7W5C

Crystal structure of Mitogen Activated Protein Kinase 4 (MPK4) from Arabidopsis thaliana

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000165	biological_process	MAPK cascade
A	0000911	biological_process	cytokinesis by cell plate formation
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	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0006468	biological_process	protein phosphorylation
A	0006972	biological_process	hyperosmotic response
A	0007112	biological_process	male meiosis cytokinesis
A	0009409	biological_process	response to cold
A	0009504	cellular_component	cell plate
A	0009555	biological_process	pollen development
A	0009620	biological_process	response to fungus
A	0009651	biological_process	response to salt stress
A	0009737	biological_process	response to abscisic acid
A	0009861	biological_process	jasmonic acid and ethylene-dependent systemic resistance
A	0009862	biological_process	systemic acquired resistance, salicylic acid mediated signaling pathway
A	0009868	biological_process	jasmonic acid and ethylene-dependent systemic resistance, jasmonic acid mediated signaling pathway
A	0010119	biological_process	regulation of stomatal movement
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0042539	biological_process	hypotonic salinity response
A	0043622	biological_process	cortical microtubule organization
A	0045087	biological_process	innate immune response
A	0071244	biological_process	cellular response to carbon dioxide
A	0090333	biological_process	regulation of stomatal closure
A	0106310	molecular_function	protein serine kinase activity
Q	0004672	molecular_function	protein kinase activity
Q	0005524	molecular_function	ATP binding
Q	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE49-LYS73

---

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

Chain	Residue	Details
A	VAL165-LEU177

---

site_id	PS01351
Number of Residues	104
Details	MAPK MAP kinase signature. FdniidakrtlREikllkhmdhenviavkdiikppqrenfndvyivyelmdtdlhqiirsnqpltddhcrfflyqllrglkyvhsanvlh.........RDlKpsnlllnanC

Chain	Residue	Details
A	PHE78-CYS181

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
Q	ASP190

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE49
A	LYS72

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:11123804

Chain	Residue	Details
A	THR201

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:11123804

Chain	Residue	Details
A	TYR203

---