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Protein

Eukaryotic translation initiation factor 3 subunit B

Gene

Eif3b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.UniRule annotation2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit BUniRule annotation
Short name:
eIF3bUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 9UniRule annotation
eIF-3-etaUniRule annotation
eIF3 p116
Gene namesi
Name:Eif3b
Synonyms:Eif3s9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:106478. Eif3b.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Embryonic death.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002234791 – 803Eukaryotic translation initiation factor 3 subunit BAdd BLAST803

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineUniRule annotationBy similarity1
Modified residuei31PhosphothreonineCombined sources1
Modified residuei37PhosphoserineCombined sources1
Modified residuei40PhosphoserineCombined sources1
Modified residuei68PhosphoserineCombined sources1
Modified residuei72PhosphothreonineCombined sources1
Modified residuei74PhosphothreonineCombined sources1
Modified residuei75PhosphoserineCombined sources1
Modified residuei79PhosphoserineCombined sources1
Modified residuei84PhosphoserineCombined sources1
Modified residuei88PhosphoserineCombined sources1
Modified residuei90PhosphoserineCombined sources1
Modified residuei111PhosphoserineCombined sources1
Modified residuei120PhosphoserineCombined sources1
Modified residuei123PhosphoserineCombined sources1
Modified residuei141PhosphoserineUniRule annotationBy similarity1
Modified residuei143PhosphoserineUniRule annotationBy similarity1
Modified residuei153PhosphoserineUniRule annotationBy similarity1
Modified residuei198N6-acetyllysineBy similarity1
Modified residuei228PhosphoserineUniRule annotationBy similarity1
Modified residuei277N6-acetyllysineBy similarity1
Modified residuei353N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8JZQ9.
MaxQBiQ8JZQ9.
PaxDbiQ8JZQ9.
PRIDEiQ8JZQ9.

PTM databases

iPTMnetiQ8JZQ9.
PhosphoSitePlusiQ8JZQ9.
SwissPalmiQ8JZQ9.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSMUSG00000056076.
ExpressionAtlasiQ8JZQ9. baseline and differential.
GenevisibleiQ8JZQ9. MM.

Interactioni

Subunit structurei

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with UPF2 and HNRPD. Interacts with METTL3.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif4g1Q6NZJ62EBI-4286513,EBI-8175606

Protein-protein interaction databases

BioGridi205699. 4 interactors.
IntActiQ8JZQ9. 12 interactors.
MINTiMINT-1899500.
STRINGi10090.ENSMUSP00000098076.

Structurei

3D structure databases

ProteinModelPortaliQ8JZQ9.
SMRiQ8JZQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini174 – 257RRMUniRule annotationAdd BLAST84
Repeati321 – 359WD 1Add BLAST39
Repeati361 – 406WD 2Add BLAST46
Repeati410 – 448WD 3Add BLAST39
Repeati549 – 590WD 4Add BLAST42
Repeati638 – 683WD 5Add BLAST46

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni113 – 402Sufficient for interaction with EIF3EUniRule annotationAdd BLAST290
Regioni159 – 263Sufficient for interaction with EIF3JUniRule annotationAdd BLAST105

Domaini

The RRM domain mediates interaction with EIF3J.UniRule annotation

Sequence similaritiesi

Belongs to the eIF-3 subunit B family.UniRule annotation
Contains 1 RRM (RNA recognition motif) domain.UniRule annotation
Contains 5 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG2314. Eukaryota.
COG5354. LUCA.
GeneTreeiENSGT00550000074913.
HOGENOMiHOG000265546.
HOVERGENiHBG006127.
InParanoidiQ8JZQ9.
KOiK03253.
OMAiAFMEYKQ.
OrthoDBiEOG091G02V5.
PhylomeDBiQ8JZQ9.
TreeFamiTF101521.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.130.10.10. 1 hit.
3.30.70.330. 1 hit.
HAMAPiMF_03001. eIF3b. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF08662. eIF2A. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF036424. eIF3b. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8JZQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDAENVAVP EAAEERAEPA RQQPASESPP TDEAAGSGGS EVGQTEDAEE
60 70 80 90 100
DAEAGPEPEV RAKPAAQSEE ETATSPAASP TPQSAERSPS QEPSAPGKAE
110 120 130 140 150
AVGEQARGHP SAGAEEEGGS DGSAAEAEPR ALENGEADEP SFSDPEDFVD
160 170 180 190 200
DVSEEELLGD VLKDRPQEAD GIDSVIVVDN VPQVGPDRLE KLKNVIHKIF
210 220 230 240 250
SKFGKIINDY YPEEDGKTKG YIFLEYASPA HAVDAVKNAD GYKLDKQHTF
260 270 280 290 300
RVNLFTDFDK YMTISDEWDI PEKQPFKDLG NLRYWLEEAE CRDQYSVIFE
310 320 330 340 350
SGDRTSIFWN DVKDPVSIEE RARWTETYVR WSPKGTYLAT FHQRGIALWG
360 370 380 390 400
GDKFKQIQRF SHQGVQLIDF SPCERYLVTF SPLMDTQDDP QAIIIWDILT
410 420 430 440 450
GHKKRGFHCE SSAHWPIFKW SHDGKFFARM TLDTLSIYET PSMGLLDKKS
460 470 480 490 500
LKISGIKDFS WSPGGNIIAF WVPEDKDIPA RVTLMQLPTR QEIRVRNLFN
510 520 530 540 550
VVDCKLHWQK NGDYLCVKVD RTPKGTQGVV TNFEIFRMRE KQVPVDVVEM
560 570 580 590 600
KETIIAFAWE PNGSKFAVLH GEAPRISVSF YHVKSNGKIE LIKMFDKQQA
610 620 630 640 650
NTIFWSPQGQ FVVLAGLRSM NGALAFVDTS DCTVMNIAEH YMASDVEWDP
660 670 680 690 700
TGRYVVTSVS WWSHKVDNAY WLWTFQGRLL QKNNKDRFCQ LLWRPRPPTL
710 720 730 740 750
LSQDQIKQIK KDLKKYSKIF EQKDRLSQSK ASKELVERRR TMMEDFRQYR
760 770 780 790 800
KMAQELYMKQ KNERLELRGG VDTDELDSNV DDWEEETIEF FVTEEVIPLG

SQE
Length:803
Mass (Da):91,370
Last modified:October 1, 2002 - v1
Checksum:iD770AC70BFE9832F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033722 mRNA. Translation: BAC28445.1.
AK167618 mRNA. Translation: BAE39671.1.
AK170938 mRNA. Translation: BAE42128.1.
BC007175 mRNA. Translation: AAH07175.1.
BC031704 mRNA. Translation: AAH31704.1.
CCDSiCCDS19819.1.
PIRiJC7862.
RefSeqiNP_598677.1. NM_133916.2.
UniGeneiMm.21671.

Genome annotation databases

EnsembliENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
GeneIDi27979.
KEGGimmu:27979.
UCSCiuc009ahr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033722 mRNA. Translation: BAC28445.1.
AK167618 mRNA. Translation: BAE39671.1.
AK170938 mRNA. Translation: BAE42128.1.
BC007175 mRNA. Translation: AAH07175.1.
BC031704 mRNA. Translation: AAH31704.1.
CCDSiCCDS19819.1.
PIRiJC7862.
RefSeqiNP_598677.1. NM_133916.2.
UniGeneiMm.21671.

3D structure databases

ProteinModelPortaliQ8JZQ9.
SMRiQ8JZQ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205699. 4 interactors.
IntActiQ8JZQ9. 12 interactors.
MINTiMINT-1899500.
STRINGi10090.ENSMUSP00000098076.

PTM databases

iPTMnetiQ8JZQ9.
PhosphoSitePlusiQ8JZQ9.
SwissPalmiQ8JZQ9.

Proteomic databases

EPDiQ8JZQ9.
MaxQBiQ8JZQ9.
PaxDbiQ8JZQ9.
PRIDEiQ8JZQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
GeneIDi27979.
KEGGimmu:27979.
UCSCiuc009ahr.1. mouse.

Organism-specific databases

CTDi8662.
MGIiMGI:106478. Eif3b.

Phylogenomic databases

eggNOGiKOG2314. Eukaryota.
COG5354. LUCA.
GeneTreeiENSGT00550000074913.
HOGENOMiHOG000265546.
HOVERGENiHBG006127.
InParanoidiQ8JZQ9.
KOiK03253.
OMAiAFMEYKQ.
OrthoDBiEOG091G02V5.
PhylomeDBiQ8JZQ9.
TreeFamiTF101521.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEif3b. mouse.
PROiQ8JZQ9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000056076.
ExpressionAtlasiQ8JZQ9. baseline and differential.
GenevisibleiQ8JZQ9. MM.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
2.130.10.10. 1 hit.
3.30.70.330. 1 hit.
HAMAPiMF_03001. eIF3b. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF08662. eIF2A. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF036424. eIF3b. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3B_MOUSE
AccessioniPrimary (citable) accession number: Q8JZQ9
Secondary accession number(s): Q922K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 136 of the entry and version 1 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. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.