Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8JZQ9 (EIF3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 3 subunit B

Short name=eIF3b
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 9
eIF-3-eta
eIF3 p116
Gene names
Name:Eif3b
Synonyms:Eif3s9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length803 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 preinitiation 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. Ref.1

Subunit structure

Interacts with UPF2 By similarity. 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 may also interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead 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. Ref.5 Ref.7

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03001.

Tissue specificity

Ubiquitously expressed. Ref.1

Domain

The RRM domain mediates interaction with EIF3J By similarity. HAMAP-Rule MF_03001

Post-translational modification

Phosphorylated. Phosphorylation is enhanced upon serum stimulation By similarity. HAMAP-Rule MF_03001

Disruption phenotype

Embryonic death. Ref.1

Sequence similarities

Belongs to the eIF-3 subunit B family.

Contains 1 RRM (RNA recognition motif) domain.

Contains 5 WD repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Eif4g1Q6NZJ62EBI-4286513,EBI-8175606

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 803803Eukaryotic translation initiation factor 3 subunit B HAMAP-Rule MF_03001
PRO_0000223479

Regions

Domain174 – 25784RRM
Repeat321 – 35939WD 1 HAMAP-Rule MF_03001
Repeat361 – 40646WD 2 HAMAP-Rule MF_03001
Repeat410 – 44839WD 3 HAMAP-Rule MF_03001
Repeat549 – 59042WD 4 HAMAP-Rule MF_03001
Repeat638 – 68346WD 5 HAMAP-Rule MF_03001
Region113 – 402290Sufficient for interaction with EIF3E By similarity
Region159 – 263105Sufficient for interaction with EIF3J By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue311Phosphothreonine Ref.4
Modified residue681Phosphoserine Ref.9
Modified residue741Phosphothreonine Ref.9 Ref.12
Modified residue751Phosphoserine Ref.9 Ref.11 Ref.12
Modified residue791Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12
Modified residue901Phosphoserine Ref.9
Modified residue1201Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10 Ref.12
Modified residue1231Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12
Modified residue1411Phosphoserine By similarity
Modified residue1431Phosphoserine By similarity
Modified residue1531Phosphoserine By similarity
Modified residue1981N6-acetyllysine By similarity
Modified residue2281Phosphoserine By similarity
Modified residue2771N6-acetyllysine By similarity
Modified residue3531N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8JZQ9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: D770AC70BFE9832F

FASTA80391,370
        10         20         30         40         50         60 
MQDAENVAVP EAAEERAEPA RQQPASESPP TDEAAGSGGS EVGQTEDAEE DAEAGPEPEV 

        70         80         90        100        110        120 
RAKPAAQSEE ETATSPAASP TPQSAERSPS QEPSAPGKAE AVGEQARGHP SAGAEEEGGS 

       130        140        150        160        170        180 
DGSAAEAEPR ALENGEADEP SFSDPEDFVD DVSEEELLGD VLKDRPQEAD GIDSVIVVDN 

       190        200        210        220        230        240 
VPQVGPDRLE KLKNVIHKIF SKFGKIINDY YPEEDGKTKG YIFLEYASPA HAVDAVKNAD 

       250        260        270        280        290        300 
GYKLDKQHTF RVNLFTDFDK YMTISDEWDI PEKQPFKDLG NLRYWLEEAE CRDQYSVIFE 

       310        320        330        340        350        360 
SGDRTSIFWN DVKDPVSIEE RARWTETYVR WSPKGTYLAT FHQRGIALWG GDKFKQIQRF 

       370        380        390        400        410        420 
SHQGVQLIDF SPCERYLVTF SPLMDTQDDP QAIIIWDILT GHKKRGFHCE SSAHWPIFKW 

       430        440        450        460        470        480 
SHDGKFFARM TLDTLSIYET PSMGLLDKKS LKISGIKDFS WSPGGNIIAF WVPEDKDIPA 

       490        500        510        520        530        540 
RVTLMQLPTR QEIRVRNLFN VVDCKLHWQK NGDYLCVKVD RTPKGTQGVV TNFEIFRMRE 

       550        560        570        580        590        600 
KQVPVDVVEM KETIIAFAWE PNGSKFAVLH GEAPRISVSF YHVKSNGKIE LIKMFDKQQA 

       610        620        630        640        650        660 
NTIFWSPQGQ FVVLAGLRSM NGALAFVDTS DCTVMNIAEH YMASDVEWDP TGRYVVTSVS 

       670        680        690        700        710        720 
WWSHKVDNAY WLWTFQGRLL QKNNKDRFCQ LLWRPRPPTL LSQDQIKQIK KDLKKYSKIF 

       730        740        750        760        770        780 
EQKDRLSQSK ASKELVERRR TMMEDFRQYR KMAQELYMKQ KNERLELRGG VDTDELDSNV 

       790        800 
DDWEEETIEF FVTEEVIPLG SQE 

« Hide

References

« Hide 'large scale' references
[1]"Embryonic lethality of mutant mice deficient in the p116 gene."
Koyanagi-Katsuta R., Akimitsu N., Hamamoto H., Arimitsu N., Hatano T., Sekimizu K.
J. Biochem. 131:833-837(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
Tissue: Embryonic stem cell.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Cecum and Placenta.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[4]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[5]"mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin."
Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr.
EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3A; EIF3F; EIF3J; EIF4A1; EIF4B; EIF4E; EIF4G1 AND RPS6.
[6]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[7]"Reconstitution reveals the functional core of mammalian eIF3."
Masutani M., Sonenberg N., Yokoyama S., Imataka H.
EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Teratocarcinoma.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; THR-74; SER-75; SER-79; SER-90; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[11]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-75; SER-79; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC7862.
RefSeqNP_598677.1. NM_133916.2.
UniGeneMm.21671.

3D structure databases

ProteinModelPortalQ8JZQ9.
SMRQ8JZQ9. Positions 159-263, 329-379, 621-659.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205699. 2 interactions.
IntActQ8JZQ9. 11 interactions.
MINTMINT-1899500.
STRING10090.ENSMUSP00000075175.

PTM databases

PhosphoSiteQ8JZQ9.

Proteomic databases

PaxDbQ8JZQ9.
PRIDEQ8JZQ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
GeneID27979.
KEGGmmu:27979.
UCSCuc009ahr.1. mouse.

Organism-specific databases

CTD8662.
MGIMGI:106478. Eif3b.

Phylogenomic databases

eggNOGCOG5354.
GeneTreeENSGT00550000074913.
HOGENOMHOG000265546.
HOVERGENHBG006127.
KOK03253.
OMAHTLRVNK.
OrthoDBEOG7KM5S6.
PhylomeDBQ8JZQ9.
TreeFamTF101521.

Gene expression databases

BgeeQ8JZQ9.
GenevestigatorQ8JZQ9.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
2.130.10.10. 1 hit.
3.30.70.330. 1 hit.
HAMAPMF_03001. eIF3b.
InterProIPR011042. 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]
PANTHERPTHR14068. PTHR14068. 1 hit.
PfamPF08662. eIF2A. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFPIRSF036424. eIF3b. 1 hit.
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3B. mouse.
NextBio306472.
PROQ8JZQ9.
SOURCESearch...

Entry information

Entry nameEIF3B_MOUSE
AccessionPrimary (citable) accession number: Q8JZQ9
Secondary accession number(s): Q922K2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

Translation initiation factors

List of translation initiation factor entries