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Protein

Serine/threonine-protein kinase B-raf

Gene

BRAF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

Activity is increased by EGF and HGF.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi235Zinc 1By similarity1
Metal bindingi248Zinc 2By similarity1
Metal bindingi251Zinc 2By similarity1
Metal bindingi261Zinc 1By similarity1
Metal bindingi264Zinc 1By similarity1
Metal bindingi269Zinc 2By similarity1
Metal bindingi272Zinc 2By similarity1
Metal bindingi280Zinc 1By similarity1
Binding sitei483ATPPROSITE-ProRule annotation1
Active sitei576Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri234 – 280Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST47
Nucleotide bindingi463 – 471ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • MAP kinase kinase kinase activity Source: Ensembl
  • protein kinase activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

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

BioCyciZFISH:HS08238-MONOMER.
BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-170968. Frs2-mediated activation.
R-HSA-170984. ARMS-mediated activation.
R-HSA-187706. Signalling to p38 via RIT and RIN.
R-HSA-442742. CREB phosphorylation through the activation of Ras.
R-HSA-5673000. RAF activation.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5674499. Negative feedback regulation of MAPK pathway.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SignaLinkiP15056.
SIGNORiP15056.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:1097. BRAF.

Subcellular locationi

GO - Cellular componenti

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.

Colorectal cancer (CRC)3 Publications
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:114500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018613462R → I in CRC. 1 PublicationCorresponds to variant rs180177032dbSNPEnsembl.1
Natural variantiVAR_018614463I → S in CRC. 1 PublicationCorresponds to variant rs180177033dbSNPEnsembl.1
Natural variantiVAR_018615464G → E in CRC. 2 PublicationsCorresponds to variant rs121913348dbSNPEnsembl.1
Natural variantiVAR_018629600V → 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. 8 PublicationsCorresponds to variant rs113488022dbSNPEnsembl.1
Natural variantiVAR_018630601K → E in CRC. 1 PublicationCorresponds to variant rs121913364dbSNPEnsembl.1
Lung cancer (LNCR)1 Publication
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA 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.
See also OMIM:211980
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018512466G → V in LNCR. 2 PublicationsCorresponds to variant rs121913351dbSNPEnsembl.1
Natural variantiVAR_018513597L → R in LNCR; also found in an ovarian serous carcinoma sample; somatic mutation. 3 PublicationsCorresponds to variant rs121913366dbSNPEnsembl.1
Familial non-Hodgkin lymphoma (NHL)1 Publication
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionCancer 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.
See also OMIM:605027
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018620469G → A in NHL; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. 3 PublicationsCorresponds to variant rs121913355dbSNPEnsembl.1
Natural variantiVAR_018622469G → R in NHL. 1 PublicationCorresponds to variant rs121913357dbSNPEnsembl.1
Natural variantiVAR_018624594D → G in NHL. 1 PublicationCorresponds to variant rs121913338dbSNPEnsembl.1
Cardiofaciocutaneous syndrome 1 (CFC1)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:115150
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058621241T → P in CFC1 and LPRD3. 2 PublicationsCorresponds to variant rs387906661dbSNPEnsembl.1
Natural variantiVAR_065171244T → P in CFC1. 1 PublicationCorresponds to variant rs397507465dbSNPEnsembl.1
Natural variantiVAR_058623245L → F in CFC1. 1 PublicationCorresponds to variant rs397507466dbSNPEnsembl.1
Natural variantiVAR_026113246A → P in CFC1. 3 PublicationsCorresponds to variant rs180177034dbSNPEnsembl.1
Natural variantiVAR_026114257Q → R in CFC1. 4 PublicationsCorresponds to variant rs180177035dbSNPEnsembl.1
Natural variantiVAR_065172262Q → K in CFC1. 1 PublicationCorresponds to variant rs397507470dbSNPEnsembl.1
Natural variantiVAR_058624275E → K in CFC1. 1 Publication1
Natural variantiVAR_035096467S → A in CFC1. 1 Publication1
Natural variantiVAR_035097468F → S in CFC1. 2 PublicationsCorresponds to variant rs397507473dbSNPEnsembl.1
Natural variantiVAR_018621469G → E in CFC1 and colon cancer. 5 PublicationsCorresponds to variant rs121913355dbSNPEnsembl.1
Natural variantiVAR_026115485L → F in CFC1. 3 PublicationsCorresponds to variant rs180177036dbSNPEnsembl.1
Natural variantiVAR_026116499K → E in CFC1. 3 PublicationsCorresponds to variant rs180177037dbSNPEnsembl.1
Natural variantiVAR_058625499K → N in CFC1. 2 PublicationsCorresponds to variant rs397507476dbSNPEnsembl.1
Natural variantiVAR_026117501E → G in CFC1. 2 PublicationsCorresponds to variant rs180177039dbSNPEnsembl.1
Natural variantiVAR_026118501E → K in CFC1. 3 PublicationsCorresponds to variant rs180177038dbSNPEnsembl.1
Natural variantiVAR_058626525L → P in CFC1. 1 Publication1
Natural variantiVAR_065173580N → D in CFC1. 1 Publication1
Natural variantiVAR_026119581N → D in CFC1. 3 PublicationsCorresponds to variant rs180177040dbSNPEnsembl.1
Natural variantiVAR_018625595F → L in colon cancer and CFC1. 4 PublicationsCorresponds to variant rs121913341dbSNPEnsembl.1
Natural variantiVAR_035098596G → V in CFC1. 1 PublicationCorresponds to variant rs397507483dbSNPEnsembl.1
Natural variantiVAR_058628599T → R in CFC1. 1 Publication1
Natural variantiVAR_058629601K → Q in CFC1. 1 PublicationCorresponds to variant rs121913364dbSNPEnsembl.1
Natural variantiVAR_058630638D → E in CFC1. 1 PublicationCorresponds to variant rs180177042dbSNPEnsembl.1
Natural variantiVAR_058631709Q → R in CFC1. 1 PublicationCorresponds to variant rs397507486dbSNPEnsembl.1
Noonan syndrome 7 (NS7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613706
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058627531W → C in NS7. 1 PublicationCorresponds to variant rs606231228dbSNPEnsembl.1
Natural variantiVAR_018627597L → V in NS7; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. 3 PublicationsCorresponds to variant rs121913369dbSNPEnsembl.1
LEOPARD syndrome 3 (LPRD3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness.
See also OMIM:613707
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058621241T → P in CFC1 and LPRD3. 2 PublicationsCorresponds to variant rs387906661dbSNPEnsembl.1

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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi483K → S: Reduces kinase activity with MAP2K1. 1 Publication1
Mutagenesisi578K → R: Blocks EGF-induced ubiquitination and ERK activation. 1 Publication1
Mutagenesisi671R → K: Increased kinase activity and stability in response to EGF treatment. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei380 – 381Breakpoint for translocation to form KIAA1549-BRAF fusion protein2
Sitei438 – 439Breakpoint for translocation to form KIAA1549-BRAF fusion protein2

Keywords - Diseasei

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

Organism-specific databases

DisGeNETi673.
MalaCardsiBRAF.
MIMi114500. phenotype.
115150. phenotype.
211980. phenotype.
605027. phenotype.
613706. phenotype.
613707. phenotype.
OpenTargetsiENSG00000157764.
Orphaneti1340. Cardiofaciocutaneous syndrome.
54595. Craniopharyngioma.
58017. Hairy cell leukemia.
99872. Hashimoto-Pritzker syndrome.
500. LEOPARD syndrome.
648. Noonan syndrome.
251612. Pilocytic astrocytoma.
PharmGKBiPA25408.

Chemistry databases

ChEMBLiCHEMBL5145.
DrugBankiDB08912. Dabrafenib.
DB08896. Regorafenib.
DB00398. Sorafenib.
DB08881. Vemurafenib.
GuidetoPHARMACOLOGYi1943.

Polymorphism and mutation databases

BioMutaiBRAF.
DMDMi50403720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000856652 – 766Serine/threonine-protein kinase B-rafAdd BLAST765

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei151PhosphoserineCombined sources1
Modified residuei333PhosphoserineBy similarity1
Modified residuei365Phosphoserine; by SGK1Combined sources2 Publications1
Modified residuei373Phosphothreonine; by autocatalysis1 Publication1
Modified residuei396Phosphothreonine1 Publication1
Modified residuei399Phosphoserine1 Publication1
Modified residuei401PhosphothreonineCombined sources1 Publication1
Modified residuei446PhosphoserineCombined sources1
Modified residuei447PhosphoserineCombined sources1
Cross-linki578Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei671Omega-N-methylarginine; by PRMT51 Publication1
Modified residuei729PhosphoserineCombined sources1 Publication1
Modified residuei750PhosphoserineBy similarity1
Modified residuei753Phosphothreonine; by MAPK11 Publication1

Post-translational modificationi

Phosphorylation at Ser-365 by SGK1 inhibits its activity.4 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

EPDiP15056.
MaxQBiP15056.
PaxDbiP15056.
PeptideAtlasiP15056.
PRIDEiP15056.

PTM databases

iPTMnetiP15056.
PhosphoSitePlusiP15056.

Miscellaneous databases

PMAP-CutDBP15056.

Expressioni

Tissue specificityi

Brain and testis.

Gene expression databases

BgeeiENSG00000157764.
CleanExiHS_BRAF.
ExpressionAtlasiP15056. baseline and differential.
GenevisibleiP15056. HS.

Organism-specific databases

HPAiCAB004552.
HPA001328.
HPA071048.

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 (PubMed:19710016). Interacts with PRMT5 (PubMed:21917714). Interacts with KSR2 (PubMed:21441910). Interacts with AKAP13, MAP2K1 and KSR1. Identified in a complex with AKAP13, MAP2K1 and KSR1 (PubMed:21102438). Interacts with FNIP1 and FNIP2 (PubMed:27353360).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-365980,EBI-365980
ARAFP103982EBI-365980,EBI-365961
HSP90AB1P082382EBI-365980,EBI-352572
Ksr1Q610973EBI-365980,EBI-1536336From a different organism.
MAP2K1Q0275054EBI-365980,EBI-492564
MAP2K2P365076EBI-365980,EBI-1056930
MAP3K1Q132332EBI-365980,EBI-49776
RAF1P0404946EBI-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
YWHAZP631044EBI-365980,EBI-347088

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi107141. 51 interactors.
DIPiDIP-1045N.
IntActiP15056. 45 interactors.
MINTiMINT-1574728.
STRINGi9606.ENSP00000288602.

Chemistry databases

BindingDBiP15056.

Structurei

Secondary structure

1766
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi156 – 161Combined sources6
Turni162 – 164Combined sources3
Beta strandi165 – 170Combined sources6
Helixi177 – 186Combined sources10
Turni187 – 189Combined sources3
Helixi192 – 194Combined sources3
Beta strandi195 – 199Combined sources5
Beta strandi206 – 208Combined sources3
Helixi214 – 217Combined sources4
Beta strandi221 – 226Combined sources6
Helixi448 – 450Combined sources3
Helixi454 – 456Combined sources3
Beta strandi458 – 466Combined sources9
Beta strandi469 – 486Combined sources18
Beta strandi487 – 489Combined sources3
Helixi492 – 506Combined sources15
Beta strandi516 – 520Combined sources5
Beta strandi522 – 524Combined sources3
Beta strandi526 – 530Combined sources5
Beta strandi534 – 536Combined sources3
Helixi537 – 542Combined sources6
Beta strandi543 – 545Combined sources3
Helixi550 – 569Combined sources20
Helixi579 – 581Combined sources3
Beta strandi582 – 585Combined sources4
Turni586 – 588Combined sources3
Beta strandi589 – 592Combined sources4
Turni598 – 600Combined sources3
Turni602 – 605Combined sources4
Helixi611 – 613Combined sources3
Turni614 – 616Combined sources3
Helixi617 – 619Combined sources3
Helixi622 – 625Combined sources4
Turni626 – 629Combined sources4
Helixi635 – 651Combined sources17
Turni655 – 659Combined sources5
Helixi662 – 670Combined sources9
Helixi678 – 680Combined sources3
Beta strandi683 – 685Combined sources3
Helixi687 – 696Combined sources10
Helixi701 – 703Combined sources3
Helixi707 – 717Combined sources11
Turni718 – 720Combined sources3
Helixi723 – 726Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/B448-720[»]
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[»]
4CQEX-ray2.30A/B448-723[»]
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[»]
4R5YX-ray3.50A/B444-723[»]
4RZVX-ray2.99A/B443-723[»]
4RZWX-ray3.49A/B443-723[»]
4WO5X-ray2.83A/B444-723[»]
4XV1X-ray2.47A/B444-705[»]
4XV2X-ray2.50A/B444-705[»]
4XV3X-ray2.80A/B444-705[»]
4XV9X-ray2.00A442-705[»]
4YHTX-ray3.05A/B449-720[»]
5C9CX-ray2.70A/B432-726[»]
5CSWX-ray2.66A/B442-721[»]
5CSXX-ray2.51A442-721[»]
5CT7X-ray3.17A/B445-723[»]
5FD2X-ray2.89A/B433-726[»]
5HI2X-ray2.51A444-737[»]
5HIDX-ray2.50A/B444-737[»]
5HIEX-ray3.00A/B/C/D432-726[»]
5ITAX-ray1.95A/B448-723[»]
5J17NMR-A151-232[»]
5J18NMR-A151-232[»]
5J2RNMR-A151-232[»]
5JRQX-ray2.29A/B448-723[»]
5JSMX-ray2.19A/B/C/D448-723[»]
5JT2X-ray2.70A/B/C/D448-723[»]
ProteinModelPortaliP15056.
SMRiP15056.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15056.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini155 – 227RBDPROSITE-ProRule annotationAdd BLAST73
Domaini457 – 717Protein kinasePROSITE-ProRule annotationAdd BLAST261

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi6 – 11Poly-Gly6
Compositional biasi122 – 129Poly-Ser8
Compositional biasi428 – 432Poly-Ser5

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)DescriptionActionsGraphical viewLength
Zinc fingeri234 – 280Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0193. Eukaryota.
ENOG410Y4UP. LUCA.
GeneTreeiENSGT00760000118807.
HOVERGENiHBG001886.
InParanoidiP15056.
KOiK04365.
OMAiCQQRERK.
OrthoDBiEOG091G09SB.
PhylomeDBiP15056.
TreeFamiTF317006.

Family and domain databases

CDDicd00029. C1. 1 hit.
InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. RBD_dom.
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.
SM00220. S_TKc. 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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        10         20         30         40         50
MAALSGGGGG GAEPGQALFN GDMEPEAGAG AGAAASSAAD PAIPEEVWNI
60 70 80 90 100
KQMIKLTQEH IEALLDKFGG EHNPPSIYLE AYEEYTSKLD ALQQREQQLL
110 120 130 140 150
ESLGNGTDFS VSSSASMDTV TSSSSSSLSV LPSSLSVFQN PTDVARSNPK
160 170 180 190 200
SPQKPIVRVF LPNKQRTVVP ARCGVTVRDS LKKALMMRGL IPECCAVYRI
210 220 230 240 250
QDGEKKPIGW DTDISWLTGE ELHVEVLENV PLTTHNFVRK TFFTLAFCDF
260 270 280 290 300
CRKLLFQGFR CQTCGYKFHQ RCSTEVPLMC VNYDQLDLLF VSKFFEHHPI
310 320 330 340 350
PQEEASLAET ALTSGSSPSA PASDSIGPQI LTSPSPSKSI PIPQPFRPAD
360 370 380 390 400
EDHRNQFGQR DRSSSAPNVH INTIEPVNID DLIRDQGFRG DGGSTTGLSA
410 420 430 440 450
TPPASLPGSL TNVKALQKSP GPQRERKSSS SSEDRNRMKT LGRRDSSDDW
460 470 480 490 500
EIPDGQITVG QRIGSGSFGT VYKGKWHGDV AVKMLNVTAP TPQQLQAFKN
510 520 530 540 550
EVGVLRKTRH VNILLFMGYS TKPQLAIVTQ WCEGSSLYHH LHIIETKFEM
560 570 580 590 600
IKLIDIARQT AQGMDYLHAK SIIHRDLKSN NIFLHEDLTV KIGDFGLATV
610 620 630 640 650
KSRWSGSHQF EQLSGSILWM APEVIRMQDK NPYSFQSDVY AFGIVLYELM
660 670 680 690 700
TGQLPYSNIN NRDQIIFMVG RGYLSPDLSK VRSNCPKAMK RLMAECLKKK
710 720 730 740 750
RDERPLFPQI LASIELLARS LPKIHRSASE PSLNRAGFQT EDFSLYACAS
760
PKTPIQAGGY GAFPVH
Length:766
Mass (Da):84,437
Last modified:July 19, 2004 - v4
Checksum:i0798C2AAB487E813
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti766H → D in AAA96495 (PubMed:3043188).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058620241T → M in a patient with Noonan syndrome. 1 PublicationCorresponds to variant rs387906660dbSNPEnsembl.1
Natural variantiVAR_058621241T → P in CFC1 and LPRD3. 2 PublicationsCorresponds to variant rs387906661dbSNPEnsembl.1
Natural variantiVAR_058622241T → R in a patient with Noonan syndrome. 1 PublicationCorresponds to variant rs387906660dbSNPEnsembl.1
Natural variantiVAR_065171244T → P in CFC1. 1 PublicationCorresponds to variant rs397507465dbSNPEnsembl.1
Natural variantiVAR_058623245L → F in CFC1. 1 PublicationCorresponds to variant rs397507466dbSNPEnsembl.1
Natural variantiVAR_026113246A → P in CFC1. 3 PublicationsCorresponds to variant rs180177034dbSNPEnsembl.1
Natural variantiVAR_026114257Q → R in CFC1. 4 PublicationsCorresponds to variant rs180177035dbSNPEnsembl.1
Natural variantiVAR_065172262Q → K in CFC1. 1 PublicationCorresponds to variant rs397507470dbSNPEnsembl.1
Natural variantiVAR_058624275E → K in CFC1. 1 Publication1
Natural variantiVAR_040391301P → S.1 PublicationCorresponds to variant rs34776339dbSNPEnsembl.1
Natural variantiVAR_018613462R → I in CRC. 1 PublicationCorresponds to variant rs180177032dbSNPEnsembl.1
Natural variantiVAR_018614463I → S in CRC. 1 PublicationCorresponds to variant rs180177033dbSNPEnsembl.1
Natural variantiVAR_018615464G → E in CRC. 2 PublicationsCorresponds to variant rs121913348dbSNPEnsembl.1
Natural variantiVAR_018616464G → V in a colorectal cancer cell line; elevated kinase activity; efficiently induces cell transformation. 1 PublicationCorresponds to variant rs121913348dbSNPEnsembl.1
Natural variantiVAR_018617466G → A in melanoma. 1 PublicationCorresponds to variant rs121913351dbSNPEnsembl.1
Natural variantiVAR_018618466G → E in melanoma. 1 PublicationCorresponds to variant rs121913351dbSNPEnsembl.1
Natural variantiVAR_018512466G → V in LNCR. 2 PublicationsCorresponds to variant rs121913351dbSNPEnsembl.1
Natural variantiVAR_035096467S → A in CFC1. 1 Publication1
Natural variantiVAR_035097468F → S in CFC1. 2 PublicationsCorresponds to variant rs397507473dbSNPEnsembl.1
Natural variantiVAR_018620469G → A in NHL; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation. 3 PublicationsCorresponds to variant rs121913355dbSNPEnsembl.1
Natural variantiVAR_018621469G → E in CFC1 and colon cancer. 5 PublicationsCorresponds to variant rs121913355dbSNPEnsembl.1
Natural variantiVAR_018622469G → R in NHL. 1 PublicationCorresponds to variant rs121913357dbSNPEnsembl.1
Natural variantiVAR_040392469G → V in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs121913355dbSNPEnsembl.1
Natural variantiVAR_026115485L → F in CFC1. 3 PublicationsCorresponds to variant rs180177036dbSNPEnsembl.1
Natural variantiVAR_026116499K → E in CFC1. 3 PublicationsCorresponds to variant rs180177037dbSNPEnsembl.1
Natural variantiVAR_058625499K → N in CFC1. 2 PublicationsCorresponds to variant rs397507476dbSNPEnsembl.1
Natural variantiVAR_026117501E → G in CFC1. 2 PublicationsCorresponds to variant rs180177039dbSNPEnsembl.1
Natural variantiVAR_026118501E → K in CFC1. 3 PublicationsCorresponds to variant rs180177038dbSNPEnsembl.1
Natural variantiVAR_058626525L → P in CFC1. 1 Publication1
Natural variantiVAR_058627531W → C in NS7. 1 PublicationCorresponds to variant rs606231228dbSNPEnsembl.1
Natural variantiVAR_065173580N → D in CFC1. 1 Publication1
Natural variantiVAR_026119581N → D in CFC1. 3 PublicationsCorresponds to variant rs180177040dbSNPEnsembl.1
Natural variantiVAR_040393581N → S in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs121913370dbSNPEnsembl.1
Natural variantiVAR_018623586E → K in ovarian cancer. 1 PublicationCorresponds to variant rs121913340dbSNPEnsembl.1
Natural variantiVAR_018624594D → G in NHL. 1 PublicationCorresponds to variant rs121913338dbSNPEnsembl.1
Natural variantiVAR_018625595F → L in colon cancer and CFC1. 4 PublicationsCorresponds to variant rs121913341dbSNPEnsembl.1
Natural variantiVAR_018626596G → R in a colorectal adenocarcinoma sample; somatic mutation. 2 PublicationsCorresponds to variant rs121913361dbSNPEnsembl.1