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Protein

5'-AMP-activated protein kinase catalytic subunit alpha-2

Gene

PRKAA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Involved in insulin receptor/INSR internalization (PubMed:25687571). 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. 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 phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation. Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1 (By similarity).By similarity13 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity
ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate.By similarity
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate.By similarity

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by phosphorylation on Thr-172. Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or PRKAG3) results in allosteric activation, inducing phosphorylation on Thr-172. AMP-binding to gamma subunit also sustains activity by preventing dephosphorylation of Thr-172. ADP also stimulates Thr-172 phosphorylation, without stimulating already phosphorylated AMPK. ATP promotes dephosphorylation of Thr-172, 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. AMPK is activated by antihyperglycemic drug metformin, a drug prescribed to patients with type 2 diabetes: in vivo, metformin seems to mainly inhibit liver gluconeogenesis. However, metformin can be used to activate AMPK in muscle and other cells in culture or ex vivo (PubMed:11602624). 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. Salicylate/aspirin directly activates kinase activity, primarily by inhibiting Thr-172 dephosphorylation.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45ATPPROSITE-ProRule annotation1
Active sitei139Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi22 – 30ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS08671-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-1632852. Macroautophagy.
R-HSA-163680. AMPK inhibits chREBP transcriptional activation activity.
R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-HSA-2151209. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
SignaLinkiP54646.
SIGNORiP54646.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase catalytic subunit alpha-2 (EC:2.7.11.1By similarity)
Short name:
AMPK subunit alpha-2
Alternative name(s):
Acetyl-CoA carboxylase kinase (EC:2.7.11.27By similarity)
Short name:
ACACA kinase
Hydroxymethylglutaryl-CoA reductase kinase (EC:2.7.11.31By similarity)
Short name:
HMGCR kinase
Gene namesi
Name:PRKAA2
Synonyms:AMPK, AMPK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9377. PRKAA2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi172T → D: Phosphomimetic mutant. 1

Organism-specific databases

DisGeNETi5563.
OpenTargetsiENSG00000162409.
PharmGKBiPA33745.

Chemistry databases

ChEMBLiCHEMBL2116.
DrugBankiDB00945. Acetylsalicylic acid.
GuidetoPHARMACOLOGYi1542.

Polymorphism and mutation databases

BioMutaiPRKAA2.
DMDMi20178276.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000855941 – 5525'-AMP-activated protein kinase catalytic subunit alpha-2Add BLAST552

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei172Phosphothreonine; by LKB1 and CaMKK21 Publication1
Modified residuei258PhosphothreonineBy similarity1
Modified residuei377PhosphoserineCombined sources1
Modified residuei491PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated.By similarity
Phosphorylated at Thr-172 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-172 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Dephosphorylated by PPM1A and PPM1B at Thr-172 (mediated by STK11/LKB1).2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP54646.
MaxQBiP54646.
PaxDbiP54646.
PeptideAtlasiP54646.
PRIDEiP54646.

PTM databases

iPTMnetiP54646.
PhosphoSitePlusiP54646.

Expressioni

Gene expression databases

BgeeiENSG00000162409.
CleanExiHS_PRKAA2.
ExpressionAtlasiP54646. baseline and differential.
GenevisibleiP54646. HS.

Organism-specific databases

HPAiHPA044540.

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. Associates with internalized insulin receptor/INSR complexes on Golgi/endosomal membranes; PRKAA2/AMPK2 together with ATIC and HACD3/PTPLAD1 is proposed to be part of a signaling network regulating INSR autophosphorylation and endocytosis (PubMed:25687571).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI2Q9NYB93EBI-1383852,EBI-743598
AESQ081173EBI-1383852,EBI-717810
AIMP2Q131553EBI-1383852,EBI-745226
APPBP2Q926243EBI-1383852,EBI-743771
CCNB1IP1Q9NPC33EBI-1383852,EBI-745269
FOSQ6FG413EBI-1383852,EBI-10198738
GLI1P081513EBI-1383852,EBI-308084
HMBOX1Q6NT763EBI-1383852,EBI-2549423
HOMEZQ8IX15-33EBI-1383852,EBI-10172004
KCTD1Q719H93EBI-1383852,EBI-9027502
KIF24Q5T7B8-23EBI-1383852,EBI-10213781
KIFC3Q9BVG84EBI-1383852,EBI-2125614
KRT31Q153233EBI-1383852,EBI-948001
L3MBTL3Q96JM73EBI-1383852,EBI-2686809
NECAB2H3BTW23EBI-1383852,EBI-10172876
NONOQ15233-23EBI-1383852,EBI-10203843
NOTCH2NLQ7Z3S93EBI-1383852,EBI-945833
NUTM1Q86Y263EBI-1383852,EBI-10178410
PRKAB1Q9Y4783EBI-1383852,EBI-719769
PRKAB2O4374111EBI-1383852,EBI-1053424
PRKAG1P546199EBI-1383852,EBI-1181439
RBPMSQ930623EBI-1383852,EBI-740322
RFX6Q8HWS33EBI-1383852,EBI-746118
TCF4P158843EBI-1383852,EBI-533224
TRIP6Q156543EBI-1383852,EBI-742327
TSC22D4Q9Y3Q83EBI-1383852,EBI-739485
USHBP1Q8N6Y03EBI-1383852,EBI-739895
VPS52Q8N1B43EBI-1383852,EBI-2799833
ZBTB8AQ96BR93EBI-1383852,EBI-742740
ZNF397Q8NF993EBI-1383852,EBI-10213894

Protein-protein interaction databases

BioGridi111550. 83 interactors.
DIPiDIP-39796N.
IntActiP54646. 110 interactors.
MINTiMINT-2804161.
STRINGi9606.ENSP00000360290.

Chemistry databases

BindingDBiP54646.

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 24Combined sources9
Beta strandi26 – 35Combined sources10
Turni36 – 38Combined sources3
Beta strandi41 – 48Combined sources8
Helixi49 – 54Combined sources6
Helixi58 – 69Combined sources12
Beta strandi79 – 84Combined sources6
Beta strandi86 – 94Combined sources9
Helixi101 – 108Combined sources8
Helixi113 – 133Combined sources21
Helixi142 – 144Combined sources3
Beta strandi145 – 147Combined sources3
Beta strandi153 – 155Combined sources3
Helixi160 – 162Combined sources3
Turni177 – 179Combined sources3
Helixi183 – 185Combined sources3
Helixi192 – 209Combined sources18
Helixi219 – 228Combined sources10
Helixi239 – 248Combined sources10
Helixi253 – 255Combined sources3
Helixi259 – 264Combined sources6
Helixi266 – 269Combined sources4
Helixi274 – 276Combined sources3
Helixi283 – 286Combined sources4
Turni291 – 295Combined sources5
Helixi304 – 311Combined sources8
Helixi323 – 336Combined sources14
Helixi338 – 341Combined sources4
Beta strandi403 – 408Combined sources6
Helixi412 – 425Combined sources14
Beta strandi429 – 443Combined sources15
Turni445 – 447Combined sources3
Beta strandi450 – 460Combined sources11
Turni461 – 463Combined sources3
Beta strandi464 – 471Combined sources8
Helixi535 – 549Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H6DX-ray1.85A6-279[»]
2LTUNMR-A282-339[»]
2YZAX-ray3.02A6-279[»]
3AQVX-ray2.08A6-279[»]
4CFEX-ray3.02A/C1-552[»]
4CFFX-ray3.92A/C1-552[»]
4ZHXX-ray2.99A/C2-552[»]
5EZVX-ray2.99A/C2-347[»]
A/C397-552[»]
ProteinModelPortaliP54646.
SMRiP54646.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54646.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 268Protein kinasePROSITE-ProRule annotationAdd BLAST253

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni291 – 376AISBy similarityAdd BLAST86

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0586. Eukaryota.
ENOG410XNQ0. LUCA.
GeneTreeiENSGT00790000122947.
HOGENOMiHOG000233016.
HOVERGENiHBG050432.
KOiK07198.
OMAiKALNYEW.
PhylomeDBiP54646.
TreeFamiTF314032.

Family and domain databases

InterProiIPR032270. AMPK_C.
IPR028375. KA1/Ssp2_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF16579. AdenylateSensor. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ
60 70 80 90 100
KIRSLDVVGK IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE
110 120 130 140 150
LFDYICKHGR VEEMEARRLF QQILSAVDYC HRHMVVHRDL KPENVLLDAH
160 170 180 190 200
MNAKIADFGL SNMMSDGEFL RTSCGSPNYA APEVISGRLY AGPEVDIWSC
210 220 230 240 250
GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPEYLNRS VATLLMHMLQ
260 270 280 290 300
VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF
310 320 330 340 350
ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS
360 370 380 390 400
FMDDSAMHIP PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA
410 420 430 440 450
KWHLGIRSQS KPYDIMAEVY RAMKQLDFEW KVVNAYHLRV RRKNPVTGNY
460 470 480 490 500
VKMSLQLYLV DNRSYLLDFK SIDDEVVEQR SGSSTPQRSC SAAGLHRPRS
510 520 530 540 550
SFDSTTAESH SLSGSLTGSL TGSTLSSVSP RLGSHTMDFF EMCASLITTL

AR
Length:552
Mass (Da):62,320
Last modified:April 16, 2002 - v2
Checksum:iC46AAFC1D5104975
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti180A → T in AAA64745 (PubMed:7959015).Curated1
Sequence conflicti271D → G in AAA64745 (PubMed:7959015).Curated1
Sequence conflicti403 – 404HL → RQ in AAA64745 (PubMed:7959015).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035623371P → T in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. 2 Publications1
Natural variantiVAR_040355407R → Q in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_035624523S → G in a breast cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06454 mRNA. Translation: AAA64745.1.
AL035705 Genomic DNA. Translation: CAC17574.2.
BC069680 mRNA. Translation: AAH69680.1.
BC069740 mRNA. Translation: AAH69740.1.
BC069823 mRNA. Translation: AAH69823.1.
CCDSiCCDS605.1.
PIRiS51025.
RefSeqiNP_006243.2. NM_006252.3.
UniGeneiHs.437039.

Genome annotation databases

EnsembliENST00000371244; ENSP00000360290; ENSG00000162409.
GeneIDi5563.
KEGGihsa:5563.
UCSCiuc001cyk.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06454 mRNA. Translation: AAA64745.1.
AL035705 Genomic DNA. Translation: CAC17574.2.
BC069680 mRNA. Translation: AAH69680.1.
BC069740 mRNA. Translation: AAH69740.1.
BC069823 mRNA. Translation: AAH69823.1.
CCDSiCCDS605.1.
PIRiS51025.
RefSeqiNP_006243.2. NM_006252.3.
UniGeneiHs.437039.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H6DX-ray1.85A6-279[»]
2LTUNMR-A282-339[»]
2YZAX-ray3.02A6-279[»]
3AQVX-ray2.08A6-279[»]
4CFEX-ray3.02A/C1-552[»]
4CFFX-ray3.92A/C1-552[»]
4ZHXX-ray2.99A/C2-552[»]
5EZVX-ray2.99A/C2-347[»]
A/C397-552[»]
ProteinModelPortaliP54646.
SMRiP54646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111550. 83 interactors.
DIPiDIP-39796N.
IntActiP54646. 110 interactors.
MINTiMINT-2804161.
STRINGi9606.ENSP00000360290.

Chemistry databases

BindingDBiP54646.
ChEMBLiCHEMBL2116.
DrugBankiDB00945. Acetylsalicylic acid.
GuidetoPHARMACOLOGYi1542.

PTM databases

iPTMnetiP54646.
PhosphoSitePlusiP54646.

Polymorphism and mutation databases

BioMutaiPRKAA2.
DMDMi20178276.

Proteomic databases

EPDiP54646.
MaxQBiP54646.
PaxDbiP54646.
PeptideAtlasiP54646.
PRIDEiP54646.

Protocols and materials databases

DNASUi5563.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371244; ENSP00000360290; ENSG00000162409.
GeneIDi5563.
KEGGihsa:5563.
UCSCiuc001cyk.5. human.

Organism-specific databases

CTDi5563.
DisGeNETi5563.
GeneCardsiPRKAA2.
HGNCiHGNC:9377. PRKAA2.
HPAiHPA044540.
MIMi600497. gene.
neXtProtiNX_P54646.
OpenTargetsiENSG00000162409.
PharmGKBiPA33745.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0586. Eukaryota.
ENOG410XNQ0. LUCA.
GeneTreeiENSGT00790000122947.
HOGENOMiHOG000233016.
HOVERGENiHBG050432.
KOiK07198.
OMAiKALNYEW.
PhylomeDBiP54646.
TreeFamiTF314032.

Enzyme and pathway databases

BioCyciZFISH:HS08671-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-1632852. Macroautophagy.
R-HSA-163680. AMPK inhibits chREBP transcriptional activation activity.
R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-HSA-2151209. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
SignaLinkiP54646.
SIGNORiP54646.

Miscellaneous databases

ChiTaRSiPRKAA2. human.
EvolutionaryTraceiP54646.
GeneWikiiPRKAA2.
GenomeRNAii5563.
PROiP54646.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000162409.
CleanExiHS_PRKAA2.
ExpressionAtlasiP54646. baseline and differential.
GenevisibleiP54646. HS.

Family and domain databases

InterProiIPR032270. AMPK_C.
IPR028375. KA1/Ssp2_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF16579. AdenylateSensor. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAAPK2_HUMAN
AccessioniPrimary (citable) accession number: P54646
Secondary accession number(s): Q9H1E8, Q9UD43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 16, 2002
Last modified: November 30, 2016
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.