MOUSE:KAPCA

Species (Taxon ID)	Mus musculus (Mouse). (10090)
Gene Name(s)	Prkaca (synonyms: Pkaca)
Protein Name(s)	cAMP-dependent protein kinase catalytic subunit alpha PKA C-alpha
External Links
UniProt	P05132
EMBL	M19960 M18240 M18241 M19953 M19954 M19955 M19956 M19957 M19958 M19959 M12303 BC003238 BC054834 AF239743
CCDS	CCDS22463.1
PIR	A28619
RefSeq	NP_001264827.1 NP_032880.1
UniGene	Mm.19111
PDB	1APM 1ATP 1BKX 1BX6 1FMO 1J3H 1JBP 1JLU 1L3R 1PVK 1RDQ 1RE8 1REJ 1REK 1SYK 2CPK 2ERZ 2QCS 2QUR 2QVS 3FHI 3FJQ 3IDB 3IDC 3J4Q 3J4R 3O7L 3OW3 3PVB 3QAL 3QAM 3TNP 3TNQ 4DFX 4DFY 4DFZ 4DG0 4DG2 4DG3 4DH1 4DH3 4DH5 4DH7 4DH8 4DIN 4HPT 4HPU 4IAC 4IAD 4IAF 4IAI 4IAK 4IAY 4IAZ 4IB0 4IB1 4IB3 4NTS 4NTT 4O21 4O22
PDBsum	1APM 1ATP 1BKX 1BX6 1FMO 1J3H 1JBP 1JLU 1L3R 1PVK 1RDQ 1RE8 1REJ 1REK 1SYK 2CPK 2ERZ 2QCS 2QUR 2QVS 3FHI 3FJQ 3IDB 3IDC 3J4Q 3J4R 3O7L 3OW3 3PVB 3QAL 3QAM 3TNP 3TNQ 4DFX 4DFY 4DFZ 4DG0 4DG2 4DG3 4DH1 4DH3 4DH5 4DH7 4DH8 4DIN 4HPT 4HPU 4IAC 4IAD 4IAF 4IAI 4IAK 4IAY 4IAZ 4IB0 4IB1 4IB3 4NTS 4NTT 4O21 4O22
ProteinModelPortal	P05132
SMR	P05132
BioGrid	202192
DIP	DIP-6086N
IntAct	P05132
MINT	MINT-4051347
STRING	10090.ENSMUSP00000005606
BindingDB	P05132
PhosphoSite	P05132
MaxQB	P05132
PaxDb	P05132
PRIDE	P05132
Ensembl	ENSMUST00000005606
GeneID	18747
KEGG	mmu:18747
UCSC	uc009mll.2 uc009mlm.1
CTD	5566
MGI	MGI:97592
eggNOG	COG0515
GeneTree	ENSGT00770000120454
HOGENOM	HOG000233033
HOVERGEN	HBG108317
InParanoid	P05132
KO	K04345
OMA	GKEFTEF
OrthoDB	EOG7VX8WD
PhylomeDB	P05132
TreeFam	TF313399
BRENDA	2.7.11.11
Reactome	REACT_196635 REACT_198649 REACT_203795 REACT_213852 REACT_213947 REACT_220108 REACT_220758 REACT_225836 REACT_236903 REACT_237855 REACT_243078 REACT_244487 REACT_245618 REACT_245720 REACT_248547 REACT_263148 REACT_263230 REACT_268522 REACT_268705 REACT_269412 REACT_270923
ChiTaRS	Prkaca
EvolutionaryTrace	P05132
NextBio	294909
PRO	PR:P05132
Proteomes	UP000000589
Bgee	P05132
CleanEx	MM_PRKACA
Genevestigator	P05132
GO	GO:0031588 GO:0005813 GO:0097546 GO:0005737 GO:0005829 GO:0070062 GO:0005739 GO:0031594 GO:0005654 GO:0005634 GO:0005886 GO:0097225 GO:0005524 GO:0004691 GO:0004672 GO:0004674 GO:0004712 GO:0071333 GO:0071374 GO:0001707 GO:1901621 GO:0001843 GO:0018105 GO:0018107 GO:0071158 GO:0046827 GO:0046777 GO:0006468 GO:0045667 GO:0061136 GO:0070613 GO:0050804 GO:2000810 GO:0048240
InterPro	IPR000961 IPR011009 IPR000719 IPR017441 IPR002290 IPR008271
Pfam	PF00069
SMART	SM00133 SM00220
SUPFAM	SSF56112
PROSITE	PS51285 PS00107 PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0004674	protein serine/threonine kinase activity	PMID:29473541^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q9VM90)	Seeded From UniProt	complete
part_of	GO:0001669	acrosomal vesicle	PMID:27105888^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0036126	sperm flagellum	PMID:27105888^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:1862342^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:9688563^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:9413984^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:1862342^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	PMID:19447092^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002608)	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:15692043^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:15692043^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005952	cAMP-dependent protein kinase complex	PMID:15692043^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0034237	protein kinase A regulatory subunit binding	PMID:15692043^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00514	F		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:9688563^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:9413984^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:1862342^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63248	F		Seeded From UniProt	complete
involved_in	GO:0071158	positive regulation of cell cycle arrest	PMID:19223768^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048240	sperm capacitation	PMID:19560455^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004691	cAMP-dependent protein kinase activity	PMID:12200423^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0051447	negative regulation of meiotic cell cycle	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0050804	modulation of chemical synaptic transmission	PMID:15590926^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0046827	positive regulation of protein export from nucleus	PMID:17043310^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0046777	protein autophosphorylation	PMID:18191828^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0046777	protein autophosphorylation	PMID:17855365^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0045667	regulation of osteoblast differentiation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
part_of	GO:0045171	intercellular bridge	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	F		Seeded From UniProt	complete
part_of	GO:0044853	plasma membrane raft	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0043457	regulation of cellular respiration	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0034605	cellular response to heat	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
enables	GO:0034237	protein kinase A regulatory subunit binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	F		Seeded From UniProt	complete
part_of	GO:0031594	neuromuscular junction	PMID:8794865^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031588	nucleotide-activated protein kinase complex	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	F		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0018107	peptidyl-threonine phosphorylation	PMID:7905001^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0018105	peptidyl-serine phosphorylation	PMID:7905001^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0018105	peptidyl-serine phosphorylation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0018105	peptidyl-serine phosphorylation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	P		Seeded From UniProt	complete
enables	GO:0017137	Rab GTPase binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	F		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0008284	positive regulation of cell population proliferation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	PMID:9218452^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	PMID:19056373^[18]	ECO:0000314	direct assay evidence used in manual assertion		P	has_participant:(MGI:MGI:95728)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	PMID:18202122^[19]	ECO:0000314	direct assay evidence used in manual assertion		P	has_participant:(MGI:MGI:2180167)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	PMID:18191828^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	PMID:17855365^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	has_participant:(MGI:MGI:3646964)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	PMID:16481613^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	PMID:15465019^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006468	protein phosphorylation	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006397	mRNA processing	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
part_of	GO:0005952	cAMP-dependent protein kinase complex	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0005952	cAMP-dependent protein kinase complex	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	C		Seeded From UniProt	complete
colocalizes_with	GO:0005930	axoneme	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:16782699^[22]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(EMAPA:35783) part_of:(CL:0000192)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:12931191^[23]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000182)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9218452^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12004056^[24]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(EMAPA:16039) part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9218452^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	C		Seeded From UniProt	complete
enables	GO:0004712	protein serine/threonine/tyrosine kinase activity	PMID:22797923^[25]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	F		Seeded From UniProt	complete
enables	GO:0004691	cAMP-dependent protein kinase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	F		Seeded From UniProt	complete
enables	GO:0004691	cAMP-dependent protein kinase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:7905001^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:18202122^[19]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(MGI:MGI:2180167)	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:17855365^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(MGI:MGI:3646964)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:2000810	regulation of bicellular tight junction assembly	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:1901621	negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning	PMID:22007132^[26]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:97760	P	occurs_in:(EMAPA:16531)	Seeded From UniProt	complete
part_of	GO:0097546	ciliary base	PMID:22007132^[26]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000134) part_of:(EMAPA:16530)\|part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0097225	sperm midpiece	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0071374	cellular response to parathyroid hormone stimulus	PMID:19723499^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0071333	cellular response to glucose stimulus	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0070613	regulation of protein processing	PMID:22007132^[26]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:97760	P	has_direct_input:(PR:Q61602-1)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0061136	regulation of proteasomal protein catabolic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0051966	regulation of synaptic transmission, glutamatergic	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:3389	P		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:15465019^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17612	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0001843	neural tube closure	PMID:22007132^[26]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:97760	P	occurs_in:(EMAPA:16530)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0001707	mesoderm formation	PMID:12004056^[24]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:97592	P		Seeded From UniProt	complete
involved_in	GO:2000810	regulation of bicellular tight junction assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	P		Seeded From UniProt	complete
involved_in	GO:0071333	cellular response to glucose stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	P		Seeded From UniProt	complete
involved_in	GO:0061136	regulation of proteasomal protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
involved_in	GO:0045667	regulation of osteoblast differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	P		Seeded From UniProt	complete
part_of	GO:0045171	intercellular bridge	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
part_of	GO:0044853	plasma membrane raft	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	P		Seeded From UniProt	complete
enables	GO:0034237	protein kinase A regulatory subunit binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	F		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	F		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	F		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	P		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	P		Seeded From UniProt	complete
involved_in	GO:0006397	mRNA processing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	P		Seeded From UniProt	complete
part_of	GO:0005952	cAMP-dependent protein kinase complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
part_of	GO:0005930	axoneme	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
enables	GO:0004712	protein serine/threonine/tyrosine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	F		Seeded From UniProt	complete
enables	GO:0004691	cAMP-dependent protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P17612 ensembl:ENSP00000309591	F		Seeded From UniProt	complete
part_of	GO:0045171	intercellular bridge	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A024R7J0 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A024R7J0 ensembl:ENSP00000309591	C		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000961 InterPro:IPR039035	F		Seeded From UniProt	complete
enables	GO:0004691	cAMP-dependent protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR039035	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR000961 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR000961 InterPro:IPR008271	P		Seeded From UniProt	complete
involved_in	GO:0010737	protein kinase A signaling	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR039035	P		Seeded From UniProt	complete
enables	GO:0034237	protein kinase A regulatory subunit binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR039035	F		Seeded From UniProt	complete
involved_in	GO:0071333	cellular response to glucose stimulus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR039035	P		Seeded From UniProt	complete
enables	GO:0004691	cAMP-dependent protein kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.11.11	F		Seeded From UniProt	complete
part_of	GO:0097225	sperm midpiece	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P17612-2	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-NUL-5610740 Reactome:R-MMU-9010662 Reactome:R-MMU-5610710 Reactome:R-MMU-164055 Reactome:R-MMU-163422	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-NUL-9615367 Reactome:R-MMU-9005872 Reactome:R-MMU-9005848 Reactome:R-MMU-164136	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004691	cAMP-dependent protein kinase activity	Reactome:R-MMU-164136 Reactome:R-MMU-164055	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	Reactome:R-NUL-9615367	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0968	C		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472 UniProtKB-SubCell:SL-0162	C		Seeded From UniProt	complete
part_of	GO:0031514	motile cilium	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0282 UniProtKB-SubCell:SL-0117	C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C		Seeded From UniProt	complete
part_of	GO:0005929	cilium	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0969	C		Seeded From UniProt	complete
part_of	GO:0001669	acrosomal vesicle	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0007	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Lee, PT et al. (2018) A kinase-dependent feedforward loop affects CREBB stability and long term memory formation. Elife 7 PubMed GONUTS page
↑ ^2.0 ^2.1 Stanger, SJ et al. (2016) A novel germ cell protein, SPIF (sperm PKA interacting factor), is essential for the formation of a PKA/TCP11 complex that undergoes conformational and phosphorylation changes upon capacitation. FASEB J. 30 2777-91 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Knighton, DR et al. (1991) Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253 407-14 PubMed GONUTS page
↑ ^4.0 ^4.1 Radhakrishnan, I et al. (1998) Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB. FEBS Lett. 430 317-22 PubMed GONUTS page
↑ ^5.0 ^5.1 Radhakrishnan, I et al. (1997) Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91 741-52 PubMed GONUTS page
↑ Zhong, H et al. (2009) Subcellular dynamics of type II PKA in neurons. Neuron 62 363-74 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Kim, C et al. (2005) Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA. Science 307 690-6 PubMed GONUTS page
↑ Pirino, G et al. (2009) Protein kinase A regulates resumption of meiosis by phosphorylation of Cdc25B in mammalian oocytes. Cell Cycle 8 665-70 PubMed GONUTS page
↑ Baker, MA et al. (2009) Phosphorylation and consequent stimulation of the tyrosine kinase c-Abl by PKA in mouse spermatozoa; its implications during capacitation. Dev. Biol. 333 57-66 PubMed GONUTS page
↑ Takemori, H et al. (2002) ACTH-induced nucleocytoplasmic translocation of salt-inducible kinase. Implication in the protein kinase A-activated gene transcription in mouse adrenocortical tumor cells. J. Biol. Chem. 277 42334-43 PubMed GONUTS page
↑ Townsend, M et al. (2004) Retina-driven dephosphorylation of the NR2A subunit correlates with faster NMDA receptor kinetics at developing retinocollicular synapses. J. Neurosci. 24 11098-107 PubMed GONUTS page
↑ Kim, JW & Lemke, G (2006) Hedgehog-regulated localization of Vax2 controls eye development. Genes Dev. 20 2833-47 PubMed GONUTS page
↑ ^13.0 ^13.1 Herr, JC et al. (2008) Distribution of RNA binding protein MOEP19 in the oocyte cortex and early embryo indicates pre-patterning related to blastomere polarity and trophectoderm specification. Dev. Biol. 314 300-16 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Li, YF et al. (2007) FSCB, a novel protein kinase A-phosphorylated calcium-binding protein, is a CABYR-binding partner involved in late steps of fibrous sheath biogenesis. J. Biol. Chem. 282 34104-19 PubMed GONUTS page
↑ Imaizumi-Scherrer, T et al. (1996) Accumulation in fetal muscle and localization to the neuromuscular junction of cAMP-dependent protein kinase A regulatory and catalytic subunits RI alpha and C alpha. J. Cell Biol. 134 1241-54 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Baude, EJ et al. (1994) Glutamic acid 203 of the cAMP-dependent protein kinase catalytic subunit participates in the inhibition by two isoforms of the protein kinase inhibitor. J. Biol. Chem. 269 2316-23 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Collins, SP & Uhler, MD (1997) Characterization of PKIgamma, a novel isoform of the protein kinase inhibitor of cAMP-dependent protein kinase. J. Biol. Chem. 272 18169-78 PubMed GONUTS page
↑ Pan, Y et al. (2009) Phosphorylation of Gli2 by protein kinase A is required for Gli2 processing and degradation and the Sonic Hedgehog-regulated mouse development. Dev. Biol. 326 177-89 PubMed GONUTS page
↑ ^19.0 ^19.1 Jha, KN et al. (2008) Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation. Endocrinology 149 2108-20 PubMed GONUTS page
↑ Huang, F et al. (2006) Analysis of calstabin2 (FKBP12.6)-ryanodine receptor interactions: rescue of heart failure by calstabin2 in mice. Proc. Natl. Acad. Sci. U.S.A. 103 3456-61 PubMed GONUTS page
↑ ^21.0 ^21.1 Keicher, C et al. (2004) Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase. Biochem. Biophys. Res. Commun. 324 308-16 PubMed GONUTS page
↑ El-Yazbi, AF et al. (2006) Caveolin-1 knockout alters beta-adrenoceptors function in mouse small intestine. Am. J. Physiol. Gastrointest. Liver Physiol. 291 G1020-30 PubMed GONUTS page
↑ Danial, NN et al. (2003) BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 424 952-6 PubMed GONUTS page
↑ ^24.0 ^24.1 Amieux, PS et al. (2002) Increased basal cAMP-dependent protein kinase activity inhibits the formation of mesoderm-derived structures in the developing mouse embryo. J. Biol. Chem. 277 27294-304 PubMed GONUTS page
↑ Hoxhaj, G et al. (2012) ZNRF2 is released from membranes by growth factors and, together with ZNRF1, regulates the Na+/K+ATPase. J. Cell. Sci. 125 4662-75 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 Tuson, M et al. (2011) Protein kinase A acts at the basal body of the primary cilium to prevent Gli2 activation and ventralization of the mouse neural tube. Development 138 4921-30 PubMed GONUTS page
↑ Terauchi, M et al. (2009) T lymphocytes amplify the anabolic activity of parathyroid hormone through Wnt10b signaling. Cell Metab. 10 229-40 PubMed GONUTS page

[PMID:29473541-1] Lee, PT et al. (2018) A kinase-dependent feedforward loop affects CREBB stability and long term memory formation. Elife 7 PubMed GONUTS page

[PMID:27105888-2] 2.0 ^2.1 Stanger, SJ et al. (2016) A novel germ cell protein, SPIF (sperm PKA interacting factor), is essential for the formation of a PKA/TCP11 complex that undergoes conformational and phosphorylation changes upon capacitation. FASEB J. 30 2777-91 PubMed GONUTS page

[PMID:1862342-3] 3.0 ^3.1 ^3.2 Knighton, DR et al. (1991) Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253 407-14 PubMed GONUTS page

[PMID:9688563-4] 4.0 ^4.1 Radhakrishnan, I et al. (1998) Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB. FEBS Lett. 430 317-22 PubMed GONUTS page

[PMID:9413984-5] 5.0 ^5.1 Radhakrishnan, I et al. (1997) Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91 741-52 PubMed GONUTS page

[PMID:19447092-6] Zhong, H et al. (2009) Subcellular dynamics of type II PKA in neurons. Neuron 62 363-74 PubMed GONUTS page

[PMID:15692043-7] 7.0 ^7.1 ^7.2 ^7.3 Kim, C et al. (2005) Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA. Science 307 690-6 PubMed GONUTS page

[PMID:19223768-8] Pirino, G et al. (2009) Protein kinase A regulates resumption of meiosis by phosphorylation of Cdc25B in mammalian oocytes. Cell Cycle 8 665-70 PubMed GONUTS page

[PMID:19560455-9] Baker, MA et al. (2009) Phosphorylation and consequent stimulation of the tyrosine kinase c-Abl by PKA in mouse spermatozoa; its implications during capacitation. Dev. Biol. 333 57-66 PubMed GONUTS page

[PMID:12200423-10] Takemori, H et al. (2002) ACTH-induced nucleocytoplasmic translocation of salt-inducible kinase. Implication in the protein kinase A-activated gene transcription in mouse adrenocortical tumor cells. J. Biol. Chem. 277 42334-43 PubMed GONUTS page

[PMID:15590926-11] Townsend, M et al. (2004) Retina-driven dephosphorylation of the NR2A subunit correlates with faster NMDA receptor kinetics at developing retinocollicular synapses. J. Neurosci. 24 11098-107 PubMed GONUTS page

[PMID:17043310-12] Kim, JW & Lemke, G (2006) Hedgehog-regulated localization of Vax2 controls eye development. Genes Dev. 20 2833-47 PubMed GONUTS page

[PMID:18191828-13] 13.0 ^13.1 Herr, JC et al. (2008) Distribution of RNA binding protein MOEP19 in the oocyte cortex and early embryo indicates pre-patterning related to blastomere polarity and trophectoderm specification. Dev. Biol. 314 300-16 PubMed GONUTS page

[PMID:17855365-14] 14.0 ^14.1 ^14.2 Li, YF et al. (2007) FSCB, a novel protein kinase A-phosphorylated calcium-binding protein, is a CABYR-binding partner involved in late steps of fibrous sheath biogenesis. J. Biol. Chem. 282 34104-19 PubMed GONUTS page

[PMID:8794865-15] Imaizumi-Scherrer, T et al. (1996) Accumulation in fetal muscle and localization to the neuromuscular junction of cAMP-dependent protein kinase A regulatory and catalytic subunits RI alpha and C alpha. J. Cell Biol. 134 1241-54 PubMed GONUTS page

[PMID:7905001-16] 16.0 ^16.1 ^16.2 Baude, EJ et al. (1994) Glutamic acid 203 of the cAMP-dependent protein kinase catalytic subunit participates in the inhibition by two isoforms of the protein kinase inhibitor. J. Biol. Chem. 269 2316-23 PubMed GONUTS page

[PMID:9218452-17] 17.0 ^17.1 ^17.2 Collins, SP & Uhler, MD (1997) Characterization of PKIgamma, a novel isoform of the protein kinase inhibitor of cAMP-dependent protein kinase. J. Biol. Chem. 272 18169-78 PubMed GONUTS page

[PMID:19056373-18] Pan, Y et al. (2009) Phosphorylation of Gli2 by protein kinase A is required for Gli2 processing and degradation and the Sonic Hedgehog-regulated mouse development. Dev. Biol. 326 177-89 PubMed GONUTS page

[PMID:18202122-19] 19.0 ^19.1 Jha, KN et al. (2008) Biochemical and structural characterization of apolipoprotein A-I binding protein, a novel phosphoprotein with a potential role in sperm capacitation. Endocrinology 149 2108-20 PubMed GONUTS page

[PMID:16481613-20] Huang, F et al. (2006) Analysis of calstabin2 (FKBP12.6)-ryanodine receptor interactions: rescue of heart failure by calstabin2 in mice. Proc. Natl. Acad. Sci. U.S.A. 103 3456-61 PubMed GONUTS page

[PMID:15465019-21] 21.0 ^21.1 Keicher, C et al. (2004) Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase. Biochem. Biophys. Res. Commun. 324 308-16 PubMed GONUTS page

[PMID:16782699-22] El-Yazbi, AF et al. (2006) Caveolin-1 knockout alters beta-adrenoceptors function in mouse small intestine. Am. J. Physiol. Gastrointest. Liver Physiol. 291 G1020-30 PubMed GONUTS page

[PMID:12931191-23] Danial, NN et al. (2003) BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 424 952-6 PubMed GONUTS page

[PMID:12004056-24] 24.0 ^24.1 Amieux, PS et al. (2002) Increased basal cAMP-dependent protein kinase activity inhibits the formation of mesoderm-derived structures in the developing mouse embryo. J. Biol. Chem. 277 27294-304 PubMed GONUTS page

[PMID:22797923-25] Hoxhaj, G et al. (2012) ZNRF2 is released from membranes by growth factors and, together with ZNRF1, regulates the Na+/K+ATPase. J. Cell. Sci. 125 4662-75 PubMed GONUTS page

[PMID:22007132-26] 26.0 ^26.1 ^26.2 ^26.3 Tuson, M et al. (2011) Protein kinase A acts at the basal body of the primary cilium to prevent Gli2 activation and ventralization of the mouse neural tube. Development 138 4921-30 PubMed GONUTS page

[PMID:19723499-27] Terauchi, M et al. (2009) T lymphocytes amplify the anabolic activity of parathyroid hormone through Wnt10b signaling. Cell Metab. 10 229-40 PubMed GONUTS page

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