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Protein

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

Gene

Prkab2

Organism
Rattus norvegicus (Rat)
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) (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: RGD
  • protein kinase binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-RNO-163680. AMPK inhibits chREBP transcriptional activation activity.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620905. Prkab2.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • cAMP-dependent protein kinase complex Source: RGD
  • cytoplasm Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleotide-activated protein kinase complex Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002043701 – 2715'-AMP-activated protein kinase subunit beta-2Add BLAST271

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38Phosphoserine; by ULK1Combined sources1 Publication1
Modified residuei39Phosphothreonine; by ULK11 Publication1
Modified residuei68Phosphoserine; by ULK11 Publication1
Modified residuei94PhosphoserineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei147PhosphothreonineBy similarity1
Modified residuei157PhosphoserineBy similarity1
Modified residuei169PhosphoserineBy similarity1
Modified residuei173Phosphoserine; by ULK11 Publication1
Modified residuei183Phosphoserine1 Publication1

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9QZH4.
PRIDEiQ9QZH4.

PTM databases

iPTMnetiQ9QZH4.
PhosphoSitePlusiQ9QZH4.

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).By similarity

GO - Molecular functioni

  • enzyme binding Source: RGD
  • protein kinase binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062137.

Structurei

Secondary structure

1271
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi73 – 75Combined sources3
Beta strandi76 – 82Combined sources7
Beta strandi89 – 93Combined sources5
Helixi94 – 96Combined sources3
Beta strandi105 – 107Combined sources3
Beta strandi110 – 117Combined sources8
Beta strandi119 – 128Combined sources10
Beta strandi131 – 133Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi140 – 142Combined sources3
Beta strandi148 – 154Combined sources7
Beta strandi157 – 160Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LU3NMR-A67-163[»]
2LU4NMR-A67-163[»]
4Y0GX-ray1.60A/B74-155[»]
4YEEX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R74-155[»]
ProteinModelPortaliQ9QZH4.
SMRiQ9QZH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiQ9QZH4.
KOiK07199.
PhylomeDBiQ9QZH4.

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.

Sequencei

Sequence statusi: Complete.

Q9QZH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS
60 70 80 90 100
KLPGDKEFVP WQQDLDDSVK PTQQARPTVI RWSEGGKEVF ISGSFNNWST
110 120 130 140 150
KIPLIKSHND FVAILDLPEG EHQYKFFVDG QWVHDPSEPV VTSQLGTINN
160 170 180 190 200
LIHVKKSDFE VFDALKLDSM ESSETSCRDL SSSPPGPYGQ EMYVFRSEER
210 220 230 240 250
FKSPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL YALSTKDSVM
260 270
VLSATHRYKK KYVTTLLYKP I
Length:271
Mass (Da):30,227
Last modified:May 1, 2000 - v1
Checksum:iD881451A03287BEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182717 mRNA. Translation: AAF01293.1.
RefSeqiNP_072149.1. NM_022627.2.
UniGeneiRn.207202.

Genome annotation databases

GeneIDi64562.
KEGGirno:64562.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182717 mRNA. Translation: AAF01293.1.
RefSeqiNP_072149.1. NM_022627.2.
UniGeneiRn.207202.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LU3NMR-A67-163[»]
2LU4NMR-A67-163[»]
4Y0GX-ray1.60A/B74-155[»]
4YEEX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R74-155[»]
ProteinModelPortaliQ9QZH4.
SMRiQ9QZH4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000062137.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

iPTMnetiQ9QZH4.
PhosphoSitePlusiQ9QZH4.

Proteomic databases

PaxDbiQ9QZH4.
PRIDEiQ9QZH4.

Protocols and materials databases

DNASUi64562.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64562.
KEGGirno:64562.

Organism-specific databases

CTDi5565.
RGDi620905. Prkab2.

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiQ9QZH4.
KOiK07199.
PhylomeDBiQ9QZH4.

Enzyme and pathway databases

ReactomeiR-RNO-163680. AMPK inhibits chREBP transcriptional activation activity.

Miscellaneous databases

PROiQ9QZH4.

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_RAT
AccessioniPrimary (citable) accession number: Q9QZH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.