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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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Abolishes myristoylation and AMP-enhanced phosphorylation of PRKAA1 or PRKAA2. 1 Publication

Organism-specific databases

PharmGKBiPA33746.

Chemistry

ChEMBLiCHEMBL2096907.
DrugBankiDB00945. Acetylsalicylic acid.
DB00131. Adenosine monophosphate.
DB00331. Metformin.
GuidetoPHARMACOLOGYi1543.

Polymorphism and mutation databases

BioMutaiPRKAB1.
DMDMi14194425.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 2702695'-AMP-activated protein kinase subunit beta-1PRO_0000204363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei4 – 41PhosphothreonineCombined sources
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei6 – 61PhosphoserineCombined sources
Modified residuei19 – 191PhosphothreonineCombined sources
Modified residuei24 – 241Phosphoserine; by autocatalysisBy similarity
Modified residuei25 – 251Phosphoserine; by autocatalysisBy similarity
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineBy similarity
Modified residuei108 – 1081PhosphoserineCombined sources
Modified residuei148 – 1481PhosphothreonineCombined sources
Modified residuei182 – 1821PhosphoserineBy similarity

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.
PhosphoSiteiQ9Y478.
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
PRKAG1P546194EBI-719769,EBI-1181439

Protein-protein interaction databases

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

Chemistry

BindingDBiQ9Y478.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi79 – 846Combined sources
Beta strandi91 – 955Combined sources
Turni96 – 994Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi120 – 12910Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi149 – 1557Combined sources
Turni158 – 1603Combined sources
Helixi162 – 17110Combined sources
Helixi208 – 2114Combined sources
Turni214 – 2163Combined sources
Beta strandi221 – 2233Combined sources
Helixi233 – 2353Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi249 – 25911Combined sources
Beta strandi261 – 2688Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 77-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 16396Glycogen-binding domainBy similarityAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101A → G in CAA73146 (PubMed:9224708).Curated
Sequence conflicti10 – 101A → G in AAC98897 (Ref. 4) Curated
Sequence conflicti15 – 151G → A in CAA12024 (Ref. 1) Curated
Sequence conflicti20 – 201P → A in CAA73146 (PubMed:9224708).Curated
Sequence conflicti20 – 201P → A in AAC98897 (Ref. 4) Curated
Sequence conflicti22 – 221R → K in AAD09237 (Ref. 3) Curated
Sequence conflicti22 – 221R → K in AAD00625 (Ref. 3) Curated
Sequence conflicti56 – 561E → Y in AAD09237 (Ref. 3) Curated
Sequence conflicti56 – 561E → Y in AAD00625 (Ref. 3) Curated

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
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. Positions 77-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ9Y478.
ChEMBLiCHEMBL2096907.
DrugBankiDB00945. Acetylsalicylic acid.
DB00131. Adenosine monophosphate.
DB00331. Metformin.
GuidetoPHARMACOLOGYi1543.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

iPTMnetiQ9Y478.
PhosphoSiteiQ9Y478.
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.
GeneCardsiPRKAB1.
HGNCiHGNC:9378. PRKAB1.
HPAiCAB005058.
HPA004247.
MIMi602740. gene.
neXtProtiNX_Q9Y478.
PharmGKBiPA33746.
GenAtlasiSearch...

Phylogenomic databases

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

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.

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: September 7, 2016
This is version 163 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.