2XS0

Linear binding motifs for JNK and for calcineurin antagonistically control the nuclear shuttling of NFAT4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004707	molecular_function	MAP kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ANP A 1367

Chain	Residue
A	ILE32
A	GLU109
A	MET111
A	ASN114
A	SER155
A	ASN156
A	LEU168
A	ASP169
A	HOH2017
A	HOH2018
A	SER34
A	GLY35
A	GLN37
A	VAL40
A	ALA53
A	LYS55
A	ILE86
A	MET108

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE147-VAL159

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site_id	PS01351
Number of Residues	103
Details	MAPK MAP kinase signature. FqnqthakrayRElvlmkcvnhkniigllnvftpqksleefqdvyivmelmdanlcqviqmeldhermsyllyqmlcgikhlhsagiih..........RDlKpsnivvksdC

Chain	Residue	Details
A	PHE61-CYS163

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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
A	ASP151

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

Chain	Residue	Details
A	LYS55
A	ILE32

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P49185

Chain	Residue	Details
A	CYS116

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by MAP2K7 => ECO:0000269|PubMed:11062067

Chain	Residue	Details
A	VAL183

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by MAP2K4 => ECO:0000269|PubMed:11062067

Chain	Residue	Details
A	PHE185

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q91Y86

Chain	Residue	Details
A	SER377

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