Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

PRKAB1

Organism
Homo sapiens (Human)
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

  • AMP-activated protein kinase activity Source: Ensembl
  • protein kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111725-MONOMER.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9378. PRKAB1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 residuei170PhosphoserineBy similarity1
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.

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

WithEntry#Exp.IntActNotes
CideaO703024EBI-719769,EBI-7927848From a different organism.
GRB2P629932EBI-719769,EBI-401755
PRKAA1Q131316EBI-719769,EBI-1181405
PRKAA2P546463EBI-719769,EBI-1383852
PRKAG1P546196EBI-719769,EBI-1181439

Protein-protein interaction databases

BioGridi111551. 51 interactors.
DIPiDIP-39736N.
IntActiQ9Y478. 18 interactors.
MINTiMINT-1400840.
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
Turni96 – 99Combined sources4
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
Turni158 – 160Combined sources3
Helixi162 – 171Combined sources10
Helixi208 – 211Combined sources4
Turni214 – 216Combined sources3
Beta strandi221 – 223Combined sources3
Helixi233 – 235Combined sources3
Beta strandi238 – 241Combined sources4
Beta strandi249 – 259Combined sources11
Beta strandi261 – 268Combined sources8

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[»]
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

Phylogenomic databases

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

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.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

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[»]
ProteinModelPortaliQ9Y478.
SMRiQ9Y478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111551. 51 interactors.
DIPiDIP-39736N.
IntActiQ9Y478. 18 interactors.
MINTiMINT-1400840.
STRINGi9606.ENSP00000229328.

Chemistry databases

BindingDBiQ9Y478.
ChEMBLiCHEMBL3847.
DrugBankiDB00945. Acetylsalicylic acid.
DB00131. Adenosine monophosphate.
DB00331. Metformin.
GuidetoPHARMACOLOGYi1543.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

iPTMnetiQ9Y478.
PhosphoSitePlusiQ9Y478.
SwissPalmiQ9Y478.

Polymorphism and mutation databases

BioMutaiPRKAB1.
DMDMi14194425.

Proteomic databases

EPDiQ9Y478.
MaxQBiQ9Y478.
PaxDbiQ9Y478.
PeptideAtlasiQ9Y478.
PRIDEiQ9Y478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5564.
DisGeNETi5564.
GeneCardsiPRKAB1.
HGNCiHGNC:9378. PRKAB1.
HPAiCAB005058.
HPA004247.
MIMi602740. gene.
neXtProtiNX_Q9Y478.
OpenTargetsiENSG00000111725.
PharmGKBiPA33746.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
KOiK07199.
OMAiSKDGDRP.
OrthoDBiEOG091G0DZR.
PhylomeDBiQ9Y478.
TreeFamiTF313827.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000111725-MONOMER.
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.

Miscellaneous databases

GeneWikiiPRKAB1.
GenomeRNAii5564.
PROiQ9Y478.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111725.
CleanExiHS_PRKAB1.
ExpressionAtlasiQ9Y478. baseline and differential.
GenevisibleiQ9Y478. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q9Y478
Secondary accession number(s): Q9UBV0
, Q9UE20, Q9UEX2, Q9Y6V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 166 of the entry and version 4 of the sequence. [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

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.