Prkaa1

Functionⁱ

Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.By similarity12 Publications

Catalytic activityⁱ

ATP + a protein = ADP + a phosphoprotein.2 Publications

ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate.1 Publication

ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate.1 Publication

ATP + [tau protein] = ADP + [tau protein] phosphate.1 Publication

Cofactorⁱ

Mg²⁺By similarity

Activity regulationⁱ

Activated by phosphorylation on Thr-183. Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or PRKAG3) results in allosteric activation, inducing phosphorylation on Thr-183. AMP-binding to gamma subunit also sustains activity by preventing dephosphorylation of Thr-183. ADP also stimulates Thr-183 phosphorylation, without stimulating already phosphorylated AMPK. ATP promotes dephosphorylation of Thr-183, rendering the enzyme inactive. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP. Selectively inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]-3-pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by resveratrol, a natural polyphenol present in red wine, and S17834, a synthetic polyphenol.5 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	56	ATPPROSITE-ProRule annotation		1
Active siteⁱ	150	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	33 – 41	ATPPROSITE-ProRule annotation		9

GO - Molecular functionⁱ

[acetyl-CoA carboxylase] kinase activity Source: UniProtKB-EC
[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity Source: UniProtKB-EC
AMP-activated protein kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
ATP binding
Source: RGD
Inferred from direct assayⁱ
- 16648175
chromatin binding Source: UniProtKB
eukaryotic elongation factor-2 kinase activator activity
Source: UniProtKB
Non-traceable author statementⁱ
- 12194824
histone serine kinase activity Source: UniProtKB
metal ion binding Source: UniProtKB-KW
protein C-terminus binding
Source: RGD
Inferred from physical interactionⁱ
- 15695819
protein serine/threonine kinase activity
Source: RGD
Inferred from direct assayⁱ
- 8955377
tau-protein kinase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

autophagy Source: UniProtKB-KW
CAMKK-AMPK signaling cascade Source: Ensembl
cellular response to calcium ion
Source: ARUK-UCL
Inferred from mutant phenotypeⁱ
- 25788287
cellular response to ethanol
Source: RGD
Inferred from expression patternⁱ
- 20164678
cellular response to glucose starvation Source: UniProtKB
cellular response to glucose stimulus
Source: ARUK-UCL
Inferred from mutant phenotypeⁱ
- 25788287
cellular response to hydrogen peroxide
Source: RGD
Inferred from expression patternⁱ
- 18081811
cellular response to hypoxia
Source: RGD
Inferred from expression patternⁱ
- 17720864
cellular response to nutrient levels Source: UniProtKB
cellular response to organonitrogen compound
Source: RGD
Inferred from expression patternⁱ
- 19236843
cellular response to prostaglandin E stimulus Source: Ensembl
cholesterol biosynthetic process Source: UniProtKB-KW
cold acclimation
Source: RGD
Inferred from direct assayⁱ
- 21945600
energy homeostasis
Source: UniProtKB
Inferred from direct assayⁱ
- 11724780
fatty acid biosynthetic process Source: UniProtKB-KW
fatty acid homeostasis
Source: UniProtKB
Inferred from direct assayⁱ
- 11724780
fatty acid oxidation Source: Ensembl
glucose homeostasis Source: UniProtKB
glucose metabolic process Source: Ensembl
intracellular signal transduction
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
lipid biosynthetic process Source: UniProtKB
motor behavior Source: Ensembl
negative regulation of apoptotic process Source: UniProtKB
negative regulation of glucose import in response to insulin stimulus
Source: RGD
Inferred from mutant phenotypeⁱ
- 20501641
negative regulation of lipid catabolic process Source: UniProtKB
negative regulation of TOR signaling Source: UniProtKB
negative regulation of translation
Source: UniProtKB
Non-traceable author statementⁱ
- 12194824
negative regulation of tubulin deacetylation Source: Ensembl
neuron cellular homeostasis Source: Ensembl
positive regulation of autophagy Source: UniProtKB
positive regulation of cell proliferation
Source: RGD
Inferred from direct assayⁱ
- 17720864
positive regulation of fatty acid oxidation
Source: UniProtKB
Non-traceable author statementⁱ
- 11997383
positive regulation of gluconeogenesis
Source: UniProtKB
Non-traceable author statementⁱ
- 11903059
positive regulation of glucose import
Source: UniProtKB
Non-traceable author statementⁱ
- 11903059
positive regulation of glycolytic process
Source: UniProtKB
Inferred from direct assayⁱ
- 11069105
positive regulation of mitochondrial transcription Source: Ensembl
positive regulation of peptidyl-lysine acetylation Source: Ensembl
positive regulation of protein targeting to mitochondrion Source: Ensembl
positive regulation of skeletal muscle tissue development Source: Ensembl
protein heterooligomerization
Source: RGD
Inferred from direct assayⁱ
- 14511394
protein phosphorylation
Source: RGD
Inferred from direct assayⁱ
- 16648175
- 8955377
regulation of circadian rhythm Source: UniProtKB
regulation of microtubule cytoskeleton organization Source: Ensembl
regulation of peptidyl-serine phosphorylation Source: Ensembl
regulation of stress granule assembly Source: Ensembl
regulation of vesicle-mediated transport
Source: RGD
Inferred from mutant phenotypeⁱ
- 19139597
response to activity
Source: RGD
Inferred from direct assayⁱ
- 17253964
response to caffeine
Source: RGD
Inferred from direct assayⁱ
- 19608206
response to camptothecin Source: Ensembl
response to gamma radiation Source: UniProtKB
response to UV Source: Ensembl
rhythmic process Source: UniProtKB-KW
Wnt signaling pathway Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase
Biological process	Autophagy, Biological rhythms, Cholesterol biosynthesis, Cholesterol metabolism, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism, Transcription, Transcription regulation, Wnt signaling pathway
Ligand	ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.11.1 5301 2.7.11.31 5301
Reactomeⁱ	R-RNO-1632852 Macroautophagy R-RNO-380972 Energy dependent regulation of mTOR by LKB1-AMPK R-RNO-5628897 TP53 Regulates Metabolic Genes R-RNO-6804756 Regulation of TP53 Activity through Phosphorylation
SABIO-RKⁱ	P54645

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 5'-AMP-activated protein kinase catalytic subunit alpha-1 (EC:2.7.11.12 Publications) Short name: AMPK subunit alpha-1 Alternative name(s): Acetyl-CoA carboxylase kinase (EC:2.7.11.271 Publication) Short name: ACACA kinase Hydroxymethylglutaryl-CoA reductase kinase (EC:2.7.11.311 Publication) Short name: HMGCR kinase Tau-protein kinase PRKAA1 (EC:2.7.11.261 Publication)
Gene namesⁱ	Name:Prkaa1 Synonyms:Ampk1
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 2

Organism-specific databases

Rat genome database More...RGDⁱ	3387 Prkaa1

RGDⁱ

3387 Prkaa1

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	183	T → E: Hinders activation. 1 Publication	1
Mutagenesisⁱ	269	T → A: Hinders activation. 1 Publication	1
Mutagenesisⁱ	269	T → D: Retains activation ability. 1 Publication	1
Mutagenesisⁱ	386 – 391	RHTLDE → AHALAA: Allosterically activated by AMP but is not protected against dephosphorylation by AMP or ADP. 1 Publication	6
Mutagenesisⁱ	496	S → A: Hinders activation. 1 Publication	1
Mutagenesisⁱ	496	S → D: Retains activation ability. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL4533

ChEMBLⁱ

CHEMBL4533

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000085593	1 – 559	5'-AMP-activated protein kinase catalytic subunit alpha-1Add BLAST		559

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	32	PhosphothreonineBy similarity	1
Modified residueⁱ	183	Phosphothreonine; by LKB1 and CaMKK25 Publications	1
Modified residueⁱ	269	Phosphothreonine1 Publication	1
Modified residueⁱ	355	PhosphothreonineBy similarity	1
Modified residueⁱ	356	PhosphoserineBy similarity	1
Modified residueⁱ	360	Phosphoserine; by ULK11 Publication	1
Modified residueⁱ	368	Phosphothreonine; by ULK11 Publication	1
Modified residueⁱ	382	PhosphothreonineBy similarity	1
Modified residueⁱ	397	Phosphoserine; by ULK11 Publication	1
Modified residueⁱ	467	PhosphoserineBy similarity	1
Modified residueⁱ	486	PhosphoserineCombined sources	1
Modified residueⁱ	486	Phosphoserine; by ULK1Combined sources1 Publication	1
Modified residueⁱ	488	Phosphothreonine; by ULK11 Publication	1
Modified residueⁱ	490	PhosphothreonineCombined sources	1
Modified residueⁱ	496	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	508	PhosphoserineBy similarity	1
Modified residueⁱ	524	PhosphoserineBy similarity	1
Modified residueⁱ	527	PhosphoserineBy similarity	1

Post-translational modificationⁱ

Ubiquitinated.By similarity

Phosphorylated at Thr-183 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-183 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-183, but at a much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. There is some ambiguity for some phosphosites: Ser-360/Thr-368 and Ser-486/Thr-488. Dephosphorylated by PPM1A and PPM1B (By similarity).By similarity

Keywords - PTMⁱ

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	P54645
PRIDEⁱ	P54645

PTM databases

iPTMnetⁱ	P54645
PhosphoSitePlusⁱ	P54645

Expressionⁱ

Tissue specificityⁱ

Low expression in kidney, liver, lung, heart and brain.

Gene expression databases

Bgeeⁱ	ENSRNOG00000012799 Expressed in 9 organ(s), highest expression level in colon
Genevisibleⁱ	P54645 RN

Interactionⁱ

Subunit structureⁱ

AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2.3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Flcn	Q76JQ2	2	EBI-7596967,EBI-7596839

With

Entry

#Exp.

IntAct

Notes

Flcn

Q76JQ2

2

EBI-7596967,EBI-7596839

GO - Molecular functionⁱ

protein C-terminus binding
Source: RGD
Inferred from physical interactionⁱ
- 15695819

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	249325, 5 interactors
CORUMⁱ	P54645
Database of interacting proteins More...DIPⁱ	DIP-57168N
IntActⁱ	P54645, 314 interactors
Molecular INTeraction database More...MINTⁱ	P54645
STRINGⁱ	10116.ENSRNOP00000017626

Chemistry databases

BindingDBⁱ

P54645

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	27 – 34	Combined sources	8
Beta strandⁱ	37 – 39	Combined sources	3
Beta strandⁱ	41 – 46	Combined sources	6
Turnⁱ	47 – 49	Combined sources	3
Beta strandⁱ	52 – 59	Combined sources	8
Helixⁱ	60 – 63	Combined sources	4
Turnⁱ	64 – 67	Combined sources	4
Helixⁱ	69 – 80	Combined sources	12
Beta strandⁱ	90 – 95	Combined sources	6
Beta strandⁱ	97 – 105	Combined sources	9
Turnⁱ	112 – 117	Combined sources	6
Beta strandⁱ	118 – 121	Combined sources	4
Helixⁱ	124 – 143	Combined sources	20
Beta strandⁱ	146 – 149	Combined sources	4
Beta strandⁱ	155 – 158	Combined sources	4
Beta strandⁱ	164 – 166	Combined sources	3
Helixⁱ	169 – 171	Combined sources	3
Beta strandⁱ	188 – 190	Combined sources	3
Helixⁱ	193 – 196	Combined sources	4
Helixⁱ	204 – 220	Combined sources	17
Helixⁱ	230 – 238	Combined sources	9
Helixⁱ	250 – 259	Combined sources	10
Turnⁱ	264 – 266	Combined sources	3
Helixⁱ	270 – 274	Combined sources	5
Helixⁱ	277 – 280	Combined sources	4
Beta strandⁱ	287 – 289	Combined sources	3
Helixⁱ	301 – 311	Combined sources	11
Helixⁱ	315 – 323	Combined sources	9
Helixⁱ	330 – 347	Combined sources	18
Helixⁱ	349 – 351	Combined sources	3
Helixⁱ	372 – 374	Combined sources	3
Helixⁱ	376 – 381	Combined sources	6
Beta strandⁱ	407 – 413	Combined sources	7
Helixⁱ	417 – 430	Combined sources	14
Beta strandⁱ	434 – 439	Combined sources	6
Beta strandⁱ	442 – 448	Combined sources	7
Turnⁱ	450 – 452	Combined sources	3
Beta strandⁱ	455 – 464	Combined sources	10
Beta strandⁱ	466 – 468	Combined sources	3
Beta strandⁱ	470 – 477	Combined sources	8
Helixⁱ	542 – 555	Combined sources	14

Show more details

3D structure databases

ProteinModelPortalⁱ	P54645
SMRⁱ	P54645
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P54645

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	27 – 279	Protein kinasePROSITE-ProRule annotationAdd BLAST		253

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	302 – 381	AISBy similarityAdd BLAST		80

Domainⁱ

The AIS (autoinhibitory sequence) region shows some sequence similarity with the ubiquitin-associated domains and represses kinase activity.By similarity

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG0586 Eukaryota ENOG410XNQ0 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00930000150880
HOGENOMⁱ	HOG000233016
HOVERGENⁱ	HBG050432
InParanoidⁱ	P54645
KEGG Orthology (KO) More...KOⁱ	K07198
OMAⁱ	QGVRRAK
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03TG
PhylomeDBⁱ	P54645
TreeFamⁱ	TF314032

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd12199 AMPKA1_C, 1 hit
InterProⁱ	View protein in InterPro IPR032270 AMPK_C IPR039137 AMPKA1_C IPR028375 KA1/Ssp2_C IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16579 AdenylateSensor, 1 hit PF00069 Pkinase, 1 hit
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF103243 SSF103243, 1 hit SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P54645-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG 
        60         70         80         90        100
HKVAVKILNR QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI 
       110        120        130        140        150
FMVMEYVSGG ELFDYICKNG RLDEKESRRL FQQILSGVDY CHRHMVVHRD 
       160        170        180        190        200
LKPENVLLDA HMNAKIADFG LSNMMSDGEF LRTSCGSPNY AAPEVISGRL 
       210        220        230        240        250
YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG IFYTPQYLNP 
       260        270        280        290        300
SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID 
       310        320        330        340        350
DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD 
       360        370        380        390        400
FYLATSPPDS FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ 
       410        420        430        440        450
GVRKAKWHLG IRSQSRPNDI MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP 
       460        470        480        490        500
VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE ITEAKSGTAT PQRSGSISNY 
       510        520        530        540        550
RSCQRSDSDA EAQGKPSEVS LTSSVTSLDS SPVDVAPRPG SHTIEFFEMC 

ANLIKILAQ

Length:559

Mass (Da):63,973

Last modified:July 28, 2009 - v2

Checksum:ⁱA869C340A85785ED

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	13 – 14	Missing in AAC52355 (PubMed:8557660).Curated		2
Sequence conflictⁱ	473	D → L AA sequence (PubMed:8557660).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CH474048 Genomic DNA No translation available. U40819 mRNA Translation: AAC52355.1
NCBI Reference Sequences More...RefSeqⁱ	NP_062015.2, NM_019142.2
UniGeneⁱ	Rn.87789

Genome annotation databases

Ensemblⁱ	ENSRNOT00000017626; ENSRNOP00000017626; ENSRNOG00000012799
GeneIDⁱ	65248
KEGGⁱ	rno:65248

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P54645	5'-AMP-activated protein kinase catalytic subunit alpha-1	)	MOUSE		559	UniRef90_Q5EG47
Non-specific serine/threonine protein kinase		DIPOR		697
Non-specific serine/threonine protein kinase		SAIBB		566
Non-specific serine/threonine protein kinase		Florida manatee		565
Non-specific serine/threonine protein kinase		RABIT		564
+87

Protein	Similar proteins		Species	Score	Length	Source
P54645	5'-AMP-activated protein kinase catalytic subunit alpha-1	)	HUMAN		559	UniRef50_Q13131
5'-AMP-activated protein kinase catalytic subunit alpha-2		MOUSE		552
5'-AMP-activated protein kinase catalytic subunit alpha-2		PONAB		552
5'-AMP-activated protein kinase catalytic subunit alpha-2		RAT		552
5'-AMP-activated protein kinase catalytic subunit alpha-2		PIG		552
+467

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CH474048 Genomic DNA No translation available. U40819 mRNA Translation: AAC52355.1
RefSeqⁱ	NP_062015.2, NM_019142.2
UniGeneⁱ	Rn.87789

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2V8Q	X-ray	2.10	A	407-559	[»]
	2V92	X-ray	2.40	A	407-559	[»]
	2V9J	X-ray	2.53	A	407-559	[»]
	2Y8L	X-ray	2.50	A	407-555	[»]
	2Y8Q	X-ray	2.80	A	407-555	[»]
	2YA3	X-ray	2.51	A	407-555	[»]
	4CFH	X-ray	3.24	A	13-481	[»]
				C	535-559	[»]
	4EAI	X-ray	2.28	A	405-479	[»]
				A	540-559	[»]
	4EAJ	X-ray	2.61	A	405-479	[»]
				A	540-559	[»]
	4EAK	X-ray	2.50	A	405-479	[»]
				A	540-559	[»]
	4EAL	X-ray	2.51	A	405-479	[»]
				A	540-559	[»]
	4F2L	X-ray	1.50	A	295-347	[»]
	4QFG	X-ray	3.46	A	11-480	[»]
				A	536-559	[»]
	4QFR	X-ray	3.34	A	11-480	[»]
				A	536-559	[»]
	4QFS	X-ray	3.55	A	11-479	[»]
				A	536-559	[»]
	5KQ5	X-ray	3.41	A	11-480	[»]
				A	536-559	[»]
	5T5T	X-ray	3.46	A	11-480	[»]
				A	536-559	[»]
	5UFU	X-ray	3.45	A	269-559	[»]
	6E4T	X-ray	3.40	A	11-480	[»]
				A	536-559	[»]
	6E4U	X-ray	3.27	A	11-480	[»]
				A	536-559	[»]
	6E4W	X-ray	3.35	A	11-480	[»]
				A	536-559	[»]
ProteinModelPortalⁱ	P54645
SMRⁱ	P54645
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	249325, 5 interactors
CORUMⁱ	P54645
DIPⁱ	DIP-57168N
IntActⁱ	P54645, 314 interactors
MINTⁱ	P54645
STRINGⁱ	10116.ENSRNOP00000017626

Chemistry databases

BindingDBⁱ	P54645
ChEMBLⁱ	CHEMBL4533

PTM databases

iPTMnetⁱ	P54645
PhosphoSitePlusⁱ	P54645

Proteomic databases

PaxDbⁱ	P54645
PRIDEⁱ	P54645

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000017626; ENSRNOP00000017626; ENSRNOG00000012799
GeneIDⁱ	65248
KEGGⁱ	rno:65248

Organism-specific databases

CTDⁱ	5562
RGDⁱ	3387 Prkaa1

Phylogenomic databases

eggNOGⁱ	KOG0586 Eukaryota ENOG410XNQ0 LUCA
GeneTreeⁱ	ENSGT00930000150880
HOGENOMⁱ	HOG000233016
HOVERGENⁱ	HBG050432
InParanoidⁱ	P54645
KOⁱ	K07198
OMAⁱ	QGVRRAK
OrthoDBⁱ	EOG091G03TG
PhylomeDBⁱ	P54645
TreeFamⁱ	TF314032

Enzyme and pathway databases

BRENDAⁱ	2.7.11.1 5301 2.7.11.31 5301
Reactomeⁱ	R-RNO-1632852 Macroautophagy R-RNO-380972 Energy dependent regulation of mTOR by LKB1-AMPK R-RNO-5628897 TP53 Regulates Metabolic Genes R-RNO-6804756 Regulation of TP53 Activity through Phosphorylation
SABIO-RKⁱ	P54645

Miscellaneous databases

EvolutionaryTraceⁱ	P54645
Protein Ontology More...PROⁱ	PR:P54645

Gene expression databases

Bgeeⁱ	ENSRNOG00000012799 Expressed in 9 organ(s), highest expression level in colon
Genevisibleⁱ	P54645 RN

Family and domain databases

CDDⁱ	cd12199 AMPKA1_C, 1 hit
InterProⁱ	View protein in InterPro IPR032270 AMPK_C IPR039137 AMPKA1_C IPR028375 KA1/Ssp2_C IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS
Pfamⁱ	View protein in Pfam PF16579 AdenylateSensor, 1 hit PF00069 Pkinase, 1 hit
SMARTⁱ	View protein in SMART SM00220 S_TKc, 1 hit
SUPFAMⁱ	SSF103243 SSF103243, 1 hit SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in PROSITE PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AAPK1_RAT
Accessionⁱ	P54645Primary (citable) accession number: P54645
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
	Last sequence update:	July 28, 2009
	Last modified:	November 7, 2018
	This is version 181 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - P54645 (AAPK1_RAT)

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5'-AMP-activated protein kinase catalytic subunit alpha-1

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