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Protein

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

Gene

Prkab1

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

  • fatty acid biosynthetic process Source: UniProtKB-KW
  • nail development Source: Ensembl
  • positive regulation of gene expression Source: Ensembl
  • protein heterooligomerization Source: RGD
  • regulation of catalytic activity Source: RGD

Keywordsi

Biological processFatty 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi71057 Prkab1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 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
IntActiP80386, 178 interactors
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[»]
5T5TX-ray3.46B68-270[»]
5UFUX-ray3.45B67-270[»]
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
OMAiKCSDMSE
OrthoDBiEOG091G0DZR
PhylomeDBiP80386
TreeFamiTF313827

Family and domain databases

Gene3Di2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR032640 AMPK1_CBM
IPR006828 ASC_dom
IPR037256 ASC_dom_sf
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
PfamiView protein in Pfam
PF16561 AMPK1_CBM, 1 hit
PF04739 AMPKBI, 1 hit
SMARTiView protein in SMART
SM01010 AMPKBI, 1 hit
SUPFAMiSSF160219 SSF160219, 1 hit
SSF81296 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

Similar proteinsi

Entry informationi

Entry nameiAAKB1_RAT
AccessioniPrimary (citable) accession number: P80386
Secondary accession number(s): Q63048
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 167 of the entry and version 4 of the sequence. See 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

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