Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4X6R

An Isoform-specific Myristylation Switch Targets RIIb PKA Holoenzymes to Membranes

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0001669	cellular_component	acrosomal vesicle
A	0001707	biological_process	mesoderm formation
A	0001843	biological_process	neural tube closure
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004691	molecular_function	cAMP-dependent protein kinase activity
A	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005811	cellular_component	lipid droplet
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005930	cellular_component	axoneme
A	0005952	cellular_component	cAMP-dependent protein kinase complex
A	0006338	biological_process	chromatin remodeling
A	0006397	biological_process	mRNA processing
A	0006468	biological_process	protein phosphorylation
A	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
A	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A	0008284	biological_process	positive regulation of cell population proliferation
A	0010898	biological_process	positive regulation of triglyceride catabolic process
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016607	cellular_component	nuclear speck
A	0016740	molecular_function	transferase activity
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0018107	biological_process	peptidyl-threonine phosphorylation
A	0019870	molecular_function	potassium channel inhibitor activity
A	0019901	molecular_function	protein kinase binding
A	0019904	molecular_function	protein domain specific binding
A	0030007	biological_process	intracellular potassium ion homeostasis
A	0030145	molecular_function	manganese ion binding
A	0031267	molecular_function	small GTPase binding
A	0031410	cellular_component	cytoplasmic vesicle
A	0031514	cellular_component	motile cilium
A	0031588	cellular_component	nucleotide-activated protein kinase complex
A	0031594	cellular_component	neuromuscular junction
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0031669	biological_process	cellular response to nutrient levels
A	0032991	cellular_component	protein-containing complex
A	0034237	molecular_function	protein kinase A regulatory subunit binding
A	0034605	biological_process	cellular response to heat
A	0036126	cellular_component	sperm flagellum
A	0038110	biological_process	interleukin-2-mediated signaling pathway
A	0038202	biological_process	TORC1 signaling
A	0043457	biological_process	regulation of cellular respiration
A	0044853	cellular_component	plasma membrane raft
A	0044877	molecular_function	protein-containing complex binding
A	0045542	biological_process	positive regulation of cholesterol biosynthetic process
A	0045667	biological_process	regulation of osteoblast differentiation
A	0045722	biological_process	positive regulation of gluconeogenesis
A	0045820	biological_process	negative regulation of glycolytic process
A	0045879	biological_process	negative regulation of smoothened signaling pathway
A	0046777	biological_process	protein autophosphorylation
A	0046827	biological_process	positive regulation of protein export from nucleus
A	0048240	biological_process	sperm capacitation
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0048792	biological_process	spontaneous exocytosis of neurotransmitter
A	0050766	biological_process	positive regulation of phagocytosis
A	0050804	biological_process	modulation of chemical synaptic transmission
A	0051447	biological_process	negative regulation of meiotic cell cycle
A	0051726	biological_process	regulation of cell cycle
A	0051966	biological_process	regulation of synaptic transmission, glutamatergic
A	0061136	biological_process	regulation of proteasomal protein catabolic process
A	0070417	biological_process	cellular response to cold
A	0070507	biological_process	regulation of microtubule cytoskeleton organization
A	0070613	biological_process	regulation of protein processing
A	0071333	biological_process	cellular response to glucose stimulus
A	0071374	biological_process	cellular response to parathyroid hormone stimulus
A	0071377	biological_process	cellular response to glucagon stimulus
A	0097225	cellular_component	sperm midpiece
A	0097546	cellular_component	ciliary base
A	0098793	cellular_component	presynapse
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
A	0099170	biological_process	postsynaptic modulation of chemical synaptic transmission
A	0106310	molecular_function	protein serine kinase activity
A	0120186	biological_process	negative regulation of protein localization to chromatin
A	0140198	molecular_function	histone H1-4S35 kinase activity
A	0141156	biological_process	cAMP/PKA signal transduction
A	1904262	biological_process	negative regulation of TORC1 signaling
A	1904539	biological_process	negative regulation of glycolytic process through fructose-6-phosphate
A	1990044	biological_process	protein localization to lipid droplet
A	2000810	biological_process	regulation of bicellular tight junction assembly
B	0001932	biological_process	regulation of protein phosphorylation
B	0005952	cellular_component	cAMP-dependent protein kinase complex
B	0008603	molecular_function	cAMP-dependent protein kinase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue SO4 A 401

Chain	Residue
A	ARG137
A	HOH539

site_id	AC2
Number of Residues	25
Details	binding site for residue ATP A 402

Chain	Residue
A	ALA70
A	LYS72
A	MET120
A	GLU121
A	VAL123
A	GLU127
A	ASP166
A	LYS168
A	GLU170
A	ASN171
A	LEU173
A	THR183
A	ASP184
A	PHE327
A	MG407
A	MG408
B	ARG94
B	ALA97
A	GLY50
A	THR51
A	GLY52
A	SER53
A	PHE54
A	GLY55
A	VAL57

site_id	AC3
Number of Residues	10
Details	binding site for residue TAM A 403

Chain	Residue
A	LYS189
A	ARG194
A	THR195
A	TRP196
A	TPO197
B	TYR103
B	THR104
B	GLU105
B	GLU106
B	HOH610

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 404

Chain	Residue
A	ASP329
A	TYR330
A	HOH560
A	HOH567
B	LYS90

site_id	AC5
Number of Residues	7
Details	binding site for residue MYR A 405

Chain	Residue
A	GLY1
A	ASN2
A	PHE18
A	LEU152
A	GLU155
A	GLN307
A	LYS309

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 A 406

Chain	Residue
A	ARG194
A	ASN216
A	LYS217
A	HOH561

site_id	AC7
Number of Residues	3
Details	binding site for residue MG A 407

Chain	Residue
A	ASN171
A	ASP184
A	ATP402

site_id	AC8
Number of Residues	3
Details	binding site for residue MG A 408

Chain	Residue
A	PHE54
A	ASP184
A	ATP402

site_id	AC9
Number of Residues	11
Details	binding site for residue SO4 B 401

Chain	Residue
B	PHE322
B	GLY323
B	GLU324
B	ILE325
B	HOH548
B	HOH550
B	HOH551
B	HOH579
B	HOH582
B	HOH619
B	HOH621

site_id	AD1
Number of Residues	5
Details	binding site for residue SO4 B 402

Chain	Residue
A	PRO258
A	SER259
B	GLN283
B	GLY284
B	ARG303

site_id	AD2
Number of Residues	7
Details	binding site for residue SO4 B 403

Chain	Residue
B	ILE163
B	GLY169
B	ASP170
B	ASN171
B	TYR173
B	ARG209
B	HOH567

site_id	AD3
Number of Residues	6
Details	binding site for residue SO4 B 404

Chain	Residue
B	ARG93
B	MET329
B	ASN330
B	ARG350
B	HOH505
B	HOH509

site_id	AD4
Number of Residues	6
Details	binding site for residue GOL B 405

Chain	Residue
A	LYS83
B	SER99
B	ALA100
B	GLU101
B	GLY206
B	ARG226

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU49-LYS72

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

Chain	Residue	Details
A	LEU162-ILE174

site_id	PS00888
Number of Residues	17
Details	CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VIqQGDeGDnFYVIdqG

Chain	Residue	Details
B	VAL162-GLY178
B	ILE280-GLY296

site_id	PS00889
Number of Residues	18
Details	CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGElALiygtp......RAAtVkA

Chain	Residue	Details
B	PHE198-ALA215

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	265
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Deamidated asparagine; partial","evidences":[{"source":"PubMed","id":"11141074","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"11141074","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8395513","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P17612","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22323819","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8395513","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"22323819","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8395513","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9707564","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21866565","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"8395513","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Lipidation: {"description":"N-myristoyl glycine","evidences":[{"source":"PubMed","id":"11141074","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Motif: {"description":"Pseudophosphorylation motif"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DBC7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09456","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)