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Entry version 135 (11 Dec 2019)
Sequence version 2 (27 Jul 2011)
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Protein

5'-AMP-activated protein kinase subunit gamma-2

Gene

Prkag2

Organism
Mus musculus (Mouse)
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

AMP/ATP-binding 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. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei299AMP, ADP or ATP 2By similarity1
Binding sitei359AMP or ATP 1; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei380AMP 3By similarity1
Binding sitei399AMP, ADP or ATP 2By similarity1
Binding sitei429AMP 3By similarity1
Binding sitei434AMP 3; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei498AMP, ADP or ATP 2By similarity1
Binding sitei506AMP, ADP or ATP 2; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei527AMP 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi316 – 319AMP, ADP or ATP 1By similarity4
Nucleotide bindingi380 – 381AMP, ADP or ATP 1By similarity2
Nucleotide bindingi455 – 456AMP 3By similarity2
Nucleotide bindingi471 – 474AMP, ADP or ATP 2By similarity4
Nucleotide bindingi527 – 528AMP, ADP or ATP 2By similarity2
Nucleotide bindingi543 – 546AMP 3By similarity4

<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

GO - Biological processi

<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
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1632852 Macroautophagy
R-MMU-163680 AMPK inhibits chREBP transcriptional activation activity
R-MMU-200425 Import of palmitoyl-CoA into the mitochondrial matrix
R-MMU-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-MMU-5628897 TP53 Regulates Metabolic Genes
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-9613354 Lipophagy

<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 gamma-2
Short name:
AMPK gamma2
Short name:
AMPK subunit gamma-2
<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:Prkag2
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1336153 Prkag2

<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 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 ‘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_00002043821 – 5665'-AMP-activated protein kinase subunit gamma-2Add BLAST566

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei65PhosphoserineCombined sources1
Modified residuei71PhosphoserineCombined sources1
Modified residuei73PhosphoserineCombined sources1
Modified residuei90PhosphoserineCombined sources1
Modified residuei138PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei158PhosphoserineCombined sources1
Modified residuei161PhosphoserineCombined sources1
Modified residuei162PhosphoserineCombined sources1
Modified residuei165PhosphothreonineCombined sources1
Modified residuei196PhosphoserineCombined sources1

<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 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

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q91WG5

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

More...
PaxDbi
Q91WG5

PRoteomics IDEntifications database

More...
PRIDEi
Q91WG5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q91WG5

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

More...
PhosphoSitePlusi
Q91WG5

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000028944 Expressed in 291 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q91WG5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q91WG5 MM

<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 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
223832, 1 interactor

Protein interaction database and analysis system

More...
IntActi
Q91WG5, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000030784

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q91WG5 protein

<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

3D structure databases

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

More...
SMRi
Q91WG5

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini272 – 332CBS 1PROSITE-ProRule annotationAdd BLAST61
Domaini354 – 412CBS 2PROSITE-ProRule annotationAdd BLAST59
Domaini427 – 489CBS 3PROSITE-ProRule annotationAdd BLAST63
Domaini501 – 559CBS 4PROSITE-ProRule annotationAdd BLAST59

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi367 – 388AMPK pseudosubstrateAdd BLAST22

<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 AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1 (By similarity).By similarity
The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 3 are occupied, designated as sites 1, 3, and 4 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Of these, site 4 appears to be a structural site that retains a tightly held AMP molecule (AMP 3). The 2 remaining sites, 1 and 3, can bind either AMP, ADP or ATP. Site 1 (AMP, ADP or ATP 1) is the high-affinity binding site and likely accommodates AMP or ADP. Site 3 (AMP, ADP or ATP 2) is the weakest nucleotide-binding site on the gamma subunit, yet it is exquisitely sensitive to changes in nucleotide levels and this allows AMPK to respond rapidly to changes in cellular energy status. Site 3 is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of AMP or ADP.By similarity

<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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1764 Eukaryota
COG0517 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183019

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000176880

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q91WG5

KEGG Orthology (KO)

More...
KOi
K07200

Identification of Orthologs from Complete Genome Data

More...
OMAi
YYCQFPD

Database of Orthologous Groups

More...
OrthoDBi
631088at2759

TreeFam database of animal gene trees

More...
TreeFami
TF313247

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039170 AMPKG-2
IPR000644 CBS_dom

The PANTHER Classification System

More...
PANTHERi
PTHR13780:SF122 PTHR13780:SF122, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00571 CBS, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00116 CBS, 4 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51371 CBS, 4 hits

<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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform A (identifier: Q91WG5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGSAAMDTKK KKEVSSPGGS SGKKNPSLKR RSLRVHIPDL SSFAMPLLDG
60 70 80 90 100
DVENSEKHSS RKVDSPFSSG SPSRGLFSRG PQPRPSSPVS APVRPKTSPG
110 120 130 140 150
SPKTVFPFSY QESPPRSPRR MSFSGIFRSS SKESSPNSNP STSPGGIRFF
160 170 180 190 200
SRSRKTSSVS SSPSTPTQVT KQHPFPLESY KQEPERPESR IYASSSPPDT
210 220 230 240 250
GQRFCLAFQS PARPPLASPT YHAPLRTAVL AAAPGPAEAG MLEKLEFQEE
260 270 280 290 300
EDSESGVYMR FMRSHKCYDI VPTSSKLVVF DTTLQVKKAF FALVANGVRA
310 320 330 340 350
APLWESKKQS FVGMLTITDF INILHRYYKS PMVQIYELEE HKIETWRELY
360 370 380 390 400
LQETFKPLVN ISPDASLFDA VYSLIKNKIH RLPVIDPISG NALYILTHKR
410 420 430 440 450
ILKFLQLFMS DMPKPAFMKQ NLDELGIGTY HNIAFIHPDT PIIKALNIFV
460 470 480 490 500
ERRISALPVV DESGKVVDIY SKFDVINLAA EKTYNNLDIT VTQALQHRSQ
510 520 530 540 550
YFEGVVKCSK LETLETIVDR IVRAEVHRLV VVNEADSIVG IISLSDILQA
560
LILTPAGAKQ KETETE
Length:566
Mass (Da):62,949
Last modified:July 27, 2011 - v2
<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:iD112BFD69D1C5ACB
GO
Isoform B (identifier: Q91WG5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-240: Missing.

Show »
Length:326
Mass (Da):37,312
Checksum:iFEA2EEAB9550999A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q8BIQ9Q8BIQ9_MOUSE
5'-AMP-activated protein kinase sub...
Prkag2
443Annotation score:

Annotation score:1 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>
D3YUS1D3YUS1_MOUSE
5'-AMP-activated protein kinase sub...
Prkag2
244Annotation score:

Annotation score:1 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>
D3YYW4D3YYW4_MOUSE
5'-AMP-activated protein kinase sub...
Prkag2
191Annotation score:

Annotation score:1 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>
D3Z5V5D3Z5V5_MOUSE
5'-AMP-activated protein kinase sub...
Prkag2
19Annotation score:

Annotation score:1 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 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 conflicti257V → F in AAH15283 (PubMed:15489334).Curated1
Sequence conflicti516T → N in AAQ55224 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0155861 – 240Missing in isoform B. 1 PublicationAdd BLAST240

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY348864 mRNA Translation: AAQ55224.1
AC116151 Genomic DNA No translation available.
AC125270 Genomic DNA No translation available.
BC015283 mRNA Translation: AAH15283.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS19130.1 [Q91WG5-1]
CCDS51437.1 [Q91WG5-2]

NCBI Reference Sequences

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RefSeqi
NP_001164027.1, NM_001170556.1 [Q91WG5-2]
NP_663376.2, NM_145401.2 [Q91WG5-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000030784; ENSMUSP00000030784; ENSMUSG00000028944 [Q91WG5-1]
ENSMUST00000114975; ENSMUSP00000110626; ENSMUSG00000028944 [Q91WG5-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
108099

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:108099

UCSC genome browser

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UCSCi
uc008wsk.2 mouse [Q91WG5-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AY348864 mRNA Translation: AAQ55224.1
AC116151 Genomic DNA No translation available.
AC125270 Genomic DNA No translation available.
BC015283 mRNA Translation: AAH15283.1
CCDSiCCDS19130.1 [Q91WG5-1]
CCDS51437.1 [Q91WG5-2]
RefSeqiNP_001164027.1, NM_001170556.1 [Q91WG5-2]
NP_663376.2, NM_145401.2 [Q91WG5-1]

3D structure databases

SMRiQ91WG5
ModBaseiSearch...

Protein-protein interaction databases

BioGridi223832, 1 interactor
IntActiQ91WG5, 1 interactor
STRINGi10090.ENSMUSP00000030784

PTM databases

iPTMnetiQ91WG5
PhosphoSitePlusiQ91WG5

Proteomic databases

jPOSTiQ91WG5
PaxDbiQ91WG5
PRIDEiQ91WG5

Genome annotation databases

EnsembliENSMUST00000030784; ENSMUSP00000030784; ENSMUSG00000028944 [Q91WG5-1]
ENSMUST00000114975; ENSMUSP00000110626; ENSMUSG00000028944 [Q91WG5-2]
GeneIDi108099
KEGGimmu:108099
UCSCiuc008wsk.2 mouse [Q91WG5-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
51422
MGIiMGI:1336153 Prkag2

Phylogenomic databases

eggNOGiKOG1764 Eukaryota
COG0517 LUCA
GeneTreeiENSGT00950000183019
HOGENOMiHOG000176880
InParanoidiQ91WG5
KOiK07200
OMAiYYCQFPD
OrthoDBi631088at2759
TreeFamiTF313247

Enzyme and pathway databases

ReactomeiR-MMU-1632852 Macroautophagy
R-MMU-163680 AMPK inhibits chREBP transcriptional activation activity
R-MMU-200425 Import of palmitoyl-CoA into the mitochondrial matrix
R-MMU-380972 Energy dependent regulation of mTOR by LKB1-AMPK
R-MMU-5628897 TP53 Regulates Metabolic Genes
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-9613354 Lipophagy

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Prkag2 mouse

Protein Ontology

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PROi
PR:Q91WG5
RNActiQ91WG5 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028944 Expressed in 291 organ(s), highest expression level in testis
ExpressionAtlasiQ91WG5 baseline and differential
GenevisibleiQ91WG5 MM

Family and domain databases

InterProiView protein in InterPro
IPR039170 AMPKG-2
IPR000644 CBS_dom
PANTHERiPTHR13780:SF122 PTHR13780:SF122, 1 hit
PfamiView protein in Pfam
PF00571 CBS, 3 hits
SMARTiView protein in SMART
SM00116 CBS, 4 hits
PROSITEiView protein in PROSITE
PS51371 CBS, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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 nameiAAKG2_MOUSE
<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: Q91WG5
Secondary accession number(s): E9QK80, Q6V7V5
<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: September 13, 2005
Last sequence update: July 27, 2011
Last modified: December 11, 2019
This is version 135 of the entry and version 2 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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