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Protein

Eukaryotic translation initiation factor 5B

Gene

Eif5b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi634 – 641GTPBy similarity8

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2441772. Eif5b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003540711 – 1216Eukaryotic translation initiation factor 5BAdd BLAST1216

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66PhosphoserineBy similarity1
Modified residuei107PhosphothreonineCombined sources1
Modified residuei108PhosphoserineCombined sources1
Modified residuei114PhosphoserineCombined sources1
Modified residuei137PhosphoserineCombined sources1
Modified residuei139PhosphoserineCombined sources1
Modified residuei145PhosphoserineCombined sources1
Modified residuei165PhosphoserineCombined sources1
Modified residuei172PhosphoserineBy similarity1
Modified residuei183PhosphoserineCombined sources1
Modified residuei184PhosphoserineCombined sources1
Modified residuei187PhosphoserineCombined sources1
Modified residuei191PhosphoserineCombined sources1
Modified residuei209PhosphoserineCombined sources1
Modified residuei215PhosphoserineCombined sources1
Modified residuei223PhosphoserineCombined sources1
Modified residuei300PhosphothreonineBy similarity1
Modified residuei437PhosphoserineBy similarity1
Modified residuei497PhosphothreonineBy similarity1
Modified residuei544PhosphoserineBy similarity1
Modified residuei553PhosphoserineBy similarity1
Modified residuei556PhosphoserineBy similarity1
Modified residuei584PhosphoserineBy similarity1
Modified residuei585PhosphoserineBy similarity1
Modified residuei587PhosphoserineBy similarity1
Modified residuei591PhosphoserineBy similarity1
Modified residuei1164PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ05D44.
MaxQBiQ05D44.
PaxDbiQ05D44.
PeptideAtlasiQ05D44.
PRIDEiQ05D44.

PTM databases

iPTMnetiQ05D44.
PhosphoSitePlusiQ05D44.
SwissPalmiQ05D44.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026083.
GenevisibleiQ05D44. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi230580. 1 interactor.
STRINGi10090.ENSMUSP00000027252.

Structurei

3D structure databases

ProteinModelPortaliQ05D44.
SMRiQ05D44.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini625 – 842tr-type GPROSITE-ProRule annotationAdd BLAST218

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni634 – 641G1PROSITE-ProRule annotation8
Regioni659 – 663G2PROSITE-ProRule annotation5
Regioni698 – 701G3PROSITE-ProRule annotation4
Regioni752 – 755G4PROSITE-ProRule annotation4
Regioni820 – 822G5PROSITE-ProRule annotation3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi39 – 452Lys-richAdd BLAST414
Compositional biasi235 – 561Glu-richAdd BLAST327

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1144. Eukaryota.
COG0532. LUCA.
GeneTreeiENSGT00730000111064.
HOVERGENiHBG019036.
InParanoidiQ05D44.
KOiK03243.
OMAiRQQNEDV.
OrthoDBiEOG091G114V.
PhylomeDBiQ05D44.
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.

Q05D44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKQKNKSE DSTKDDTDLG ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK
60 70 80 90 100
QDFDENDILR ELEELSLEAQ GIRADRDAAA VKPTENNEEE SASKQDKKKK
110 120 130 140 150
GQKGKKTSFD ENDSEELEDK DSKSKKTARP NSEAPLSGSE DADDSNKLSK
160 170 180 190 200
KGKKAQKSTK KRDGSEEDED NSKRSKERSR VNSSGESGGE SDEFLQSRKG
210 220 230 240 250
QKKNQKNKSV PTVDSGNEDD DSSFKIKTVA QKKAEKKERE KKKRDEEKAK
260 270 280 290 300
LRKMKEKEEL EKGKKEQSKQ REPQKRPEEE VLTLRGTPDT GAASEEKGDT
310 320 330 340 350
AAALEDDNEG DKKKKDKKKK KTEKDEKEKE KKKGPSKSTV KAIQEALAKL
360 370 380 390 400
KEEEERQKRE EEERIKRLEE LEAKRKEEER LEQEKRERKK QKEKERKERL
410 420 430 440 450
KKEGKLLTKS QREARARAEV TLRHLQAQGV EVPSKDSLPK KRPVYEDKKK
460 470 480 490 500
KKTPQQLESK EVSETLEISA PVEAVDQGGP EKEETPPSVE PEEEEDTEDA
510 520 530 540 550
GLDDWEAMAS DEEREKEGNM IHIEVEENPE EEEEEEEEEE EEESEDEEEE
560 570 580 590 600
GDSEGSDGDE EDCKLSDEKD SGKAGDTKPS KDASSDSEYD SDDDRTKEER
610 620 630 640 650
AYDKAKRRIE KRRLEHGKNV NTEKLRAPII CVLGHVDTGK TKILDKLRHT
660 670 680 690 700
HVQDGEAGGI TQQIGATNVP LEAINEQTKM IKNFDRENVR IPGMLIIDTP
710 720 730 740 750
GHESFSNLRN RGSSLCDIAI LVVDIMHGLE PQTIESINIL KSKKCPFIVA
760 770 780 790 800
LNKIDRLYDW KKSPDSDVAV TLKKQKKNTK DEFEERAKAI IVEFAQQGLN
810 820 830 840 850
AALFYENKDP RTFVSLVPTS AHTGDGMGSL IYLLVELTQT MLSKRLAHCE
860 870 880 890 900
ELRAQVMEVK ALPGMGTTID VILINGRLKE GDTIIVPGVE GPIVTQIRGL
910 920 930 940 950
LLPPPMKELR VKNQYEKHKE VEAAQGVKIL GKDLEKTLAG LPLLVAYKDD
960 970 980 990 1000
EIPVLKDELI HELKQTLNAI KLEEKGVYVQ ASTLGSLEAL LEFLKTSEVP
1010 1020 1030 1040 1050
YAGINIGPVH KKDVMKASVM LEHDPQYAVI LAFDVRIERD AQEMADSLGV
1060 1070 1080 1090 1100
RIFSAEIIYH LFDAFTKYRQ DYKKQKQEEF KHIAVFPCKM KILPQYIFNS
1110 1120 1130 1140 1150
RDPIVIGVTV EAGQVKQGTP MCVPSKNFVD IGIVTSIEIN HKQVDVAKKG
1160 1170 1180 1190 1200
QEVCVKIEPI PGESPKMFGR HFEATDILVS KISRQSIDAL KDWFRDEMQK
1210
SDWQLIVELK KVFEII
Length:1,216
Mass (Da):137,616
Last modified:November 25, 2008 - v2
Checksum:i38D1C21648E4EAEC
GO

Sequence cautioni

The sequence AAH18347 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH37150 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH40746 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH60288 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121D → N in BAE26259 (PubMed:16141072).Curated1
Sequence conflicti188G → C in BAE26259 (PubMed:16141072).Curated1
Sequence conflicti254M → L in BAE26259 (PubMed:16141072).Curated1
Sequence conflicti302A → V in BAE26259 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114583 Genomic DNA. No translation available.
AK145146 mRNA. Translation: BAE26259.1.
AK145732 mRNA. Translation: BAE26614.1.
AK163527 mRNA. Translation: BAE37384.1.
BC018347 mRNA. Translation: AAH18347.1. Sequence problems.
BC037150 mRNA. Translation: AAH37150.1. Sequence problems.
BC040746 mRNA. Translation: AAH40746.1. Sequence problems.
BC060288 mRNA. Translation: AAH60288.1. Sequence problems.
CCDSiCCDS35544.1.
RefSeqiNP_938045.2. NM_198303.2.
UniGeneiMm.260943.

Genome annotation databases

EnsembliENSMUST00000027252; ENSMUSP00000027252; ENSMUSG00000026083.
GeneIDi226982.
KEGGimmu:226982.
UCSCiuc007aso.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114583 Genomic DNA. No translation available.
AK145146 mRNA. Translation: BAE26259.1.
AK145732 mRNA. Translation: BAE26614.1.
AK163527 mRNA. Translation: BAE37384.1.
BC018347 mRNA. Translation: AAH18347.1. Sequence problems.
BC037150 mRNA. Translation: AAH37150.1. Sequence problems.
BC040746 mRNA. Translation: AAH40746.1. Sequence problems.
BC060288 mRNA. Translation: AAH60288.1. Sequence problems.
CCDSiCCDS35544.1.
RefSeqiNP_938045.2. NM_198303.2.
UniGeneiMm.260943.

3D structure databases

ProteinModelPortaliQ05D44.
SMRiQ05D44.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230580. 1 interactor.
STRINGi10090.ENSMUSP00000027252.

PTM databases

iPTMnetiQ05D44.
PhosphoSitePlusiQ05D44.
SwissPalmiQ05D44.

Proteomic databases

EPDiQ05D44.
MaxQBiQ05D44.
PaxDbiQ05D44.
PeptideAtlasiQ05D44.
PRIDEiQ05D44.

Protocols and materials databases

DNASUi226982.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027252; ENSMUSP00000027252; ENSMUSG00000026083.
GeneIDi226982.
KEGGimmu:226982.
UCSCiuc007aso.1. mouse.

Organism-specific databases

CTDi9669.
MGIiMGI:2441772. Eif5b.

Phylogenomic databases

eggNOGiKOG1144. Eukaryota.
COG0532. LUCA.
GeneTreeiENSGT00730000111064.
HOVERGENiHBG019036.
InParanoidiQ05D44.
KOiK03243.
OMAiRQQNEDV.
OrthoDBiEOG091G114V.
PhylomeDBiQ05D44.
TreeFamiTF101535.

Enzyme and pathway databases

ReactomeiR-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEif5b. mouse.
PROiQ05D44.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026083.
GenevisibleiQ05D44. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q05D44
Secondary accession number(s): Q3SYI4
, Q3TQJ8, Q3UL37, Q3UM39, Q6PAI0, Q8CFF4, Q8CGD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: November 2, 2016
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.