homeostasis; IMP:MGI.
GO; GO:0071550; P:death-inducing signaling complex assembly; IMP:MGI.
GO; GO:0060324; P:face development; IGI:MGI.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; TAS:MGI.
GO; GO:0000165; P:MAPK cascade; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
GO; GO:0031333; P:negative regulation of protein complex assembly; ISO:MGI.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IMP:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0035994; P:response to muscle stretch; IMP:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
GO; GO:0048538; P:thymus development; IGI:MGI.
GO; GO:0030878; P:thyroid gland development; IGI:MGI.
CDD; cd00029; C1; 1.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR003116; RBD_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR029071; Ubiquitin-like_domsf.
Pfam; PF00130; C1_1; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF02196; RBD; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00455; RBD; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50898; RBD; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Cytoplasm; Kinase; Membrane; Metal-binding; Methylation;
Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Proto-oncogene; Reference proteome; Serine/threonine-protein kinase;
Transferase; Zinc; Zinc-finger.
CHAIN 1 648 RAF proto-oncogene serine/threonine-
protein kinase.
/FTId=PRO_0000086597.
DOMAIN 56 131 RBD. {ECO:0000255|PROSITE-
ProRule:PRU00262}.
DOMAIN 349 609 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 138 184 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 355 363 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 331 349 Interaction with PEBP1/RKIP.
{ECO:0000250}.
ACT_SITE 468 468 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 139 139 Zinc 1. {ECO:0000250}.
METAL 152 152 Zinc 2. {ECO:0000250}.
METAL 155 155 Zinc 2. {ECO:0000250}.
METAL 165 165 Zinc 1. {ECO:0000250}.
METAL 168 168 Zinc 1. {ECO:0000250}.
METAL 173 173 Zinc 2. {ECO:0000250}.
METAL 176 176 Zinc 2. {ECO:0000250}.
METAL 184 184 Zinc 1. {ECO:0000250}.
BINDING 375 375 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 29 29 Phosphoserine; by MAPK1.
{ECO:0000269|PubMed:15664191}.
MOD_RES 43 43 Phosphoserine; by PKA and MAPK1.
{ECO:0000269|PubMed:15664191}.
MOD_RES 233 233 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 259 259 Phosphoserine; by PKA, PKC and PKB/AKT1.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 268 268 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 269 269 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 289 289 Phosphoserine; by MAPK1.
{ECO:0000269|PubMed:15664191}.
MOD_RES 296 296 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15664191}.
MOD_RES 301 301 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15664191}.
MOD_RES 338 338 Phosphoserine; by PAK1, PAK2, PAK3 and
PAK5. {ECO:0000250|UniProtKB:P04049}.
MOD_RES 339 339 Phosphoserine; by PAK1, PAK2 and PAK3.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 340 340 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 341 341 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 491 491 Phosphothreonine.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 497 497 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 499 499 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 563 563 Symmetric dimethylarginine; by PRMT5.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 621 621 Phosphoserine.
{ECO:0000269|PubMed:15664191}.
MOD_RES 642 642 Phosphoserine; by MAPK1.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:15664191}.
VAR_SEQ 278 278 E -> ESNSLNASPRACSRRFCLRGR (in isoform
2). {ECO:0000305}.
/FTId=VSP_034629.
CONFLICT 522 522 D -> N (in Ref. 3; AAH92040).
{ECO:0000305}.
CONFLICT 543 543 A -> T (in Ref. 3; AAH92040).
{ECO:0000305}.
SEQUENCE 648 AA; 72917 MW; B70104AEF51C44A5 CRC64;
MEHIQGAWKT ISNGFGLKDA VFDGSSCISP TIVQQFGYQR RASDDGKLTD SSKTSNTIRV
FLPNKQRTVV NVRNGMSLHD CLMKALKVRG LQPECCAVFR LLQEHKGKKA RLDWNTDAAS
LIGEELQVDF LDHVPLTTHN FARKTFLKLA FCDICQKFLL NGFRCQTCGY KFHEHCSTKV
PTMCVDWSNI RQLLLFPNST VGDSGVPAPP SFPMRRMRES VSRMPASSQH RYSTPHAFTF
NTSSPSSEGS LSQRQRSTST PNVHMVSTTL HVDSRMIEDA IRSHSESASP SALSSSPNNL
SPTGWSQPKT PVPAQRERAP GSGTQEKNKI RPRGQRDSSY YWEIEASEVM LSTRIGSGSF
GTVYKGKWHG DVAVKILKVV DPTPEQLQAF RNEVAVLRKT RHVNILLFMG YMTKDNLAIV
TQWCEGSSLY KHLHVQETKF QMFQLIDIAR QTAQGMDYLH AKNIIHRDMK SNNIFLHEGL
TVKIGDFGLA TVKSRWSGSQ QVEQPTGSVL WMAPEVIRMQ DDNPFSFQSD VYSYGIVLYE
LMAGELPYAH INNRDQIIFM VGRGYASPDL SRLYKNCPKA MKRLVADCVK KVKEERPLFP
QILSSIELLQ HSLPKINRSA SEPSLHRAAH TEDINACTLT TSPRLPVF


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