UniProtKB - P80386 (AAKB1_RAT)
5'-AMP-activated protein kinase subunit beta-1
Prkab1
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).
GO - Molecular functioni
- protein kinase activity Source: RGD
- protein kinase binding Source: RGD
GO - Biological processi
- cellular response to nutrient levels Source: RGD
- fatty acid biosynthetic process Source: UniProtKB-KW
- nail development Source: RGD
- positive regulation of cold-induced thermogenesis Source: YuBioLab
- positive regulation of gene expression Source: RGD
- protein phosphorylation Source: RGD
- regulation of catalytic activity Source: InterPro
- signal transduction Source: GO_Central
Keywordsi
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Enzyme and pathway databases
BRENDAi | 2.7.11.31, 5301 |
Reactomei | R-RNO-1632852, Macroautophagy R-RNO-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-RNO-5628897, TP53 Regulates Metabolic Genes R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation |
Protein family/group databases
CAZyi | CBM48, Carbohydrate-Binding Module Family 48 |
Names & Taxonomyi
Protein namesi | Recommended name: 5'-AMP-activated protein kinase subunit beta-1Short name: AMPK subunit beta-1 Short name: AMPKb Alternative name(s): 5'-AMP-activated protein kinase 40 kDa subunit |
Gene namesi | Name:Prkab1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 71057, Prkab1 |
Subcellular locationi
Cytosol
- cytosol Source: Reactome
Nucleus
- nucleus Source: RGD
Other locations
- cytoplasm Source: GO_Central
- nucleotide-activated protein kinase complex Source: RGD
- protein-containing complex Source: RGD
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 100 | W → G: Abolishes glycogen-binding. 1 Publication | 1 | |
Mutagenesisi | 100 | W → L: Partially inhibits glycogen-binding. 1 Publication | 1 | |
Mutagenesisi | 126 | K → Q: Abolishes glycogen-binding. 1 Publication | 1 | |
Mutagenesisi | 146 | L → A: Significantly reduces glycogen-binding. 1 Publication | 1 | |
Mutagenesisi | 150 | N → K: Abolishes glycogen-binding. 1 Publication | 1 | |
Mutagenesisi | 150 | N → Q: Significantly reduces glycogen-binding. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3885503 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000204367 | 2 – 270 | 5'-AMP-activated protein kinase subunit beta-1Add BLAST | 269 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine2 Publications | 1 | |
Modified residuei | 4 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 5 | PhosphoserineBy similarity | 1 | |
Modified residuei | 6 | PhosphoserineBy similarity | 1 | |
Modified residuei | 19 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 24 | Phosphoserine; by autocatalysis2 Publications | 1 | |
Modified residuei | 25 | Phosphoserine; by autocatalysis2 Publications | 1 | |
Modified residuei | 40 | PhosphoserineCombined sources | 1 | |
Modified residuei | 96 | Phosphoserine1 Publication | 1 | |
Modified residuei | 101 | Phosphoserine1 Publication | 1 | |
Modified residuei | 108 | Phosphoserine; by autocatalysisCombined sources3 Publications | 1 | |
Modified residuei | 148 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 182 | Phosphoserine2 Publications | 1 | |
Modified residuei | 201 | N6-succinyllysineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Lipoprotein, Myristate, PhosphoproteinProteomic databases
jPOSTi | P80386 |
PaxDbi | P80386 |
PTM databases
iPTMneti | P80386 |
PhosphoSitePlusi | P80386 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSRNOG00000001142, Expressed in heart and 22 other tissues |
Genevisiblei | P80386, RN |
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.
1 PublicationGO - Molecular functioni
- protein kinase binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 249839, 243 interactors |
DIPi | DIP-59127N |
IntActi | P80386, 178 interactors |
STRINGi | 10116.ENSRNOP00000001508 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P80386 |
SMRi | P80386 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P80386 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 43 | DisorderedSequence analysisAdd BLAST | 43 | |
Regioni | 68 – 163 | Glycogen-binding domainAdd BLAST | 96 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 11 – 43 | Basic and acidic residuesSequence analysisAdd BLAST | 33 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1616, Eukaryota |
GeneTreei | ENSGT00940000155307 |
HOGENOMi | CLU_070949_2_0_1 |
InParanoidi | P80386 |
OMAi | NDRAPTQ |
OrthoDBi | 956412at2759 |
PhylomeDBi | P80386 |
TreeFami | TF313827 |
Family and domain databases
Gene3Di | 2.60.40.10, 1 hit |
InterProi | View protein in InterPro IPR032640, AMPK1_CBM IPR039160, AMPKB IPR006828, ASC_dom IPR037256, ASC_dom_sf IPR013783, Ig-like_fold IPR014756, Ig_E-set |
PANTHERi | PTHR10343:SF89, PTHR10343:SF89, 1 hit |
Pfami | View protein in Pfam PF16561, AMPK1_CBM, 1 hit PF04739, AMPKBI, 1 hit |
SMARTi | View protein in SMART SM01010, AMPKBI, 1 hit |
SUPFAMi | SSF160219, SSF160219, 1 hit SSF81296, SSF81296, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MGNTSSERAA LERQAGHKTP RRDSSGGTKD GDRPKILMDS PEDADIFHTE
60 70 80 90 100
EMKAPEKEEF LAWQHDLEVN EKAPAQARPT VFRWTGGGKE VYLSGSFNNW
110 120 130 140 150
SKLPLTRSQN NFVAILDLPE GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN
160 170 180 190 200
NIIQVKKTDF EVFDALMVDS QKCSDVSELS SSPPGPYHQE PYISKPEERF
210 220 230 240 250
KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY ALSIKDGVMV
260 270
LSATHRYKKK YVTTLLYKPI
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 26 | G → E in AAC52579 (PubMed:8621499).Curated | 1 | |
Sequence conflicti | 52 | M → I AA sequence (PubMed:7961907).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U42411 mRNA Translation: AAC52579.1 BC062008 mRNA Translation: AAH62008.1 X95577 mRNA Translation: CAA64830.1 |
RefSeqi | NP_114182.1, NM_031976.1 XP_006249543.1, XM_006249481.3 |
Genome annotation databases
Ensembli | ENSRNOT00000001508; ENSRNOP00000001508; ENSRNOG00000001142 |
GeneIDi | 83803 |
KEGGi | rno:83803 |
UCSCi | RGD:71057, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U42411 mRNA Translation: AAC52579.1 BC062008 mRNA Translation: AAH62008.1 X95577 mRNA Translation: CAA64830.1 |
RefSeqi | NP_114182.1, NM_031976.1 XP_006249543.1, XM_006249481.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1Z0M | X-ray | 1.91 | A/B/C | 68-163 | [»] | |
1Z0N | X-ray | 1.49 | A/B/C | 68-163 | [»] | |
4EAG | X-ray | 2.70 | B | 187-270 | [»] | |
4EAK | X-ray | 2.50 | B | 200-270 | [»] | |
4EAL | X-ray | 2.51 | B | 200-270 | [»] | |
4QFG | X-ray | 3.46 | B | 68-270 | [»] | |
4QFR | X-ray | 3.34 | B | 68-270 | [»] | |
4QFS | X-ray | 3.55 | B | 68-270 | [»] | |
4YEF | X-ray | 1.72 | A/B/C/D/E/F/G | 76-156 | [»] | |
5KQ5 | X-ray | 3.41 | B | 68-270 | [»] | |
5T5T | X-ray | 3.46 | B | 68-270 | [»] | |
5UFU | X-ray | 3.45 | B | 67-270 | [»] | |
6E4T | X-ray | 3.40 | B | 67-270 | [»] | |
6E4U | X-ray | 3.27 | B | 67-270 | [»] | |
6E4W | X-ray | 3.35 | B | 67-270 | [»] | |
AlphaFoldDBi | P80386 | |||||
SMRi | P80386 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 249839, 243 interactors |
DIPi | DIP-59127N |
IntActi | P80386, 178 interactors |
STRINGi | 10116.ENSRNOP00000001508 |
Chemistry databases
ChEMBLi | CHEMBL3885503 |
Protein family/group databases
CAZyi | CBM48, Carbohydrate-Binding Module Family 48 |
PTM databases
iPTMneti | P80386 |
PhosphoSitePlusi | P80386 |
Proteomic databases
jPOSTi | P80386 |
PaxDbi | P80386 |
Protocols and materials databases
DNASUi | 83803 |
Genome annotation databases
Ensembli | ENSRNOT00000001508; ENSRNOP00000001508; ENSRNOG00000001142 |
GeneIDi | 83803 |
KEGGi | rno:83803 |
UCSCi | RGD:71057, rat |
Organism-specific databases
CTDi | 5564 |
RGDi | 71057, Prkab1 |
Phylogenomic databases
eggNOGi | KOG1616, Eukaryota |
GeneTreei | ENSGT00940000155307 |
HOGENOMi | CLU_070949_2_0_1 |
InParanoidi | P80386 |
OMAi | NDRAPTQ |
OrthoDBi | 956412at2759 |
PhylomeDBi | P80386 |
TreeFami | TF313827 |
Enzyme and pathway databases
BRENDAi | 2.7.11.31, 5301 |
Reactomei | R-RNO-1632852, Macroautophagy R-RNO-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-RNO-5628897, TP53 Regulates Metabolic Genes R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation |
Miscellaneous databases
EvolutionaryTracei | P80386 |
PROi | PR:P80386 |
Gene expression databases
Bgeei | ENSRNOG00000001142, Expressed in heart and 22 other tissues |
Genevisiblei | P80386, RN |
Family and domain databases
Gene3Di | 2.60.40.10, 1 hit |
InterProi | View protein in InterPro IPR032640, AMPK1_CBM IPR039160, AMPKB IPR006828, ASC_dom IPR037256, ASC_dom_sf IPR013783, Ig-like_fold IPR014756, Ig_E-set |
PANTHERi | PTHR10343:SF89, PTHR10343:SF89, 1 hit |
Pfami | View protein in Pfam PF16561, AMPK1_CBM, 1 hit PF04739, AMPKBI, 1 hit |
SMARTi | View protein in SMART SM01010, AMPKBI, 1 hit |
SUPFAMi | SSF160219, SSF160219, 1 hit SSF81296, SSF81296, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AAKB1_RAT | |
Accessioni | P80386Primary (citable) accession number: P80386 Secondary accession number(s): Q63048 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1995 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 189 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families