LipidDB ID

LipidDB-10116-01027

Entry Name

UniProt Accession

P80386; Q63048;

Theoretical PI

5.81

Molecular Weight

30394.36

Genbank Protein ID

AAC52579.1; AAH62008.1; CAA64830.1;

Genbank Nucleotide ID

U42411; BC062008; X95577;

Protein Name

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

Protein Synonyms/Alias

AMPK subunit beta-1; AMPKb; 5'-AMP-activated protein kinase 40 kDa subunit;

Gene Name

Prkab1

Gene Synonyms/Alias

Created Date

01-FEB-1995

Organism

Rattus norvegicus (Rat)

NCBI Taxa ID

10116

Reference

[1] Warden SM, Richardson C, O'Donnell J Jr, Stapleton D, Kemp BE, Witters LA.Post-translational modifications of the beta-1 subunit of AMP-activated proteinkinase affect enzyme activity and cellular localization. Biochem J. 2001 Mar1;354(Pt 2):275-83.[PMID:11171104]
[2] Mitchelhill KI, Michell BJ, House CM, Stapleton D, Dyck J, Gamble J, UllrichC, Witters LA, Kemp BE. Posttranslational modifications of the 5'-AMP-activatedprotein kinase beta1 subunit. J Biol Chem. 1997 Sep 26;272(39):24475-9. PubMedPMID: 9305909.[PMID:9305909]

Functional Description

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).

Sequence Annotation

Region: 68 163 Glycogen-binding domain.
Modified residue: 4 4 Phosphothreonine.
Modified residue: 5 5 Phosphoserine.
Modified residue: 6 6 Phosphoserine.
Modified residue: 19 19 Phosphothreonine.
Modified residue: 24 24 Phosphoserine; by autocatalysis.
Modified residue: 25 25 Phosphoserine; by autocatalysis.
Modified residue: 40 40 Phosphoserine.
Modified residue: 96 96 Phosphoserine.
Modified residue: 101 101 Phosphoserine.
Modified residue: 108 108 Phosphoserine; by autocatalysis.
Modified residue: 148 148 Phosphothreonine.
Modified residue: 182 182 Phosphoserine.
Modified residue: 201 201 N6-succinyllysine.

Protein Length

270 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0031588; C:AMP-activated protein kinase complex; IDA:RGD
GO:0005634; C:nucleus; IEA:Ensembl
GO:0043234; C:protein complex; IDA:RGD
GO:0004672; F:protein kinase activity; IEA:Ensembl
GO:0019901; F:protein kinase binding; IPI:RGD
GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW
GO:0010628; P:positive regulation of gene expression; IEA:Ensembl
GO:0051291; P:protein heterooligomerization; IDA:RGD
GO:0050790; P:regulation of catalytic activity; IDA:RGD

Interpro

InterPro; IPR006828; AMP_prot_kin_bsu_interact-dom
InterPro; IPR014756; Ig_E-set

Pfam

Pfam; PF04739; AMPKBI;

SMART

SMART; SM01010; AMPKBI;

PROSITE

PRINTS