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Protein

Eukaryotic translation initiation factor 5B

Gene

EIF5B

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

Functioni

Plays a role in translation initiation. Translational GTPase that catalyzes the joining of the 40S and 60S subunits to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. GTP binding and hydrolysis induces conformational changes in the enzyme that renders it active for productive interactions with the ribosome. The release of the enzyme after formation of the initiation complex is a prerequisite to form elongation-competent ribosomes.By similarity

Catalytic activityi

GTP + H2O = GDP + phosphate.By similarity

Cofactori

a monovalent cationBy similarityNote: Binds 1 monovalent cation per monomer in the active site. Structural cofactor that stabilizes the GTP-bound "on" state. May also act as a transition state stabilizer of the hydrolysis reaction.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi638 – 645GTPBy similarity8

GO - Molecular functioni

  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB

GO - Biological processi

  • regulation of translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000158417-MONOMER.
ReactomeiR-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 5B (EC:3.6.5.3)
Short name:
eIF-5B
Alternative name(s):
Translation initiation factor IF-2
Gene namesi
Name:EIF5B
Synonyms:IF2, KIAA0741
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:30793. EIF5B.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi640V → G: Loss of activity in vivo. Retains full activity in vitro. 1 Publication1
Mutagenesisi706H → E: Loss of activity; both in vivo and in vitro. 1 Publication1
Mutagenesisi706H → Q: Loss of activity in vivo. Partial activity in vitro. 1 Publication1
Mutagenesisi759D → N: Loss of activity; both in vivo and in vitro. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000158417.
PharmGKBiPA134864457.

Polymorphism and mutation databases

BioMutaiEIF5B.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001372941 – 1220Eukaryotic translation initiation factor 5BAdd BLAST1220

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66PhosphoserineCombined sources1
Modified residuei107PhosphoserineCombined sources1
Modified residuei113PhosphoserineCombined sources1
Modified residuei134PhosphotyrosineCombined sources1
Modified residuei135PhosphoserineCombined sources1
Modified residuei137PhosphoserineCombined sources1
Modified residuei164PhosphoserineCombined sources1
Modified residuei171PhosphoserineCombined sources1
Modified residuei182PhosphoserineCombined sources1
Modified residuei183PhosphoserineCombined sources1
Modified residuei186PhosphoserineCombined sources1
Modified residuei190PhosphoserineCombined sources1 Publication1
Modified residuei214PhosphoserineCombined sources1
Modified residuei222PhosphoserineCombined sources1
Modified residuei301PhosphothreonineCombined sources1
Modified residuei438PhosphoserineCombined sources1
Modified residuei498PhosphothreonineCombined sources1
Modified residuei547PhosphoserineCombined sources1
Modified residuei557PhosphoserineBy similarity1
Modified residuei560PhosphoserineCombined sources1
Modified residuei588PhosphoserineCombined sources1
Modified residuei589PhosphoserineCombined sources1
Modified residuei591PhosphoserineCombined sources1
Modified residuei595PhosphoserineCombined sources1
Modified residuei1168PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO60841.
MaxQBiO60841.
PaxDbiO60841.
PeptideAtlasiO60841.
PRIDEiO60841.

PTM databases

iPTMnetiO60841.
PhosphoSitePlusiO60841.
SwissPalmiO60841.

Miscellaneous databases

PMAP-CutDBO60841.

Expressioni

Gene expression databases

BgeeiENSG00000158417.
CleanExiHS_EIF5B.
ExpressionAtlasiO60841. baseline and differential.
GenevisibleiO60841. HS.

Organism-specific databases

HPAiHPA034648.
HPA040095.

Interactioni

Subunit structurei

Interacts with ANXA5 in a calcium and phospholipid-dependent manner.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF1AYO146022EBI-928530,EBI-286439
ETS1P149212EBI-928530,EBI-913209

Protein-protein interaction databases

BioGridi115024. 52 interactors.
IntActiO60841. 22 interactors.
MINTiMINT-3000520.
STRINGi9606.ENSP00000289371.

Structurei

3D structure databases

ProteinModelPortaliO60841.
SMRiO60841.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini629 – 846tr-type GPROSITE-ProRule annotationAdd BLAST218

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni638 – 645G1PROSITE-ProRule annotation8
Regioni663 – 667G2PROSITE-ProRule annotation5
Regioni702 – 705G3PROSITE-ProRule annotation4
Regioni756 – 759G4PROSITE-ProRule annotation4
Regioni824 – 826G5PROSITE-ProRule annotation3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi39 – 50Poly-LysAdd BLAST12
Compositional biasi94 – 99Poly-Lys6
Compositional biasi138 – 142Poly-Asp5
Compositional biasi313 – 322Poly-Lys10
Compositional biasi353 – 356Poly-Glu4
Compositional biasi361 – 364Poly-Glu4
Compositional biasi491 – 496Poly-Glu6
Compositional biasi529 – 567Asp/Glu-rich (acidic)Add BLAST39

Sequence similaritiesi

Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1144. Eukaryota.
COG0532. LUCA.
GeneTreeiENSGT00730000111064.
HOGENOMiHOG000105770.
HOVERGENiHBG019036.
InParanoidiO60841.
KOiK03243.
OMAiREPRYAV.
PhylomeDBiO60841.
TreeFamiTF101535.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60841-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK
60 70 80 90 100
QDFDEDDILK ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG
110 120 130 140 150
QKGKKQSFDD NDSEELEDKD SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA
160 170 180 190 200
KGKAQKSNKK WDGSEEDEDN SKKIKERSRI NSSGESGDES DEFLQSRKGQ
210 220 230 240 250
KKNQKNKPGP NIESGNEDDD ASFKIKTVAQ KKAEKKERER KKRDEEKAKL
260 270 280 290 300
RKLKEKEELE TGKKDQSKQK ESQRKFEEET VKSKVTVDTG VIPASEEKAE
310 320 330 340 350
TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK
360 370 380 390 400
LKEEEERQKR EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER
410 420 430 440 450
LKKEGKLLTK SQREARARAE ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK
460 470 480 490 500
RKKIPQQLES KEVSESMELC AAVEVMEQGV PEKEETPPPV EPEEEEDTED
510 520 530 540 550
AGLDDWEAMA SDEETEKVEG NKVHIEVKEN PEEEEEEEEE EEEDEESEEE
560 570 580 590 600
EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT
610 620 630 640 650
KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK
660 670 680 690 700
LRHTHVQDGE AGGITQQIGA TNVPLEAINE QTKMIKNFDR ENVRIPGMLI
710 720 730 740 750
IDTPGHESFS NLRNRGSSLC DIAILVVDIM HGLEPQTIES INLLKSKKCP
760 770 780 790 800
FIVALNKIDR LYDWKKSPDS DVAATLKKQK KNTKDEFEER AKAIIVEFAQ
810 820 830 840 850
QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE LTQTMLSKRL
860 870 880 890 900
AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ
910 920 930 940 950
IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA
960 970 980 990 1000
YKEDEIPVLK DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT
1010 1020 1030 1040 1050
SEVPYAGINI GPVHKKDVMK ASVMLEHDPQ YAVILAFDVR IERDAQEMAD
1060 1070 1080 1090 1100
SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK QEEFKHIAVF PCKIKILPQY
1110 1120 1130 1140 1150
IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS IEINHKQVDV
1160 1170 1180 1190 1200
AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD
1210 1220
EMQKSDWQLI VELKKVFEII
Length:1,220
Mass (Da):138,827
Last modified:November 24, 2009 - v4
Checksum:i454C29FB90AA768E
GO

Sequence cautioni

The sequence BAA34461 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64E → G in BAA34461 (PubMed:9872452).Curated1
Sequence conflicti92T → I in CAB44357 (PubMed:10432305).Curated1
Sequence conflicti180I → M in AAD16006 (PubMed:10200264).Curated1
Sequence conflicti256K → R in AAD16006 (PubMed:10200264).Curated1
Sequence conflicti549E → V in AAD16006 (PubMed:10200264).Curated1
Sequence conflicti669G → W in AAD16006 (PubMed:10200264).Curated1
Sequence conflicti894E → K in CAB44357 (PubMed:10432305).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055954337S → G.Corresponds to variant rs10642dbSNPEnsembl.1
Natural variantiVAR_055955360R → G.Corresponds to variant rs3205296dbSNPEnsembl.1
Natural variantiVAR_060587522K → T.Combined sources2 PublicationsCorresponds to variant rs7558074dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006776 mRNA. Translation: CAB44357.1.
AF078035 mRNA. Translation: AAD16006.1.
AC018690 Genomic DNA. Translation: AAY24313.1.
AC079447 Genomic DNA. Translation: AAX93258.1.
AB018284 mRNA. Translation: BAA34461.2. Different initiation.
AL133563 mRNA. Translation: CAB63717.1.
AJ006412 mRNA. Translation: CAA07018.1.
CCDSiCCDS42721.1.
PIRiT43483.
RefSeqiNP_056988.3. NM_015904.3.
UniGeneiHs.158688.

Genome annotation databases

EnsembliENST00000289371; ENSP00000289371; ENSG00000158417.
GeneIDi9669.
KEGGihsa:9669.
UCSCiuc002tab.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ006776 mRNA. Translation: CAB44357.1.
AF078035 mRNA. Translation: AAD16006.1.
AC018690 Genomic DNA. Translation: AAY24313.1.
AC079447 Genomic DNA. Translation: AAX93258.1.
AB018284 mRNA. Translation: BAA34461.2. Different initiation.
AL133563 mRNA. Translation: CAB63717.1.
AJ006412 mRNA. Translation: CAA07018.1.
CCDSiCCDS42721.1.
PIRiT43483.
RefSeqiNP_056988.3. NM_015904.3.
UniGeneiHs.158688.

3D structure databases

ProteinModelPortaliO60841.
SMRiO60841.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115024. 52 interactors.
IntActiO60841. 22 interactors.
MINTiMINT-3000520.
STRINGi9606.ENSP00000289371.

PTM databases

iPTMnetiO60841.
PhosphoSitePlusiO60841.
SwissPalmiO60841.

Polymorphism and mutation databases

BioMutaiEIF5B.

Proteomic databases

EPDiO60841.
MaxQBiO60841.
PaxDbiO60841.
PeptideAtlasiO60841.
PRIDEiO60841.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000289371; ENSP00000289371; ENSG00000158417.
GeneIDi9669.
KEGGihsa:9669.
UCSCiuc002tab.4. human.

Organism-specific databases

CTDi9669.
GeneCardsiEIF5B.
H-InvDBHIX0002308.
HGNCiHGNC:30793. EIF5B.
HPAiHPA034648.
HPA040095.
MIMi606086. gene.
neXtProtiNX_O60841.
OpenTargetsiENSG00000158417.
PharmGKBiPA134864457.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1144. Eukaryota.
COG0532. LUCA.
GeneTreeiENSGT00730000111064.
HOGENOMiHOG000105770.
HOVERGENiHBG019036.
InParanoidiO60841.
KOiK03243.
OMAiREPRYAV.
PhylomeDBiO60841.
TreeFamiTF101535.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000158417-MONOMER.
ReactomeiR-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEIF5B. human.
GeneWikiiEIF5B.
GenomeRNAii9669.
PMAP-CutDBO60841.
PROiO60841.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000158417.
CleanExiHS_EIF5B.
ExpressionAtlasiO60841. baseline and differential.
GenevisibleiO60841. HS.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIF2P_HUMAN
AccessioniPrimary (citable) accession number: O60841
Secondary accession number(s): O95805
, Q53RV7, Q53SI8, Q9UF81, Q9UMN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 24, 2009
Last modified: November 2, 2016
This is version 165 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.