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Q99N57

- RAF1_MOUSE

UniProt

Q99N57 - RAF1_MOUSE

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Protein

RAF proto-oncogene serine/threonine-protein kinase

Gene

Raf1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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.By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Zn2+By similarityNote: Binds 2 Zn(2+) 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

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase kinase kinase activity Source: Ensembl
  3. metal ion binding Source: UniProtKB-KW
  4. protein kinase activity Source: MGI
  5. Ras GTPase binding Source: MGI

GO - Biological processi

  1. cell differentiation Source: MGI
  2. death-inducing signaling complex assembly Source: MGI
  3. heart development Source: Ensembl
  4. intermediate filament cytoskeleton organization Source: MGI
  5. intracellular signal transduction Source: MGI
  6. negative regulation of apoptotic process Source: Ensembl
  7. negative regulation of cell proliferation Source: Ensembl
  8. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  9. negative regulation of protein complex assembly Source: Ensembl
  10. neurotrophin TRK receptor signaling pathway Source: MGI
  11. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  12. response to hypoxia Source: Ensembl
  13. somatic stem cell maintenance Source: MGI
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

ReactomeiREACT_196640. Stimuli-sensing channels.
REACT_198246. CREB phosphorylation through the activation of Ras.
REACT_237640. RAF activation.
REACT_237855. Rap1 signalling.
REACT_245546. GP1b-IX-V activation signalling.
REACT_247566. MEK activation.
REACT_257146. RAF phosphorylates MEK.

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:Craf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:97847. Raf1.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity. Mitochondrion By similarity. Nucleus 1 Publication
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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: MGI
  3. Golgi apparatus Source: MGI
  4. mitochondrion Source: UniProtKB-KW
  5. nucleus Source: UniProtKB-KW
  6. plasma membrane Source: UniProtKB
  7. pseudopodium Source: UniProtKB
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_0000086597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphoserine; by MAPK11 Publication
Modified residuei43 – 431Phosphoserine; by PKA and MAPK11 Publication
Modified residuei233 – 2331Phosphoserine; by PKABy similarity
Modified residuei252 – 2521PhosphoserineBy similarity
Modified residuei259 – 2591Phosphoserine; by PKA, PKC and PKB/AKT1By similarity
Modified residuei268 – 2681Phosphothreonine; by autocatalysisBy similarity
Modified residuei269 – 2691Phosphothreonine; by PKABy similarity
Modified residuei289 – 2891Phosphoserine; by MAPK11 Publication
Modified residuei296 – 2961Phosphoserine; by MAPK11 Publication
Modified residuei301 – 3011Phosphoserine; by MAPK11 Publication
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 – 6211Phosphoserine1 Publication
Modified residuei642 – 6421Phosphoserine; by MAPK11 Publication

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 at Arg-563 in response to EGF treatment. This modification leads to destabilization of the protein, possibly through proteasomal degradation.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ99N57.
PaxDbiQ99N57.
PRIDEiQ99N57.

PTM databases

PhosphoSiteiQ99N57.

Expressioni

Tissue specificityi

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 2.2 Publications

Gene expression databases

BgeeiQ99N57.
CleanExiMM_RAF1.
ExpressionAtlasiQ99N57. baseline and differential.
GenevestigatoriQ99N57.

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. 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). 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 (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, PPP1R12A, PKB/AKT1, SPRY2, SPRY4, CNKSR1/CNK1, KSR2 and PHB/prohibitin (By similarity). The phosphorylated form interacts with PIN1. Interacts with PPP2CA, PPP2R1B and ROCK2. In its active form, interacts with PRMT5 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BRAFP150563EBI-397757,EBI-365980From a different organism.
BrafP280282EBI-397757,EBI-2584830
KrasP32883-23EBI-397757,EBI-644285

Protein-protein interaction databases

BioGridi225343. 15 interactions.
DIPiDIP-31555N.
IntActiQ99N57. 9 interactions.
MINTiMINT-1582303.

Structurei

3D structure databases

ProteinModelPortaliQ99N57.
SMRiQ99N57. Positions 56-131, 136-187, 307-615.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118807.
HOGENOMiHOG000252972.
HOVERGENiHBG001886.
InParanoidiQ99N57.
KOiK04366.
OMAiDGPSCIS.
OrthoDBiEOG7F5128.
PhylomeDBiQ99N57.
TreeFamiTF317006.

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. Raf-like_ras-bd.
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.
[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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99N57-1) [UniParc]FASTAAdd to Basket

Also known as: 6C

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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
VGDSGVPAPP SFPMRRMRES VSRMPASSQH RYSTPHAFTF NTSSPSSEGS
260 270 280 290 300
LSQRQRSTST PNVHMVSTTL HVDSRMIEDA 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 DDNPFSFQSD VYSYGIVLYE LMAGELPYAH
560 570 580 590 600
INNRDQIIFM VGRGYASPDL SRLYKNCPKA MKRLVADCVK KVKEERPLFP
610 620 630 640
QILSSIELLQ HSLPKINRSA SEPSLHRAAH TEDINACTLT TSPRLPVF
Length:648
Mass (Da):72,917
Last modified:March 1, 2002 - v2
Checksum:iB70104AEF51C44A5
GO
Isoform 2 (identifier: Q99N57-2) [UniParc]FASTAAdd to Basket

Also known as: 1A

The sequence of this isoform differs from the canonical sequence as follows:
     278-278: E → ESNSLNASPRACSRRFCLRGR

Show »
Length:668
Mass (Da):75,151
Checksum:iD70FF05B80BCF8ED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti522 – 5221D → N in AAH92040. (PubMed:15489334)Curated
Sequence conflicti543 – 5431A → T in AAH92040. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei278 – 2781E → ESNSLNASPRACSRRFCLRG R in isoform 2. CuratedVSP_034629

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB057655 mRNA. Translation: BAB39748.1.
AB057663 mRNA. Translation: BAB39743.2.
AK141745 mRNA. Translation: BAE24820.1.
BC015273 mRNA. Translation: AAH15273.1.
BC092040 mRNA. Translation: AAH92040.1.
X55432 Genomic DNA. No translation available.
CCDSiCCDS20441.1. [Q99N57-1]
RefSeqiNP_084056.1. NM_029780.3. [Q99N57-1]
XP_006505426.1. XM_006505363.1. [Q99N57-2]
XP_006505427.1. XM_006505364.1. [Q99N57-2]
XP_006505428.1. XM_006505365.1. [Q99N57-1]
UniGeneiMm.184163.

Genome annotation databases

EnsembliENSMUST00000000451; ENSMUSP00000000451; ENSMUSG00000000441. [Q99N57-1]
ENSMUST00000112949; ENSMUSP00000108571; ENSMUSG00000000441. [Q99N57-1]
GeneIDi110157.
KEGGimmu:110157.
UCSCiuc009dix.1. mouse. [Q99N57-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB057655 mRNA. Translation: BAB39748.1 .
AB057663 mRNA. Translation: BAB39743.2 .
AK141745 mRNA. Translation: BAE24820.1 .
BC015273 mRNA. Translation: AAH15273.1 .
BC092040 mRNA. Translation: AAH92040.1 .
X55432 Genomic DNA. No translation available.
CCDSi CCDS20441.1. [Q99N57-1 ]
RefSeqi NP_084056.1. NM_029780.3. [Q99N57-1 ]
XP_006505426.1. XM_006505363.1. [Q99N57-2 ]
XP_006505427.1. XM_006505364.1. [Q99N57-2 ]
XP_006505428.1. XM_006505365.1. [Q99N57-1 ]
UniGenei Mm.184163.

3D structure databases

ProteinModelPortali Q99N57.
SMRi Q99N57. Positions 56-131, 136-187, 307-615.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 225343. 15 interactions.
DIPi DIP-31555N.
IntActi Q99N57. 9 interactions.
MINTi MINT-1582303.

PTM databases

PhosphoSitei Q99N57.

Proteomic databases

MaxQBi Q99N57.
PaxDbi Q99N57.
PRIDEi Q99N57.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000451 ; ENSMUSP00000000451 ; ENSMUSG00000000441 . [Q99N57-1 ]
ENSMUST00000112949 ; ENSMUSP00000108571 ; ENSMUSG00000000441 . [Q99N57-1 ]
GeneIDi 110157.
KEGGi mmu:110157.
UCSCi uc009dix.1. mouse. [Q99N57-1 ]

Organism-specific databases

CTDi 5894.
MGIi MGI:97847. Raf1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118807.
HOGENOMi HOG000252972.
HOVERGENi HBG001886.
InParanoidi Q99N57.
KOi K04366.
OMAi DGPSCIS.
OrthoDBi EOG7F5128.
PhylomeDBi Q99N57.
TreeFami TF317006.

Enzyme and pathway databases

Reactomei REACT_196640. Stimuli-sensing channels.
REACT_198246. CREB phosphorylation through the activation of Ras.
REACT_237640. RAF activation.
REACT_237855. Rap1 signalling.
REACT_245546. GP1b-IX-V activation signalling.
REACT_247566. MEK activation.
REACT_257146. RAF phosphorylates MEK.

Miscellaneous databases

ChiTaRSi Raf1. mouse.
NextBioi 363431.
PROi Q99N57.
SOURCEi Search...

Gene expression databases

Bgeei Q99N57.
CleanExi MM_RAF1.
ExpressionAtlasi Q99N57. baseline and differential.
Genevestigatori Q99N57.

Family and domain databases

InterProi IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. Raf-like_ras-bd.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view ]
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Phylogenetic conservation of the makorin-2 gene, encoding a multiple zinc-finger protein, antisense to the raf1 proto-oncogene."
    Gray T.A., Azama K., Whitmore K., Min A., Abe S., Nicholls R.D.
    Genomics 77:119-126(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "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] (ISOFORM 1).
    Strain: Czech II and FVB/N.
    Tissue: Kidney and Mammary tumor.
  4. "An alternatively spliced c-mil/raf mRNA is predominantly expressed in chicken muscular tissues and conserved among vertebrate species."
    Dozier C., Ansieau S., Ferreira E., Coll J., Stehelin D.
    Oncogene 6:1307-1311(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  5. Cited for: FUNCTION, INTERACTION WITH ROCK2.
  6. Cited for: PHOSPHORYLATION AT SER-29; SER-43; SER-259; SER-289; SER-296; SER-301; SER-338; SER-621 AND SER-642, ENZYME REGULATION, INTERACTION WITH PIN1; PPP2CA AND PPP2R1B.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Retinoic acid induces nuclear accumulation of Raf1 during differentiation of HL-60 cells."
    Smith J., Bunaciu R.P., Reiterer G., Coder D., George T., Asaly M., Yen A.
    Exp. Cell Res. 315:2241-2248(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRAF1_MOUSE
AccessioniPrimary (citable) accession number: Q99N57
Secondary accession number(s): Q3UR68
, Q58E75, Q91WH1, Q99N58, Q9QUU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2002
Last modified: November 26, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3