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Q9R078 - AAKB1_MOUSE

UniProt

Q9R078 - AAKB1_MOUSE

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Protein

5'-AMP-activated protein kinase subunit beta-1

Gene

Prkab1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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).By similarity

GO - Molecular functioni

  1. AMP-activated protein kinase activity Source: MGI
  2. protein kinase activity Source: MGI

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. positive regulation of gene expression Source: MGI
  3. protein heterooligomerization Source: Ensembl
  4. protein phosphorylation Source: MGI
  5. regulation of catalytic activity Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_220701. Regulation of AMPK activity via LKB1.
REACT_257725. Regulation of Rheb GTPase activity by AMPK.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit beta-1
Short name:
AMPK subunit beta-1
Short name:
AMPKb
Gene namesi
Name:Prkab1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1336167. Prkab1.

Subcellular locationi

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: Ensembl
  2. cytosol Source: Reactome
  3. nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 2702695'-AMP-activated protein kinase subunit beta-1PRO_0000204364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei4 – 41PhosphothreonineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei19 – 191PhosphothreonineBy similarity
Modified residuei24 – 241Phosphoserine; by autocatalysisBy similarity
Modified residuei25 – 251Phosphoserine; by autocatalysisBy similarity
Modified residuei40 – 401PhosphoserineBy similarity
Modified residuei96 – 961PhosphoserineBy similarity
Modified residuei101 – 1011PhosphoserineBy similarity
Modified residuei108 – 1081Phosphoserine; by autocatalysis2 Publications
Modified residuei148 – 1481PhosphothreonineBy similarity
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei201 – 2011N6-succinyllysine1 Publication

Post-translational modificationi

Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK.3 Publications

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ9R078.
PaxDbiQ9R078.
PRIDEiQ9R078.

PTM databases

PhosphoSiteiQ9R078.

Expressioni

Gene expression databases

BgeeiQ9R078.
ExpressionAtlasiQ9R078. baseline and differential.
GenevestigatoriQ9R078.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi202363. 4 interactions.
IntActiQ9R078. 10 interactions.
MINTiMINT-4086419.

Structurei

3D structure databases

ProteinModelPortaliQ9R078.
SMRiQ9R078. Positions 77-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 16396Glycogen-binding domainBy similarityAdd
BLAST

Domaini

The glycogen-binding domain may target AMPK to glycogen so that other factors like glycogen-bound debranching enzyme or protein phosphatases can directly affect AMPK activity.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG238368.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiQ9R078.
KOiK07199.
OMAiSKDGDRP.
OrthoDBiEOG7SXW3Z.
PhylomeDBiQ9R078.
TreeFamiTF313827.

Family and domain databases

InterProiIPR030080. AMPK_beta-1.
IPR006828. ASC_dom.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10343:SF16. PTHR10343:SF16. 1 hit.
PfamiPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R078-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGNTSSERAA LERQAGHKTP RRDSSGGAKD GDRPKILMDS PEDADIFHSE 
        60         70         80         90        100
EIKAPEKEEF LAWQHDLEAN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW 
       110        120        130        140        150
SKLPLTRSQN NFVAILDLPE GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN 
       160        170        180        190        200
NIIQVKKTDF EVFDALMVDS QKCSDVSELS SSPPGPYHQE PYMSKPEERF 
       210        220        230        240        250
KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY ALSIKDGVMV 
       260        270
LSATHRYKKK YVTTLLYKPI
Length:270
Mass (Da):30,308
Last modified:January 23, 2007 - v2
Checksum:i6B520A95A0A844E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF108215 mRNA. Translation: AAF14222.1.
BC016398 mRNA. Translation: AAH16398.1.
CCDSiCCDS19598.1.
RefSeqiNP_114075.1. NM_031869.2.
XP_006530264.1. XM_006530201.1.
UniGeneiMm.458152.

Genome annotation databases

EnsembliENSMUST00000031486; ENSMUSP00000031486; ENSMUSG00000029513.
ENSMUST00000111999; ENSMUSP00000107630; ENSMUSG00000029513.
GeneIDi19079.
KEGGimmu:19079.
UCSCiuc008zew.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF108215 mRNA. Translation: AAF14222.1.
BC016398 mRNA. Translation: AAH16398.1.
CCDSiCCDS19598.1.
RefSeqiNP_114075.1. NM_031869.2.
XP_006530264.1. XM_006530201.1.
UniGeneiMm.458152.

3D structure databases

ProteinModelPortaliQ9R078.
SMRiQ9R078. Positions 77-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202363. 4 interactions.
IntActiQ9R078. 10 interactions.
MINTiMINT-4086419.

PTM databases

PhosphoSiteiQ9R078.

Proteomic databases

MaxQBiQ9R078.
PaxDbiQ9R078.
PRIDEiQ9R078.

Protocols and materials databases

DNASUi19079.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031486; ENSMUSP00000031486; ENSMUSG00000029513.
ENSMUST00000111999; ENSMUSP00000107630; ENSMUSG00000029513.
GeneIDi19079.
KEGGimmu:19079.
UCSCiuc008zew.1. mouse.

Organism-specific databases

CTDi5564.
MGIiMGI:1336167. Prkab1.

Phylogenomic databases

eggNOGiNOG238368.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiQ9R078.
KOiK07199.
OMAiSKDGDRP.
OrthoDBiEOG7SXW3Z.
PhylomeDBiQ9R078.
TreeFamiTF313827.

Enzyme and pathway databases

ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_220701. Regulation of AMPK activity via LKB1.
REACT_257725. Regulation of Rheb GTPase activity by AMPK.

Miscellaneous databases

ChiTaRSiPrkab1. mouse.
NextBioi295614.
PROiQ9R078.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R078.
ExpressionAtlasiQ9R078. baseline and differential.
GenevestigatoriQ9R078.

Family and domain databases

InterProiIPR030080. AMPK_beta-1.
IPR006828. ASC_dom.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10343:SF16. PTHR10343:SF16. 1 hit.
PfamiPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "5'-AMP-activated protein kinase subunit beta interacts with the p42 subunit of translation initiation factor eIF3."
    Valentijn L.J., Hoff E.I., Baas F.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  5. "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.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Entry informationi

Entry nameiAAKB1_MOUSE
AccessioniPrimary (citable) accession number: Q9R078
Secondary accession number(s): Q91YN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.