SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9QZH4

- AAKB2_RAT

UniProt

Q9QZH4 - AAKB2_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene
Prkab2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 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.

GO - Molecular functioni

  1. protein kinase binding Source: RGD

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. protein phosphorylation Source: GOC
Complete GO annotation...

Keywords - Biological processi

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

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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620905. Prkab2.

Subcellular locationi

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: RGD
  2. apical plasma membrane Source: UniProtKB
  3. cAMP-dependent protein kinase complex Source: RGD
  4. cytoplasm Source: UniProtKB
  5. nucleoplasm Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2712715'-AMP-activated protein kinase subunit beta-2PRO_0000204370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Phosphoserine; by ULK11 Publication
Modified residuei39 – 391Phosphothreonine; by ULK11 Publication
Modified residuei68 – 681Phosphoserine; by ULK11 Publication
Modified residuei107 – 1071Phosphoserine By similarity
Modified residuei173 – 1731Phosphoserine; by ULK11 Publication
Modified residuei183 – 1831Phosphoserine1 Publication

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

PTM databases

PhosphoSiteiQ9QZH4.

Expressioni

Gene expression databases

GenevestigatoriQ9QZH4.

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.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi73 – 753
Beta strandi80 – 823
Beta strandi89 – 935
Helixi94 – 963
Beta strandi111 – 1133
Beta strandi119 – 1224
Beta strandi124 – 1285
Beta strandi131 – 1333
Beta strandi136 – 1383
Beta strandi140 – 1423
Beta strandi152 – 1543
Beta strandi157 – 1604

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LU3NMR-A67-163[»]
2LU4NMR-A67-163[»]
ProteinModelPortaliQ9QZH4.
SMRiQ9QZH4. Positions 74-162, 189-271.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG238368.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiQ9QZH4.
KOiK07199.
PhylomeDBiQ9QZH4.

Family and domain databases

InterProiIPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF04739. 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

MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS    50
KLPGDKEFVP WQQDLDDSVK PTQQARPTVI RWSEGGKEVF ISGSFNNWST 100
KIPLIKSHND FVAILDLPEG EHQYKFFVDG QWVHDPSEPV VTSQLGTINN 150
LIHVKKSDFE VFDALKLDSM ESSETSCRDL SSSPPGPYGQ EMYVFRSEER 200
FKSPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL YALSTKDSVM 250
VLSATHRYKK KYVTTLLYKP I 271
Length:271
Mass (Da):30,227
Last modified:May 1, 2000 - v1
Checksum:iD881451A03287BEA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF182717 mRNA. Translation: AAF01293.1 .
RefSeqi NP_072149.1. NM_022627.2.
UniGenei Rn.207202.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LU3 NMR - A 67-163 [» ]
2LU4 NMR - A 67-163 [» ]
ProteinModelPortali Q9QZH4.
SMRi Q9QZH4. Positions 74-162, 189-271.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM48. Carbohydrate-Binding Module Family 48.

PTM databases

PhosphoSitei Q9QZH4.

Protocols and materials databases

DNASUi 64562.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 64562.
KEGGi rno:64562.

Organism-specific databases

CTDi 5565.
RGDi 620905. Prkab2.

Phylogenomic databases

eggNOGi NOG238368.
HOGENOMi HOG000230597.
HOVERGENi HBG050430.
InParanoidi Q9QZH4.
KOi K07199.
PhylomeDBi Q9QZH4.

Miscellaneous databases

NextBioi 613490.
PROi Q9QZH4.

Gene expression databases

Genevestigatori Q9QZH4.

Family and domain databases

InterProi IPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF04739. AMPKBI. 1 hit.
[Graphical view ]
SMARTi SM01010. AMPKBI. 1 hit.
[Graphical view ]
SUPFAMi SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

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: September 3, 2014
This is version 89 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

External Data

Dasty 3

Similar proteinsi