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Protein

5'-AMP-activated protein kinase subunit beta-2

Gene

PRKAB2

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

Functioni

Non-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. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywordsi

Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciZFISH:ENSG00000131791-MONOMER.
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.
SignaLinkiO43741.
SIGNORiO43741.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit beta-2
Short name:
AMPK subunit beta-2
Gene namesi
Name:PRKAB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9379. PRKAB2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleotide-activated protein kinase complex Source: UniProtKB

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi235H → A: Results in an AMPK enzyme that is activable by phosphorylation but has significantly increased rate of dephosphorylation in phosphatase assays. 1 Publication1

Organism-specific databases

DisGeNETi5565.
OpenTargetsiENSG00000131791.
PharmGKBiPA33747.

Chemistry databases

ChEMBLiCHEMBL3038456.
DrugBankiDB00945. Acetylsalicylic acid.
DB00131. Adenosine monophosphate.
GuidetoPHARMACOLOGYi1544.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002043681 – 2725'-AMP-activated protein kinase subunit beta-2Add BLAST272

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei39Phosphoserine; by ULK11 Publication1
Modified residuei40Phosphothreonine; by ULK11 Publication1
Modified residuei69Phosphoserine; by ULK1By similarity1
Modified residuei95PhosphoserineCombined sources1
Modified residuei108PhosphoserineCombined sources1
Modified residuei148PhosphothreonineCombined sources1
Modified residuei158PhosphoserineCombined sources1
Modified residuei170PhosphoserineCombined sources1
Modified residuei174PhosphoserineBy similarity1
Modified residuei184PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). 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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43741.
PaxDbiO43741.
PeptideAtlasiO43741.
PRIDEiO43741.

PTM databases

iPTMnetiO43741.
PhosphoSitePlusiO43741.

Expressioni

Gene expression databases

BgeeiENSG00000131791.
CleanExiHS_PRKAB2.
GenevisibleiO43741. HS.

Organism-specific databases

HPAiHPA044342.

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).2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi111552. 99 interactors.
DIPiDIP-39763N.
IntActiO43741. 101 interactors.
STRINGi9606.ENSP00000254101.

Structurei

Secondary structure

1272
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi76 – 83Combined sources8
Beta strandi90 – 94Combined sources5
Helixi95 – 97Combined sources3
Beta strandi112 – 129Combined sources18
Beta strandi132 – 134Combined sources3
Beta strandi141 – 143Combined sources3
Beta strandi149 – 155Combined sources7
Turni159 – 162Combined sources4
Beta strandi201 – 204Combined sources4
Helixi210 – 213Combined sources4
Beta strandi214 – 217Combined sources4
Turni236 – 239Combined sources4
Beta strandi242 – 244Combined sources3
Beta strandi250 – 259Combined sources10
Beta strandi262 – 271Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F15X-ray2.00A69-163[»]
2V8QX-ray2.10B187-272[»]
2V92X-ray2.40B187-272[»]
2V9JX-ray2.53B187-272[»]
2Y8LX-ray2.50B187-272[»]
2Y8QX-ray2.80B187-270[»]
2YA3X-ray2.51B187-272[»]
4CFHX-ray3.24B187-272[»]
4EAIX-ray2.28B189-272[»]
4EAJX-ray2.61B189-272[»]
4RERX-ray4.05B76-272[»]
4REWX-ray4.58B76-272[»]
ProteinModelPortaliO43741.
SMRiO43741.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43741.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
KOiK07199.
OMAiGERHGTK.
OrthoDBiEOG091G0DZR.
PhylomeDBiO43741.
TreeFamiTF313827.

Family and domain databases

InterProiIPR032640. AMPK1_CBM.
IPR030081. AMPK_beta-2.
IPR006828. ASC_dom.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10343:SF43. PTHR10343:SF43. 1 hit.
PfamiPF16561. AMPK1_CBM. 1 hit.
PF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43741-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGNTTSDRVS GERHGAKAAR SEGAGGHAPG KEHKIMVGST DDPSVFSLPD
60 70 80 90 100
SKLPGDKEFV SWQQDLEDSV KPTQQARPTV IRWSEGGKEV FISGSFNNWS
110 120 130 140 150
TKIPLIKSHN DFVAILDLPE GEHQYKFFVD GQWVHDPSEP VVTSQLGTIN
160 170 180 190 200
NLIHVKKSDF EVFDALKLDS MESSETSCRD LSSSPPGPYG QEMYAFRSEE
210 220 230 240 250
RFKSPPILPP HLLQVILNKD TNISCDPALL PEPNHVMLNH LYALSIKDSV
260 270
MVLSATHRYK KKYVTTLLYK PI
Length:272
Mass (Da):30,302
Last modified:June 1, 1998 - v1
Checksum:i42B23BD70B92519C
GO
Isoform 2 (identifier: O43741-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MGNTTSDRVSGERHGAKAARSEGAG → MPRGRSTRSWWGVRTTPACSASLTP
     26-107: Missing.

Note: No experimental confirmation available.
Show »
Length:190
Mass (Da):21,485
Checksum:iBB41913AB4FDEB54
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0558201 – 25MGNTT…SEGAG → MPRGRSTRSWWGVRTTPACS ASLTP in isoform 2. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_05582126 – 107Missing in isoform 2. 1 PublicationAdd BLAST82

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224538 mRNA. Translation: CAA12030.1.
AF504543
, AF504538, AF504539, AF504540, AF504541, AF504542 Genomic DNA. Translation: AAM74153.1.
AK292820 mRNA. Translation: BAF85509.1.
AK294863 mRNA. Translation: BAG57967.1.
AK316005 mRNA. Translation: BAH14376.1.
AL356378 Genomic DNA. Translation: CAH72644.1.
CH471223 Genomic DNA. Translation: EAW50945.1.
BC053610 mRNA. Translation: AAH53610.1.
CCDSiCCDS925.1. [O43741-1]
RefSeqiNP_005390.1. NM_005399.4. [O43741-1]
UniGeneiHs.50732.

Genome annotation databases

EnsembliENST00000254101; ENSP00000254101; ENSG00000131791. [O43741-1]
GeneIDi5565.
KEGGihsa:5565.
UCSCiuc001epe.5. human. [O43741-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224538 mRNA. Translation: CAA12030.1.
AF504543
, AF504538, AF504539, AF504540, AF504541, AF504542 Genomic DNA. Translation: AAM74153.1.
AK292820 mRNA. Translation: BAF85509.1.
AK294863 mRNA. Translation: BAG57967.1.
AK316005 mRNA. Translation: BAH14376.1.
AL356378 Genomic DNA. Translation: CAH72644.1.
CH471223 Genomic DNA. Translation: EAW50945.1.
BC053610 mRNA. Translation: AAH53610.1.
CCDSiCCDS925.1. [O43741-1]
RefSeqiNP_005390.1. NM_005399.4. [O43741-1]
UniGeneiHs.50732.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F15X-ray2.00A69-163[»]
2V8QX-ray2.10B187-272[»]
2V92X-ray2.40B187-272[»]
2V9JX-ray2.53B187-272[»]
2Y8LX-ray2.50B187-272[»]
2Y8QX-ray2.80B187-270[»]
2YA3X-ray2.51B187-272[»]
4CFHX-ray3.24B187-272[»]
4EAIX-ray2.28B189-272[»]
4EAJX-ray2.61B189-272[»]
4RERX-ray4.05B76-272[»]
4REWX-ray4.58B76-272[»]
ProteinModelPortaliO43741.
SMRiO43741.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111552. 99 interactors.
DIPiDIP-39763N.
IntActiO43741. 101 interactors.
STRINGi9606.ENSP00000254101.

Chemistry databases

ChEMBLiCHEMBL3038456.
DrugBankiDB00945. Acetylsalicylic acid.
DB00131. Adenosine monophosphate.
GuidetoPHARMACOLOGYi1544.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

iPTMnetiO43741.
PhosphoSitePlusiO43741.

Proteomic databases

MaxQBiO43741.
PaxDbiO43741.
PeptideAtlasiO43741.
PRIDEiO43741.

Protocols and materials databases

DNASUi5565.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254101; ENSP00000254101; ENSG00000131791. [O43741-1]
GeneIDi5565.
KEGGihsa:5565.
UCSCiuc001epe.5. human. [O43741-1]

Organism-specific databases

CTDi5565.
DisGeNETi5565.
GeneCardsiPRKAB2.
HGNCiHGNC:9379. PRKAB2.
HPAiHPA044342.
MIMi602741. gene.
neXtProtiNX_O43741.
OpenTargetsiENSG00000131791.
PharmGKBiPA33747.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
KOiK07199.
OMAiGERHGTK.
OrthoDBiEOG091G0DZR.
PhylomeDBiO43741.
TreeFamiTF313827.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000131791-MONOMER.
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.
SignaLinkiO43741.
SIGNORiO43741.

Miscellaneous databases

ChiTaRSiPRKAB2. human.
EvolutionaryTraceiO43741.
GeneWikiiPRKAB2.
GenomeRNAii5565.
PROiO43741.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000131791.
CleanExiHS_PRKAB2.
GenevisibleiO43741. HS.

Family and domain databases

InterProiIPR032640. AMPK1_CBM.
IPR030081. AMPK_beta-2.
IPR006828. ASC_dom.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10343:SF43. PTHR10343:SF43. 1 hit.
PfamiPF16561. AMPK1_CBM. 1 hit.
PF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAAKB2_HUMAN
AccessioniPrimary (citable) accession number: O43741
Secondary accession number(s): A8K9V5, B4DH06, Q5VXY0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: January 18, 2017
This is version 161 of the entry and version 1 of the sequence. See 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.