Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XAG

Apo BRAF dimer bound to 14-3-3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0001525	biological_process	angiogenesis
A	0003016	biological_process	respiratory system process
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005925	cellular_component	focal adhesion
A	0006468	biological_process	protein phosphorylation
A	0007165	biological_process	signal transduction
A	0008039	biological_process	synaptic target recognition
A	0008104	biological_process	intracellular protein localization
A	0019901	molecular_function	protein kinase binding
A	0019903	molecular_function	protein phosphatase binding
A	0019904	molecular_function	protein domain specific binding
A	0030324	biological_process	lung development
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0031647	biological_process	regulation of protein stability
A	0031982	cellular_component	vesicle
A	0035148	biological_process	tube formation
A	0042149	biological_process	cellular response to glucose starvation
A	0042470	cellular_component	melanosome
A	0042802	molecular_function	identical protein binding
A	0043066	biological_process	negative regulation of apoptotic process
A	0044325	molecular_function	transmembrane transporter binding
A	0045296	molecular_function	cadherin binding
A	0045824	biological_process	negative regulation of innate immune response
A	0050815	molecular_function	phosphoserine residue binding
A	0051683	biological_process	establishment of Golgi localization
A	0070062	cellular_component	extracellular exosome
A	0070372	biological_process	regulation of ERK1 and ERK2 cascade
A	0072562	cellular_component	blood microparticle
A	0090128	biological_process	regulation of synapse maturation
A	0090168	biological_process	Golgi reassembly
A	0098686	cellular_component	hippocampal mossy fiber to CA3 synapse
A	0098978	cellular_component	glutamatergic synapse
A	0140297	molecular_function	DNA-binding transcription factor binding
A	0140311	molecular_function	protein sequestering activity
A	1900181	biological_process	negative regulation of protein localization to nucleus
A	1904262	biological_process	negative regulation of TORC1 signaling
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0001525	biological_process	angiogenesis
B	0003016	biological_process	respiratory system process
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005925	cellular_component	focal adhesion
B	0006468	biological_process	protein phosphorylation
B	0007165	biological_process	signal transduction
B	0008039	biological_process	synaptic target recognition
B	0008104	biological_process	intracellular protein localization
B	0019901	molecular_function	protein kinase binding
B	0019903	molecular_function	protein phosphatase binding
B	0019904	molecular_function	protein domain specific binding
B	0030324	biological_process	lung development
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0031647	biological_process	regulation of protein stability
B	0031982	cellular_component	vesicle
B	0035148	biological_process	tube formation
B	0042149	biological_process	cellular response to glucose starvation
B	0042470	cellular_component	melanosome
B	0042802	molecular_function	identical protein binding
B	0043066	biological_process	negative regulation of apoptotic process
B	0044325	molecular_function	transmembrane transporter binding
B	0045296	molecular_function	cadherin binding
B	0045824	biological_process	negative regulation of innate immune response
B	0050815	molecular_function	phosphoserine residue binding
B	0051683	biological_process	establishment of Golgi localization
B	0070062	cellular_component	extracellular exosome
B	0070372	biological_process	regulation of ERK1 and ERK2 cascade
B	0072562	cellular_component	blood microparticle
B	0090128	biological_process	regulation of synapse maturation
B	0090168	biological_process	Golgi reassembly
B	0098686	cellular_component	hippocampal mossy fiber to CA3 synapse
B	0098978	cellular_component	glutamatergic synapse
B	0140297	molecular_function	DNA-binding transcription factor binding
B	0140311	molecular_function	protein sequestering activity
B	1900181	biological_process	negative regulation of protein localization to nucleus
B	1904262	biological_process	negative regulation of TORC1 signaling
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue EDO D 801

Chain	Residue
C	ARG506
D	TRP450
D	ARG506

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	21
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK

Chain	Residue	Details
C	ILE463-LYS483

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL

Chain	Residue	Details
C	ILE572-LEU584

site_id	PS00796
Number of Residues	11
Details	1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV

Chain	Residue	Details
A	ARG41-VAL51

site_id	PS00797
Number of Residues	20
Details	1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS

Chain	Residue	Details
A	TYR211-SER230

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Site: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"source":"UniProtKB","id":"P63103","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by MAPK8","evidences":[{"source":"PubMed","id":"15071501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15696159","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63102","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"21917714","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23907581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)