SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P15056

- BRAF_HUMAN

UniProt

P15056 - BRAF_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein kinase B-raf

Gene
BRAF, BRAF1, RAFB1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1 By similarity
Metal bindingi248 – 2481Zinc 2 By similarity
Metal bindingi251 – 2511Zinc 2 By similarity
Metal bindingi261 – 2611Zinc 1 By similarity
Metal bindingi264 – 2641Zinc 1 By similarity
Metal bindingi269 – 2691Zinc 2 By similarity
Metal bindingi272 – 2721Zinc 2 By similarity
Metal bindingi280 – 2801Zinc 1 By similarity
Sitei380 – 3812Breakpoint for translocation to form KIAA1549-BRAF fusion protein
Sitei438 – 4392Breakpoint for translocation to form KIAA1549-BRAF fusion protein
Binding sitei483 – 4831ATP By similarity
Active sitei576 – 5761Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri234 – 28047Phorbol-ester/DAG-typeAdd
BLAST
Nucleotide bindingi463 – 4719ATP By similarity

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: BHF-UCL
  15. response to peptide hormone Source: Ensembl
  16. small GTPase mediated signal transduction Source: Reactome
  17. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.10.2. 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
Complete GO annotation...

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.
Note: The disease may be caused by mutations affecting the gene represented in this entry.4 Publications
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. 7 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.
Note: The gene represented in this entry is involved in disease pathogenesis.2 Publications
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.
Note: The gene represented in this entry is involved in disease pathogenesis.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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)1 Publication
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.
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 KSR2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-365980,EBI-365980
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. 36 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.

Miscellaneous databases

EvolutionaryTraceiP15056.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini155 – 22773RBDAdd
BLAST
Domaini457 – 717261Protein kinaseAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri234 – 28047Phorbol-ester/DAG-typeAdd
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

« Hide

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.

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. 7 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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti766 – 7661H → D in AAA96495. 1 Publication

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. 36 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 Search...

Gene expression databases

ArrayExpressi P15056.
Bgeei P15056.
CleanExi HS_BRAF.
Genevestigatori P15056.

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

« Hide 'large scale' publications
  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.
    , 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.
    , 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."
    Sit