Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9QZH4 (AAKB2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5'-AMP-activated protein kinase subunit beta-2

Short name=AMPK subunit beta-2
Gene names
Name:Prkab2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Post-translational modification

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. Ref.1 Ref.2

Sequence similarities

Belongs to the 5'-AMP-activated protein kinase beta subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2712715'-AMP-activated protein kinase subunit beta-2
PRO_0000204370

Amino acid modifications

Modified residue381Phosphoserine; by ULK1 Ref.2
Modified residue391Phosphothreonine; by ULK1 Ref.2
Modified residue681Phosphoserine; by ULK1 Ref.2
Modified residue1071Phosphoserine By similarity
Modified residue1731Phosphoserine; by ULK1 Ref.2
Modified residue1831Phosphoserine Ref.1

Secondary structure

........................ 271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QZH4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D881451A03287BEA

FASTA27130,227
        10         20         30         40         50         60 
MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS KLPGDKEFVP 

        70         80         90        100        110        120 
WQQDLDDSVK PTQQARPTVI RWSEGGKEVF ISGSFNNWST KIPLIKSHND FVAILDLPEG 

       130        140        150        160        170        180 
EHQYKFFVDG QWVHDPSEPV VTSQLGTINN LIHVKKSDFE VFDALKLDSM ESSETSCRDL 

       190        200        210        220        230        240 
SSSPPGPYGQ EMYVFRSEER FKSPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL 

       250        260        270 
YALSTKDSVM VLSATHRYKK KYVTTLLYKP I 

« Hide

References

[1]"Expression of the AMP-activated protein kinase beta1 and beta2 subunits in skeletal muscle."
Chen Z., Heierhorst J., Mann R.J., Mitchelhill K.I., Michell B.J., Witters L.A., Lynch G.S., Kemp B.E., Stapleton D.
FEBS Lett. 460:343-348(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-183.
Strain: Sprague-Dawley.
Tissue: Skeletal muscle.
[2]"Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop."
Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.
Autophagy 7:696-706(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY ULK1 AND ULK2, PHOSPHORYLATION AT SER-38; THR-39; SER-68 AND SER-173.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF182717 mRNA. Translation: AAF01293.1.
RefSeqNP_072149.1. NM_022627.2.
UniGeneRn.207202.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LU3NMR-A67-163[»]
2LU4NMR-A67-163[»]
ProteinModelPortalQ9QZH4.
SMRQ9QZH4. Positions 74-162, 189-271.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

PhosphoSiteQ9QZH4.

Protocols and materials databases

DNASU64562.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64562.
KEGGrno:64562.

Organism-specific databases

CTD5565.
RGD620905. Prkab2.

Phylogenomic databases

eggNOGNOG238368.
HOGENOMHOG000230597.
HOVERGENHBG050430.
InParanoidQ9QZH4.
KOK07199.
PhylomeDBQ9QZH4.

Enzyme and pathway databases

ReactomeREACT_205051. Metabolism.

Gene expression databases

GenevestigatorQ9QZH4.

Family and domain databases

InterProIPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

NextBio613490.
PROQ9QZH4.

Entry information

Entry nameAAKB2_RAT
AccessionPrimary (citable) accession number: Q9QZH4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references