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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8VYV

Cryo-EM Structure of the BRAF K601E monomer

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0001525biological_processangiogenesis
A0003016biological_processrespiratory system process
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0008039biological_processsynaptic target recognition
A0008104biological_processintracellular protein localization
A0019901molecular_functionprotein kinase binding
A0019903molecular_functionprotein phosphatase binding
A0019904molecular_functionprotein domain specific binding
A0030324biological_processlung development
A0031625molecular_functionubiquitin protein ligase binding
A0031647biological_processregulation of protein stability
A0031982cellular_componentvesicle
A0035148biological_processtube formation
A0042149biological_processcellular response to glucose starvation
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0043066biological_processnegative regulation of apoptotic process
A0044325molecular_functiontransmembrane transporter binding
A0045296molecular_functioncadherin binding
A0045824biological_processnegative regulation of innate immune response
A0050815molecular_functionphosphoserine residue binding
A0051683biological_processestablishment of Golgi localization
A0070062cellular_componentextracellular exosome
A0070372biological_processregulation of ERK1 and ERK2 cascade
A0072562cellular_componentblood microparticle
A0090128biological_processregulation of synapse maturation
A0090168biological_processGolgi reassembly
A0098686cellular_componenthippocampal mossy fiber to CA3 synapse
A0098978cellular_componentglutamatergic synapse
A0140297molecular_functionDNA-binding transcription factor binding
A0140311molecular_functionprotein sequestering activity
A1900181biological_processnegative regulation of protein localization to nucleus
A1904262biological_processnegative regulation of TORC1 signaling
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0001525biological_processangiogenesis
B0003016biological_processrespiratory system process
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006468biological_processprotein phosphorylation
B0007165biological_processsignal transduction
B0008039biological_processsynaptic target recognition
B0008104biological_processintracellular protein localization
B0019901molecular_functionprotein kinase binding
B0019903molecular_functionprotein phosphatase binding
B0019904molecular_functionprotein domain specific binding
B0030324biological_processlung development
B0031625molecular_functionubiquitin protein ligase binding
B0031647biological_processregulation of protein stability
B0031982cellular_componentvesicle
B0035148biological_processtube formation
B0042149biological_processcellular response to glucose starvation
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0043066biological_processnegative regulation of apoptotic process
B0044325molecular_functiontransmembrane transporter binding
B0045296molecular_functioncadherin binding
B0045824biological_processnegative regulation of innate immune response
B0050815molecular_functionphosphoserine residue binding
B0051683biological_processestablishment of Golgi localization
B0070062cellular_componentextracellular exosome
B0070372biological_processregulation of ERK1 and ERK2 cascade
B0072562cellular_componentblood microparticle
B0090128biological_processregulation of synapse maturation
B0090168biological_processGolgi reassembly
B0098686cellular_componenthippocampal mossy fiber to CA3 synapse
B0098978cellular_componentglutamatergic synapse
B0140297molecular_functionDNA-binding transcription factor binding
B0140311molecular_functionprotein sequestering activity
B1900181biological_processnegative regulation of protein localization to nucleus
B1904262biological_processnegative regulation of TORC1 signaling
C0000165biological_processMAPK cascade
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004708molecular_functionMAP kinase kinase activity
C0004709molecular_functionMAP kinase kinase kinase activity
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006468biological_processprotein phosphorylation
C0007165biological_processsignal transduction
C0007173biological_processepidermal growth factor receptor signaling pathway
C0008270molecular_functionzinc ion binding
C0009887biological_processanimal organ morphogenesis
C0010628biological_processpositive regulation of gene expression
C0010828biological_processpositive regulation of D-glucose transmembrane transport
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0031267molecular_functionsmall GTPase binding
C0033138biological_processpositive regulation of peptidyl-serine phosphorylation
C0042802molecular_functionidentical protein binding
C0043005cellular_componentneuron projection
C0043066biological_processnegative regulation of apoptotic process
C0044297cellular_componentcell body
C0046872molecular_functionmetal ion binding
C0070374biological_processpositive regulation of ERK1 and ERK2 cascade
C0071277biological_processcellular response to calcium ion
C0090150biological_processestablishment of protein localization to membrane
C0097110molecular_functionscaffold protein binding
C0098794cellular_componentpostsynapse
C0098978cellular_componentglutamatergic synapse
C0099170biological_processpostsynaptic modulation of chemical synaptic transmission
C0106310molecular_functionprotein serine kinase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
CILE829-LYS849
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL
ChainResidueDetails
CILE938-LEU950
site_idPS00479
Number of Residues46
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HnFvrktfftlaf.CdfCrklLfqgfr.....CqtCgykfHqrCstevplm..C
ChainResidueDetails
CHIS235-CYS280
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG41-VAL51
site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR211-SER230
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"source":"UniProtKB","id":"P63103","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKA and PKB/AKT1","evidences":[{"source":"PubMed","id":"11956222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12865427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15883165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16376338","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by MAPK8","evidences":[{"source":"PubMed","id":"15071501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15696159","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63102","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Potts A.","Barblan J.","Claeys D.","Quadroni M."]}},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by SGK1","evidences":[{"source":"PubMed","id":"11410590","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23907581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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