Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8PVU

Cryo-EM structure of DHS-ERK2 complex with 1:1 stoichiometry refined in C1 symmetry

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0008216	biological_process	spermidine metabolic process
A	0008284	biological_process	positive regulation of cell population proliferation
A	0008612	biological_process	peptidyl-lysine modification to peptidyl-hypusine
A	0016740	molecular_function	transferase activity
A	0034038	molecular_function	deoxyhypusine synthase activity
A	0042802	molecular_function	identical protein binding
A	0046203	biological_process	spermidine catabolic process
A	0051604	biological_process	protein maturation
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0008216	biological_process	spermidine metabolic process
B	0008284	biological_process	positive regulation of cell population proliferation
B	0008612	biological_process	peptidyl-lysine modification to peptidyl-hypusine
B	0016740	molecular_function	transferase activity
B	0034038	molecular_function	deoxyhypusine synthase activity
B	0042802	molecular_function	identical protein binding
B	0046203	biological_process	spermidine catabolic process
B	0051604	biological_process	protein maturation
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0008216	biological_process	spermidine metabolic process
C	0008284	biological_process	positive regulation of cell population proliferation
C	0008612	biological_process	peptidyl-lysine modification to peptidyl-hypusine
C	0016740	molecular_function	transferase activity
C	0034038	molecular_function	deoxyhypusine synthase activity
C	0042802	molecular_function	identical protein binding
C	0046203	biological_process	spermidine catabolic process
C	0051604	biological_process	protein maturation
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0008216	biological_process	spermidine metabolic process
D	0008284	biological_process	positive regulation of cell population proliferation
D	0008612	biological_process	peptidyl-lysine modification to peptidyl-hypusine
D	0016740	molecular_function	transferase activity
D	0034038	molecular_function	deoxyhypusine synthase activity
D	0042802	molecular_function	identical protein binding
D	0046203	biological_process	spermidine catabolic process
D	0051604	biological_process	protein maturation
E	0000165	biological_process	MAPK cascade
E	0000166	molecular_function	nucleotide binding
E	0001784	molecular_function	phosphotyrosine residue binding
E	0003677	molecular_function	DNA binding
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0004707	molecular_function	MAP kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005576	cellular_component	extracellular region
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005769	cellular_component	early endosome
E	0005770	cellular_component	late endosome
E	0005788	cellular_component	endoplasmic reticulum lumen
E	0005794	cellular_component	Golgi apparatus
E	0005813	cellular_component	centrosome
E	0005819	cellular_component	spindle
E	0005829	cellular_component	cytosol
E	0005856	cellular_component	cytoskeleton
E	0005886	cellular_component	plasma membrane
E	0005901	cellular_component	caveola
E	0005925	cellular_component	focal adhesion
E	0006351	biological_process	DNA-templated transcription
E	0006357	biological_process	regulation of transcription by RNA polymerase II
E	0006468	biological_process	protein phosphorylation
E	0006915	biological_process	apoptotic process
E	0006935	biological_process	chemotaxis
E	0007165	biological_process	signal transduction
E	0007166	biological_process	cell surface receptor signaling pathway
E	0007173	biological_process	epidermal growth factor receptor signaling pathway
E	0007268	biological_process	chemical synaptic transmission
E	0007611	biological_process	learning or memory
E	0008286	biological_process	insulin receptor signaling pathway
E	0008353	molecular_function	RNA polymerase II CTD heptapeptide repeat kinase activity
E	0010759	biological_process	positive regulation of macrophage chemotaxis
E	0010800	biological_process	positive regulation of peptidyl-threonine phosphorylation
E	0014044	biological_process	Schwann cell development
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0019902	molecular_function	phosphatase binding
E	0031143	cellular_component	pseudopodium
E	0032206	biological_process	positive regulation of telomere maintenance
E	0032872	biological_process	regulation of stress-activated MAPK cascade
E	0034198	biological_process	cellular response to amino acid starvation
E	0035094	biological_process	response to nicotine
E	0035556	biological_process	intracellular signal transduction
E	0035578	cellular_component	azurophil granule lumen
E	0038127	biological_process	ERBB signaling pathway
E	0038133	biological_process	ERBB2-ERBB3 signaling pathway
E	0042552	biological_process	myelination
E	0042802	molecular_function	identical protein binding
E	0045202	cellular_component	synapse
E	0045542	biological_process	positive regulation of cholesterol biosynthetic process
E	0048009	biological_process	insulin-like growth factor receptor signaling pathway
E	0051403	biological_process	stress-activated MAPK cascade
E	0051493	biological_process	regulation of cytoskeleton organization
E	0061514	biological_process	interleukin-34-mediated signaling pathway
E	0070098	biological_process	chemokine-mediated signaling pathway
E	0070371	biological_process	ERK1 and ERK2 cascade
E	0070849	biological_process	response to epidermal growth factor
E	0072584	biological_process	caveolin-mediated endocytosis
E	0072686	cellular_component	mitotic spindle
E	0090170	biological_process	regulation of Golgi inheritance
E	0106310	molecular_function	protein serine kinase activity
E	0120041	biological_process	positive regulation of macrophage proliferation
E	0150078	biological_process	positive regulation of neuroinflammatory response
E	1904813	cellular_component	ficolin-1-rich granule lumen
E	2000641	biological_process	regulation of early endosome to late endosome transport

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGMVCsAydnvnkvrv.........AIKK

Chain	Residue	Details
E	ILE31-LYS55

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

Chain	Residue	Details
E	VAL145-LEU157

site_id	PS01351
Number of Residues	103
Details	MAPK MAP kinase signature. FehqtycqrtlREikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsndhicyflyqilrglkyihsanvlh..........RDlKpsnlllnttC

Chain	Residue	Details
E	PHE59-CYS161

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	DNA binding: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Motif: {"description":"TXY","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Motif: {"description":"Cytoplasmic retention motif","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
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_FI5
Number of Residues	1
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":"19447520","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by MAP2K1 and MAP2K2","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","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":"Phosphotyrosine; by MAP2K1 and MAP2K2","evidences":[{"source":"PubMed","id":"19053285","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19494114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"19060905","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9405486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9493264","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	42
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 687

Chain	Residue	Details
B	GLU137	electrostatic stabiliser
B	HIS288	proton acceptor, proton donor
B	LYS329	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	3
Details	M-CSA 687

Chain	Residue	Details
C	GLU137	electrostatic stabiliser
C	HIS288	proton acceptor, proton donor
C	LYS329	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	3
Details	M-CSA 687

Chain	Residue	Details
D	GLU137	electrostatic stabiliser
D	HIS288	proton acceptor, proton donor
D	LYS329	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	3
Details	M-CSA 687

Chain	Residue	Details
E	LEU137	electrostatic stabiliser
E	ASP288	proton acceptor, proton donor
E	PHE329	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

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