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Q99N57

- RAF1_MOUSE

UniProt

Q99N57 - RAF1_MOUSE

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
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 Mar 2002)
      Previous versions | rss
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    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

    Binds 2 zinc 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 binding Source: IntAct
    5. protein kinase activity Source: MGI
    6. 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

    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.

    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-SubCell
    5. nucleus Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB
    7. pseudopodium Source: UniProtKB

    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

    ArrayExpressiQ99N57.
    BgeeiQ99N57.
    CleanExiMM_RAF1.
    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.
    GeneTreeiENSGT00750000117324.
    HOGENOMiHOG000252972.
    HOVERGENiHBG001886.
    InParanoidiQ99N57.
    KOiK04366.
    OMAiDGPSCIS.
    OrthoDBiEOG7F5128.
    PhylomeDBiQ99N57.
    TreeFamiTF317006.

    Family and domain databases

    InterProiIPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR002219. Prot_Kinase_C-like_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

    MEHIQGAWKT ISNGFGLKDA VFDGSSCISP TIVQQFGYQR RASDDGKLTD    50
    SSKTSNTIRV FLPNKQRTVV NVRNGMSLHD CLMKALKVRG LQPECCAVFR 100
    LLQEHKGKKA RLDWNTDAAS LIGEELQVDF LDHVPLTTHN FARKTFLKLA 150
    FCDICQKFLL NGFRCQTCGY KFHEHCSTKV PTMCVDWSNI RQLLLFPNST 200
    VGDSGVPAPP SFPMRRMRES VSRMPASSQH RYSTPHAFTF NTSSPSSEGS 250
    LSQRQRSTST PNVHMVSTTL HVDSRMIEDA IRSHSESASP SALSSSPNNL 300
    SPTGWSQPKT PVPAQRERAP GSGTQEKNKI RPRGQRDSSY YWEIEASEVM 350
    LSTRIGSGSF GTVYKGKWHG DVAVKILKVV DPTPEQLQAF RNEVAVLRKT 400
    RHVNILLFMG YMTKDNLAIV TQWCEGSSLY KHLHVQETKF QMFQLIDIAR 450
    QTAQGMDYLH AKNIIHRDMK SNNIFLHEGL TVKIGDFGLA TVKSRWSGSQ 500
    QVEQPTGSVL WMAPEVIRMQ DDNPFSFQSD VYSYGIVLYE LMAGELPYAH 550
    INNRDQIIFM VGRGYASPDL SRLYKNCPKA MKRLVADCVK KVKEERPLFP 600
    QILSSIELLQ HSLPKINRSA SEPSLHRAAH TEDINACTLT TSPRLPVF 648
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ENSGT00750000117324.
    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.

    Miscellaneous databases

    ChiTaRSi RAF1. mouse.
    NextBioi 363431.
    PROi Q99N57.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99N57.
    Bgeei Q99N57.
    CleanExi MM_RAF1.
    Genevestigatori Q99N57.

    Family and domain databases

    InterProi IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR002219. Prot_Kinase_C-like_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

    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: October 1, 2014
    This is version 132 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