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P15056

- BRAF_HUMAN

UniProt

P15056 - BRAF_HUMAN

Protein

Serine/threonine-protein kinase B-raf

Gene

BRAF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 185 (01 Oct 2014)
      Sequence version 4 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron. Phosphorylates MAP2K1, and thereby contributes to the MAP kinase signal transduction pathway.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Binds 2 zinc ions per subunit.By similarity

    Enzyme regulationi

    Activity is increased by EGF and HGF.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi235 – 2351Zinc 1By similarity
    Metal bindingi248 – 2481Zinc 2By similarity
    Metal bindingi251 – 2511Zinc 2By similarity
    Metal bindingi261 – 2611Zinc 1By similarity
    Metal bindingi264 – 2641Zinc 1By similarity
    Metal bindingi269 – 2691Zinc 2By similarity
    Metal bindingi272 – 2721Zinc 2By similarity
    Metal bindingi280 – 2801Zinc 1By similarity
    Sitei380 – 3812Breakpoint for translocation to form KIAA1549-BRAF fusion protein
    Sitei438 – 4392Breakpoint for translocation to form KIAA1549-BRAF fusion protein
    Binding sitei483 – 4831ATPPROSITE-ProRule annotation
    Active sitei576 – 5761Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri234 – 28047Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi463 – 4719ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: BHF-UCL
    3. identical protein binding Source: IntAct
    4. MAP kinase kinase kinase activity Source: Ensembl
    5. protein binding Source: IntAct
    6. protein kinase activity Source: BHF-UCL
    7. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of MAPKK activity Source: Reactome
    2. cellular response to calcium ion Source: BHF-UCL
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. negative regulation of apoptotic process Source: UniProtKB
    5. negative regulation of neuron apoptotic process Source: Ensembl
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. organ morphogenesis Source: ProtInc
    8. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    9. positive regulation of gene expression Source: BHF-UCL
    10. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
    11. protein heterooligomerization Source: Ensembl
    12. protein phosphorylation Source: BHF-UCL
    13. response to cAMP Source: Ensembl
    14. response to epidermal growth factor Source: Ensembl
    15. response to peptide hormone Source: Ensembl
    16. small GTPase mediated signal transduction Source: Reactome
    17. synaptic transmission Source: Reactome

    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. 2681.
    ReactomeiREACT_111080. Spry regulation of FGF signaling.
    REACT_12002. ARMS-mediated activation.
    REACT_12076. Frs2-mediated activation.
    REACT_12077. Signalling to p38 via RIT and RIN.
    REACT_20568. CREB phosphorylation through the activation of Ras.
    SignaLinkiP15056.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase B-raf (EC:2.7.11.1)
    Alternative name(s):
    Proto-oncogene B-Raf
    p94
    v-Raf murine sarcoma viral oncogene homolog B1
    Gene namesi
    Name:BRAF
    Synonyms:BRAF1, RAFB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1097. BRAF.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm. Cell membrane By similarity
    Note: Colocalizes with RGS14 and RAF1 in both the cytoplasm and membranes.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. neuron projection Source: Ensembl
    3. nucleus Source: UniProtKB-SubCell
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Defects in BRAF are found in a wide range of cancers.1 Publication
    Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.2 Publications
    Note: The disease may be caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti462 – 4621R → I in CRC. 1 Publication
    VAR_018613
    Natural varianti463 – 4631I → S in CRC. 1 Publication
    VAR_018614
    Natural varianti464 – 4641G → E in CRC. 2 Publications
    VAR_018615
    Natural varianti600 – 6001V → E in CRC; also found in sarcoma, metastatic melanoma, ovarian serous carcinoma, pilocytic astrocytoma; somatic mutation; most common mutation; constitutive and elevated kinase activity; efficiently induces cell transformation; suppression of mutation in melanoma causes growth arrest and promotes apoptosis; loss of regulation by PMRT5. 5 Publications
    VAR_018629
    Natural varianti601 – 6011K → E in CRC. 1 Publication
    VAR_018630
    Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti466 – 4661G → V in LNCR. 2 Publications
    VAR_018512
    Natural varianti597 – 5971L → R in LNCR; also found in an ovarian serous carcinoma sample; somatic mutation. 3 Publications
    VAR_018513
    Familial non-Hodgkin lymphoma (NHL) [MIM:605027]: Cancer that starts in cells of the lymph system, which is part of the body's immune system. NHLs can occur at any age and are often marked by enlarged lymph nodes, fever and weight loss.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti469 – 4691G → A in NHL; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. 3 Publications
    VAR_018620
    Natural varianti469 – 4691G → R in NHL. 1 Publication
    VAR_018622
    Natural varianti594 – 5941D → G in NHL. 1 Publication
    VAR_018624
    Cardiofaciocutaneous syndrome 1 (CFC1) [MIM:115150]: A multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti241 – 2411T → P in CFC1 and LEOPARD3. 2 Publications
    VAR_058621
    Natural varianti244 – 2441T → P in CFC1. 1 Publication
    VAR_065171
    Natural varianti245 – 2451L → F in CFC1. 1 Publication
    VAR_058623
    Natural varianti246 – 2461A → P in CFC1. 3 Publications
    VAR_026113
    Natural varianti257 – 2571Q → R in CFC1. 4 Publications
    VAR_026114
    Natural varianti262 – 2621Q → K in CFC1. 1 Publication
    VAR_065172
    Natural varianti275 – 2751E → K in CFC1. 1 Publication
    VAR_058624
    Natural varianti467 – 4671S → A in CFC1. 1 Publication
    VAR_035096
    Natural varianti468 – 4681F → S in CFC1. 2 Publications
    VAR_035097
    Natural varianti469 – 4691G → E in CFC1 and colon cancer. 5 Publications
    VAR_018621
    Natural varianti485 – 4851L → F in CFC1. 3 Publications
    VAR_026115
    Natural varianti499 – 4991K → E in CFC1. 3 Publications
    VAR_026116
    Natural varianti499 – 4991K → N in CFC1. 2 Publications
    VAR_058625
    Natural varianti501 – 5011E → G in CFC1. 2 Publications
    VAR_026117
    Natural varianti501 – 5011E → K in CFC1. 3 Publications
    VAR_026118
    Natural varianti525 – 5251L → P in CFC1. 1 Publication
    VAR_058626
    Natural varianti580 – 5801N → D in CFC1. 1 Publication
    VAR_065173
    Natural varianti581 – 5811N → D in CFC1. 3 Publications
    VAR_026119
    Natural varianti595 – 5951F → L in colon cancer and CFC1. 4 Publications
    VAR_018625
    Natural varianti596 – 5961G → V in CFC1. 1 Publication
    VAR_035098
    Natural varianti599 – 5991T → R in CFC1. 1 Publication
    VAR_058628
    Natural varianti601 – 6011K → Q in CFC1. 1 Publication
    VAR_058629
    Natural varianti638 – 6381D → E in CFC1. 1 Publication
    VAR_058630
    Natural varianti709 – 7091Q → R in CFC1. 1 Publication
    VAR_058631
    Noonan syndrome 7 (NS7) [MIM:613706]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti531 – 5311W → C in NS7. 1 Publication
    VAR_058627
    Natural varianti597 – 5971L → V in NS7; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. 3 Publications
    VAR_018627
    LEOPARD syndrome 3 (LEOPARD3) [MIM:613707]: A disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti241 – 2411T → P in CFC1 and LEOPARD3. 2 Publications
    VAR_058621
    A chromosomal aberration involving BRAF is found in pilocytic astrocytomas. A tandem duplication of 2 Mb at 7q34 leads to the expression of a KIAA1549-BRAF fusion protein with a constitutive kinase activity and inducing cell transformation.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi483 – 4831K → S: Reduces kinase activity with MAP2K1. 1 Publication
    Mutagenesisi578 – 5781K → R: Blocks EGF-induced ubiquitination and ERK activation. 1 Publication
    Mutagenesisi671 – 6711R → K: Increased kinase activity and stability in response to EGF treatment. 1 Publication

    Keywords - Diseasei

    Cardiomyopathy, Deafness, Disease mutation, Ectodermal dysplasia, Mental retardation, Proto-oncogene

    Organism-specific databases

    MIMi114500. phenotype.
    115150. phenotype.
    211980. phenotype.
    605027. phenotype.
    613706. phenotype.
    613707. phenotype.
    Orphaneti1340. Cardiofaciocutaneous syndrome.
    54595. Craniopharyngioma.
    58017. Hairy cell leukemia.
    99872. Hashimoto-Pritzker syndrome.
    500. LEOPARD syndrome.
    648. Noonan syndrome.
    251612. Pilocytic astrocytoma.
    PharmGKBiPA25408.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 766765Serine/threonine-protein kinase B-rafPRO_0000085665Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei365 – 3651Phosphoserine; by SGK12 Publications
    Modified residuei373 – 3731Phosphothreonine; by autocatalysis1 Publication
    Modified residuei396 – 3961Phosphothreonine1 Publication
    Modified residuei399 – 3991Phosphoserine1 Publication
    Modified residuei401 – 4011Phosphothreonine3 Publications
    Modified residuei446 – 4461Phosphoserine1 Publication
    Modified residuei447 – 4471Phosphoserine1 Publication
    Cross-linki578 – 578Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei671 – 6711Omega-N-methylarginine; by PRMT51 Publication
    Modified residuei729 – 7291Phosphoserine3 Publications
    Modified residuei753 – 7531Phosphothreonine; by MAPK11 Publication

    Post-translational modificationi

    Phosphorylation at Ser-365 by SGK1 inhibits its activity.7 Publications
    Methylation at Arg-671 decreases stability and kinase activity.1 Publication
    Ubiquitinated by RNF149; which leads to proteasomal degradation. Polyubiquitinated at Lys-578 in response to EGF.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP15056.
    PaxDbiP15056.
    PRIDEiP15056.

    PTM databases

    PhosphoSiteiP15056.

    Miscellaneous databases

    PMAP-CutDBP15056.

    Expressioni

    Tissue specificityi

    Brain and testis.

    Gene expression databases

    ArrayExpressiP15056.
    BgeeiP15056.
    CleanExiHS_BRAF.
    GenevestigatoriP15056.

    Organism-specific databases

    HPAiCAB004552.
    HPA001328.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Heterodimerizes with RAF1, and the 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 by phosphorylating BRAF at Thr-753. Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIT1. Interacts (via N-terminus) with RGS14 (via RBD domains); the interaction mediates the formation of a ternary complex with RAF1, a ternary complex inhibited by GNAI1 By similarity. Interacts with DGKH. Interacts with PRMT5. Interacts with KSR2.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself8EBI-365980,EBI-365980
    ARAFP103982EBI-365980,EBI-365961
    HSP90AB1P082382EBI-365980,EBI-352572
    Ksr1Q610973EBI-365980,EBI-1536336From a different organism.
    MAP3K1Q132332EBI-365980,EBI-49776
    RAF1P0404939EBI-365980,EBI-365996
    Raf1Q99N573EBI-365980,EBI-397757From a different organism.
    Rgs12Q8CGE92EBI-365980,EBI-7340552From a different organism.
    RPS6KA2Q153492EBI-365980,EBI-1384149
    TRAF3Q131142EBI-365980,EBI-357631
    YWHABP319463EBI-365980,EBI-359815
    YWHAZP631043EBI-365980,EBI-347088

    Protein-protein interaction databases

    BioGridi107141. 41 interactions.
    DIPiDIP-1045N.
    IntActiP15056. 38 interactions.
    MINTiMINT-1574728.
    STRINGi9606.ENSP00000288602.

    Structurei

    Secondary structure

    1
    766
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi156 – 1616
    Turni162 – 1643
    Beta strandi165 – 1706
    Helixi177 – 18610
    Turni187 – 1893
    Helixi192 – 1943
    Beta strandi195 – 1995
    Beta strandi206 – 2083
    Helixi214 – 2174
    Beta strandi221 – 2266
    Beta strandi458 – 4658
    Beta strandi467 – 48620
    Beta strandi487 – 4893
    Helixi492 – 50514
    Beta strandi516 – 5205
    Beta strandi522 – 5243
    Beta strandi526 – 5305
    Beta strandi534 – 5363
    Helixi537 – 5415
    Turni542 – 5443
    Helixi550 – 56920
    Beta strandi581 – 5855
    Turni586 – 5883
    Beta strandi589 – 5924
    Beta strandi599 – 6013
    Helixi617 – 6193
    Helixi622 – 6254
    Beta strandi629 – 6313
    Helixi635 – 65117
    Turni655 – 6584
    Helixi662 – 6709
    Helixi678 – 6803
    Beta strandi683 – 6853
    Helixi687 – 69610
    Helixi701 – 7033
    Helixi707 – 71610
    Helixi718 – 7203

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UWHX-ray2.95A/B448-723[»]
    1UWJX-ray3.50A/B448-723[»]
    2FB8X-ray2.90A/B445-723[»]
    2L05NMR-A149-232[»]
    3C4CX-ray2.57A/B444-721[»]
    3D4QX-ray2.80A/B433-726[»]
    3IDPX-ray2.70A/B434-727[»]
    3II5X-ray2.79A/B432-726[»]
    3NY5X-ray1.99A/B/C/D153-237[»]
    3OG7X-ray2.45A/B449-766[»]
    3PPJX-ray3.70A/B432-726[»]
    3PPKX-ray3.00A/B432-726[»]
    3PRFX-ray2.90A/B432-726[»]
    3PRIX-ray3.50A/B432-726[»]
    3PSBX-ray3.40A/B433-726[»]
    3PSDX-ray3.60A/B433-726[»]
    3Q4CX-ray3.20A/B432-726[»]
    3Q96X-ray3.10A/B446-727[»]
    3SKCX-ray3.20A/B432-726[»]
    3TV4X-ray3.40A/B432-726[»]
    3TV6X-ray3.30A/B432-726[»]
    4DBNX-ray3.15A/B445-726[»]
    4E26X-ray2.55A/B432-726[»]
    4E4XX-ray3.60A/B432-726[»]
    4EHEX-ray3.30A/B432-726[»]
    4EHGX-ray3.50A/B432-726[»]
    4FC0X-ray2.95A/B445-726[»]
    4FK3X-ray2.65A/B444-723[»]
    4G9CX-ray3.50A/B432-726[»]
    4G9RX-ray3.20A/B432-726[»]
    4H58X-ray3.10A/B/C448-722[»]
    4JVGX-ray3.09A/B/C/D444-723[»]
    4KSPX-ray2.93A/B445-726[»]
    4KSQX-ray3.30A/B445-726[»]
    4MBJX-ray3.60A/B432-723[»]
    4MNEX-ray2.85B/C/F/G432-726[»]
    4MNFX-ray2.80A/B432-736[»]
    4PP7X-ray3.40A/B432-726[»]
    ProteinModelPortaliP15056.
    SMRiP15056. Positions 149-283, 448-723.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15056.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini155 – 22773RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini457 – 717261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 116Poly-Gly
    Compositional biasi122 – 1298Poly-Ser
    Compositional biasi428 – 4325Poly-Ser

    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 fingeri234 – 28047Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG001886.
    InParanoidiP15056.
    KOiK04365.
    OMAiHRTRTSS.
    OrthoDBiEOG7F5128.
    PhylomeDBiP15056.
    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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15056-1 [UniParc]FASTAAdd to Basket

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    MAALSGGGGG GAEPGQALFN GDMEPEAGAG AGAAASSAAD PAIPEEVWNI    50
    KQMIKLTQEH IEALLDKFGG EHNPPSIYLE AYEEYTSKLD ALQQREQQLL 100
    ESLGNGTDFS VSSSASMDTV TSSSSSSLSV LPSSLSVFQN PTDVARSNPK 150
    SPQKPIVRVF LPNKQRTVVP ARCGVTVRDS LKKALMMRGL IPECCAVYRI 200
    QDGEKKPIGW DTDISWLTGE ELHVEVLENV PLTTHNFVRK TFFTLAFCDF 250
    CRKLLFQGFR CQTCGYKFHQ RCSTEVPLMC VNYDQLDLLF VSKFFEHHPI 300
    PQEEASLAET ALTSGSSPSA PASDSIGPQI LTSPSPSKSI PIPQPFRPAD 350
    EDHRNQFGQR DRSSSAPNVH INTIEPVNID DLIRDQGFRG DGGSTTGLSA 400
    TPPASLPGSL TNVKALQKSP GPQRERKSSS SSEDRNRMKT LGRRDSSDDW 450
    EIPDGQITVG QRIGSGSFGT VYKGKWHGDV AVKMLNVTAP TPQQLQAFKN 500
    EVGVLRKTRH VNILLFMGYS TKPQLAIVTQ WCEGSSLYHH LHIIETKFEM 550
    IKLIDIARQT AQGMDYLHAK SIIHRDLKSN NIFLHEDLTV KIGDFGLATV 600
    KSRWSGSHQF EQLSGSILWM APEVIRMQDK NPYSFQSDVY AFGIVLYELM 650
    TGQLPYSNIN NRDQIIFMVG RGYLSPDLSK VRSNCPKAMK RLMAECLKKK 700
    RDERPLFPQI LASIELLARS LPKIHRSASE PSLNRAGFQT EDFSLYACAS 750
    PKTPIQAGGY GAFPVH 766
    Length:766
    Mass (Da):84,437
    Last modified:July 19, 2004 - v4
    Checksum:i0798C2AAB487E813
    GO

    Sequence cautioni

    The sequence CAQ43111.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAQ43112.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAQ43113.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAQ43114.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAQ43115.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAQ43116.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAD43193.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti766 – 7661H → D in AAA96495. (PubMed:3043188)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti241 – 2411T → M in a patient with Noonan syndrome. 1 Publication
    VAR_058620
    Natural varianti241 – 2411T → P in CFC1 and LEOPARD3. 2 Publications
    VAR_058621
    Natural varianti241 – 2411T → R in a patient with Noonan syndrome. 1 Publication
    VAR_058622
    Natural varianti244 – 2441T → P in CFC1. 1 Publication
    VAR_065171
    Natural varianti245 – 2451L → F in CFC1. 1 Publication
    VAR_058623
    Natural varianti246 – 2461A → P in CFC1. 3 Publications
    VAR_026113
    Natural varianti257 – 2571Q → R in CFC1. 4 Publications
    VAR_026114
    Natural varianti262 – 2621Q → K in CFC1. 1 Publication
    VAR_065172
    Natural varianti275 – 2751E → K in CFC1. 1 Publication
    VAR_058624
    Natural varianti301 – 3011P → S.1 Publication
    Corresponds to variant rs34776339 [ dbSNP | Ensembl ].
    VAR_040391
    Natural varianti462 – 4621R → I in CRC. 1 Publication
    VAR_018613
    Natural varianti463 – 4631I → S in CRC. 1 Publication
    VAR_018614
    Natural varianti464 – 4641G → E in CRC. 2 Publications
    VAR_018615
    Natural varianti464 – 4641G → V in a colorectal cancer cell line; elevated kinase activity; efficiently induces cell transformation. 1 Publication
    VAR_018616
    Natural varianti466 – 4661G → A in melanoma. 1 Publication
    VAR_018617
    Natural varianti466 – 4661G → E in melanoma. 1 Publication
    VAR_018618
    Natural varianti466 – 4661G → V in LNCR. 2 Publications
    VAR_018512
    Natural varianti467 – 4671S → A in CFC1. 1 Publication
    VAR_035096
    Natural varianti468 – 4681F → S in CFC1. 2 Publications
    VAR_035097
    Natural varianti469 – 4691G → A in NHL; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. 3 Publications
    VAR_018620
    Natural varianti469 – 4691G → E in CFC1 and colon cancer. 5 Publications
    VAR_018621
    Natural varianti469 – 4691G → R in NHL. 1 Publication
    VAR_018622
    Natural varianti469 – 4691G → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040392
    Natural varianti485 – 4851L → F in CFC1. 3 Publications
    VAR_026115
    Natural varianti499 – 4991K → E in CFC1. 3 Publications
    VAR_026116
    Natural varianti499 – 4991K → N in CFC1. 2 Publications
    VAR_058625
    Natural varianti501 – 5011E → G in CFC1. 2 Publications
    VAR_026117
    Natural varianti501 – 5011E → K in CFC1. 3 Publications
    VAR_026118
    Natural varianti525 – 5251L → P in CFC1. 1 Publication
    VAR_058626
    Natural varianti531 – 5311W → C in NS7. 1 Publication
    VAR_058627
    Natural varianti580 – 5801N → D in CFC1. 1 Publication
    VAR_065173
    Natural varianti581 – 5811N → D in CFC1. 3 Publications
    VAR_026119
    Natural varianti581 – 5811N → S in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040393
    Natural varianti586 – 5861E → K in ovarian cancer. 1 Publication
    VAR_018623
    Natural varianti594 – 5941D → G in NHL. 1 Publication
    VAR_018624
    Natural varianti595 – 5951F → L in colon cancer and CFC1. 4 Publications
    VAR_018625
    Natural varianti596 – 5961G → R in a colorectal adenocarcinoma sample; somatic mutation. 2 Publications
    VAR_018626
    Natural varianti596 – 5961G → V in CFC1. 1 Publication
    VAR_035098
    Natural varianti597 – 5971L → R in LNCR; also found in an ovarian serous carcinoma sample; somatic mutation. 3 Publications
    VAR_018513
    Natural varianti597 – 5971L → V in NS7; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. 3 Publications
    VAR_018627
    Natural varianti599 – 5991T → R in CFC1. 1 Publication
    VAR_058628
    Natural varianti600 – 6001V → D in a melanoma cell line; requires 2 nucleotide substitutions. 1 Publication
    VAR_018628
    Natural varianti600 – 6001V → E in CRC; also found in sarcoma, metastatic melanoma, ovarian serous carcinoma, pilocytic astrocytoma; somatic mutation; most common mutation; constitutive and elevated kinase activity; efficiently induces cell transformation; suppression of mutation in melanoma causes growth arrest and promotes apoptosis; loss of regulation by PMRT5. 5 Publications
    VAR_018629
    Natural varianti601 – 6011K → E in CRC. 1 Publication
    VAR_018630
    Natural varianti601 – 6011K → Q in CFC1. 1 Publication
    VAR_058629
    Natural varianti638 – 6381D → E in CFC1. 1 Publication
    VAR_058630
    Natural varianti709 – 7091Q → R in CFC1. 1 Publication
    VAR_058631

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95712 mRNA. Translation: AAA35609.2.
    AC006344 Genomic DNA. Translation: AAD43193.1. Sequence problems.
    EU600171 Genomic DNA. Translation: ACD11489.1.
    AC006347 Genomic DNA. Translation: AAD15551.1.
    CH236950 Genomic DNA. Translation: EAL24023.1.
    BC101757 mRNA. Translation: AAI01758.1.
    BC112079 mRNA. Translation: AAI12080.1.
    X65187 Genomic DNA. Translation: CAA46301.1.
    M21001 mRNA. Translation: AAA96495.1.
    AM989472 mRNA. Translation: CAQ43111.1. Different initiation.
    AM989473 mRNA. Translation: CAQ43112.1. Different initiation.
    AM989474 mRNA. Translation: CAQ43113.1. Different initiation.
    AM989475 mRNA. Translation: CAQ43114.1. Different initiation.
    AM989476 mRNA. Translation: CAQ43115.1. Different initiation.
    AM989477 mRNA. Translation: CAQ43116.1. Different initiation.
    CCDSiCCDS5863.1.
    PIRiA57977. TVHUBF.
    RefSeqiNP_004324.2. NM_004333.4.
    UniGeneiHs.550061.
    Hs.600998.
    Hs.605380.
    Hs.659507.

    Genome annotation databases

    EnsembliENST00000288602; ENSP00000288602; ENSG00000157764.
    GeneIDi673.
    KEGGihsa:673.
    UCSCiuc003vwc.4. human.

    Polymorphism databases

    DMDMi50403720.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95712 mRNA. Translation: AAA35609.2 .
    AC006344 Genomic DNA. Translation: AAD43193.1 . Sequence problems.
    EU600171 Genomic DNA. Translation: ACD11489.1 .
    AC006347 Genomic DNA. Translation: AAD15551.1 .
    CH236950 Genomic DNA. Translation: EAL24023.1 .
    BC101757 mRNA. Translation: AAI01758.1 .
    BC112079 mRNA. Translation: AAI12080.1 .
    X65187 Genomic DNA. Translation: CAA46301.1 .
    M21001 mRNA. Translation: AAA96495.1 .
    AM989472 mRNA. Translation: CAQ43111.1 . Different initiation.
    AM989473 mRNA. Translation: CAQ43112.1 . Different initiation.
    AM989474 mRNA. Translation: CAQ43113.1 . Different initiation.
    AM989475 mRNA. Translation: CAQ43114.1 . Different initiation.
    AM989476 mRNA. Translation: CAQ43115.1 . Different initiation.
    AM989477 mRNA. Translation: CAQ43116.1 . Different initiation.
    CCDSi CCDS5863.1.
    PIRi A57977. TVHUBF.
    RefSeqi NP_004324.2. NM_004333.4.
    UniGenei Hs.550061.
    Hs.600998.
    Hs.605380.
    Hs.659507.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UWH X-ray 2.95 A/B 448-723 [» ]
    1UWJ X-ray 3.50 A/B 448-723 [» ]
    2FB8 X-ray 2.90 A/B 445-723 [» ]
    2L05 NMR - A 149-232 [» ]
    3C4C X-ray 2.57 A/B 444-721 [» ]
    3D4Q X-ray 2.80 A/B 433-726 [» ]
    3IDP X-ray 2.70 A/B 434-727 [» ]
    3II5 X-ray 2.79 A/B 432-726 [» ]
    3NY5 X-ray 1.99 A/B/C/D 153-237 [» ]
    3OG7 X-ray 2.45 A/B 449-766 [» ]
    3PPJ X-ray 3.70 A/B 432-726 [» ]
    3PPK X-ray 3.00 A/B 432-726 [» ]
    3PRF X-ray 2.90 A/B 432-726 [» ]
    3PRI X-ray 3.50 A/B 432-726 [» ]
    3PSB X-ray 3.40 A/B 433-726 [» ]
    3PSD X-ray 3.60 A/B 433-726 [» ]
    3Q4C X-ray 3.20 A/B 432-726 [» ]
    3Q96 X-ray 3.10 A/B 446-727 [» ]
    3SKC X-ray 3.20 A/B 432-726 [» ]
    3TV4 X-ray 3.40 A/B 432-726 [» ]
    3TV6 X-ray 3.30 A/B 432-726 [» ]
    4DBN X-ray 3.15 A/B 445-726 [» ]
    4E26 X-ray 2.55 A/B 432-726 [» ]
    4E4X X-ray 3.60 A/B 432-726 [» ]
    4EHE X-ray 3.30 A/B 432-726 [» ]
    4EHG X-ray 3.50 A/B 432-726 [» ]
    4FC0 X-ray 2.95 A/B 445-726 [» ]
    4FK3 X-ray 2.65 A/B 444-723 [» ]
    4G9C X-ray 3.50 A/B 432-726 [» ]
    4G9R X-ray 3.20 A/B 432-726 [» ]
    4H58 X-ray 3.10 A/B/C 448-722 [» ]
    4JVG X-ray 3.09 A/B/C/D 444-723 [» ]
    4KSP X-ray 2.93 A/B 445-726 [» ]
    4KSQ X-ray 3.30 A/B 445-726 [» ]
    4MBJ X-ray 3.60 A/B 432-723 [» ]
    4MNE X-ray 2.85 B/C/F/G 432-726 [» ]
    4MNF X-ray 2.80 A/B 432-736 [» ]
    4PP7 X-ray 3.40 A/B 432-726 [» ]
    ProteinModelPortali P15056.
    SMRi P15056. Positions 149-283, 448-723.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107141. 41 interactions.
    DIPi DIP-1045N.
    IntActi P15056. 38 interactions.
    MINTi MINT-1574728.
    STRINGi 9606.ENSP00000288602.

    Chemistry

    BindingDBi P15056.
    ChEMBLi CHEMBL5145.
    DrugBanki DB00398. Sorafenib.
    GuidetoPHARMACOLOGYi 1943.

    PTM databases

    PhosphoSitei P15056.

    Polymorphism databases

    DMDMi 50403720.

    Proteomic databases

    MaxQBi P15056.
    PaxDbi P15056.
    PRIDEi P15056.

    Protocols and materials databases

    DNASUi 673.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288602 ; ENSP00000288602 ; ENSG00000157764 .
    GeneIDi 673.
    KEGGi hsa:673.
    UCSCi uc003vwc.4. human.

    Organism-specific databases

    CTDi 673.
    GeneCardsi GC07M140424.
    GeneReviewsi BRAF.
    H-InvDB HIX0167822.
    HGNCi HGNC:1097. BRAF.
    HPAi CAB004552.
    HPA001328.
    MIMi 114500. phenotype.
    115150. phenotype.
    164757. gene.
    211980. phenotype.
    605027. phenotype.
    613706. phenotype.
    613707. phenotype.
    neXtProti NX_P15056.
    Orphaneti 1340. Cardiofaciocutaneous syndrome.
    54595. Craniopharyngioma.
    58017. Hairy cell leukemia.
    99872. Hashimoto-Pritzker syndrome.
    500. LEOPARD syndrome.
    648. Noonan syndrome.
    251612. Pilocytic astrocytoma.
    PharmGKBi PA25408.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG001886.
    InParanoidi P15056.
    KOi K04365.
    OMAi HRTRTSS.
    OrthoDBi EOG7F5128.
    PhylomeDBi P15056.
    TreeFami TF317006.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_111080. Spry regulation of FGF signaling.
    REACT_12002. ARMS-mediated activation.
    REACT_12076. Frs2-mediated activation.
    REACT_12077. Signalling to p38 via RIT and RIN.
    REACT_20568. CREB phosphorylation through the activation of Ras.
    SignaLinki P15056.

    Miscellaneous databases

    ChiTaRSi BRAF. human.
    EvolutionaryTracei P15056.
    GeneWikii BRAF_(gene).
    GenomeRNAii 673.
    NextBioi 2776.
    PMAP-CutDB P15056.
    PROi P15056.
    SOURCEi