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P15056 (BRAF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:BRAF
Synonyms:BRAF1, RAFB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length766 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.19

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.19

Cofactor

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

Activity is increased by EGF and HGF.

Subunit structure

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. Ref.16 Ref.19 Ref.20

Subcellular location

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

Tissue specificity

Brain and testis.

Post-translational modification

Phosphorylation at Ser-365 by SGK1 inhibits its activity.

Methylation at Arg-671 decreases stability and kinase activity. Ref.20

Ubiquitinated by RNF149; which leads to proteasomal degradation. Polyubiquitinated at Lys-578 in response to EGF. Ref.22 Ref.23

Involvement in disease

Defects in BRAF are found in a wide range of cancers. Ref.10

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.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.10 Ref.20 Ref.27 Ref.36

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.
Note: The gene represented in this entry is involved in disease pathogenesis. Ref.10 Ref.25

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.
Note: The gene represented in this entry is involved in disease pathogenesis. Ref.10 Ref.28

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.30 Ref.32 Ref.34 Ref.35

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.35

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.35

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. Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 protein kinase domain.

Contains 1 RBD (Ras-binding) domain.

Sequence caution

The sequence AAD43193.1 differs from that shown. Reason: Erroneous gene model prediction.

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.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseCardiomyopathy
Deafness
Disease mutation
Ectodermal dysplasia
Mental retardation
Proto-oncogene
   DomainZinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPKK activity

Traceable author statement. Source: Reactome

cellular response to calcium ion

Inferred from direct assay PubMed 18567582. Source: BHF-UCL

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from direct assay PubMed 19667065. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

organ morphogenesis

Traceable author statement PubMed 9207797. Source: ProtInc

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 22065586. Source: BHF-UCL

positive regulation of gene expression

Inferred from mutant phenotype PubMed 22065586. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 19667065. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 17563371. Source: BHF-UCL

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to epidermal growth factor

Inferred from direct assay PubMed 17563371. Source: BHF-UCL

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from direct assay PubMed 18567582. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 16858395PubMed 22169110PubMed 22510884. Source: IntAct

protein binding

Inferred from physical interaction PubMed 12620389PubMed 15161933PubMed 16810323PubMed 16888650PubMed 17380122PubMed 17979178PubMed 20141835PubMed 22169110PubMed 22510884PubMed 22939624PubMed 23153539PubMed 23680146PubMed 24255178. Source: IntAct

protein kinase activity

Inferred from direct assay PubMed 17563371. Source: BHF-UCL

protein serine/threonine kinase activity

Inferred from direct assay PubMed 19667065. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 766765Serine/threonine-protein kinase B-raf
PRO_0000085665

Regions

Domain155 – 22773RBD
Domain457 – 717261Protein kinase
Zinc finger234 – 28047Phorbol-ester/DAG-type
Nucleotide binding463 – 4719ATP By similarity
Compositional bias6 – 116Poly-Gly
Compositional bias122 – 1298Poly-Ser
Compositional bias428 – 4325Poly-Ser

Sites

Active site5761Proton acceptor By similarity
Metal binding2351Zinc 1 By similarity
Metal binding2481Zinc 2 By similarity
Metal binding2511Zinc 2 By similarity
Metal binding2611Zinc 1 By similarity
Metal binding2641Zinc 1 By similarity
Metal binding2691Zinc 2 By similarity
Metal binding2721Zinc 2 By similarity
Metal binding2801Zinc 1 By similarity
Binding site4831ATP By similarity
Site380 – 3812Breakpoint for translocation to form KIAA1549-BRAF fusion protein
Site438 – 4392Breakpoint for translocation to form KIAA1549-BRAF fusion protein

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue3651Phosphoserine; by SGK1 Ref.8 Ref.12
Modified residue3731Phosphothreonine; by autocatalysis Ref.1
Modified residue3961Phosphothreonine Ref.8
Modified residue3991Phosphoserine Ref.8
Modified residue4011Phosphothreonine Ref.8 Ref.13 Ref.15
Modified residue4461Phosphoserine Ref.15
Modified residue4471Phosphoserine Ref.15
Modified residue6711Omega-N-methylarginine; by PRMT5 Ref.20
Modified residue7291Phosphoserine Ref.8 Ref.15 Ref.21
Modified residue7531Phosphothreonine; by MAPK1 Ref.16
Cross-link578Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

Natural variations

Natural variant2411T → M in a patient with Noonan syndrome. Ref.35
VAR_058620
Natural variant2411T → P in CFC1 and LEOPARD3. Ref.34 Ref.35
VAR_058621
Natural variant2411T → R in a patient with Noonan syndrome. Ref.35
VAR_058622
Natural variant2441T → P in CFC1. Ref.34
VAR_065171
Natural variant2451L → F in CFC1. Ref.35
VAR_058623
Natural variant2461A → P in CFC1. Ref.30 Ref.34 Ref.35
VAR_026113
Natural variant2571Q → R in CFC1. Ref.30 Ref.32 Ref.34 Ref.35
VAR_026114
Natural variant2621Q → K in CFC1. Ref.34
VAR_065172
Natural variant2751E → K in CFC1. Ref.35
VAR_058624
Natural variant3011P → S. Ref.33
Corresponds to variant rs34776339 [ dbSNP | Ensembl ].
VAR_040391
Natural variant4621R → I in CRC. Ref.27
VAR_018613
Natural variant4631I → S in CRC. Ref.27
VAR_018614
Natural variant4641G → E in CRC. Ref.26 Ref.27
VAR_018615
Natural variant4641G → V in a colorectal cancer cell line; elevated kinase activity; efficiently induces cell transformation. Ref.26
VAR_018616
Natural variant4661G → A in melanoma. Ref.26
VAR_018617
Natural variant4661G → E in melanoma. Ref.26
VAR_018618
Natural variant4661G → V in LNCR. Ref.25 Ref.26
VAR_018512
Natural variant4671S → A in CFC1. Ref.32
VAR_035096
Natural variant4681F → S in CFC1. Ref.32 Ref.34
VAR_035097
Natural variant4691G → A in NHL; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. Ref.26 Ref.28 Ref.33
VAR_018620
Natural variant4691G → E in CFC1 and colon cancer. Ref.26 Ref.30 Ref.32 Ref.34 Ref.35
VAR_018621
Natural variant4691G → R in NHL. Ref.28
VAR_018622
Natural variant4691G → V in a colorectal adenocarcinoma sample; somatic mutation. Ref.33
VAR_040392
Natural variant4851L → F in CFC1. Ref.30 Ref.32 Ref.35
VAR_026115
Natural variant4991K → E in CFC1. Ref.30 Ref.32 Ref.34
VAR_026116
Natural variant4991K → N in CFC1. Ref.34 Ref.35
VAR_058625
Natural variant5011E → G in CFC1. Ref.30 Ref.32
VAR_026117
Natural variant5011E → K in CFC1. Ref.30 Ref.32 Ref.35
VAR_026118
Natural variant5251L → P in CFC1. Ref.35
VAR_058626
Natural variant5311W → C in NS7. Ref.35
VAR_058627
Natural variant5801N → D in CFC1. Ref.34
VAR_065173
Natural variant5811N → D in CFC1. Ref.30 Ref.32 Ref.34
VAR_026119
Natural variant5811N → S in a colorectal adenocarcinoma sample; somatic mutation. Ref.33
VAR_040393
Natural variant5861E → K in ovarian cancer. Ref.26
VAR_018623
Natural variant5941D → G in NHL. Ref.28
VAR_018624
Natural variant5951F → L in colon cancer and CFC1. Ref.26 Ref.32 Ref.34 Ref.35
VAR_018625
Natural variant5961G → R in a colorectal adenocarcinoma sample; somatic mutation. Ref.26 Ref.33
VAR_018626
Natural variant5961G → V in CFC1. Ref.32
VAR_035098
Natural variant5971L → R in LNCR; also found in an ovarian serous carcinoma sample; somatic mutation. Ref.25 Ref.26 Ref.33
VAR_018513
Natural variant5971L → V in NS7; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. Ref.26 Ref.33 Ref.35
VAR_018627
Natural variant5991T → R in CFC1. Ref.35
VAR_058628
Natural variant6001V → D in a melanoma cell line; requires 2 nucleotide substitutions. Ref.26
VAR_018628
Natural variant6001V → 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. Ref.20 Ref.26 Ref.27 Ref.29 Ref.31 Ref.33 Ref.36
VAR_018629
Natural variant6011K → E in CRC. Ref.27
VAR_018630
Natural variant6011K → Q in CFC1. Ref.35
VAR_058629
Natural variant6381D → E in CFC1. Ref.35
VAR_058630
Natural variant7091Q → R in CFC1. Ref.35
VAR_058631

Experimental info

Mutagenesis4831K → S: Reduces kinase activity with MAP2K1. Ref.19
Mutagenesis5781K → R: Blocks EGF-induced ubiquitination and ERK activation. Ref.23
Mutagenesis6711R → K: Increased kinase activity and stability in response to EGF treatment. Ref.20
Sequence conflict7661H → D in AAA96495. Ref.11

Secondary structure

.................................................................. 766
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15056 [UniParc].

Last modified July 19, 2004. Version 4.
Checksum: 0798C2AAB487E813

FASTA76684,437
        10         20         30         40         50         60 
MAALSGGGGG GAEPGQALFN GDMEPEAGAG AGAAASSAAD PAIPEEVWNI KQMIKLTQEH 

        70         80         90        100        110        120 
IEALLDKFGG EHNPPSIYLE AYEEYTSKLD ALQQREQQLL ESLGNGTDFS VSSSASMDTV 

       130        140        150        160        170        180 
TSSSSSSLSV LPSSLSVFQN PTDVARSNPK SPQKPIVRVF LPNKQRTVVP ARCGVTVRDS 

       190        200        210        220        230        240 
LKKALMMRGL IPECCAVYRI QDGEKKPIGW DTDISWLTGE ELHVEVLENV PLTTHNFVRK 

       250        260        270        280        290        300 
TFFTLAFCDF CRKLLFQGFR CQTCGYKFHQ RCSTEVPLMC VNYDQLDLLF VSKFFEHHPI 

       310        320        330        340        350        360 
PQEEASLAET ALTSGSSPSA PASDSIGPQI LTSPSPSKSI PIPQPFRPAD EDHRNQFGQR 

       370        380        390        400        410        420 
DRSSSAPNVH INTIEPVNID DLIRDQGFRG DGGSTTGLSA TPPASLPGSL TNVKALQKSP 

       430        440        450        460        470        480 
GPQRERKSSS SSEDRNRMKT LGRRDSSDDW EIPDGQITVG QRIGSGSFGT VYKGKWHGDV 

       490        500        510        520        530        540 
AVKMLNVTAP TPQQLQAFKN EVGVLRKTRH VNILLFMGYS TKPQLAIVTQ WCEGSSLYHH 

       550        560        570        580        590        600 
LHIIETKFEM IKLIDIARQT AQGMDYLHAK SIIHRDLKSN NIFLHEDLTV KIGDFGLATV 

       610        620        630        640        650        660 
KSRWSGSHQF EQLSGSILWM APEVIRMQDK NPYSFQSDVY AFGIVLYELM TGQLPYSNIN 

       670        680        690        700        710        720 
NRDQIIFMVG RGYLSPDLSK VRSNCPKAMK RLMAECLKKK RDERPLFPQI LASIELLARS 

       730        740        750        760 
LPKIHRSASE PSLNRAGFQT EDFSLYACAS PKTPIQAGGY GAFPVH 

« Hide

References

« Hide 'large scale' references
[1]"95-kilodalton B-Raf serine/threonine kinase: identification of the protein and its major autophosphorylation site."
Stephens R.M., Sithanandam G., Copeland T.D., Kaplan D.R., Rapp U.R., Morrison D.K.
Mol. Cell. Biol. 12:3733-3742(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT THR-373.
Tissue: Testis.
[2]Albert S., Wixler L., Rapp U.R.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 31-33.
[3]NIEHS SNPs program
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Liver.
[7]"Chromosomal assignment of two human B-raf(Rmil) proto-oncogene loci: B-raf-1 encoding the p94Braf/Rmil and B-raf-2, a processed pseudogene."
Eychene A., Barnier J.V., Apiou F., Dutrillaux B., Calothy G.
Oncogene 7:1657-1660(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200.
Tissue: Placenta.
[8]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-51; 56-95; 151-158; 189-199; 253-260; 294-354; 361-424; 444-507; 510-522; 559-570; 579-626; 663-680; 692-698; 702-719; 727-735 AND 753-766, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-365; THR-396; SER-399; THR-401 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Hepatoma.
[9]"Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies."
Sithanandam G., Kolch W., Duh F.-M., Rapp U.R.
Oncogene 5:1775-1780(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-766.
Tissue: Testis.
[10]"Tandem duplication producing a novel oncogenic BRAF fusion gene defines the majority of pilocytic astrocytomas."
Jones D.T.W., Kocialkowski S., Liu L., Pearson D.M., Backlund L.M., Ichimura K., Collins V.P.
Cancer Res. 68:8673-8677(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 381-766, DISEASE, CHROMOSOMAL REARRANGEMENT.
Tissue: Brain.
[11]"B-raf, a new member of the raf family, is activated by DNA rearrangement."
Ikawa S., Fukui M., Ueyama Y., Tamaoki N., Yamamoto T., Toyoshima K.
Mol. Cell. Biol. 8:2651-2654(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 439-766.
[12]"Serum- and glucocorticoid-inducible kinase SGK phosphorylates and negatively regulates B-Raf."
Zhang B.H., Tang E.D., Zhu T., Greenberg M.E., Vojtek A.B., Guan K.L.
J. Biol. Chem. 276:31620-31626(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-365 BY SGK1.
[13]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-446; SER-447 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Diacylglycerol kinase eta augments C-Raf activity and B-Raf/C-Raf heterodimerization."
Yasuda S., Kai M., Imai S., Takeishi K., Taketomi A., Toyota M., Kanoh H., Sakane F.
J. Biol. Chem. 284:29559-29570(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH DGKH, PHOSPHORYLATION AT THR-753 BY MAPK1.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"A Raf-induced allosteric transition of KSR stimulates phosphorylation of MEK."
Brennan D.F., Dar A.C., Hertz N.T., Chao W.C., Burlingame A.L., Shokat K.M., Barford D.
Nature 472:366-369(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KSR2, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF LYS-483.
[20]"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: INTERACTION WITH PRMT5, METHYLATION AT ARG-671, CHARACTERIZATION OF VARIANT CRC GLU-600, MUTAGENESIS OF ARG-671.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Ring finger protein 149 is an E3 ubiquitin ligase active on wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF)."
Hong S.W., Jin D.H., Shin J.S., Moon J.H., Na Y.S., Jung K.A., Kim S.M., Kim J.C., Kim K.P., Hong Y.S., Lee J.L., Choi E.K., Lee J.S., Kim T.W.
J. Biol. Chem. 287:24017-24025(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY RNF149.
[23]"Lys63-linked polyubiquitination of BRAF at lysine 578 is required for BRAF-mediated signaling."
An L., Jia W., Yu Y., Zou N., Liang L., Zhao Y., Fan Y., Cheng J., Shi Z., Xu G., Li G., Yang J., Zhang H.
Sci. Rep. 3:2344-2344(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-578, MUTAGENESIS OF LYS-578.
[24]"Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity."
Tsai J., Lee J.T., Wang W., Zhang J., Cho H., Mamo S., Bremer R., Gillette S., Kong J., Haass N.K., Sproesser K., Li L., Smalley K.S., Fong D., Zhu Y.L., Marimuthu A., Nguyen H., Lam B. expand/collapse author list , Liu J., Cheung I., Rice J., Suzuki Y., Luu C., Settachatgul C., Shellooe R., Cantwell J., Kim S.H., Schlessinger J., Zhang K.Y., West B.L., Powell B., Habets G., Zhang C., Ibrahim P.N., Hirth P., Artis D.R., Herlyn M., Bollag G.
Proc. Natl. Acad. Sci. U.S.A. 105:3041-3046(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 444-719 IN COMPLEX WITH INHIBITOR.
[25]"Missense mutations of the BRAF gene in human lung adenocarcinoma."
Naoki K., Chen T.-H., Richards W.G., Sugarbaker D.J., Meyerson M.
Cancer Res. 62:7001-7003(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LNCR VAL-466 AND ARG-597.
[26]"Mutations of the BRAF gene in human cancer."
Davies H., Bignell G.R., Cox C., Stephens P., Edkins S., Clegg S., Teague J., Woffendin H., Garnett M.J., Bottomley W., Davis N., Dicks E., Ewing R., Floyd Y., Gray K., Hall S., Hawes R., Hughes J. expand/collapse author list , Kosmidou V., Menzies A., Mould C., Parker A., Stevens C., Watt S., Hooper S., Wilson R., Jayatilake H., Gusterson B.A., Cooper C., Shipley J., Hargrave D., Pritchard-Jones K., Maitland N., Chenevix-Trench G., Riggins G.J., Bigner D.D., Palmieri G., Cossu A., Flanagan A., Nicholson A., Ho J.W.C., Leung S.Y., Yuen S.T., Weber B.L., Seigler H.F., Darrow T.L., Paterson H., Marais R., Marshall C.J., Wooster R., Stratton M.R., Futreal P.A.
Nature 417:949-954(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CANCER GLU-464; VAL-464; ALA-466; GLU-466; VAL-466; ALA-469; GLU-469; LYS-586; LEU-595; ARG-596; ARG-597; VAL-597; GLU-600 AND ASP-600, CHARACTERIZATION OF VARIANTS CANCER VAL-464; ALA-469; VAL-597 AND GLU-600.
[27]"Tumorigenesis: RAF/RAS oncogenes and mismatch-repair status."
Rajagopalan H., Bardelli A., Lengauer C., Kinzler K.W., Vogelstein B., Velculescu V.E.
Nature 418:934-934(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRC ILE-462; SER-463; GLU-464; GLU-600 AND GLU-601.
[28]"BRAF mutations in non-Hodgkin's lymphoma."
Lee J.W., Yoo N.J., Soung Ark W.S., Kim S.Y., Lee J.H., Park J.Y., Cho Y.G., Kim C.J., Ko Y.H., Kim S.H., Nam S.W., Lee J.Y., Lee S.H.
Br. J. Cancer 89:1958-1960(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NHL ALA-469; ARG-469 AND GLY-594.
[29]"Suppression of BRAF(V599E) in human melanoma abrogates transformation."
Hingorani S.R., Jacobetz M.A., Robertson G.P., Herlyn M., Tuveson D.A.
Cancer Res. 63:5198-5202(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT MELANOMA GLU-600.
[30]"Germline KRAS and BRAF mutations in cardio-facio-cutaneous syndrome."
Niihori T., Aoki Y., Narumi Y., Neri G., Cave H., Verloes A., Okamoto N., Hennekam R.C.M., Gillessen-Kaesbach G., Wieczorek D., Kavamura M.I., Kurosawa K., Ohashi H., Wilson L., Heron D., Bonneau D., Corona G., Kaname T. expand/collapse author list , Naritomi K., Baumann C., Matsumoto N., Kato K., Kure S., Matsubara Y.
Nat. Genet. 38:294-296(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFC1 PRO-246; ARG-257; GLU-469; PHE-485; GLU-499; LYS-501; GLY-501 AND ASP-581.
[31]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-600.
[32]"Germline mutations in genes within the MAPK pathway cause cardio-facio-cutaneous syndrome."
Rodriguez-Viciana P., Tetsu O., Tidyman W.E., Estep A.L., Conger B.A., Cruz M.S., McCormick F., Rauen K.A.
Science 311:1287-1290(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFC1 ARG-257; ALA-467; SER-468; GLU-469; PHE-485; GLU-499; LYS-501; GLY-501; ASP-581; LEU-595 AND VAL-596.
[33]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-301; ALA-469; VAL-469; SER-581; ARG-596; ARG-597; VAL-597; GLU-600; GLU-600 AND GLU-600.
[34]"Mutation and phenotypic spectrum in patients with cardio-facio-cutaneous and Costello syndrome."
Schulz A.L., Albrecht B., Arici C., van der Burgt I., Buske A., Gillessen-Kaesbach G., Heller R., Horn D., Hubner C.A., Korenke G.C., Konig R., Kress W., Kruger G., Meinecke P., Mucke J., Plecko B., Rossier E., Schinzel A. expand/collapse author list , Schulze A., Seemanova E., Seidel H., Spranger S., Tuysuz B., Uhrig S., Wieczorek D., Kutsche K., Zenker M.
Clin. Genet. 73:62-70(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFC1 PRO-241; PRO-244; PRO-246; ARG-257; LYS-262; SER-468; GLU-469; GLU-499; ASN-499; ASP-580; ASP-581 AND LEU-595.
[35]"Germline BRAF mutations in Noonan, LEOPARD, and cardiofaciocutaneous syndromes: molecular diversity and associated phenotypic spectrum."
Sarkozy A., Carta C., Moretti S., Zampino G., Digilio M.C., Pantaleoni F., Scioletti A.P., Esposito G., Cordeddu V., Lepri F., Petrangeli V., Dentici M.L., Mancini G.M., Selicorni A., Rossi C., Mazzanti L., Marino B., Ferrero G.B. expand/collapse author list , Silengo M.C., Memo L., Stanzial F., Faravelli F., Stuppia L., Puxeddu E., Gelb B.D., Dallapiccola B., Tartaglia M.
Hum. Mutat. 30:695-702(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEOPARD3 PRO-241, VARIANTS NS7 CYS-531 AND VAL-597, VARIANTS CFC1 PHE-245; PRO-246; ARG-257; LYS-275; GLU-469; PHE-485; ASN-499; LYS-501; PRO-525; LEU-595; ARG-599; GLN-601; GLU-638 AND ARG-709, VARIANTS ARG-241 AND MET-241.
[36]"Germline mutations affecting the proofreading domains of POLE and POLD1 predispose to colorectal adenomas and carcinomas."
CORGI Consortium, WGS500 Consortium
Palles C., Cazier J.B., Howarth K.M., Domingo E., Jones A.M., Broderick P., Kemp Z., Spain S.L., Guarino Almeida E., Salguero I., Sherborne A., Chubb D., Carvajal-Carmona L.G., Ma Y., Kaur K., Dobbins S., Barclay E., Gorman M. expand/collapse author list , Martin L., Kovac M.B., Humphray S., Lucassen A., Holmes C.C., Bentley D., Donnelly P., Taylor J., Petridis C., Roylance R., Sawyer E.J., Kerr D.J., Clark S., Grimes J., Kearsey S.E., Thomas H.J., McVean G., Houlston R.S., Tomlinson I.
Nat. Genet. 45:136-144(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CRC GLU-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5863.1.
PIRTVHUBF. A57977.
RefSeqNP_004324.2. NM_004333.4.
UniGeneHs.550061.
Hs.600998.
Hs.605380.
Hs.659507.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
4PP7X-ray3.40A/B432-726[»]
ProteinModelPortalP15056.
SMRP15056. Positions 149-283, 448-723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107141. 41 interactions.
DIPDIP-1045N.
IntActP15056. 36 interactions.
MINTMINT-1574728.
STRING9606.ENSP00000288602.

Chemistry

BindingDBP15056.
ChEMBLCHEMBL5145.
DrugBankDB00398. Sorafenib.
GuidetoPHARMACOLOGY1943.

PTM databases

PhosphoSiteP15056.

Polymorphism databases

DMDM50403720.

Proteomic databases

MaxQBP15056.
PaxDbP15056.
PRIDEP15056.

Protocols and materials databases

DNASU673.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288602; ENSP00000288602; ENSG00000157764.
GeneID673.
KEGGhsa:673.
UCSCuc003vwc.4. human.

Organism-specific databases

CTD673.
GeneCardsGC07M140424.
GeneReviewsBRAF.
H-InvDBHIX0167822.
HGNCHGNC:1097. BRAF.
HPACAB004552.
HPA001328.
MIM114500. phenotype.
115150. phenotype.
164757. gene.
211980. phenotype.
605027. phenotype.
613706. phenotype.
613707. phenotype.
neXtProtNX_P15056.
Orphanet1340. Cardiofaciocutaneous syndrome.
54595. Craniopharyngioma.
58017. Hairy cell leukemia.
99872. Hashimoto-Pritzker syndrome.
500. LEOPARD syndrome.
648. Noonan syndrome.
251612. Pilocytic astrocytoma.
PharmGKBPA25408.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG001886.
InParanoidP15056.
KOK04365.
OMAHRTRTSS.
OrthoDBEOG7F5128.
PhylomeDBP15056.
TreeFamTF317006.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_13685. Neuronal System.
SignaLinkP15056.

Gene expression databases

ArrayExpressP15056.
BgeeP15056.
CleanExHS_BRAF.
GenevestigatorP15056.

Family and domain databases

InterProIPR020454. 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]
PfamPF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view]
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Other

ChiTaRSBRAF. human.
EvolutionaryTraceP15056.
GeneWikiBRAF_(gene).
GenomeRNAi673.
NextBio2776.
PMAP-CutDBP15056.
PROP15056.
SOURCESearch...

Entry information

Entry nameBRAF_HUMAN
AccessionPrimary (citable) accession number: P15056
Secondary accession number(s): A4D1T4 expand/collapse secondary AC list , B6HY61, B6HY62, B6HY63, B6HY64, B6HY65, B6HY66, Q13878, Q3MIN6, Q9UDP8, Q9Y6T3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 183 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM