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Protein

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

Gene

Prkab1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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).

GO - Molecular functioni

  • protein kinase activity Source: Ensembl
  • protein kinase binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

BRENDAi2.7.11.31. 5301.
ReactomeiR-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

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit beta-1
Short name:
AMPK subunit beta-1
Short name:
AMPKb
Alternative name(s):
5'-AMP-activated protein kinase 40 kDa subunit
Gene namesi
Name:Prkab1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi71057. Prkab1.

Subcellular locationi

GO - Cellular componenti

  • nucleotide-activated protein kinase complex Source: RGD
  • nucleus Source: Ensembl
  • protein complex Source: RGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi100W → G: Abolishes glycogen-binding. 1 Publication1
Mutagenesisi100W → L: Partially inhibits glycogen-binding. 1 Publication1
Mutagenesisi126K → Q: Abolishes glycogen-binding. 1 Publication1
Mutagenesisi146L → A: Significantly reduces glycogen-binding. 1 Publication1
Mutagenesisi150N → K: Abolishes glycogen-binding. 1 Publication1
Mutagenesisi150N → Q: Significantly reduces glycogen-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002043672 – 2705'-AMP-activated protein kinase subunit beta-1Add BLAST269

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine2 Publications1
Modified residuei4PhosphothreonineBy similarity1
Modified residuei5PhosphoserineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Modified residuei19PhosphothreonineBy similarity1
Modified residuei24Phosphoserine; by autocatalysis2 Publications1
Modified residuei25Phosphoserine; by autocatalysis2 Publications1
Modified residuei40PhosphoserineCombined sources1
Modified residuei96Phosphoserine1 Publication1
Modified residuei101Phosphoserine1 Publication1
Modified residuei108Phosphoserine; by autocatalysisCombined sources3 Publications1
Modified residuei148PhosphothreonineBy similarity1
Modified residuei170PhosphoserineBy similarity1
Modified residuei182Phosphoserine2 Publications1
Modified residuei201N6-succinyllysineBy similarity1

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.4 Publications

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP80386.
PRIDEiP80386.

PTM databases

iPTMnetiP80386.
PhosphoSitePlusiP80386.

Expressioni

Tissue specificityi

Highly expressed in kidney, heart, white adipose tissue, lung and spleen.

Gene expression databases

BgeeiENSRNOG00000001142.
GenevisibleiP80386. 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 Publication

GO - Molecular functioni

  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi249839. 1 interactor.
DIPiDIP-59127N.
STRINGi10116.ENSRNOP00000001508.

Structurei

Secondary structure

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi78 – 84Combined sources7
Beta strandi91 – 95Combined sources5
Helixi96 – 98Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi106 – 108Combined sources3
Beta strandi111 – 118Combined sources8
Beta strandi120 – 129Combined sources10
Beta strandi132 – 134Combined sources3
Beta strandi141 – 143Combined sources3
Beta strandi149 – 155Combined sources7
Turni158 – 160Combined sources3
Beta strandi161 – 163Combined sources3
Helixi164 – 170Combined sources7
Helixi208 – 211Combined sources4
Turni214 – 216Combined sources3
Beta strandi225 – 227Combined sources3
Helixi233 – 235Combined sources3
Beta strandi240 – 245Combined sources6
Beta strandi248 – 257Combined sources10
Beta strandi260 – 269Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z0MX-ray1.91A/B/C68-163[»]
1Z0NX-ray1.49A/B/C68-163[»]
4EAGX-ray2.70B187-270[»]
4EAKX-ray2.50B200-270[»]
4EALX-ray2.51B200-270[»]
4QFGX-ray3.46B68-270[»]
4QFRX-ray3.34B68-270[»]
4QFSX-ray3.55B68-270[»]
4YEFX-ray1.72A/B/C/D/E/F/G76-156[»]
5KQ5X-ray3.41B68-270[»]
ProteinModelPortaliP80386.
SMRiP80386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80386.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni68 – 163Glycogen-binding domainAdd BLAST96

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.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiP80386.
KOiK07199.
OMAiSKDGDRP.
OrthoDBiEOG091G0DZR.
PhylomeDBiP80386.
TreeFamiTF313827.

Family and domain databases

InterProiIPR032640. AMPK1_CBM.
IPR030080. AMPK_beta-1.
IPR006828. ASC_dom.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10343:SF16. PTHR10343:SF16. 1 hit.
PfamiPF16561. AMPK1_CBM. 1 hit.
PF04739. 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.

P80386-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:270
Mass (Da):30,394
Last modified:January 23, 2007 - v4
Checksum:i62726DD357F36C7C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26G → E in AAC52579 (PubMed:8621499).Curated1
Sequence conflicti52M → I AA sequence (PubMed:7961907).Curated1

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.
RefSeqiNP_114182.1. NM_031976.1.
XP_006249543.1. XM_006249481.3.
UniGeneiRn.3619.

Genome annotation databases

EnsembliENSRNOT00000001508; ENSRNOP00000001508; ENSRNOG00000001142.
GeneIDi83803.
KEGGirno:83803.
UCSCiRGD:71057. rat.

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.
RefSeqiNP_114182.1. NM_031976.1.
XP_006249543.1. XM_006249481.3.
UniGeneiRn.3619.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z0MX-ray1.91A/B/C68-163[»]
1Z0NX-ray1.49A/B/C68-163[»]
4EAGX-ray2.70B187-270[»]
4EAKX-ray2.50B200-270[»]
4EALX-ray2.51B200-270[»]
4QFGX-ray3.46B68-270[»]
4QFRX-ray3.34B68-270[»]
4QFSX-ray3.55B68-270[»]
4YEFX-ray1.72A/B/C/D/E/F/G76-156[»]
5KQ5X-ray3.41B68-270[»]
ProteinModelPortaliP80386.
SMRiP80386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249839. 1 interactor.
DIPiDIP-59127N.
STRINGi10116.ENSRNOP00000001508.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

iPTMnetiP80386.
PhosphoSitePlusiP80386.

Proteomic databases

PaxDbiP80386.
PRIDEiP80386.

Protocols and materials databases

DNASUi83803.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001508; ENSRNOP00000001508; ENSRNOG00000001142.
GeneIDi83803.
KEGGirno:83803.
UCSCiRGD:71057. rat.

Organism-specific databases

CTDi5564.
RGDi71057. Prkab1.

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiP80386.
KOiK07199.
OMAiSKDGDRP.
OrthoDBiEOG091G0DZR.
PhylomeDBiP80386.
TreeFamiTF313827.

Enzyme and pathway databases

BRENDAi2.7.11.31. 5301.
ReactomeiR-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

EvolutionaryTraceiP80386.
PROiP80386.

Gene expression databases

BgeeiENSRNOG00000001142.
GenevisibleiP80386. RN.

Family and domain databases

InterProiIPR032640. AMPK1_CBM.
IPR030080. AMPK_beta-1.
IPR006828. ASC_dom.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10343:SF16. PTHR10343:SF16. 1 hit.
PfamiPF16561. AMPK1_CBM. 1 hit.
PF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAAKB1_RAT
AccessioniPrimary (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: November 2, 2016
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.