UniProtKB - Q5EG47 (AAPK1_MOUSE)
Protein
5'-AMP-activated protein kinase catalytic subunit alpha-1
Gene
Prkaa1
Organism
Mus musculus (Mouse)
Status
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 that process also activates WDR45. In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (PubMed:23283301). 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 SLC12A1.13 Publications
Catalytic activityi
- EC:2.7.11.1By similarity
- EC:2.7.11.1By similarity
- ATP + L-seryl-[acetyl-CoA carboxylase] = ADP + H+ + O-phospho-L-seryl-[acetyl-CoA carboxylase]By similarityEC:2.7.11.27By similarity
- ATP + L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase] = ADP + H+ + O-phospho-L-seryl-[3-hydroxy-3-methylglutaryl-coenzyme A reductase]By similarityEC:2.7.11.31By similarity
- EC:2.7.11.26
- EC:2.7.11.26
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.3 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
- ATP binding Source: MGI
- chromatin binding Source: UniProtKB
- histone serine kinase activity Source: UniProtKB
- kinase binding Source: MGI
- metal ion binding Source: UniProtKB-KW
- protein-containing complex binding Source: MGI
- protein C-terminus binding Source: MGI
- protein kinase activity Source: MGI
- protein serine/threonine kinase activity Source: MGI
- protein serine kinase activity Source: UniProtKB-EC
- protein threonine kinase activity Source: UniProtKB-EC
- tau-protein kinase activity Source: UniProtKB-EC
GO - Biological processi
- autophagy Source: UniProtKB-KW
- bile acid and bile salt transport Source: Ensembl
- bile acid signaling pathway Source: Ensembl
- CAMKK-AMPK signaling cascade Source: MGI
- cellular response to calcium ion Source: ARUK-UCL
- cellular response to drug Source: Ensembl
- cellular response to ethanol Source: Ensembl
- cellular response to glucose starvation Source: UniProtKB
- cellular response to glucose stimulus Source: ARUK-UCL
- cellular response to hydrogen peroxide Source: Ensembl
- cellular response to hypoxia Source: Ensembl
- cellular response to nutrient levels Source: UniProtKB
- cellular response to organonitrogen compound Source: Ensembl
- cellular response to oxidative stress Source: ARUK-UCL
- cellular response to prostaglandin E stimulus Source: MGI
- cholesterol biosynthetic process Source: UniProtKB-KW
- cold acclimation Source: MGI
- energy homeostasis Source: UniProtKB
- fatty acid biosynthetic process Source: UniProtKB-KW
- fatty acid homeostasis Source: UniProtKB
- fatty acid oxidation Source: MGI
- glucose homeostasis Source: UniProtKB
- glucose metabolic process Source: MGI
- intracellular signal transduction Source: GO_Central
- lipid biosynthetic process Source: UniProtKB
- motor behavior Source: MGI
- negative regulation of apoptotic process Source: UniProtKB
- negative regulation of gene expression Source: ARUK-UCL
- negative regulation of insulin receptor signaling pathway Source: MGI
- negative regulation of lipid catabolic process Source: UniProtKB
- negative regulation of TOR signaling Source: UniProtKB
- negative regulation of tubulin deacetylation Source: ARUK-UCL
- neuron cellular homeostasis Source: MGI
- positive regulation of autophagy Source: UniProtKB
- positive regulation of cell population proliferation Source: MGI
- positive regulation of cellular protein localization Source: ARUK-UCL
- positive regulation of gene expression Source: MGI
- positive regulation of glycolytic process Source: UniProtKB
- positive regulation of mitochondrial transcription Source: UniProtKB
- positive regulation of peptidyl-lysine acetylation Source: ARUK-UCL
- positive regulation of protein targeting to mitochondrion Source: UniProtKB
- positive regulation of skeletal muscle tissue development Source: MGI
- protein phosphorylation Source: MGI
- regulation of bile acid secretion Source: Ensembl
- regulation of circadian rhythm Source: UniProtKB
- regulation of microtubule cytoskeleton organization Source: ARUK-UCL
- regulation of peptidyl-serine phosphorylation Source: MGI
- regulation of stress granule assembly Source: ARUK-UCL
- regulation of vesicle-mediated transport Source: MGI
- response to 17alpha-ethynylestradiol Source: Ensembl
- response to activity Source: MGI
- response to caffeine Source: MGI
- response to camptothecin Source: UniProtKB
- response to gamma radiation Source: UniProtKB
- response to hydrogen peroxide Source: UniProtKB
- response to UV Source: UniProtKB
- rhythmic process Source: UniProtKB-KW
- Wnt signaling pathway Source: UniProtKB-KW
Keywordsi
Enzyme and pathway databases
Reactomei | R-MMU-1632852, Macroautophagy R-MMU-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-MMU-5628897, TP53 Regulates Metabolic Genes R-MMU-6804756, Regulation of TP53 Activity through Phosphorylation |
Names & Taxonomyi
Protein namesi | Recommended name: 5'-AMP-activated protein kinase catalytic subunit alpha-1 (EC:2.7.11.1By similarity)Short name: AMPK subunit alpha-1 Alternative name(s): |
Gene namesi | Name:Prkaa1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:2145955, Prkaa1 |
Subcellular locationi
Cytosol
- cytosol Source: MGI
Nucleus
- nuclear speck Source: MGI
- nucleus Source: UniProtKB
Plasma Membrane
- apical plasma membrane Source: MGI
Other locations
- axon Source: ARUK-UCL
- cytoplasm Source: ARUK-UCL
- dendrite Source: ARUK-UCL
- neuronal cell body Source: ARUK-UCL
- nucleotide-activated protein kinase complex Source: UniProtKB
- protein-containing complex Source: MGI
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 168 | D → A: Loss of kinase activity. 2 Publications | 1 |
Chemistry databases
ChEMBLi | CHEMBL1075161 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000085590 | 1 – 559 | 5'-AMP-activated protein kinase catalytic subunit alpha-1Add BLAST | 559 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 32 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 183 | Phosphothreonine; by LKB1 and CaMKK23 Publications | 1 | |
Modified residuei | 355 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 356 | PhosphoserineBy similarity | 1 | |
Modified residuei | 360 | Phosphoserine; by ULK1By similarity | 1 | |
Modified residuei | 368 | Phosphothreonine; by ULK1By similarity | 1 | |
Modified residuei | 382 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 397 | Phosphoserine; by ULK1By similarity | 1 | |
Modified residuei | 467 | PhosphoserineBy similarity | 1 | |
Modified residuei | 486 | PhosphoserineCombined sources | 1 | |
Modified residuei | 488 | Phosphothreonine; by ULK1By similarity | 1 | |
Modified residuei | 490 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 496 | PhosphoserineCombined sources | 1 | |
Modified residuei | 508 | PhosphoserineBy similarity | 1 | |
Modified residuei | 524 | PhosphoserineBy similarity | 1 | |
Modified residuei | 527 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
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. Dephosphorylated by PPM1A and PPM1B (By similarity).By similarity
Ubiquitinated.1 Publication
Keywords - PTMi
Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q5EG47 |
jPOSTi | Q5EG47 |
MaxQBi | Q5EG47 |
PaxDbi | Q5EG47 |
PRIDEi | Q5EG47 |
PTM databases
CarbonylDBi | Q5EG47 |
iPTMneti | Q5EG47 |
PhosphoSitePlusi | Q5EG47 |
SwissPalmi | Q5EG47 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000050697, Expressed in islet of Langerhans and 256 other tissues |
ExpressionAtlasi | Q5EG47, baseline and differential |
Genevisiblei | Q5EG47, MM |
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.
Binary interactionsi
Q5EG47
With | #Exp. | IntAct |
---|---|---|
YAP1 [P46937] from Homo sapiens. | 2 | EBI-7282395,EBI-1044059 |
GO - Molecular functioni
- kinase binding Source: MGI
- protein C-terminus binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 222923, 34 interactors |
ComplexPortali | CPX-5698, AMPK complex, alpha1-beta1-gamma1 variant CPX-5849, AMPK complex, alpha1-beta1-gamma2 variant CPX-5853, AMPK complex, alpha1-beta2-gamma1 variant CPX-5855, AMPK complex, alpha1-beta2-gamma3 variant CPX-5856, AMPK complex, alpha1-beta1-gamma3 variant CPX-5860, AMPK complex, alpha1-beta2-gamma2 variant |
CORUMi | Q5EG47 |
DIPi | DIP-47622N |
IntActi | Q5EG47, 27 interactors |
MINTi | Q5EG47 |
STRINGi | 10090.ENSMUSP00000063166 |
Miscellaneous databases
RNActi | Q5EG47, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q5EG47 |
ModBasei | Search... |
PDBe-KBi | Search... |
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 | KOG0583, Eukaryota |
GeneTreei | ENSGT00940000158865 |
HOGENOMi | CLU_000288_59_3_1 |
InParanoidi | Q5EG47 |
OrthoDBi | 1127668at2759 |
PhylomeDBi | Q5EG47 |
TreeFami | TF314032 |
Family and domain databases
CDDi | cd12199, AMPKA1_C, 1 hit cd14403, UBA_AID_AAPK1, 1 hit |
InterProi | View protein in InterPro IPR032270, AMPK_C IPR039137, AMPKA1_C IPR028375, KA1/Ssp2_C IPR011009, Kinase-like_dom_sf IPR028797, PRKAA1_UBA 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 |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
Q5EG47-1 [UniParc]FASTAAdd to basket
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 QVDPMKRAAI 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 EAQGKPSDVS LTSSVTSLDS SPVDVAPRPG SHTIEFFEMC
ANLIKILAQ
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketQ3TUQ7 | Q3TUQ7_MOUSE | Acetyl-CoA carboxylase kinase | Prkaa1 | 550 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 11 – 12 | Missing in AAW79567 (Ref. 2) Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AC131919 Genomic DNA No translation available. AC135079 Genomic DNA No translation available. AY885266 mRNA Translation: AAW79567.1 |
CCDSi | CCDS49574.1 |
RefSeqi | NP_001013385.3, NM_001013367.3 |
Genome annotation databases
Ensembli | ENSMUST00000051186; ENSMUSP00000063166; ENSMUSG00000050697 |
GeneIDi | 105787 |
KEGGi | mmu:105787 |
UCSCi | uc007vct.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AC131919 Genomic DNA No translation available. AC135079 Genomic DNA No translation available. AY885266 mRNA Translation: AAW79567.1 |
CCDSi | CCDS49574.1 |
RefSeqi | NP_001013385.3, NM_001013367.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5UFU | X-ray | 3.45 | A | 11-480 | [»] | |
A | 536-559 | [»] | ||||
SMRi | Q5EG47 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 222923, 34 interactors |
ComplexPortali | CPX-5698, AMPK complex, alpha1-beta1-gamma1 variant CPX-5849, AMPK complex, alpha1-beta1-gamma2 variant CPX-5853, AMPK complex, alpha1-beta2-gamma1 variant CPX-5855, AMPK complex, alpha1-beta2-gamma3 variant CPX-5856, AMPK complex, alpha1-beta1-gamma3 variant CPX-5860, AMPK complex, alpha1-beta2-gamma2 variant |
CORUMi | Q5EG47 |
DIPi | DIP-47622N |
IntActi | Q5EG47, 27 interactors |
MINTi | Q5EG47 |
STRINGi | 10090.ENSMUSP00000063166 |
Chemistry databases
ChEMBLi | CHEMBL1075161 |
PTM databases
CarbonylDBi | Q5EG47 |
iPTMneti | Q5EG47 |
PhosphoSitePlusi | Q5EG47 |
SwissPalmi | Q5EG47 |
Proteomic databases
EPDi | Q5EG47 |
jPOSTi | Q5EG47 |
MaxQBi | Q5EG47 |
PaxDbi | Q5EG47 |
PRIDEi | Q5EG47 |
Protocols and materials databases
Antibodypediai | 3564, 1400 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000051186; ENSMUSP00000063166; ENSMUSG00000050697 |
GeneIDi | 105787 |
KEGGi | mmu:105787 |
UCSCi | uc007vct.1, mouse |
Organism-specific databases
CTDi | 5562 |
MGIi | MGI:2145955, Prkaa1 |
Phylogenomic databases
eggNOGi | KOG0583, Eukaryota |
GeneTreei | ENSGT00940000158865 |
HOGENOMi | CLU_000288_59_3_1 |
InParanoidi | Q5EG47 |
OrthoDBi | 1127668at2759 |
PhylomeDBi | Q5EG47 |
TreeFami | TF314032 |
Enzyme and pathway databases
Reactomei | R-MMU-1632852, Macroautophagy R-MMU-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-MMU-5628897, TP53 Regulates Metabolic Genes R-MMU-6804756, Regulation of TP53 Activity through Phosphorylation |
Miscellaneous databases
BioGRID-ORCSi | 105787, 4 hits in 20 CRISPR screens |
ChiTaRSi | Prkaa1, mouse |
PROi | PR:Q5EG47 |
RNActi | Q5EG47, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000050697, Expressed in islet of Langerhans and 256 other tissues |
ExpressionAtlasi | Q5EG47, baseline and differential |
Genevisiblei | Q5EG47, MM |
Family and domain databases
CDDi | cd12199, AMPKA1_C, 1 hit cd14403, UBA_AID_AAPK1, 1 hit |
InterProi | View protein in InterPro IPR032270, AMPK_C IPR039137, AMPKA1_C IPR028375, KA1/Ssp2_C IPR011009, Kinase-like_dom_sf IPR028797, PRKAA1_UBA 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... |
MobiDBi | Search... |
Entry informationi
Entry namei | AAPK1_MOUSE | |
Accessioni | Q5EG47Primary (citable) accession number: Q5EG47 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 13, 2005 |
Last sequence update: | July 28, 2009 | |
Last modified: | February 10, 2021 | |
This is version 152 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human and mouse protein kinases
Human and mouse protein kinases: classification and index