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Protein

Elongation factor 2

Gene

EEF2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).By similarity

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 bindingi26 – 33GTPBy similarity8
Nucleotide bindingi104 – 108GTPBy similarity5
Nucleotide bindingi158 – 161GTPBy 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

Molecular functionElongation factor
Biological processProtein biosynthesis
LigandGTP-binding, Nucleotide-binding

<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:
Elongation factor 2
Short name:
EF-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:EEF2
<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>OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
<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 identifieri9601 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
<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
  • UP000001595 <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 19

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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_00002234871 – 858Elongation factor 2Add BLAST858

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 residuei54PhosphothreonineBy similarity1
Modified residuei57Phosphothreonine; by EEF2KBy similarity1
Modified residuei59PhosphothreonineBy similarity1
Modified residuei152N6-succinyllysineBy similarity1
Modified residuei235N6-acetyllysineBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei265Phosphotyrosine; by CSKBy similarity1
Modified residuei272N6-acetyllysine; alternateBy similarity1
Modified residuei272N6-succinyllysine; alternateBy similarity1
Modified residuei275N6-acetyllysineBy similarity1
Cross-linki322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei325PhosphoserineBy similarity1
Modified residuei373Phosphotyrosine; by CSKBy similarity1
Modified residuei435PhosphothreonineBy similarity1
Modified residuei439N6-acetyllysineBy similarity1
Modified residuei445N6-acetyllysineBy similarity1
Modified residuei502PhosphoserineBy similarity1
Modified residuei525N6,N6,N6-trimethyllysine; by EEF2KMTBy similarity1
Cross-linki529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei572N6-succinyllysineBy similarity1
Modified residuei595Phosphoserine; by CDK2By similarity1
Modified residuei619N6-acetyllysineBy similarity1
Modified residuei715DiphthamideBy similarity1

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

Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic cleavage, and nuclear translocation if the C-terminal fragment.By similarity
Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis (By similarity).By similarity
ISGylated.By similarity
Proteolytically processed at two sites following phosphorylation by CSK.By similarity
SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei586 – 587CleavageBy similarity2
Sitei605 – 606CleavageBy similarity2

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q5R8Z3

<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

Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9. Interacts with RBPMS2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9601.ENSPPYP00000010534

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q5R8Z3

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

More...
SMRi
Q5R8Z3

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Domaini17 – 362tr-type GPROSITE-ProRule annotationAdd BLAST346

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0469 Eukaryota
COG0480 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154662

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG001838

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5R8Z3

KEGG Orthology (KO)

More...
KOi
K03234

Identification of Orthologs from Complete Genome Data

More...
OMAi
HLISGMG

Database of Orthologous Groups

More...
OrthoDBi
140796at2759

TreeFam database of animal gene trees

More...
TreeFami
TF300575

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035647 EFG_III/V
IPR000640 EFG_V-like
IPR004161 EFTu-like_2
IPR031157 G_TR_CS
IPR027417 P-loop_NTPase
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR005225 Small_GTP-bd_dom
IPR000795 TF_GTP-bd_dom
IPR009000 Transl_B-barrel_sf
IPR005517 Transl_elong_EFG/EF2_IV

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00679 EFG_C, 1 hit
PF03764 EFG_IV, 1 hit
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00315 ELONGATNFCT

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00838 EFG_C, 1 hit
SM00889 EFG_IV, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50447 SSF50447, 1 hit
SSF52540 SSF52540, 1 hit
SSF54211 SSF54211, 1 hit
SSF54980 SSF54980, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00301 G_TR_1, 1 hit
PS51722 G_TR_2, 1 hit

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

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

Q5R8Z3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR
60 70 80 90 100
AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI
110 120 130 140 150
NLIDSPGHVD FSSEVTAALR VTDGALVVVD CVSGVCVQTE TVLRQAIAER
160 170 180 190 200
IKPVLMMNKM DRALLELQLE PEELYQTFQR IVENVNVIIS TYGEGESGPM
210 220 230 240 250
GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG EGQLGPAERA
260 270 280 290 300
KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV
310 320 330 340 350
FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL
360 370 380 390 400
LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK
410 420 430 440 450
MVPTSDKGRF YAFGRVFSGL VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT
460 470 480 490 500
ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV KTGTITTFEH AHNMRVMKFS
510 520 530 540 550
VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE SGEHIIAGAG
560 570 580 590 600
ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN
610 620 630 640 650
RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW
660 670 680 690 700
CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV
710 720 730 740 750
RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ
760 770 780 790 800
CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL
810 820 830 840 850
RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA

LDNFLDKL
Length:858
Mass (Da):95,338
Last modified:January 23, 2007 - 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:i78BD1710236C0D9C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti233V → A in CAH90954 (Ref. 1) Curated1
Sequence conflicti286P → A in CAH91767 (Ref. 1) Curated1
Sequence conflicti794F → L in CAH91767 (Ref. 1) 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
CR858745 mRNA Translation: CAH90954.1
CR859604 mRNA Translation: CAH91767.1

NCBI Reference Sequences

More...
RefSeqi
NP_001125547.1, NM_001132075.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSPPYT00000010948; ENSPPYP00000010534; ENSPPYG00000009393

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100172460

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pon:100172460

<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
CR858745 mRNA Translation: CAH90954.1
CR859604 mRNA Translation: CAH91767.1
RefSeqiNP_001125547.1, NM_001132075.1

3D structure databases

ProteinModelPortaliQ5R8Z3
SMRiQ5R8Z3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000010534

Proteomic databases

PRIDEiQ5R8Z3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSPPYT00000010948; ENSPPYP00000010534; ENSPPYG00000009393
GeneIDi100172460
KEGGipon:100172460

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1938

Phylogenomic databases

eggNOGiKOG0469 Eukaryota
COG0480 LUCA
GeneTreeiENSGT00940000154662
HOVERGENiHBG001838
InParanoidiQ5R8Z3
KOiK03234
OMAiHLISGMG
OrthoDBi140796at2759
TreeFamiTF300575

Family and domain databases

Gene3Di3.30.230.10, 1 hit
InterProiView protein in InterPro
IPR035647 EFG_III/V
IPR000640 EFG_V-like
IPR004161 EFTu-like_2
IPR031157 G_TR_CS
IPR027417 P-loop_NTPase
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR005225 Small_GTP-bd_dom
IPR000795 TF_GTP-bd_dom
IPR009000 Transl_B-barrel_sf
IPR005517 Transl_elong_EFG/EF2_IV
PfamiView protein in Pfam
PF00679 EFG_C, 1 hit
PF03764 EFG_IV, 1 hit
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit
PRINTSiPR00315 ELONGATNFCT
SMARTiView protein in SMART
SM00838 EFG_C, 1 hit
SM00889 EFG_IV, 1 hit
SUPFAMiSSF50447 SSF50447, 1 hit
SSF52540 SSF52540, 1 hit
SSF54211 SSF54211, 1 hit
SSF54980 SSF54980, 2 hits
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS00301 G_TR_1, 1 hit
PS51722 G_TR_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiEF2_PONAB
<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: Q5R8Z3
Secondary accession number(s): Q5RBA6
<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 21, 2006
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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