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Protein

RAF proto-oncogene serine/threonine-protein kinase

Gene

Raf1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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). Phosphorylates TNNT2/cardiac muscle troponin T.By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Zinc 1By similarity
Metal bindingi152 – 1521Zinc 2By similarity
Metal bindingi155 – 1551Zinc 2By similarity
Metal bindingi165 – 1651Zinc 1By similarity
Metal bindingi168 – 1681Zinc 1By similarity
Metal bindingi173 – 1731Zinc 2By similarity
Metal bindingi176 – 1761Zinc 2By similarity
Metal bindingi184 – 1841Zinc 1By similarity
Binding sitei375 – 3751ATPPROSITE-ProRule annotation
Active sitei468 – 4681Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri138 – 18447Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi355 – 3639ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: RGD
  • MAP kinase kinase kinase activity Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • mitogen-activated protein kinase kinase binding Source: RGD
  • protein heterodimerization activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.10.2. 5301.
ReactomeiR-RNO-2672351. Stimuli-sensing channels.
R-RNO-392517. Rap1 signalling.
R-RNO-430116. GP1b-IX-V activation signalling.
R-RNO-442742. CREB phosphorylation through the activation of Ras.
R-RNO-5621575. CD209 (DC-SIGN) signaling.
R-RNO-5673000. RAF activation.
R-RNO-5674135. MAP2K and MAPK activation.
R-RNO-5674499. Negative feedback regulation of MAPK pathway.
R-RNO-5675221. Negative regulation of MAPK pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
RAF proto-oncogene serine/threonine-protein kinase (EC:2.7.11.1)
Alternative name(s):
Proto-oncogene c-RAF
Short name:
cRaf
Raf-1
Gene namesi
Name:Raf1
Synonyms:Raf
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi3531. Raf1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity
  • Mitochondrion By similarity
  • Nucleus By similarity

  • 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).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
  • Golgi apparatus Source: Ensembl
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • pseudopodium Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648RAF proto-oncogene serine/threonine-protein kinasePRO_0000086598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphoserine; by MAPK1By similarity
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei233 – 2331Phosphoserine; by PKABy similarity
Modified residuei252 – 2521PhosphoserineBy similarity
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei268 – 2681Phosphothreonine; by autocatalysisBy similarity
Modified residuei269 – 2691Phosphothreonine; by PKABy similarity
Modified residuei289 – 2891Phosphoserine; by MAPK1By similarity
Modified residuei296 – 2961Phosphoserine; by MAPK1By similarity
Modified residuei301 – 3011Phosphoserine; by MAPK1By similarity
Modified residuei338 – 3381Phosphoserine; by PAK1, PAK2, PAK3 and PAK7/PAK5By similarity
Modified residuei339 – 3391Phosphoserine; by PAK1, PAK2 and PAK3By similarity
Modified residuei340 – 3401Phosphotyrosine; by SRCBy similarity
Modified residuei341 – 3411Phosphotyrosine; by SRCBy similarity
Modified residuei471 – 4711PhosphoserineBy similarity
Modified residuei491 – 4911PhosphothreonineBy similarity
Modified residuei494 – 4941PhosphoserineBy similarity
Modified residuei497 – 4971Phosphoserine; by PKCBy similarity
Modified residuei499 – 4991Phosphoserine; by PKCBy similarity
Modified residuei563 – 5631Symmetric dimethylarginine; by PRMT5By similarity
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei642 – 6421Phosphoserine; by MAPK1By similarity

Post-translational modificationi

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 PAK7/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).By similarity
Methylated in response to EGF treatment. This modification leads to destabilization of the protein, possibly through proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiP11345.

PTM databases

iPTMnetiP11345.
PhosphoSiteiP11345.

Expressioni

Gene expression databases

ExpressionAtlasiP11345. baseline and differential.
GenevisibleiP11345. RN.

Interactioni

Subunit structurei

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 (By similarity). Interacts with STK3/MST2; the interaction inhibits its pro-apoptotic activity. Interacts (when phosphorylated at Ser-259) with YWHAZ (unphosphorylated at 'Thr-232') (By similarity). 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, ROCK2, PPP1R12A, PKB/AKT1, PPP2CA, PPP2R1B, SPRY2, SPRY4, CNKSR1/CNK1, KSR2 and PHB/prohibitin (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. Interacts with MAP2K1/MEK1 and MAP2K2/MEK2. In its active form, interacts with PRMT5 (By similarity). Interacts with FAM83B; displaces 14-3-3 proteins from RAF1 and activates RAF1 (By similarity).By similarity

GO - Molecular functioni

  • mitogen-activated protein kinase kinase binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi246833. 7 interactions.
DIPiDIP-1073N.
IntActiP11345. 1 interaction.
STRINGi10116.ENSRNOP00000013831.

Structurei

Secondary structure

1
648
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 615Combined sources
Turni63 – 653Combined sources
Beta strandi68 – 714Combined sources
Helixi78 – 8912Combined sources
Turni93 – 953Combined sources
Beta strandi96 – 1005Combined sources
Beta strandi106 – 1083Combined sources
Helixi118 – 1214Combined sources
Beta strandi124 – 1307Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RRBNMR-A51-131[»]
ProteinModelPortaliP11345.
SMRiP11345. Positions 56-131, 136-187, 342-615.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11345.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13176RBDPROSITE-ProRule annotationAdd
BLAST
Domaini349 – 609261Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni331 – 34919Interaction with PEBP1/RKIPBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 RBD (Ras-binding) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri138 – 18447Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0193. Eukaryota.
ENOG410Y4UP. LUCA.
HOGENOMiHOG000252972.
HOVERGENiHBG001886.
InParanoidiP11345.
KOiK04366.

Family and domain databases

InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. RBD_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50898. RBD. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11345-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEHIQGAWKT ISNGFGLKDA VFDGSSCISP TIVQQFGYQR RASDDGKLTD
60 70 80 90 100
SSKTSNTIRV FLPNKQRTVV NVRNGMSLHD CLMKALKVRG LQPECCAVFR
110 120 130 140 150
LLQEHKGKKA RLDWNTDAAS LIGEELQVDF LDHVPLTTHN FARKTFLKLA
160 170 180 190 200
FCDICQKFLL NGFRCQTCGY KFHEHCSTKV PTMCVDWSNI RQLLLFPNST
210 220 230 240 250
ASDSGVPAPP SFTMRRMRES VSRMPASSQH RYSTPHAFTF NTSSPSSEGS
260 270 280 290 300
LSQRQRSTST PNVHMVSTTL PVDSRMIEDA IRSHSESASP SALSSSPNNL
310 320 330 340 350
SPTGWSQPKT PVPAQRERAP GSGTQEKNKI RPRGQRDSSY YWEIEASEVM
360 370 380 390 400
LSTRIGSGSF GTVYKGKWHG DVAVKILKVV DPTPEQLQAF RNEVAVLRKT
410 420 430 440 450
RHVNILLFMG YMTKDNLAIV TQWCEGSSLY KHLHVQETKF QMFQLIDIAR
460 470 480 490 500
QTAQGMDYLH AKNIIHRDMK SNNIFLHEGL TVKIGDFGLA TVKSRWSGSQ
510 520 530 540 550
QVEQPTGSVL WMAPEVIRMQ DNNPFSFQSD VYSYGIVLYE LMTGELPYSH
560 570 580 590 600
INNRDQIIFM VGRGYASPDL SRLYKNCPKA MKRLVADCVK KVKEERPLFP
610 620 630 640
QILSSIELLQ HSLPKINRSA SEPSLHRAAH TEDINACTLT TSPRLPVF
Length:648
Mass (Da):72,928
Last modified:July 1, 1989 - v1
Checksum:iE9AFB5975064193E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15427 mRNA. Translation: AAA42001.1.
BC062071 mRNA. Translation: AAH62071.1.
PIRiA26126. TVRTRF.
RefSeqiNP_036771.1. NM_012639.2.
UniGeneiRn.33262.

Genome annotation databases

EnsembliENSRNOT00000013831; ENSRNOP00000013831; ENSRNOG00000010153.
GeneIDi24703.
KEGGirno:24703.
UCSCiRGD:3531. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15427 mRNA. Translation: AAA42001.1.
BC062071 mRNA. Translation: AAH62071.1.
PIRiA26126. TVRTRF.
RefSeqiNP_036771.1. NM_012639.2.
UniGeneiRn.33262.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RRBNMR-A51-131[»]
ProteinModelPortaliP11345.
SMRiP11345. Positions 56-131, 136-187, 342-615.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246833. 7 interactions.
DIPiDIP-1073N.
IntActiP11345. 1 interaction.
STRINGi10116.ENSRNOP00000013831.

PTM databases

iPTMnetiP11345.
PhosphoSiteiP11345.

Proteomic databases

PaxDbiP11345.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000013831; ENSRNOP00000013831; ENSRNOG00000010153.
GeneIDi24703.
KEGGirno:24703.
UCSCiRGD:3531. rat.

Organism-specific databases

CTDi5894.
RGDi3531. Raf1.

Phylogenomic databases

eggNOGiKOG0193. Eukaryota.
ENOG410Y4UP. LUCA.
HOGENOMiHOG000252972.
HOVERGENiHBG001886.
InParanoidiP11345.
KOiK04366.

Enzyme and pathway databases

BRENDAi2.7.10.2. 5301.
ReactomeiR-RNO-2672351. Stimuli-sensing channels.
R-RNO-392517. Rap1 signalling.
R-RNO-430116. GP1b-IX-V activation signalling.
R-RNO-442742. CREB phosphorylation through the activation of Ras.
R-RNO-5621575. CD209 (DC-SIGN) signaling.
R-RNO-5673000. RAF activation.
R-RNO-5674135. MAP2K and MAPK activation.
R-RNO-5674499. Negative feedback regulation of MAPK pathway.
R-RNO-5675221. Negative regulation of MAPK pathway.

Miscellaneous databases

ChiTaRSiRaf1. rat.
EvolutionaryTraceiP11345.
NextBioi604169.
PROiP11345.

Gene expression databases

ExpressionAtlasiP11345. baseline and differential.
GenevisibleiP11345. RN.

Family and domain databases

InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. RBD_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50898. RBD. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat c-raf oncogene activation by a rearrangement that produces a fused protein."
    Ishikawa F., Takaku F., Nagao M., Sugimura T.
    Mol. Cell. Biol. 7:1226-1232(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. Cited for: FUNCTION IN PHOSPHORYLATION OF TNNT2.
  4. Cited for: INTERACTION WITH RGS14.
  5. "RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf MAPkinase signalling pathways."
    Shu F.J., Ramineni S., Hepler J.R.
    Cell. Signal. 22:366-376(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RGS14, SUBCELLULAR LOCATION.
  6. "A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function."
    Catling A.D., Schaeffer H.J., Reuter C.W., Reddy G.R., Weber M.J.
    Mol. Cell. Biol. 15:5214-5225(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP2K1/MEK1 AND MAP2K2/MEK2, FUNCTION.
  7. "Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
    Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
    Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Nuclear magnetic resonance and molecular dynamics studies on the interactions of the Ras-binding domain of Raf-1 with wild-type and mutant Ras proteins."
    Terada T., Ito Y., Shirouzu M., Tateno M., Hashimoto K., Kigawa T., Ebisuzaki T., Takio K., Shibata T., Yokoyama S., Smith B.O., Laue E.D., Cooper J.A.
    J. Mol. Biol. 286:219-232(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 51-131.

Entry informationi

Entry nameiRAF1_RAT
AccessioniPrimary (citable) accession number: P11345
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 11, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.