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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.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001W → G: Abolishes glycogen-binding. 1 Publication
Mutagenesisi100 – 1001W → L: Partially inhibits glycogen-binding. 1 Publication
Mutagenesisi126 – 1261K → Q: Abolishes glycogen-binding. 1 Publication
Mutagenesisi146 – 1461L → A: Significantly reduces glycogen-binding. 1 Publication
Mutagenesisi150 – 1501N → K: Abolishes glycogen-binding. 1 Publication
Mutagenesisi150 – 1501N → Q: Significantly reduces glycogen-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 2702695'-AMP-activated protein kinase subunit beta-1PRO_0000204367Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine2 Publications
Modified residuei4 – 41PhosphothreonineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei19 – 191PhosphothreonineBy similarity
Modified residuei24 – 241Phosphoserine; by autocatalysis2 Publications
Modified residuei25 – 251Phosphoserine; by autocatalysis2 Publications
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei101 – 1011Phosphoserine1 Publication
Modified residuei108 – 1081Phosphoserine; by autocatalysisCombined sources3 Publications
Modified residuei148 – 1481PhosphothreonineBy similarity
Modified residuei182 – 1821Phosphoserine2 Publications
Modified residuei201 – 2011N6-succinyllysineBy 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.4 Publications

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP80386.
PRIDEiP80386.

PTM databases

iPTMnetiP80386.
PhosphoSiteiP80386.

Expressioni

Tissue specificityi

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

Gene expression databases

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 interaction.
DIPiDIP-59127N.
STRINGi10116.ENSRNOP00000001508.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi78 – 847Combined sources
Beta strandi91 – 955Combined sources
Helixi96 – 983Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi120 – 12910Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi149 – 1557Combined sources
Turni158 – 1603Combined sources
Beta strandi161 – 1633Combined sources
Helixi164 – 1707Combined sources
Helixi208 – 2114Combined sources
Turni214 – 2163Combined sources
Beta strandi225 – 2273Combined sources
Helixi233 – 2353Combined sources
Beta strandi240 – 2456Combined sources
Beta strandi248 – 25710Combined sources
Beta strandi260 – 26910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP80386.
SMRiP80386. Positions 77-163, 189-270.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80386.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 16396Glycogen-binding domainAdd
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.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiP80386.
KOiK07199.
OMAiSKDGDRP.
OrthoDBiEOG7SXW3Z.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261G → E in AAC52579 (PubMed:8621499).Curated
Sequence conflicti52 – 521M → I AA sequence (PubMed:7961907).Curated

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_006249481.2.
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_006249481.2.
UniGeneiRn.3619.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP80386.
SMRiP80386. Positions 77-163, 189-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

iPTMnetiP80386.
PhosphoSiteiP80386.

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.
OrthoDBiEOG7SXW3Z.
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.

Miscellaneous databases

EvolutionaryTraceiP80386.
NextBioi616395.
PROiP80386.

Gene expression databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase."
    Gao G., Fernandez C.S., Stapleton D., Auster A.S., Widmer J., Dyck J.R.B., Kemp B.E., Witters L.A.
    J. Biol. Chem. 271:8675-8681(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro."
    Woods A., Cheung P.C.F., Smith F.C., Davison M.D., Scott J., Beri R.K., Carling D.
    J. Biol. Chem. 271:10282-10290(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  4. "Mammalian 5'-AMP-activated protein kinase non-catalytic subunits are homologs of proteins that interact with yeast Snf1 protein kinase."
    Stapleton D., Gao G., Michell B.J., Widmer J., Mitchelhill K.I., Teh T., House C.M., Witters L.A., Kemp B.E.
    J. Biol. Chem. 269:29343-29346(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-159, PROTEIN SEQUENCE OF 36-72; 79-83 AND 90-159.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. "Posttranslational modifications of the 5'-AMP-activated protein kinase beta1 subunit."
    Mitchelhill K.I., Michell B.J., House C.M., Stapleton D., Dyck J., Gamble J., Ullrich C., Witters L.A., Kemp B.E.
    J. Biol. Chem. 272:24475-24479(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-24; SER-25; SER-108 AND SER-182.
  6. "Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization."
    Warden S.M., Richardson C., O'Donnell J. Jr., Stapleton D., Kemp B.E., Witters L.A.
    Biochem. J. 354:275-283(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-24; SER-25; SER-108 AND SER-182.
  7. "Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis."
    Woods A., Vertommen D., Neumann D., Turk R., Bayliss J., Schlattner U., Wallimann T., Carling D., Rider M.H.
    J. Biol. Chem. 278:28434-28442(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-96; SER-101 AND SER-108.
  8. "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop."
    Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.
    Autophagy 7:696-706(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY ULK1.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Structural basis for glycogen recognition by AMP-activated protein kinase."
    Polekhina G., Gupta A., van Denderen B.J., Feil S.C., Kemp B.E., Stapleton D., Parker M.W.
    Structure 13:1453-1462(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 68-162 IN COMPLEX WITH BETA-CYCLODEXTRIN, DOMAIN GLYCOGEN-BINDING, MUTAGENESIS OF TRP-100; LYS-126; LEU-146 AND ASN-150.

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: January 20, 2016
This is version 151 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.