2EVA

Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004672	molecular_function	protein kinase activity
A	0004709	molecular_function	MAP kinase kinase kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007165	biological_process	signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADN A 498

Chain	Residue
A	ARG44
A	ASP175
A	HOH537
A	HOH584
A	HOH589
A	HOH685
A	GLY45
A	ALA61
A	GLU105
A	TYR106
A	ALA107
A	SER111
A	PRO160
A	LEU163

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	22
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGAFGVVCkAkwrakd............VAIK

Chain	Residue	Details
A	VAL42-LYS63

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

Chain	Residue	Details
A	LEU152-LEU164

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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	ASP156

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	VAL42

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	LYS63

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis; alternate => ECO:0000269|PubMed:37832545, ECO:0000305|PubMed:10838074

Chain	Residue	Details
A	THR184

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis; alternate => ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:19675569, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:37832545

Chain	Residue	Details
A	THR187

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:10702308, ECO:0000269|PubMed:10838074

Chain	Residue	Details
A	SER192

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site_id	SWS_FT_FI7
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22406003

Chain	Residue	Details
A	LYS72

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site_id	SWS_FT_FI8
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q62073

Chain	Residue	Details
A	LYS158
A	LYS209

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