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RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
RAF1_BOVIN Reviewed; 648 AA.
A7E3S4; A7YY51;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 1.
28-FEB-2018, entry version 84.
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 {ECO:0000312|EMBL:ABS45011.1};
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1] {ECO:0000305, ECO:0000312|EMBL:ABS45011.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2] {ECO:0000305, ECO:0000312|EMBL:AAI51320.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Hereford {ECO:0000312|EMBL:AAI51320.1};
TISSUE=Heart ventricle {ECO:0000312|EMBL:AAI51320.1};
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
-!- 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. Regulates
Rho signaling and migration, and is required for normal wound
healing. 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:P04049}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P04049};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000250|UniProtKB:P04049};
-!- 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. Homodimer. Heterodimerizes with BRAF and this
heterodimer possesses a highly increased kinase activity compared
to the respective homodimers or monomers. Heterodimerization is
mitogen-regulated and enhanced by 14-3-3 proteins. MAPK1/ERK2
activation can induce a negative feedback that promotes the
dissociation of the heterodimer. Forms a multiprotein complex with
Ras (M-Ras/MRAS), SHOC2 and protein phosphatase 1 (PPP1CA, PPP1CB
and PPP1CC). Interacts with Ras proteins; the interaction is
antagonized by RIN1. Weakly interacts with RIT1. 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. Interacts with STK3/MST2; the interaction
inhibits its pro-apoptotic activity. Interacts (when
phosphorylated at Ser-259) with YWHAZ (unphosphorylated at 'Thr-
232'). Interacts with MAP2K1/MEK1 and MAP2K2/MEK2. Interacts with
MAP3K5/ASF1 (via N-terminus) and this interaction inhibits the
proapoptotic function of MAP3K5/ASK1. Interacts with PAK1 (via
kinase domain). The phosphorylated form interacts with PIN1. The
Ser-338 and Ser-339 phosphorylated form (by PAK1) interacts with
BCL2. Interacts with PEBP1/RKIP and this interaction is enhanced
if RAF1 is phosphorylated on residues Ser-338, Ser-339, Tyr-340
and Tyr-341. Interacts with ADCY2, ADCY5, ADCY6, DGKH,
RCAN1/DSCR1, PPP1R12A, PKB/AKT1, PPP2CA, PPP2R1B, SPRY2, SPRY4,
CNKSR1/CNK1, KSR2 and PHB/prohibitin. Interacts with ROCK2. In its
active form, interacts with PRMT5. Interacts with FAM83B;
displaces 14-3-3 proteins from RAF1 and activates RAF1. Interacts
with PDE8A; the interaction promotes RAF1 activity.
{ECO:0000250|UniProtKB:P04049, ECO:0000250|UniProtKB:P11345,
ECO:0000250|UniProtKB:Q99N57}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}.
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. Retinoic acid-induced
Ser-621 phosphorylated form of RAF1 is predominantly localized at
the nucleus (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:16305752};
IsoId=A7E3S4-1; Sequence=Displayed;
Name=2;
IsoId=A7E3S4-2; Sequence=VSP_052844;
-!- 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:0000255}.
-----------------------------------------------------------------------
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EMBL; BT030695; ABS45011.1; -; mRNA.
EMBL; BC151319; AAI51320.1; -; mRNA.
RefSeq; NP_001095975.1; NM_001102505.1. [A7E3S4-2]
RefSeq; XP_005223216.2; XM_005223159.2. [A7E3S4-1]
RefSeq; XP_015324294.1; XM_015468808.1. [A7E3S4-1]
UniGene; Bt.4968; -.
ProteinModelPortal; A7E3S4; -.
SMR; A7E3S4; -.
IntAct; A7E3S4; 1.
STRING; 9913.ENSBTAP00000005930; -.
iPTMnet; A7E3S4; -.
PaxDb; A7E3S4; -.
GeneID; 107131151; -.
GeneID; 521196; -.
KEGG; bta:107131151; -.
KEGG; bta:521196; -.
CTD; 5894; -.
HOGENOM; HOG000252972; -.
HOVERGEN; HBG001886; -.
InParanoid; A7E3S4; -.
KO; K04366; -.
ChiTaRS; RAF1; cattle.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
GO; GO:0009968; P:negative regulation of signal transduction; IBA:GO_Central.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
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.
2: Evidence at transcript 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_0000348937.
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:0000250|UniProtKB:P12931,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 331 349 Interaction with PEBP1/RKIP.
{ECO:0000250}.
ACT_SITE 468 468 Proton acceptor.
{ECO:0000250|UniProtKB:P04049,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
METAL 139 139 Zinc 1. {ECO:0000250|UniProtKB:P04049}.
METAL 152 152 Zinc 2. {ECO:0000250|UniProtKB:P04049}.
METAL 155 155 Zinc 2. {ECO:0000250|UniProtKB:P04049}.
METAL 165 165 Zinc 1. {ECO:0000250|UniProtKB:P04049}.
METAL 168 168 Zinc 1. {ECO:0000250|UniProtKB:P04049}.
METAL 173 173 Zinc 2. {ECO:0000250|UniProtKB:P04049}.
METAL 176 176 Zinc 2. {ECO:0000250|UniProtKB:P04049}.
METAL 184 184 Zinc 1. {ECO:0000250|UniProtKB:P04049}.
BINDING 375 375 ATP. {ECO:0000250|UniProtKB:P12931,
ECO:0000255|PROSITE-ProRule:PRU00159}.
MOD_RES 29 29 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:Q99N57}.
MOD_RES 43 43 Phosphoserine; by PKA and MAPK1.
{ECO:0000250|UniProtKB:P04049}.
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 269 269 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 289 289 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:P04049}.
MOD_RES 296 296 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:Q99N57}.
MOD_RES 301 301 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:P04049}.
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:0000250|UniProtKB:P04049}.
MOD_RES 642 642 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:P04049}.
VAR_SEQ 278 278 E -> ENNSLNASPRAWSRRFCVRGR (in isoform
2). {ECO:0000303|Ref.2}.
/FTId=VSP_052844.
SEQUENCE 648 AA; 72874 MW; 283F6CEBFD9274E4 CRC64;
MEHIQGAWKT ISNGFGFKDT VFDGTSCISP TIVQQFGYQR RASDDGKLTD PSKTSNTIRV
FLPNKQRTVV NVRNGMSLHD CLMKALKVRG LQPECCAVFR LLHEHKGKKA RLDWNTDAAS
LIGEELQVDF LDHVPLTTHN FARKTFLKLA FCDICQKFLL NGFRCQTCGY KFHEHCSTKV
PTMCVDWSNI RQLLLFPNST VGDGGVPALP SLTMRRMRES VSRIPPGSQH RYSTPHAFTF
SASSPSSEGS LSQRQRSTST PNVHMVSATL PVDSRMIEDA IRSHSESGSP SALSSSPNNL
SPTGWSQPKT PAPAQRERAP GSSTQEKNKI RPRGQRDSSY YWEIEASEVM LSTRIGSGSF
GTVYKGKWHG DVAVKILKVV DPTPEQFQAF RNEVAVLRKT RHVNILLFMG YMTKDNLAIV
TQWCEGSSLY KHLHVQETKF QMFQLIDIAR QTAQGMDYLH AKNIIHRDMK SNNIFLHEGL
TVKIGDFGLA TVKSRWSGSQ QVEQPTGSIL WMAPEVIRMQ DNNPFSFQSD VYSYGIVLYE
LMTGELPYSH INNRDQIIFM VGRGYASPDL SKLYKNCPKA MKRLVADCVK KVKEERPLFP
QILSSIELLQ HSLPKINRSA SEPSLHRAAH TEDINACTLT TSPRLPVF
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Pathways :
WP1659: Glycine, serine and threonine metabolism
WP1493: Carbon assimilation C4 pathway
WP2185: Purine metabolism
WP2199: Seed Development
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP152: FGF signaling pathway
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1567: Glycolysis and Gluconeogenesis
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1619: Amino sugar and nucleotide sugar metabolism
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1653: Galactose metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
Related Genes :
[RAF1 RAF] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[Raf1 Raf] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[Raf1 Craf] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[RAF1] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[RAF1] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[Raf ph phl CG2845] Raf homolog serine/threonine-protein kinase Raf (D-Raf) (dRAF-1) (EC 2.7.11.1) (Protein pole-hole)
[BRAF BRAF1 RAFB1] Serine/threonine-protein kinase B-raf (EC 2.7.11.1) (Proto-oncogene B-Raf) (p94) (v-Raf murine sarcoma viral oncogene homolog B1)
[Araf A-raf Araf1] Serine/threonine-protein kinase A-Raf (EC 2.7.11.1) (Proto-oncogene A-Raf) (Proto-oncogene A-Raf-1)
[ARAF ARAF1 PKS PKS2] Serine/threonine-protein kinase A-Raf (EC 2.7.11.1) (Proto-oncogene A-Raf) (Proto-oncogene A-Raf-1) (Proto-oncogene Pks)
[Braf B-raf] Serine/threonine-protein kinase B-raf (EC 2.7.11.1) (Proto-oncogene B-Raf)
[RAF1 MIL] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (C-MIL) (C-RAF) (MIL proto-oncogene serine/threonine-protein kinase) (RAF-1)
[Araf A-raf Araf1] Serine/threonine-protein kinase A-Raf (EC 2.7.11.1) (Proto-oncogene A-Raf)
[lin-45 raf-1 Y73B6A.5] Raf homolog serine/threonine-protein kinase (EC 2.7.11.1) (Abnormal cell lineage protein 45)
[BRAF RMIL] Serine/threonine-protein kinase B-raf (EC 2.7.11.1) (Proto-oncogene B-Raf) (Proto-oncogene c-Rmil) (Serine/threonine-protein kinase Rmil)
[BRAF RMIL] Serine/threonine-protein kinase B-raf (EC 2.7.11.1) (Proto-oncogene B-Raf) (Proto-oncogene c-Rmil) (Serine/threonine-protein kinase Rmil)
[lilli l(2)00632 SS2-1 Su(Raf)2A CG8817] AF4/FMR2 family member 4 (Protein lilliputian) (Suppressor of Raf at 2A) (Suppressor of sina 2-1)
[PEBP1 PBP PEBP] Phosphatidylethanolamine-binding protein 1 (PEBP-1) (HCNPpp) (Neuropolypeptide h3) (Prostatic-binding protein) (Raf kinase inhibitor protein) (RKIP) [Cleaved into: Hippocampal cholinergic neurostimulating peptide (HCNP)]
[ARAF ARAF1] Serine/threonine-protein kinase A-Raf (EC 2.7.11.1) (Proto-oncogene A-Raf) (Proto-oncogene A-Raf-1)
[Dsor1 CG15793] Dual specificity mitogen-activated protein kinase kinase dSOR1 (Downstream of RAF) (MAPKK) (EC 2.7.12.2)
[raf1 clr8 cmc1 dos1 SPCC613.12c] Rik1-associated factor 1 (Cryptic loci regulator 8) (De-localization of swi6 protein 1)
[raf2 clr7 cmc2 dos2 SPCC970.07c] Rik1-associated factor 2 (Cryptic loci regulator 7) (De-localization of swi6 protein 2)
[raf1 raf] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (C-RAF)
[RREB1 FINB] Ras-responsive element-binding protein 1 (RREB-1) (Finger protein in nuclear bodies) (Raf-responsive zinc finger protein LZ321) (Zinc finger motif enhancer-binding protein 1) (Zep-1)
[PAQR3] Progestin and adipoQ receptor family member 3 (Progestin and adipoQ receptor family member III) (Raf kinase trapping to Golgi) (RKTG)
[lin-45 raf-1 CBG05382] Raf homolog serine/threonine-protein kinase (EC 2.7.11.1) (Abnormal cell lineage protein 45)
[RXT2 RAF60 YBR095C YBR0822] Transcriptional regulatory protein RXT2
[RAF1 R0030W] Trans-acting factor D (REP-antagonizing factor) (Recombinase-activating factor) (RAF)
[Braf] B-Raf proto-oncogene, serine/threonine kinase
[RAF1] Raf-1 proto-oncogene, serine/threonine kinase
[BRAF] B-Raf proto-oncogene, serine/threonine kinase
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