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UniProtKB - Q9Y478 (AAKB1_HUMAN)

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Protein

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

Gene

PRKAB1

Organism
Homo sapiens (Human)
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

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell cycle arrest Source: Reactome
  • fatty acid biosynthetic process Source: UniProtKB-KW
  • macroautophagy Source: Reactome
  • nail development Source: Ensembl
  • positive regulation of gene expression Source: UniProtKB
  • protein heterooligomerization Source: Ensembl
  • protein phosphorylation Source: UniProtKB
  • regulation of catalytic activity Source: Ensembl
  • signal transduction Source: ProtInc
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of GLUT4 to the plasma membrane
R-HSA-1632852 Macroautophagy
R-HSA-2151209 Activation of PPARGC1A (PGC-1alpha) by phosphorylation
R-HSA-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-HSA-5628897 TP53 Regulates Metabolic Genes
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
SignaLinkiQ9Y478
SIGNORiQ9Y478

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
Gene namesi
Name:PRKAB1
Synonyms:AMPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000111725.10
HGNCiHGNC:9378 PRKAB1
MIMi602740 gene
neXtProtiNX_Q9Y478

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
Mutagenesisi2G → A: Abolishes myristoylation and AMP-enhanced phosphorylation of PRKAA1 or PRKAA2. 1 Publication1

Organism-specific databases

DisGeNETi5564
OpenTargetsiENSG00000111725
PharmGKBiPA33746

Chemistry databases

ChEMBLiCHEMBL3847
DrugBankiDB00945 Acetylsalicylic acid
DB00131 Adenosine monophosphate
DB00331 Metformin
GuidetoPHARMACOLOGYi1543

Polymorphism and mutation databases

BioMutaiPRKAB1
DMDMi14194425

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002043632 – 2705'-AMP-activated protein kinase subunit beta-1Add BLAST269

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Modified residuei4PhosphothreonineCombined sources1
Modified residuei5PhosphoserineCombined sources1
Modified residuei6PhosphoserineCombined sources1
Modified residuei19PhosphothreonineCombined sources1
Modified residuei24Phosphoserine; by autocatalysisBy similarity1
Modified residuei25Phosphoserine; by autocatalysisBy similarity1
Modified residuei40PhosphoserineCombined sources1
Modified residuei96PhosphoserineCombined sources1
Modified residuei101PhosphoserineBy similarity1
Modified residuei108PhosphoserineCombined sources1
Modified residuei148PhosphothreonineCombined sources1
Modified residuei182PhosphoserineBy 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.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ9Y478
MaxQBiQ9Y478
PaxDbiQ9Y478
PeptideAtlasiQ9Y478
PRIDEiQ9Y478
ProteomicsDBi86122

PTM databases

iPTMnetiQ9Y478
PhosphoSitePlusiQ9Y478
SwissPalmiQ9Y478

Expressioni

Gene expression databases

BgeeiENSG00000111725
CleanExiHS_PRKAB1
ExpressionAtlasiQ9Y478 baseline and differential
GenevisibleiQ9Y478 HS

Organism-specific databases

HPAiCAB005058
HPA004247

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 FNIP2.3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111551, 59 interactors
DIPiDIP-39736N
IntActiQ9Y478, 19 interactors
MINTiQ9Y478
STRINGi9606.ENSP00000229328

Chemistry databases

BindingDBiQ9Y478

Structurei

Secondary structure

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi79 – 84Combined sources6
Beta strandi91 – 95Combined sources5
Helixi96 – 98Combined sources3
Beta strandi106 – 110Combined sources5
Beta strandi112 – 117Combined sources6
Beta strandi120 – 129Combined sources10
Beta strandi132 – 134Combined sources3
Beta strandi137 – 139Combined sources3
Beta strandi141 – 143Combined sources3
Beta strandi145 – 147Combined sources3
Beta strandi149 – 155Combined sources7
Helixi157 – 159Combined sources3
Helixi162 – 176Combined sources15
Helixi208 – 211Combined sources4
Helixi214 – 216Combined sources3
Beta strandi221 – 223Combined sources3
Helixi233 – 235Combined sources3
Beta strandi238 – 241Combined sources4
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
4CFEX-ray3.02B/D1-270[»]
4CFFX-ray3.92B/D1-270[»]
4ZHXX-ray2.99B/D1-270[»]
5EZVX-ray2.99B/D1-270[»]
5ISOX-ray2.63B/D1-270[»]
6B1UX-ray2.77B/D1-270[»]
ProteinModelPortaliQ9Y478
SMRiQ9Y478
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni68 – 163Glycogen-binding domainBy similarityAdd 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.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1616 Eukaryota
ENOG410XRB3 LUCA
GeneTreeiENSGT00390000001416
HOGENOMiHOG000230597
HOVERGENiHBG050430
KOiK07199
OMAiKCSDMSE
OrthoDBiEOG091G0DZR
PhylomeDBiQ9Y478
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.

Q9Y478-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNTSSERAA LERHGGHKTP RRDSSGGTKD GDRPKILMDS PEDADLFHSE 
        60         70         80         90        100
EIKAPEKEEF LAWQHDLEVN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW 
       110        120        130        140        150
SKLPLTRSHN NFVAILDLPE GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN 
       160        170        180        190        200
NIIQVKKTDF EVFDALMVDS QKCSDVSELS SSPPGPYHQE PYVCKPEERF 
       210        220        230        240        250
RAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY ALSIKDGVMV 
       260        270
LSATHRYKKK YVTTLLYKPI
Length:270
Mass (Da):30,382
Last modified:January 23, 2007 - v4
Checksum:iF0BCAA94D5BC15FC
GO

Sequence cautioni

The sequence AAB71326 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAC98897 differs from that shown. Reason: Frameshift at position 245.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10A → G in CAA73146 (PubMed:9224708).Curated1
Sequence conflicti10A → G in AAC98897 (Ref. 4) Curated1
Sequence conflicti15G → A in CAA12024 (Ref. 1) Curated1
Sequence conflicti20P → A in CAA73146 (PubMed:9224708).Curated1
Sequence conflicti20P → A in AAC98897 (Ref. 4) Curated1
Sequence conflicti22R → K in AAD09237 (Ref. 3) Curated1
Sequence conflicti22R → K in AAD00625 (Ref. 3) Curated1
Sequence conflicti56E → Y in AAD09237 (Ref. 3) Curated1
Sequence conflicti56E → Y in AAD00625 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224515 mRNA Translation: CAA12024.1
Y12556 mRNA Translation: CAA73146.1
U83994 mRNA Translation: AAD09237.1
U87276
, U87271, U87272, U87273, U87274, U87275 Genomic DNA Translation: AAD00625.1
AF022116 mRNA Translation: AAC98897.1 Frameshift.
AC002563 Genomic DNA Translation: AAB71326.1 Sequence problems.
BC001007 mRNA Translation: AAH01007.1
BC001056 mRNA Translation: AAH01056.1
BC001823 mRNA Translation: AAH01823.1
BC017671 mRNA Translation: AAH17671.1
CCDSiCCDS9191.1
PIRiT09514
RefSeqiNP_006244.2, NM_006253.4
XP_005253966.1, XM_005253909.1
UniGeneiHs.741184

Genome annotation databases

EnsembliENST00000229328; ENSP00000229328; ENSG00000111725
ENST00000541640; ENSP00000441369; ENSG00000111725
GeneIDi5564
KEGGihsa:5564
UCSCiuc001txg.4 human

Similar proteinsi

Entry informationi

Entry nameiAAKB1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y478
Secondary accession number(s): Q9UBV0
, Q9UE20, Q9UEX2, Q9Y6V8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 180 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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