1YRP

Catalytic domain of human ZIP kinase phosphorylated at Thr265

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE DTT B 278

Chain	Residue
B	ILE177

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAIVRkCrqkgtgkeyaak......FIKK

Chain	Residue	Details
A	LEU19-LYS46

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

Chain	Residue	Details
A	ILE135-LEU147

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP139
B	ASP139

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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	LEU19
B	LEU19

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS42
B	LYS42

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:18239682, ECO:0007744|PDB:2J90

Chain	Residue	Details
A	GLU94
A	VAL96
B	GLU94
B	VAL96

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18239682

Chain	Residue	Details
A	SER50
B	SER50

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17158456

Chain	Residue	Details
A	THR180
B	THR180

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15611134

Chain	Residue	Details
A	THR225
B	THR225

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site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis and ROCK1 => ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18239682

Chain	Residue	Details
A	TPO265
B	TPO265

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