P80386 (AAKB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Prkab1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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).
Subunit structure	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.
Tissue specificity	Highly expressed in kidney, heart, white adipose tissue, lung and spleen.
Domain	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. Ref.10
Post-translational modification	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. Ref.5 Ref.6 Ref.7 Ref.9
Sequence similarities	Belongs to the 5'-AMP-activated protein kinase beta subunit family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW protein heterooligomerization Inferred from direct assay PubMed 14511394. Source: RGD regulation of catalytic activity Inferred from direct assay PubMed 15695819. Source: RGD response to stress Traceable author statement Ref.2. Source: RGD
Cellular_component	AMP-activated protein kinase complex Inferred from direct assay PubMed 16648175. Source: RGD nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	AMP-activated protein kinase activity Traceable author statement Ref.2. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

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

PRO_0000204367

Regions

Region

68 – 163

96

Glycogen-binding domain

Amino acid modifications

Modified residue

4

1

Phosphothreonine By similarity

Modified residue

5

1

Phosphoserine By similarity

Modified residue

6

1

Phosphoserine By similarity

Modified residue

19

1

Phosphothreonine By similarity

Modified residue

24

1

Phosphoserine; by autocatalysis Ref.5 Ref.6

Modified residue

25

1

Phosphoserine; by autocatalysis Ref.5 Ref.6

Modified residue

40

1

Phosphoserine By similarity

Modified residue

96

1

Phosphoserine Ref.7

Modified residue

101

1

Phosphoserine Ref.7

Modified residue

108

1

Phosphoserine; by autocatalysis Ref.5 Ref.6 Ref.7 Ref.8

Modified residue

148

1

Phosphothreonine By similarity

Modified residue

182

1

Phosphoserine Ref.5 Ref.6

Lipidation

2

1

N-myristoyl glycine Ref.5 Ref.6

Experimental info

Mutagenesis

100

1

W → G: Abolishes glycogen-binding. Ref.10

Mutagenesis

100

1

W → L: Partially inhibits glycogen-binding. Ref.10

Mutagenesis

126

1

K → Q: Abolishes glycogen-binding. Ref.10

Mutagenesis

146

1

L → A: Significantly reduces glycogen-binding. Ref.10

Mutagenesis

150

1

N → K: Abolishes glycogen-binding. Ref.10

Mutagenesis

150

1

N → Q: Significantly reduces glycogen-binding. Ref.10

Sequence conflict

26

1

G → E in AAC52579. Ref.1

Sequence conflict

52

1

M → I AA sequence Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

270

Helix Strand Turn

Details...

Beta strand

78 – 84

7

Beta strand

91 – 95

5

Helix

96 – 98

3

Beta strand

106 – 108

3

Beta strand

111 – 118

8

Beta strand

120 – 129

10

Beta strand

132 – 134

3

Beta strand

141 – 143

3

Beta strand

149 – 155

7

Beta strand

240 – 245

6

Beta strand

248 – 257

10

Beta strand

260 – 269

10

Sequences

	Sequence		Length	Mass (Da)
	P80386 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 62726DD357F36C7C	FASTA	270	30,394
	10 20 30 40 50 60 MGNTSSERAA LERQAGHKTP RRDSSGGTKD GDRPKILMDS PEDADIFHTE EMKAPEKEEF 70 80 90 100 110 120 LAWQHDLEVN EKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSQN NFVAILDLPE 130 140 150 160 170 180 GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS 190 200 210 220 230 240 SSPPGPYHQE PYISKPEERF KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY 250 260 270 ALSIKDGVMV LSATHRYKKK YVTTLLYKPI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
[9]	"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.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U42411 mRNA. Translation: AAC52579.1.
BC062008 mRNA. Translation: AAH62008.1.
X95577 mRNA. Translation: CAA64830.1.

IPI

IPI00231108.

RefSeq

NP_114182.1. NM_031976.1.

UniGene

Rn.3619.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z0M	X-ray	1.91	A/B/C	68-162	[»]
1Z0N	X-ray	1.49	A/B/C	68-162	[»]
4EAG	X-ray	2.70	B	187-270	[»]
4EAK	X-ray	2.50	B	200-270	[»]
4EAL	X-ray	2.51	B	200-270	[»]

ProteinModelPortal

P80386.

SMR

P80386. Positions 77-163, 189-270.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59127N.

STRING

10116.ENSRNOP00000001508.

Protein family/group databases

CAZy

CBM48. Carbohydrate-Binding Module Family 48.

PTM databases

PhosphoSite

P80386.

Proteomic databases

PaxDb

P80386.

PRIDE

P80386.

Protocols and materials databases

DNASU

83803.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000001508; ENSRNOP00000001508; ENSRNOG00000001142.

GeneID

83803.

KEGG

rno:83803.

UCSC

RGD:71057. rat.

Organism-specific databases

CTD

5564.

RGD

71057. Prkab1.

Phylogenomic databases

eggNOG

NOG238368.

GeneTree

ENSGT00390000001416.

HOGENOM

HOG000230597.

HOVERGEN

HBG050430.

InParanoid

P80386.

KO

K07199.

OMA

PYICKPE.

OrthoDB

EOG4G1MH4.

Gene expression databases

Genevestigator

P80386.

GermOnline

ENSRNOG00000001142. Rattus norvegicus.

Family and domain databases

InterPro

IPR006828. AMP_prot_kin_bsu_interact-dom.
[Graphical view]

Pfam

PF04739. AMPKBI. 1 hit.
[Graphical view]

SMART

SM01010. AMPKBI. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5054.

EvolutionaryTrace

P80386.

NextBio

616395.

Entry information

Entry name

AAKB1_RAT

Accession

Primary (citable) accession number: P80386
Secondary accession number(s): Q63048

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 125 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program