Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8DGS

Cryo-EM structure of a RAS/RAF complex (state 1)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000165	biological_process	MAPK cascade
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004708	molecular_function	MAP kinase kinase activity
A	0004709	molecular_function	MAP kinase kinase kinase activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006468	biological_process	protein phosphorylation
A	0007165	biological_process	signal transduction
A	0007173	biological_process	epidermal growth factor receptor signaling pathway
A	0008270	molecular_function	zinc ion binding
A	0009887	biological_process	animal organ morphogenesis
A	0010628	biological_process	positive regulation of gene expression
A	0010828	biological_process	positive regulation of D-glucose transmembrane transport
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0031267	molecular_function	small GTPase binding
A	0033138	biological_process	positive regulation of peptidyl-serine phosphorylation
A	0042802	molecular_function	identical protein binding
A	0043005	cellular_component	neuron projection
A	0043066	biological_process	negative regulation of apoptotic process
A	0044297	cellular_component	cell body
A	0046872	molecular_function	metal ion binding
A	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
A	0071277	biological_process	cellular response to calcium ion
A	0090150	biological_process	establishment of protein localization to membrane
A	0097110	molecular_function	scaffold protein binding
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
A	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
A	0106310	molecular_function	protein serine kinase activity
B	0000165	biological_process	MAPK cascade
B	0000166	molecular_function	nucleotide binding
B	0000187	biological_process	obsolete activation of MAPK activity
B	0003056	biological_process	regulation of vascular associated smooth muscle contraction
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004708	molecular_function	MAP kinase kinase activity
B	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005078	molecular_function	MAP-kinase scaffold activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005769	cellular_component	early endosome
B	0005770	cellular_component	late endosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005794	cellular_component	Golgi apparatus
B	0005813	cellular_component	centrosome
B	0005829	cellular_component	cytosol
B	0005874	cellular_component	microtubule
B	0005886	cellular_component	plasma membrane
B	0005925	cellular_component	focal adhesion
B	0005938	cellular_component	cell cortex
B	0006468	biological_process	protein phosphorylation
B	0006935	biological_process	chemotaxis
B	0006979	biological_process	response to oxidative stress
B	0007165	biological_process	signal transduction
B	0007528	biological_process	neuromuscular junction development
B	0008285	biological_process	negative regulation of cell population proliferation
B	0010508	biological_process	positive regulation of autophagy
B	0010628	biological_process	positive regulation of gene expression
B	0010629	biological_process	negative regulation of gene expression
B	0014044	biological_process	Schwann cell development
B	0014069	cellular_component	postsynaptic density
B	0016020	cellular_component	membrane
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0019901	molecular_function	protein kinase binding
B	0030182	biological_process	neuron differentiation
B	0030295	molecular_function	protein kinase activator activity
B	0030335	biological_process	positive regulation of cell migration
B	0030424	cellular_component	axon
B	0030425	cellular_component	dendrite
B	0031267	molecular_function	small GTPase binding
B	0031435	molecular_function	mitogen-activated protein kinase kinase kinase binding
B	0032402	biological_process	melanosome transport
B	0032839	cellular_component	dendrite cytoplasm
B	0032872	biological_process	regulation of stress-activated MAPK cascade
B	0032968	biological_process	positive regulation of transcription elongation by RNA polymerase II
B	0034111	biological_process	negative regulation of homotypic cell-cell adhesion
B	0036064	cellular_component	ciliary basal body
B	0038127	biological_process	ERBB signaling pathway
B	0038133	biological_process	ERBB2-ERBB3 signaling pathway
B	0042552	biological_process	myelination
B	0043204	cellular_component	perikaryon
B	0043410	biological_process	positive regulation of MAPK cascade
B	0043539	molecular_function	protein serine/threonine kinase activator activity
B	0044877	molecular_function	protein-containing complex binding
B	0045893	biological_process	positive regulation of DNA-templated transcription
B	0045933	biological_process	positive regulation of muscle contraction
B	0047496	biological_process	vesicle transport along microtubule
B	0048009	biological_process	insulin-like growth factor receptor signaling pathway
B	0048313	biological_process	Golgi inheritance
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0048678	biological_process	response to axon injury
B	0048812	biological_process	neuron projection morphogenesis
B	0051384	biological_process	response to glucocorticoid
B	0070328	biological_process	triglyceride homeostasis
B	0070371	biological_process	ERK1 and ERK2 cascade
B	0070372	biological_process	regulation of ERK1 and ERK2 cascade
B	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
B	0071902	biological_process	positive regulation of protein serine/threonine kinase activity
B	0090170	biological_process	regulation of Golgi inheritance
B	0090398	biological_process	cellular senescence
B	0097110	molecular_function	scaffold protein binding
B	0098696	biological_process	regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
B	0098978	cellular_component	glutamatergic synapse
B	0106310	molecular_function	protein serine kinase activity
B	1903298	biological_process	negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
B	2000641	biological_process	regulation of early endosome to late endosome transport
B	2001171	biological_process	positive regulation of ATP biosynthetic process
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
E	0007165	biological_process	signal transduction
E	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK

Chain	Residue	Details
B	LEU74-LYS97
A	ILE463-LYS483

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

Chain	Residue	Details
B	ILE186-VAL198
A	ILE572-LEU584

site_id	PS00479
Number of Residues	46
Details	ZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HnFvrktfftlaf.CdfCrklLfqgfr.....CqtCgykfHqrCstevplm..C

Chain	Residue	Details
A	HIS235-CYS280

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

Chain	Residue	Details
C	ARG41-VAL51

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

Chain	Residue	Details
C	TYR211-SER230

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	260
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	46
Details	Zinc finger: {"description":"Phorbol-ester/DAG-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00226","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
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_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"21917714","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
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_FI11
Number of Residues	2
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

site_id	SWS_FT_FI12
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15543157","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17880056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18951019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19019675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19706763","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21310613","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19161339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EQH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19161339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EQF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by BRAF and RAF1","evidences":[{"source":"PubMed","id":"10409742","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20956560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29433126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8131746","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by BRAF and RAF1","evidences":[{"source":"PubMed","id":"20956560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29433126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8131746","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	8
Details	Motif: {"description":"Effector region"}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22431598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22566140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34380736","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine; in GTPase KRas; alternate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"N-acetylthreonine; in GTPase KRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	1
Details	Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)