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Protein

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

Gene

PRKAB1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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) (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-BTA-1632852. Macroautophagy.
R-BTA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-BTA-5628897. TP53 Regulates Metabolic Genes.
R-BTA-6804756. Regulation of TP53 Activity through Phosphorylation.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 17

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 2702695'-AMP-activated protein kinase subunit beta-1PRO_0000239699Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiQ5BIS9.
PRIDEiQ5BIS9.

Expressioni

Gene expression databases

BgeeiENSBTAG00000005940.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007798.

Structurei

3D structure databases

ProteinModelPortaliQ5BIS9.
SMRiQ5BIS9. Positions 77-163, 189-270.
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.
InParanoidiQ5BIS9.
KOiK07199.
OMAiSKDGDRP.
OrthoDBiEOG091G0DZR.
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.

Q5BIS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNTSSERAA LDRQGGHKTP RRDSSGGSKD GDRPKILMDS PEDADLFHSE
60 70 80 90 100
EIKAPEKEEF LAWQHDLEVN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW
110 120 130 140 150
SKLPLTRSHN NFVAILDLPE GEHQYKFFVD GQWTHDPSEP VVTSQLGTVN
160 170 180 190 200
NVIQVKKTDF EVFDALMVDS QKCSDVSELS SSPPGPYHQE PYISKPEERF
210 220 230 240 250
KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY ALSIKDGVMV
260 270
LSATHRYKKK YVTTLLYKPI
Length:270
Mass (Da):30,287
Last modified:January 23, 2007 - v3
Checksum:i0ADEE97863AF8680
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021145 mRNA. Translation: AAX31327.1.
BC150021 mRNA. Translation: AAI50022.1.
RefSeqiNP_001019729.1. NM_001024558.1.
XP_005217938.1. XM_005217881.3.
UniGeneiBt.20256.

Genome annotation databases

EnsembliENSBTAT00000007798; ENSBTAP00000007798; ENSBTAG00000005940.
GeneIDi534107.
KEGGibta:534107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021145 mRNA. Translation: AAX31327.1.
BC150021 mRNA. Translation: AAI50022.1.
RefSeqiNP_001019729.1. NM_001024558.1.
XP_005217938.1. XM_005217881.3.
UniGeneiBt.20256.

3D structure databases

ProteinModelPortaliQ5BIS9.
SMRiQ5BIS9. Positions 77-163, 189-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007798.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

Proteomic databases

PaxDbiQ5BIS9.
PRIDEiQ5BIS9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000007798; ENSBTAP00000007798; ENSBTAG00000005940.
GeneIDi534107.
KEGGibta:534107.

Organism-specific databases

CTDi5564.

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
ENOG410XRB3. LUCA.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiQ5BIS9.
KOiK07199.
OMAiSKDGDRP.
OrthoDBiEOG091G0DZR.
TreeFamiTF313827.

Enzyme and pathway databases

ReactomeiR-BTA-1632852. Macroautophagy.
R-BTA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-BTA-5628897. TP53 Regulates Metabolic Genes.
R-BTA-6804756. Regulation of TP53 Activity through Phosphorylation.

Gene expression databases

BgeeiENSBTAG00000005940.

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_BOVIN
AccessioniPrimary (citable) accession number: Q5BIS9
Secondary accession number(s): A6QQW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.