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UniProtKB - P80386 (AAKB1_RAT)

Entry version 173 (16 Jan 2019)
Sequence version 4 (23 Jan 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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).

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.31 5301

Reactome - a knowledgebase of biological pathways and processes

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

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		CBM48 Carbohydrate-Binding Module Family 48

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Prkab1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Rat genome database

More...RGDi		71057 Prkab1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi100W → G: Abolishes glycogen-binding. 1 Publication1
Mutagenesisi100W → L: Partially inhibits glycogen-binding. 1 Publication1
Mutagenesisi126K → Q: Abolishes glycogen-binding. 1 Publication1
Mutagenesisi146L → A: Significantly reduces glycogen-binding. 1 Publication1
Mutagenesisi150N → K: Abolishes glycogen-binding. 1 Publication1
Mutagenesisi150N → Q: Significantly reduces glycogen-binding. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3885503

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002043672 – 2705'-AMP-activated protein kinase subunit beta-1Add BLAST269

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine2 Publications1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei4PhosphothreonineBy similarity1
Modified residuei5PhosphoserineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Modified residuei19PhosphothreonineBy similarity1
Modified residuei24Phosphoserine; by autocatalysis2 Publications1
Modified residuei25Phosphoserine; by autocatalysis2 Publications1
Modified residuei40PhosphoserineCombined sources1
Modified residuei96Phosphoserine1 Publication1
Modified residuei101Phosphoserine1 Publication1
Modified residuei108Phosphoserine; by autocatalysisCombined sources3 Publications1
Modified residuei148PhosphothreonineBy similarity1
Modified residuei182Phosphoserine2 Publications1
Modified residuei201N6-succinyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P80386

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P80386

PRoteomics IDEntifications database

More...PRIDEi		P80386

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P80386

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P80386

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000001142 Expressed in 10 organ(s), highest expression level in heart

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P80386 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		249839, 1 interactor

Database of interacting proteins

More...DIPi		DIP-59127N

Protein interaction database and analysis system

More...IntActi		P80386, 178 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000001508

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
5KQ5X-ray3.41B68-270[»]
5T5TX-ray3.46B68-270[»]
5UFUX-ray3.45B67-270[»]
6E4TX-ray3.40B67-270[»]
6E4UX-ray3.27B67-270[»]
6E4WX-ray3.35B67-270[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P80386

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P80386

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P80386

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni68 – 163Glycogen-binding domainAdd BLAST96

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the 5'-AMP-activated protein kinase beta subunit family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1616 Eukaryota
ENOG410XRB3 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155307

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000230597

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG050430

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P80386

KEGG Orthology (KO)

More...KOi		K07199

Identification of Orthologs from Complete Genome Data

More...OMAi		QWTHDPA

Database of Orthologous Groups

More...OrthoDBi		956412at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P80386

TreeFam database of animal gene trees

More...TreeFami		TF313827

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR032640 AMPK1_CBM
IPR039160 AMPKB
IPR006828 ASC_dom
IPR037256 ASC_dom_sf
IPR013783 Ig-like_fold
IPR014756 Ig_E-set

The PANTHER Classification System

More...PANTHERi		PTHR10343:SF80 PTHR10343:SF80, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16561 AMPK1_CBM, 1 hit
PF04739 AMPKBI, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01010 AMPKBI, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF160219 SSF160219, 1 hit
SSF81296 SSF81296, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i62726DD357F36C7C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti26G → E in AAC52579 (PubMed:8621499).Curated1
Sequence conflicti52M → I AA sequence (PubMed:7961907).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U42411 mRNA Translation: AAC52579.1
BC062008 mRNA Translation: AAH62008.1
X95577 mRNA Translation: CAA64830.1

NCBI Reference Sequences

More...RefSeqi		NP_114182.1, NM_031976.1
XP_006249543.1, XM_006249481.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Rn.3619

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000001508; ENSRNOP00000001508; ENSRNOG00000001142

Database of genes from NCBI RefSeq genomes

More...GeneIDi		83803

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:83803

UCSC genome browser

More...UCSCi		RGD:71057 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_006249481.3
UniGeneiRn.3619

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5KQ5X-ray3.41B68-270[»]
5T5TX-ray3.46B68-270[»]
5UFUX-ray3.45B67-270[»]
6E4TX-ray3.40B67-270[»]
6E4UX-ray3.27B67-270[»]
6E4WX-ray3.35B67-270[»]
ProteinModelPortaliP80386
SMRiP80386
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249839, 1 interactor
DIPiDIP-59127N
IntActiP80386, 178 interactors
STRINGi10116.ENSRNOP00000001508

Chemistry databases

ChEMBLiCHEMBL3885503

Protein family/group databases

CAZyiCBM48 Carbohydrate-Binding Module Family 48

PTM databases

iPTMnetiP80386
PhosphoSitePlusiP80386

Proteomic databases

jPOSTiP80386
PaxDbiP80386
PRIDEiP80386

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		83803
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001508; ENSRNOP00000001508; ENSRNOG00000001142
GeneIDi83803
KEGGirno:83803
UCSCiRGD:71057 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5564
RGDi71057 Prkab1

Phylogenomic databases

eggNOGiKOG1616 Eukaryota
ENOG410XRB3 LUCA
GeneTreeiENSGT00940000155307
HOGENOMiHOG000230597
HOVERGENiHBG050430
InParanoidiP80386
KOiK07199
OMAiQWTHDPA
OrthoDBi956412at2759
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
R-RNO-6804756 Regulation of TP53 Activity through Phosphorylation

Miscellaneous databases

EvolutionaryTraceiP80386

Protein Ontology

More...PROi		PR:P80386

Gene expression databases

BgeeiENSRNOG00000001142 Expressed in 10 organ(s), highest expression level in heart
GenevisibleiP80386 RN

Family and domain databases

Gene3Di2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR032640 AMPK1_CBM
IPR039160 AMPKB
IPR006828 ASC_dom
IPR037256 ASC_dom_sf
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
PANTHERiPTHR10343:SF80 PTHR10343:SF80, 1 hit
PfamiView protein in Pfam
PF16561 AMPK1_CBM, 1 hit
PF04739 AMPKBI, 1 hit
SMARTiView protein in SMART
SM01010 AMPKBI, 1 hit
SUPFAMiSSF160219 SSF160219, 1 hit
SSF81296 SSF81296, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAAKB1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P80386
Secondary accession number(s): Q63048
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 173 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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