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Protein

Elongation factor 1-beta

Gene

EEF1B2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.

GO - Molecular functioni

  • translation elongation factor activity Source: UniProtKB

GO - Biological processi

  • translational elongation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000114942-MONOMER.
ReactomeiR-HSA-156842. Eukaryotic Translation Elongation.
SIGNORiP24534.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-beta
Short name:
EF-1-beta
Gene namesi
Name:EEF1B2
Synonyms:EEF1B, EF1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3208. EEF1B2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • eukaryotic translation elongation factor 1 complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi1933.
OpenTargetsiENSG00000114942.
ENSG00000283391.
PharmGKBiPA27644.

Polymorphism and mutation databases

BioMutaiEEF1B2.
DMDMi119163.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001550212 – 225Elongation factor 1-betaAdd BLAST224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7N6-acetyllysineCombined sources1
Modified residuei8PhosphoserineCombined sources1
Modified residuei42PhosphoserineCombined sources1
Modified residuei88PhosphothreonineBy similarity1
Modified residuei93PhosphothreonineCombined sources1
Modified residuei95PhosphoserineCombined sources1
Modified residuei106PhosphoserineCombined sources1
Modified residuei174PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation affects the GDP/GTP exchange rate.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP24534.
MaxQBiP24534.
PaxDbiP24534.
PeptideAtlasiP24534.
PRIDEiP24534.
TopDownProteomicsiP24534.

2D gel databases

DOSAC-COBS-2DPAGEP24534.
OGPiP24534.
SWISS-2DPAGEP24534.

PTM databases

iPTMnetiP24534.
PhosphoSitePlusiP24534.
SwissPalmiP24534.

Miscellaneous databases

PMAP-CutDBP24534.

Expressioni

Inductioni

By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress.1 Publication

Gene expression databases

BgeeiENSG00000114942.
CleanExiHS_EEF1B2.
ExpressionAtlasiP24534. baseline and differential.
GenevisibleiP24534. HS.

Organism-specific databases

HPAiCAB012477.
HPA035029.

Interactioni

Subunit structurei

EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.

Binary interactionsi

WithEntry#Exp.IntActNotes
EEF1GP266415EBI-354334,EBI-351467
EEF1GP26641-23EBI-354334,EBI-10177695

Protein-protein interaction databases

BioGridi108253. 64 interactors.
IntActiP24534. 30 interactors.
MINTiMINT-4999956.
STRINGi9606.ENSP00000236957.

Structurei

Secondary structure

1225
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi140 – 150Combined sources11
Helixi155 – 164Combined sources10
Beta strandi171 – 183Combined sources13
Beta strandi185 – 193Combined sources9
Helixi200 – 207Combined sources8
Turni211 – 213Combined sources3
Beta strandi214 – 220Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B64NMR-A136-225[»]
5DQSX-ray2.10D1-88[»]
ProteinModelPortaliP24534.
SMRiP24534.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24534.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 84GST C-terminalAdd BLAST83

Sequence similaritiesi

Belongs to the EF-1-beta/EF-1-delta family.Curated
Contains 1 GST C-terminal domain.Curated

Phylogenomic databases

eggNOGiKOG1668. Eukaryota.
COG2092. LUCA.
GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207273.
HOVERGENiHBG000787.
InParanoidiP24534.
KOiK03232.
OMAiMAVAFYD.
OrthoDBiEOG091G0P0Z.
PhylomeDBiP24534.
TreeFamiTF313134.

Family and domain databases

CDDicd00292. EF1B. 1 hit.
Gene3Di1.20.1050.10. 1 hit.
3.30.70.60. 1 hit.
InterProiIPR018940. EF-1_beta_acid_region_euk.
IPR014038. EF1B_bsu/dsu_GNE.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
[Graphical view]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM01182. EF-1_beta_acid. 1 hit.
SM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24534-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC
60 70 80 90 100
HALRWYNHIK SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD
110 120 130 140 150
IDLFGSDDEE ESEEAKRLRE ERLAQYESKK AKKPALVAKS SILLDVKPWD
160 170 180 190 200
DETDMAKLEE CVRSIQADGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT
210 220
DMLEEQITAF EDYVQSMDVA AFNKI
Length:225
Mass (Da):24,764
Last modified:January 23, 2007 - v3
Checksum:iCDE763ADBF127822
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60489 mRNA. Translation: CAA43019.1.
X60656 mRNA. Translation: CAA43063.1.
BT007079 mRNA. Translation: AAP35742.1.
CR456825 mRNA. Translation: CAG33106.1.
AK291910 mRNA. Translation: BAF84599.1.
AC007383 Genomic DNA. Translation: AAY15062.1.
CH471063 Genomic DNA. Translation: EAW70381.1.
BC000211 mRNA. Translation: AAH00211.1.
BC004931 mRNA. Translation: AAH04931.1.
BC067787 mRNA. Translation: AAH67787.1.
CCDSiCCDS2367.1.
PIRiS25432.
RefSeqiNP_001032752.1. NM_001037663.1.
NP_001950.1. NM_001959.3.
NP_066944.1. NM_021121.3.
UniGeneiHs.421608.

Genome annotation databases

EnsembliENST00000236957; ENSP00000236957; ENSG00000114942.
ENST00000392221; ENSP00000376055; ENSG00000114942.
ENST00000392222; ENSP00000376056; ENSG00000114942.
ENST00000635728; ENSP00000489993; ENSG00000283391.
ENST00000636275; ENSP00000490326; ENSG00000283391.
ENST00000637253; ENSP00000490214; ENSG00000283391.
GeneIDi1933.
KEGGihsa:1933.
UCSCiuc002vbf.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60489 mRNA. Translation: CAA43019.1.
X60656 mRNA. Translation: CAA43063.1.
BT007079 mRNA. Translation: AAP35742.1.
CR456825 mRNA. Translation: CAG33106.1.
AK291910 mRNA. Translation: BAF84599.1.
AC007383 Genomic DNA. Translation: AAY15062.1.
CH471063 Genomic DNA. Translation: EAW70381.1.
BC000211 mRNA. Translation: AAH00211.1.
BC004931 mRNA. Translation: AAH04931.1.
BC067787 mRNA. Translation: AAH67787.1.
CCDSiCCDS2367.1.
PIRiS25432.
RefSeqiNP_001032752.1. NM_001037663.1.
NP_001950.1. NM_001959.3.
NP_066944.1. NM_021121.3.
UniGeneiHs.421608.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B64NMR-A136-225[»]
5DQSX-ray2.10D1-88[»]
ProteinModelPortaliP24534.
SMRiP24534.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108253. 64 interactors.
IntActiP24534. 30 interactors.
MINTiMINT-4999956.
STRINGi9606.ENSP00000236957.

PTM databases

iPTMnetiP24534.
PhosphoSitePlusiP24534.
SwissPalmiP24534.

Polymorphism and mutation databases

BioMutaiEEF1B2.
DMDMi119163.

2D gel databases

DOSAC-COBS-2DPAGEP24534.
OGPiP24534.
SWISS-2DPAGEP24534.

Proteomic databases

EPDiP24534.
MaxQBiP24534.
PaxDbiP24534.
PeptideAtlasiP24534.
PRIDEiP24534.
TopDownProteomicsiP24534.

Protocols and materials databases

DNASUi1933.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236957; ENSP00000236957; ENSG00000114942.
ENST00000392221; ENSP00000376055; ENSG00000114942.
ENST00000392222; ENSP00000376056; ENSG00000114942.
ENST00000635728; ENSP00000489993; ENSG00000283391.
ENST00000636275; ENSP00000490326; ENSG00000283391.
ENST00000637253; ENSP00000490214; ENSG00000283391.
GeneIDi1933.
KEGGihsa:1933.
UCSCiuc002vbf.2. human.

Organism-specific databases

CTDi1933.
DisGeNETi1933.
GeneCardsiEEF1B2.
HGNCiHGNC:3208. EEF1B2.
HPAiCAB012477.
HPA035029.
MIMi600655. gene.
neXtProtiNX_P24534.
OpenTargetsiENSG00000114942.
ENSG00000283391.
PharmGKBiPA27644.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1668. Eukaryota.
COG2092. LUCA.
GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207273.
HOVERGENiHBG000787.
InParanoidiP24534.
KOiK03232.
OMAiMAVAFYD.
OrthoDBiEOG091G0P0Z.
PhylomeDBiP24534.
TreeFamiTF313134.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000114942-MONOMER.
ReactomeiR-HSA-156842. Eukaryotic Translation Elongation.
SIGNORiP24534.

Miscellaneous databases

ChiTaRSiEEF1B2. human.
EvolutionaryTraceiP24534.
GeneWikiiEEF1B2.
GenomeRNAii1933.
PMAP-CutDBP24534.
PROiP24534.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000114942.
CleanExiHS_EEF1B2.
ExpressionAtlasiP24534. baseline and differential.
GenevisibleiP24534. HS.

Family and domain databases

CDDicd00292. EF1B. 1 hit.
Gene3Di1.20.1050.10. 1 hit.
3.30.70.60. 1 hit.
InterProiIPR018940. EF-1_beta_acid_region_euk.
IPR014038. EF1B_bsu/dsu_GNE.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
[Graphical view]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM01182. EF-1_beta_acid. 1 hit.
SM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEF1B_HUMAN
AccessioniPrimary (citable) accession number: P24534
Secondary accession number(s): A8K795, Q6IBH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 190 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.