Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GPH

Docking motif interactions in the MAP kinase ERK2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000165	biological_process	MAPK cascade
A	0003690	molecular_function	double-stranded DNA binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004707	molecular_function	MAP kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005769	cellular_component	early endosome
A	0005770	cellular_component	late endosome
A	0005794	cellular_component	Golgi apparatus
A	0005813	cellular_component	centrosome
A	0005819	cellular_component	spindle
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0005901	cellular_component	caveola
A	0005925	cellular_component	focal adhesion
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006468	biological_process	protein phosphorylation
A	0007166	biological_process	cell surface receptor signaling pathway
A	0008284	biological_process	positive regulation of cell population proliferation
A	0009636	biological_process	response to toxic substance
A	0014069	cellular_component	postsynaptic density
A	0015966	biological_process	diadenosine tetraphosphate biosynthetic process
A	0016301	molecular_function	kinase activity
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0019233	biological_process	sensory perception of pain
A	0019901	molecular_function	protein kinase binding
A	0030335	biological_process	positive regulation of cell migration
A	0030424	cellular_component	axon
A	0031435	molecular_function	mitogen-activated protein kinase kinase kinase binding
A	0032355	biological_process	response to estradiol
A	0032839	cellular_component	dendrite cytoplasm
A	0032872	biological_process	regulation of stress-activated MAPK cascade
A	0032991	cellular_component	protein-containing complex
A	0033574	biological_process	response to testosterone
A	0035094	biological_process	response to nicotine
A	0035556	biological_process	intracellular signal transduction
A	0036120	biological_process	cellular response to platelet-derived growth factor stimulus
A	0042220	biological_process	response to cocaine
A	0042307	biological_process	positive regulation of protein import into nucleus
A	0042542	biological_process	response to hydrogen peroxide
A	0043204	cellular_component	perikaryon
A	0043627	biological_process	response to estrogen
A	0044849	biological_process	estrous cycle
A	0045727	biological_process	positive regulation of translation
A	0045880	biological_process	positive regulation of smoothened signaling pathway
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0046697	biological_process	decidualization
A	0051493	biological_process	regulation of cytoskeleton organization
A	0060045	biological_process	positive regulation of cardiac muscle cell proliferation
A	0061431	biological_process	cellular response to methionine
A	0070371	biological_process	ERK1 and ERK2 cascade
A	0070849	biological_process	response to epidermal growth factor
A	0071320	biological_process	cellular response to cAMP
A	0071364	biological_process	cellular response to epidermal growth factor stimulus
A	0071375	biological_process	cellular response to peptide hormone stimulus
A	0071380	biological_process	cellular response to prostaglandin E stimulus
A	0071396	biological_process	cellular response to lipid
A	0072584	biological_process	caveolin-mediated endocytosis
A	0072686	cellular_component	mitotic spindle
A	0090170	biological_process	regulation of Golgi inheritance
A	0097237	biological_process	cellular response to toxic substance
A	0097305	biological_process	response to alcohol
A	0106310	molecular_function	protein serine kinase activity
A	1990314	biological_process	cellular response to insulin-like growth factor stimulus
A	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. IGEGAYGMVCsAydnlnkvrv.........AIKK

Chain	Residue	Details
A	ILE29-LYS53

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

Chain	Residue	Details
A	VAL143-LEU155

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

Chain	Residue	Details
A	PHE57-CYS159

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	288
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	2
Details	Motif: {"description":"TXY"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8639522","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by SGK1","evidences":[{"source":"UniProtKB","id":"P28482","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"P28482","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P28482","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	13
Details	Region: {"description":"Interaction with MAP kinases"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"10559944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14613483","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	SER151
A	ASP147

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS149
A	ASP147

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS149
A	ASP147
A	THR188

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASN152
A	LYS149
A	ASP147

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