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Entry version 149 (16 Jan 2019)
Sequence version 3 (01 Nov 1997)
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Protein

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

Gene

Prkag1

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

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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei69AMP, ADP or ATP 21 Publication1
Binding sitei129AMP, ADP or ATP 1; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei150AMP 31 Publication1
Binding sitei169AMP, ADP or ATP 21 Publication1
Binding sitei199AMP 31 Publication1
Binding sitei204AMP 3; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei268AMP, ADP or ATP 21 Publication1
Binding sitei276AMP, ADP or ATP 2; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei297AMP 31 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi86 – 89AMP, ADP or ATP 11 Publication4
Nucleotide bindingi150 – 151AMP, ADP or ATP 11 Publication2
Nucleotide bindingi225 – 226AMP 31 Publication2
Nucleotide bindingi241 – 244AMP, ADP or ATP 21 Publication4
Nucleotide bindingi297 – 298AMP, ADP or ATP 21 Publication2
Nucleotide bindingi313 – 316AMP 31 Publication4

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.31 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-201722 Formation of the beta-catenin:TCF transactivating complex
R-RNO-3214841 PKMTs methylate histone lysines
R-RNO-3769402 Deactivation of the beta-catenin transactivating complex
R-RNO-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function

<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-1
Short name:
AMPK gamma1
Short name:
AMPK subunit gamma-1
Short name:
AMPKg
<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:Prkag1
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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 7

Organism-specific databases

Rat genome database

More...
RGDi
3388 Prkag1

<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

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 ‘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_00002043801 – 3305'-AMP-activated protein kinase subunit gamma-1Add BLAST330

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 residuei260Phosphoserine; by ULK11 Publication1
Modified residuei262Phosphothreonine; by ULK11 Publication1
Modified residuei269Phosphoserine; by ULK11 Publication1

<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 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. There is some ambiguity for a phosphosite: Ser-260/Thr-262.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P80385

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

More...
PaxDbi
P80385

PRoteomics IDEntifications database

More...
PRIDEi
P80385

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P80385

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

More...
PhosphoSitePlusi
P80385

<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 heart and brain, also found in kidney, white adipose tissue, lung and spleen.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000061499 Expressed in 10 organ(s), highest expression level in heart

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P80385 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P80385 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 FNIP2.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-37278N

Protein interaction database and analysis system

More...
IntActi
P80385, 4 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000020093

<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

1330
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
2V8QX-ray2.10E1-330[»]
2V92X-ray2.40E1-330[»]
2V9JX-ray2.53E1-330[»]
2Y8LX-ray2.50E1-330[»]
2Y8QX-ray2.80E1-330[»]
2YA3X-ray2.51E1-330[»]
4CFHX-ray3.24E1-330[»]
4EAGX-ray2.70C1-330[»]
4EAIX-ray2.28C1-330[»]
4EAJX-ray2.61C1-330[»]
4EAKX-ray2.50C1-330[»]
4EALX-ray2.51C1-330[»]
4QFGX-ray3.46C1-330[»]
4QFRX-ray3.34C1-330[»]
4QFSX-ray3.55C1-330[»]
5KQ5X-ray3.41C1-330[»]
5T5TX-ray3.46C1-330[»]
5UFUX-ray3.45C1-330[»]
6E4TX-ray3.40C1-330[»]
6E4UX-ray3.27C1-330[»]
6E4WX-ray3.35C1-330[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P80385

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

More...
SMRi
P80385

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
P80385

<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>Domaini42 – 102CBS 1PROSITE-ProRule annotationAdd BLAST61
Domaini124 – 186CBS 2PROSITE-ProRule annotationAdd BLAST63
Domaini197 – 259CBS 3PROSITE-ProRule annotationAdd BLAST63
Domaini271 – 328CBS 4PROSITE-ProRule annotationAdd BLAST58

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>Motifi137 – 158AMPK 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.4 Publications

<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
ENSGT00940000156707

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000176880

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG050431

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P80385

KEGG Orthology (KO)

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KOi
K07200

Database of Orthologous Groups

More...
OrthoDBi
631088at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P80385

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
IPR039166 AMPKG-1
IPR000644 CBS_dom

The PANTHER Classification System

More...
PANTHERi
PTHR13780:SF38 PTHR13780:SF38, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P80385-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MESVAAESAP APENEHSQET PESNSSVYTT FMKSHRCYDL IPTSSKLVVF
60 70 80 90 100
DTSLQVKKAF FALVTNGVRA APLWDSKKQS FVGMLTITDF INILHRYYKS
110 120 130 140 150
ALVQIYELEE HKIETWREVY LQDSFKPLVC ISPNASLFDA VSSLIRNKIH
160 170 180 190 200
RLPVIDPESG NTLYILTHKR ILKFLKLFIT EFPKPEFMSK SLEELQIGTY
210 220 230 240 250
ANIAMVRTTT PVYVALGIFV QHRVSALPVV DEKGRVVDIY SKFDVINLAA
260 270 280 290 300
EKTYNNLDVS VTKALQHRSH YFEGVLKCYL HETLEAIINR LVEAEVHRLV
310 320 330
VVDEHDVVKG IVSLSDILQA LVLTGGEKKP
Length:330
Mass (Da):37,386
Last modified:November 1, 1997 - v3
<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:i36031E526C1F1E97
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JVD6A0A0G2JVD6_RAT
Lysine methyltransferase 2D
Kmt2d
5,840Annotation score:

Annotation score:2 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>
A0A0G2K913A0A0G2K913_RAT
Lysine methyltransferase 2D
Prkag1 Kmt2d
329Annotation 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 conflicti114E → Q AA sequence (PubMed:7961907).Curated1
Sequence conflicti201A → P 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
X95578 mRNA Translation: CAA64831.1
BC097940 mRNA Translation: AAH97940.1
U42413 mRNA Translation: AAC52580.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T10759

NCBI Reference Sequences

More...
RefSeqi
NP_037142.1, NM_013010.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.11089

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000083354; ENSRNOP00000070458; ENSRNOG00000061499

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25520

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25520

UCSC genome browser

More...
UCSCi
RGD:3388 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
X95578 mRNA Translation: CAA64831.1
BC097940 mRNA Translation: AAH97940.1
U42413 mRNA Translation: AAC52580.1
PIRiT10759
RefSeqiNP_037142.1, NM_013010.2
UniGeneiRn.11089

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V8QX-ray2.10E1-330[»]
2V92X-ray2.40E1-330[»]
2V9JX-ray2.53E1-330[»]
2Y8LX-ray2.50E1-330[»]
2Y8QX-ray2.80E1-330[»]
2YA3X-ray2.51E1-330[»]
4CFHX-ray3.24E1-330[»]
4EAGX-ray2.70C1-330[»]
4EAIX-ray2.28C1-330[»]
4EAJX-ray2.61C1-330[»]
4EAKX-ray2.50C1-330[»]
4EALX-ray2.51C1-330[»]
4QFGX-ray3.46C1-330[»]
4QFRX-ray3.34C1-330[»]
4QFSX-ray3.55C1-330[»]
5KQ5X-ray3.41C1-330[»]
5T5TX-ray3.46C1-330[»]
5UFUX-ray3.45C1-330[»]
6E4TX-ray3.40C1-330[»]
6E4UX-ray3.27C1-330[»]
6E4WX-ray3.35C1-330[»]
ProteinModelPortaliP80385
SMRiP80385
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37278N
IntActiP80385, 4 interactors
STRINGi10116.ENSRNOP00000020093

Chemistry databases

ChEMBLiCHEMBL3885503

PTM databases

iPTMnetiP80385
PhosphoSitePlusiP80385

Proteomic databases

jPOSTiP80385
PaxDbiP80385
PRIDEiP80385

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000083354; ENSRNOP00000070458; ENSRNOG00000061499
GeneIDi25520
KEGGirno:25520
UCSCiRGD:3388 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5571
RGDi3388 Prkag1

Phylogenomic databases

eggNOGiKOG1764 Eukaryota
COG0517 LUCA
GeneTreeiENSGT00940000156707
HOGENOMiHOG000176880
HOVERGENiHBG050431
InParanoidiP80385
KOiK07200
OrthoDBi631088at2759
PhylomeDBiP80385
TreeFamiTF313247

Enzyme and pathway databases

BRENDAi2.7.11.31 5301
ReactomeiR-RNO-201722 Formation of the beta-catenin:TCF transactivating complex
R-RNO-3214841 PKMTs methylate histone lysines
R-RNO-3769402 Deactivation of the beta-catenin transactivating complex
R-RNO-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function

Miscellaneous databases

EvolutionaryTraceiP80385

Protein Ontology

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PROi
PR:P80385

Gene expression databases

BgeeiENSRNOG00000061499 Expressed in 10 organ(s), highest expression level in heart
ExpressionAtlasiP80385 baseline and differential
GenevisibleiP80385 RN

Family and domain databases

InterProiView protein in InterPro
IPR039166 AMPKG-1
IPR000644 CBS_dom
PANTHERiPTHR13780:SF38 PTHR13780:SF38, 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
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 nameiAAKG1_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: P80385
Secondary accession number(s): Q4QQW6
<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: November 1, 1997
Last modified: January 16, 2019
This is version 149 of the entry and version 3 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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