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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7MFF

Dimeric (BRAF)2:(14-3-3)2 complex bound to SB590885 Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004708molecular_functionMAP kinase kinase activity
A0004709molecular_functionMAP kinase kinase kinase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0007173biological_processepidermal growth factor receptor signaling pathway
A0008270molecular_functionzinc ion binding
A0009887biological_processanimal organ morphogenesis
A0010628biological_processpositive regulation of gene expression
A0010828biological_processpositive regulation of D-glucose transmembrane transport
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0031267molecular_functionsmall GTPase binding
A0033138biological_processpositive regulation of peptidyl-serine phosphorylation
A0042802molecular_functionidentical protein binding
A0043005cellular_componentneuron projection
A0043066biological_processnegative regulation of apoptotic process
A0044297cellular_componentcell body
A0046872molecular_functionmetal ion binding
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0071277biological_processcellular response to calcium ion
A0090150biological_processestablishment of protein localization to membrane
A0097110molecular_functionscaffold protein binding
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
A0106310molecular_functionprotein serine kinase activity
B0000165biological_processMAPK cascade
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004708molecular_functionMAP kinase kinase activity
B0004709molecular_functionMAP kinase kinase kinase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006468biological_processprotein phosphorylation
B0007165biological_processsignal transduction
B0007173biological_processepidermal growth factor receptor signaling pathway
B0008270molecular_functionzinc ion binding
B0009887biological_processanimal organ morphogenesis
B0010628biological_processpositive regulation of gene expression
B0010828biological_processpositive regulation of D-glucose transmembrane transport
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0031267molecular_functionsmall GTPase binding
B0033138biological_processpositive regulation of peptidyl-serine phosphorylation
B0042802molecular_functionidentical protein binding
B0043005cellular_componentneuron projection
B0043066biological_processnegative regulation of apoptotic process
B0044297cellular_componentcell body
B0046872molecular_functionmetal ion binding
B0070374biological_processpositive regulation of ERK1 and ERK2 cascade
B0071277biological_processcellular response to calcium ion
B0090150biological_processestablishment of protein localization to membrane
B0097110molecular_functionscaffold protein binding
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099170biological_processpostsynaptic modulation of chemical synaptic transmission
B0106310molecular_functionprotein serine kinase activity
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0001525biological_processangiogenesis
C0003016biological_processrespiratory system process
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005925cellular_componentfocal adhesion
C0006468biological_processprotein phosphorylation
C0007165biological_processsignal transduction
C0008039biological_processsynaptic target recognition
C0008104biological_processintracellular protein localization
C0019901molecular_functionprotein kinase binding
C0019903molecular_functionprotein phosphatase binding
C0019904molecular_functionprotein domain specific binding
C0030324biological_processlung development
C0031625molecular_functionubiquitin protein ligase binding
C0031647biological_processregulation of protein stability
C0031982cellular_componentvesicle
C0035148biological_processtube formation
C0042149biological_processcellular response to glucose starvation
C0042470cellular_componentmelanosome
C0042802molecular_functionidentical protein binding
C0043066biological_processnegative regulation of apoptotic process
C0044325molecular_functiontransmembrane transporter binding
C0045296molecular_functioncadherin binding
C0045824biological_processnegative regulation of innate immune response
C0050815molecular_functionphosphoserine residue binding
C0051683biological_processestablishment of Golgi localization
C0070062cellular_componentextracellular exosome
C0070372biological_processregulation of ERK1 and ERK2 cascade
C0072562cellular_componentblood microparticle
C0090128biological_processregulation of synapse maturation
C0090168biological_processGolgi reassembly
C0098686cellular_componenthippocampal mossy fiber to CA3 synapse
C0098978cellular_componentglutamatergic synapse
C0140297molecular_functionDNA-binding transcription factor binding
C0140311molecular_functionprotein sequestering activity
C1900181biological_processnegative regulation of protein localization to nucleus
C1904262biological_processnegative regulation of TORC1 signaling
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0001525biological_processangiogenesis
D0003016biological_processrespiratory system process
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005925cellular_componentfocal adhesion
D0006468biological_processprotein phosphorylation
D0007165biological_processsignal transduction
D0008039biological_processsynaptic target recognition
D0008104biological_processintracellular protein localization
D0019901molecular_functionprotein kinase binding
D0019903molecular_functionprotein phosphatase binding
D0019904molecular_functionprotein domain specific binding
D0030324biological_processlung development
D0031625molecular_functionubiquitin protein ligase binding
D0031647biological_processregulation of protein stability
D0031982cellular_componentvesicle
D0035148biological_processtube formation
D0042149biological_processcellular response to glucose starvation
D0042470cellular_componentmelanosome
D0042802molecular_functionidentical protein binding
D0043066biological_processnegative regulation of apoptotic process
D0044325molecular_functiontransmembrane transporter binding
D0045296molecular_functioncadherin binding
D0045824biological_processnegative regulation of innate immune response
D0050815molecular_functionphosphoserine residue binding
D0051683biological_processestablishment of Golgi localization
D0070062cellular_componentextracellular exosome
D0070372biological_processregulation of ERK1 and ERK2 cascade
D0072562cellular_componentblood microparticle
D0090128biological_processregulation of synapse maturation
D0090168biological_processGolgi reassembly
D0098686cellular_componenthippocampal mossy fiber to CA3 synapse
D0098978cellular_componentglutamatergic synapse
D0140297molecular_functionDNA-binding transcription factor binding
D0140311molecular_functionprotein sequestering activity
D1900181biological_processnegative regulation of protein localization to nucleus
D1904262biological_processnegative regulation of TORC1 signaling
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
AILE463-LYS483
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL
ChainResidueDetails
AILE572-LEU584
site_idPS00479
Number of Residues46
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HnFvrktfftlaf.CdfCrklLfqgfr.....CqtCgykfHqrCstevplm..C
ChainResidueDetails
AHIS235-CYS280
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
CARG41-VAL51
site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
CTYR211-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 Residues2
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 Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"21917714","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23907581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
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

246333

PDB entries from 2025-12-17

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