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UniProtKB - P70531 (EF2K_RAT)

Entry version 154 (02 Jun 2021)
Sequence version 1 (01 Feb 1997)
Previous versions | rss
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Protein

Eukaryotic elongation factor 2 kinase

Gene

Eef2k

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

Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Undergoes calcium/calmodulin-dependent intramolecular autophosphorylation, and this results in it becoming partially calcium/calmodulin-independent.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi295 – 301ATPBy similarity7

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

Molecular functionCalmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.20, 5301

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-166208, mTORC1-mediated signalling

<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%5Fand%5Ftaxonomy%5Fsection">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:
Eukaryotic elongation factor 2 kinase (EC:2.7.11.20)
Short name:
eEF-2 kinase
Short name:
eEF-2K
Alternative name(s):
Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Eef2k
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 1

Organism-specific databases

Rat genome database

More...RGDi		2538, Eef2k

<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

<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		CHEMBL3325307

<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%5Fprocessing%5Fsection">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 methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000869382 – 724Eukaryotic elongation factor 2 kinaseAdd BLAST723

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 residuei2N-acetylalanineBy similarity1
Modified residuei18PhosphoserineBy similarity1
Modified residuei27PhosphoserineBy similarity1
Modified residuei70PhosphoserineBy similarity1
Modified residuei73PhosphoserineCombined sources1
Modified residuei77Phosphoserine; by autocatalysis and TRPM7By similarity1
Modified residuei242PhosphoserineBy similarity1
Modified residuei347PhosphothreonineCombined sources1
Modified residuei352Phosphothreonine; by autocatalysisBy similarity1
Modified residuei358Phosphoserine; by MAPK13 and CDK1By similarity1
Modified residuei365PhosphoserineCombined sources1
Modified residuei391PhosphoserineBy similarity1
Modified residuei397Phosphoserine; by AMPKBy similarity1
Modified residuei434PhosphoserineBy similarity1
Modified residuei444PhosphoserineCombined sources1
Modified residuei469PhosphoserineCombined sources1
Modified residuei473PhosphoserineCombined sources1
Modified residuei476PhosphoserineCombined sources1
Modified residuei499Phosphoserine; by PKA1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

The N-terminus is blocked.
Autophosphorylated at multiple residues, Thr-347 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-397 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-77 resulting in improved protein stability, higher EE2F phosphorylated and subsequently reduced rate of protein synthesis. Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-358 or RPS6KA1 and RPS6KB1 at Ser-365 instead decrease EEF2K activity and promote protein synthesis (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

More...PaxDbi		P70531

PRoteomics IDEntifications database

More...PRIDEi		P70531

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P70531

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

More...PhosphoSitePlusi		P70531

<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

Widely expressed, with high levels in reticulocytes and skeletal muscle.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000016448, Expressed in skeletal muscle tissue and 22 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P70531, 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer or homodimer (Probable).

Interacts with Calmodulin/CALM1; this interaction is strictly required for phosphorylation activity (By similarity).

By similarityCurated

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P70531

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000022726

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P70531

<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		P70531

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%5Fand%5Fdomains%5Fsection">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>Domaini115 – 325Alpha-type protein kinasePROSITE-ProRule annotationAdd BLAST211

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>Regioni11 – 35DisorderedSequence analysisAdd BLAST25
Regioni80 – 93Calmodulin-bindingBy similarityAdd BLAST14
Regioni353 – 476DisorderedSequence analysisAdd BLAST124

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi378 – 404Polar residuesSequence analysisAdd BLAST27
Compositional biasi419 – 473Basic and acidic residuesSequence analysisAdd BLAST55

<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 catalytic domain is located to N-terminal region. The neighbor region contains the calmodulin-binding domain (By similarity).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

Belongs to the protein kinase superfamily. Alpha-type protein kinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QVA3, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157839

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_382143_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P70531

Identification of Orthologs from Complete Genome Data

More...OMAi		HWPVFGD

Database of Orthologous Groups

More...OrthoDBi		741011at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P70531

TreeFam database of animal gene trees

More...TreeFami		TF316085

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR017400, eEF-2K
IPR011009, Kinase-like_dom_sf
IPR004166, MHCK_EF2_kinase
IPR006597, Sel1-like
IPR011990, TPR-like_helical_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02816, Alpha_kinase, 1 hit
PF08238, Sel1, 4 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF038139, Elongation_factor_2_kinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00811, Alpha_kinase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51158, ALPHA_KINASE, 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P70531-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADEDLIFRL EGVDGGGSSG AGRHGDSDTD SDDDEGYFIC PITDDHMSNQ 
        60         70         80         90        100
NVNSKGQGYY NNLLKTECGS TGSPASSFHF KEAWKHAIEK AKHMPDPWAE 
       110        120        130        140        150
FHLEDIATEH ATRHRYNAVT GEWLKDEVLI KMASQPFGRG AMRECFRTKK 
       160        170        180        190        200
LSNFLHAQHW KGASNYVAKR YLEPVDRSVY FEDVQLQMEA KLWGEEYNRH 
       210        220        230        240        250
KPPKQVDIMQ MCIIELKDRQ GQPLFHLEHY IEGKYIKYNS NSGFVRDDNI 
       260        270        280        290        300
RLTPQAFSHF TFERSGHQLI VVDIQGVGDL YTDPQIHTEK GTDFGDGNLG 
       310        320        330        340        350
VRGMALFFYS HACNRICQSM GLAPFDLSPR EQDAVNQSTK LLQSAKTILR 
       360        370        380        390        400
GTEEKCGSPR IRTLSGSRPP LLLRLSENSG DENMSDVTFD SLPSSPSSAT 
       410        420        430        440        450
PHSQKLDHLH WPVFGDLDNM GPRDHDRMDN HRDSENSGDS GYPSEKRSDL 
       460        470        480        490        500
DDPEPREHGH SNGNRRPESD EDSLGSSGRV CVETWNLLNP SRLHLPRPSA 
       510        520        530        540        550
VALEVQRLNA LDLGRKIGKS VLGKVHLAMV RYHEGGRFCE KDEEWDQESA 
       560        570        580        590        600
IFHLEHAADL GELEAIVGLG LMYSQLPHHI LADVSLEETE ENKTKGFDYL 
       610        620        630        640        650
LKAAEAGDRQ SMILVARAFD TGLNLSPDRC QDWSEALHWY NTALETTDCD 
       660        670        680        690        700
EGGEYDGIQD EPQYALLARE AEMLLTGGFG LDKNPQRSGD LYTQAAEAAM 
       710        720 
EAMKGRLANQ YYEKAEEAWA QMEE
Length:724
Mass (Da):81,489
Last modified:February 1, 1997 - v1
<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:iE4DDD832AE9F7165
GO

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
X96426 mRNA Translation: CAA65286.1
U93849 mRNA Translation: AAB58272.1

NCBI Reference Sequences

More...RefSeqi		NP_037079.1, NM_012947.2
XP_006230218.1, XM_006230156.3
XP_006230219.1, XM_006230157.3
XP_006230220.1, XM_006230158.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000022726; ENSRNOP00000022726; ENSRNOG00000016448

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25435

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25435

UCSC genome browser

More...UCSCi		RGD:2538, 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
X96426 mRNA Translation: CAA65286.1
U93849 mRNA Translation: AAB58272.1
RefSeqiNP_037079.1, NM_012947.2
XP_006230218.1, XM_006230156.3
XP_006230219.1, XM_006230157.3
XP_006230220.1, XM_006230158.3

3D structure databases

SMRiP70531
ModBaseiSearch...

Protein-protein interaction databases

ELMiP70531
STRINGi10116.ENSRNOP00000022726

Chemistry databases

BindingDBiP70531
ChEMBLiCHEMBL3325307

PTM databases

iPTMnetiP70531
PhosphoSitePlusiP70531

Proteomic databases

PaxDbiP70531
PRIDEiP70531

Genome annotation databases

EnsembliENSRNOT00000022726; ENSRNOP00000022726; ENSRNOG00000016448
GeneIDi25435
KEGGirno:25435
UCSCiRGD:2538, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		29904
RGDi2538, Eef2k

Phylogenomic databases

eggNOGiENOG502QVA3, Eukaryota
GeneTreeiENSGT00940000157839
HOGENOMiCLU_382143_0_0_1
InParanoidiP70531
OMAiHWPVFGD
OrthoDBi741011at2759
PhylomeDBiP70531
TreeFamiTF316085

Enzyme and pathway databases

BRENDAi2.7.11.20, 5301
ReactomeiR-RNO-166208, mTORC1-mediated signalling

Miscellaneous databases

Protein Ontology

More...PROi		PR:P70531

Gene expression databases

BgeeiENSRNOG00000016448, Expressed in skeletal muscle tissue and 22 other tissues
GenevisibleiP70531, RN

Family and domain databases

Gene3Di1.25.40.10, 1 hit
InterProiView protein in InterPro
IPR017400, eEF-2K
IPR011009, Kinase-like_dom_sf
IPR004166, MHCK_EF2_kinase
IPR006597, Sel1-like
IPR011990, TPR-like_helical_dom_sf
PfamiView protein in Pfam
PF02816, Alpha_kinase, 1 hit
PF08238, Sel1, 4 hits
PIRSFiPIRSF038139, Elongation_factor_2_kinase, 1 hit
SMARTiView protein in SMART
SM00811, Alpha_kinase, 1 hit
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51158, ALPHA_KINASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...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 nameiEF2K_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: P70531
Secondary accession number(s): O09089
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: June 2, 2021
This is version 154 of the entry and version 1 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
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