2Y4I

KSR2-MEK1 heterodimer

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0000165	biological_process	MAPK cascade
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0004708	molecular_function	MAP kinase kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005769	cellular_component	early endosome
C	0005770	cellular_component	late endosome
C	0005813	cellular_component	centrosome
C	0005816	cellular_component	spindle pole body
C	0005856	cellular_component	cytoskeleton
C	0005925	cellular_component	focal adhesion
C	0006468	biological_process	protein phosphorylation
C	0016020	cellular_component	membrane
C	0016310	biological_process	phosphorylation
C	0032872	biological_process	regulation of stress-activated MAPK cascade
C	0090170	biological_process	regulation of Golgi inheritance
C	0106310	molecular_function	protein serine kinase activity
C	2000641	biological_process	regulation of early endosome to late endosome transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP B 1932

Chain	Residue
B	ILE672
B	LYS788
B	LYS790
B	ASN791
B	PHE793
B	ASP803
B	GLN825
B	MG1933
B	LYS674
B	GLY675
B	ARG676
B	ARG692
B	THR739
B	SER740
B	LEU741
B	CYS742

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 1933

Chain	Residue
B	ASN791
B	ASP803
B	ATP1932

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site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP C 1382

Chain	Residue
C	ALA76
C	GLY77
C	VAL82
C	ALA95
C	LYS97
C	MET143
C	GLU144
C	MET146
C	GLY149
C	SER150
C	GLN153
C	ASP190
C	LYS192
C	SER194
C	ASN195
C	LEU197
C	ASP208
C	MG1383

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1383

Chain	Residue
C	SER194
C	ASN195
C	CYS207
C	ASP208
C	ATP1382

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL C 1384

Chain	Residue
C	ASN319
C	ALA347

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK

Chain	Residue	Details
C	LEU74-LYS97

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

Chain	Residue	Details
C	ILE186-VAL198
B	ILE782-TYR794

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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
C	ASP190

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:21441910

Chain	Residue	Details
C	LEU74
C	LYS97

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Cleavage; by anthrax lethal factor => ECO:0000250

Chain	Residue	Details
C	PRO8
B	ASP803

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine; by RAF => ECO:0000269|PubMed:8157000

Chain	Residue	Details
C	SER218
C	SER222

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q02750

Chain	Residue	Details
C	THR286

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986

Chain	Residue	Details
C	THR292

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PAK => ECO:0000250|UniProtKB:Q02750

Chain	Residue	Details
C	SER298

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