6G54

Crystal structure of ERK2 covalently bound to SM1-71

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000165	biological_process	MAPK cascade
A	0000166	molecular_function	nucleotide binding
A	0001784	molecular_function	phosphotyrosine residue binding
A	0003677	molecular_function	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	0005576	cellular_component	extracellular region
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	0005788	cellular_component	endoplasmic reticulum lumen
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	0005929	cellular_component	cilium
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006468	biological_process	protein phosphorylation
A	0006915	biological_process	apoptotic process
A	0006935	biological_process	chemotaxis
A	0006974	biological_process	DNA damage response
A	0007165	biological_process	signal transduction
A	0007166	biological_process	cell surface receptor signaling pathway
A	0007173	biological_process	epidermal growth factor receptor signaling pathway
A	0007268	biological_process	chemical synaptic transmission
A	0007507	biological_process	heart development
A	0007611	biological_process	learning or memory
A	0008286	biological_process	insulin receptor signaling pathway
A	0008353	molecular_function	RNA polymerase II CTD heptapeptide repeat kinase activity
A	0009887	biological_process	animal organ morphogenesis
A	0010759	biological_process	positive regulation of macrophage chemotaxis
A	0010800	biological_process	positive regulation of peptidyl-threonine phosphorylation
A	0014032	biological_process	neural crest cell development
A	0014044	biological_process	Schwann cell development
A	0015630	cellular_component	microtubule cytoskeleton
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0018107	biological_process	peptidyl-threonine phosphorylation
A	0019858	biological_process	cytosine metabolic process
A	0019902	molecular_function	phosphatase binding
A	0030278	biological_process	regulation of ossification
A	0030641	biological_process	regulation of cellular pH
A	0030878	biological_process	thyroid gland development
A	0031143	cellular_component	pseudopodium
A	0031647	biological_process	regulation of protein stability
A	0031663	biological_process	lipopolysaccharide-mediated signaling pathway
A	0032206	biological_process	positive regulation of telomere maintenance
A	0032496	biological_process	response to lipopolysaccharide
A	0032872	biological_process	regulation of stress-activated MAPK cascade
A	0033598	biological_process	mammary gland epithelial cell proliferation
A	0034198	biological_process	cellular response to amino acid starvation
A	0035094	biological_process	response to nicotine
A	0035556	biological_process	intracellular signal transduction
A	0035578	cellular_component	azurophil granule lumen
A	0036064	cellular_component	ciliary basal body
A	0038127	biological_process	ERBB signaling pathway
A	0038133	biological_process	ERBB2-ERBB3 signaling pathway
A	0042473	biological_process	outer ear morphogenesis
A	0042552	biological_process	myelination
A	0042802	molecular_function	identical protein binding
A	0043330	biological_process	response to exogenous dsRNA
A	0045202	cellular_component	synapse
A	0045542	biological_process	positive regulation of cholesterol biosynthetic process
A	0045596	biological_process	negative regulation of cell differentiation
A	0048009	biological_process	insulin-like growth factor receptor signaling pathway
A	0048538	biological_process	thymus development
A	0050852	biological_process	T cell receptor signaling pathway
A	0050853	biological_process	B cell receptor signaling pathway
A	0051403	biological_process	stress-activated MAPK cascade
A	0051493	biological_process	regulation of cytoskeleton organization
A	0060020	biological_process	Bergmann glial cell differentiation
A	0060291	biological_process	long-term synaptic potentiation
A	0060324	biological_process	face development
A	0060425	biological_process	lung morphogenesis
A	0060440	biological_process	trachea formation
A	0060716	biological_process	labyrinthine layer blood vessel development
A	0061308	biological_process	cardiac neural crest cell development involved in heart development
A	0061514	biological_process	interleukin-34-mediated signaling pathway
A	0070098	biological_process	chemokine-mediated signaling pathway
A	0070161	cellular_component	anchoring junction
A	0070371	biological_process	ERK1 and ERK2 cascade
A	0070849	biological_process	response to epidermal growth factor
A	0071356	biological_process	cellular response to tumor necrosis factor
A	0072584	biological_process	caveolin-mediated endocytosis
A	0072686	cellular_component	mitotic spindle
A	0090170	biological_process	regulation of Golgi inheritance
A	0106310	molecular_function	protein serine kinase activity
A	0120041	biological_process	positive regulation of macrophage proliferation
A	0150078	biological_process	positive regulation of neuroinflammatory response
A	1904813	cellular_component	ficolin-1-rich granule lumen
A	2000641	biological_process	regulation of early endosome to late endosome transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue SO4 A 401

Chain	Residue
A	ARG191
A	HOH615
A	ARG194
A	HIS232
A	HIS232
A	TYR233
A	HOH523
A	HOH596
A	HOH596
A	HOH615

---

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 402

Chain	Residue
A	ARG15
A	SER29
A	TYR30
A	HOH568

---

site_id	AC3
Number of Residues	15
Details	binding site for residue 6H3 A 403

Chain	Residue
A	ILE31
A	GLU33
A	VAL39
A	ALA52
A	GLN105
A	ASP106
A	MET108
A	GLU109
A	LYS114
A	CYS166
A	ASP167
A	EDO404
A	HOH522
A	HOH571
A	HOH599

---

site_id	AC4
Number of Residues	2
Details	binding site for residue EDO A 404

Chain	Residue
A	LYS114
A	6H3403

---

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 405

Chain	Residue
A	LYS292
A	ILE302
A	HIS310

---

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO A 406

Chain	Residue
A	ARG67
A	ARG70
A	ARG172
A	HOH580

---

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO A 407

Chain	Residue
A	HIS61
A	GLN62
A	LYS340
A	HOH610

---

site_id	AC8
Number of Residues	6
Details	binding site for residue EDO A 408

Chain	Residue
A	ARG91
A	ALA92
A	GLN97
A	MET98
A	LYS99
A	ASP100

---

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO A 409

Chain	Residue
A	LYS151
A	SER153
A	EDO410
A	EDO416
A	HOH646

---

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 410

Chain	Residue
A	LYS151
A	THR190
A	EDO409
A	HOH622

---

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO A 411

Chain	Residue
A	TYR139
A	ASN271
A	ALA325
A	GLU326
A	HOH537

---

site_id	AD3
Number of Residues	2
Details	binding site for residue EDO A 412

Chain	Residue
A	ASN158
A	HOH637

---

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO A 413

Chain	Residue
A	SER122
A	ASN123
A	HOH518

---

site_id	AD5
Number of Residues	4
Details	binding site for residue EDO A 414

Chain	Residue
A	LYS285
A	ASP288
A	HIS310
A	PRO311

---

site_id	AD6
Number of Residues	5
Details	binding site for residue EDO A 415

Chain	Residue
A	SER142
A	ARG277
A	HOH501
A	HOH504
A	HOH506

---

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO A 416

Chain	Residue
A	LYS151
A	EDO409
A	HOH529
A	HOH629

---

site_id	AD8
Number of Residues	4
Details	binding site for residue CL A 417

Chain	Residue
A	LEU234
A	LEU234
A	HOH620
A	HOH620

---

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
A	ILE31-LYS55

---

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

Chain	Residue	Details
A	VAL145-LEU157

---

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

Chain	Residue	Details
A	PHE59-CYS161

---

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	18
Details	DNA binding: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Motif: {"description":"TXY","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
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_FI5
Number of Residues	6
Details	Motif: {"description":"Nuclear translocation motif","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
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_FI7
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
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_FI9
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_FI10
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_FI11
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_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18760948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---