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Protein

Eukaryotic translation initiation factor 3 subunit J-B

Gene

Eif3j2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

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 J-BUniRule annotation
Short name:
eIF3j-BUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 1-BUniRule annotation
eIF-3-alpha-BUniRule annotation
eIF3 p35UniRule annotation
Gene namesi
Name:Eif3j2
Synonyms:Eif3s1-2, Gm9781
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:3704486. Eif3j2.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 263262Eukaryotic translation initiation factor 3 subunit J-BPRO_0000123507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei16 – 161PhosphoserineUniRule annotationBy similarity
Modified residuei18 – 181PhosphoserineUniRule annotationBy similarity
Modified residuei25 – 251PhosphoserineUniRule annotationBy similarity
Modified residuei114 – 1141PhosphothreonineUniRule annotationBy similarity
Modified residuei132 – 1321PhosphoserineUniRule annotationBy similarity
Modified residuei259 – 2591PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ66JS6.
PaxDbiQ66JS6.
PRIDEiQ66JS6.

PTM databases

iPTMnetiQ66JS6.
PhosphoSiteiQ66JS6.

Expressioni

Gene expression databases

BgeeiQ66JS6.
GenevisibleiQ66JS6. 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.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054421.

Structurei

3D structure databases

ProteinModelPortaliQ66JS6.
SMRiQ66JS6. Positions 147-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 7469Sufficient for interaction with EIF3BUniRule annotationAdd
BLAST
Regioni248 – 26316Promotes stable association with the 40S ribosomeUniRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili75 – 14066UniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit J family.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4813. Eukaryota.
ENOG4111U5G. LUCA.
GeneTreeiENSGT00390000018400.
HOGENOMiHOG000238746.
HOVERGENiHBG066230.
InParanoidiQ66JS6.
KOiK03245.
OMAiSSREDFT.
OrthoDBiEOG7J70H8.
PhylomeDBiQ66JS6.
TreeFamiTF101514.

Family and domain databases

Gene3Di1.10.246.60. 1 hit.
HAMAPiMF_03009. eIF3j.
InterProiIPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view]
PANTHERiPTHR21681. PTHR21681. 1 hit.
PfamiPF08597. eIF3_subunit. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q66JS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAAAAAA AAAGDSDSWD ADTFSMEDPV RKVAGGGTAG GDRWEGEDED
60 70 80 90 100
EDVKDNWDDD DDENKEEAEV KPEVKISEKK KIAEKIKEKE RQQKKRQEEI
110 120 130 140 150
KKRLEEPEES KVLTPEEQLA DKLRLKKLQE ESDLELAKET FGVNNTVYGI
160 170 180 190 200
DAMNPSSRDD FTEFGKLLKD KITQYEKSLY YASFLEALVR DVCISLEIDD
210 220 230 240 250
LKKITNSLTV LCSEKQKQEK QSKAKKKKKG VVPGGGLKAT MKDDLADYGG
260
YEGGYVQDYE DFM
Length:263
Mass (Da):29,486
Last modified:October 11, 2004 - v1
Checksum:i7040416E40650960
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911D → N in BAC38399 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC080788 mRNA. Translation: AAH80788.1.
AK082048 mRNA. Translation: BAC38399.1.
CCDSiCCDS57122.1.
RefSeqiNP_001242984.1. NM_001256055.1.
UniGeneiMm.329403.
Mm.458184.

Genome annotation databases

EnsembliENSMUST00000057110; ENSMUSP00000054421; ENSMUSG00000043424.
GeneIDi100042807.
KEGGimmu:100042807.
UCSCiuc008mab.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC080788 mRNA. Translation: AAH80788.1.
AK082048 mRNA. Translation: BAC38399.1.
CCDSiCCDS57122.1.
RefSeqiNP_001242984.1. NM_001256055.1.
UniGeneiMm.329403.
Mm.458184.

3D structure databases

ProteinModelPortaliQ66JS6.
SMRiQ66JS6. Positions 147-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054421.

PTM databases

iPTMnetiQ66JS6.
PhosphoSiteiQ66JS6.

Proteomic databases

EPDiQ66JS6.
PaxDbiQ66JS6.
PRIDEiQ66JS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057110; ENSMUSP00000054421; ENSMUSG00000043424.
GeneIDi100042807.
KEGGimmu:100042807.
UCSCiuc008mab.3. mouse.

Organism-specific databases

CTDi100042807.
MGIiMGI:3704486. Eif3j2.

Phylogenomic databases

eggNOGiKOG4813. Eukaryota.
ENOG4111U5G. LUCA.
GeneTreeiENSGT00390000018400.
HOGENOMiHOG000238746.
HOVERGENiHBG066230.
InParanoidiQ66JS6.
KOiK03245.
OMAiSSREDFT.
OrthoDBiEOG7J70H8.
PhylomeDBiQ66JS6.
TreeFamiTF101514.

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

NextBioi454728.
PROiQ66JS6.
SOURCEiSearch...

Gene expression databases

BgeeiQ66JS6.
GenevisibleiQ66JS6. MM.

Family and domain databases

Gene3Di1.10.246.60. 1 hit.
HAMAPiMF_03009. eIF3j.
InterProiIPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view]
PANTHERiPTHR21681. PTHR21681. 1 hit.
PfamiPF08597. eIF3_subunit. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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: FVB/N.
    Tissue: Salivary gland.
  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.
    , 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] OF 42-263.
    Strain: C57BL/6J.
    Tissue: Head.
  3. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiEI3JB_MOUSE
AccessioniPrimary (citable) accession number: Q66JS6
Secondary accession number(s): Q8BUW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: October 11, 2004
Last modified: May 11, 2016
This is version 105 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. 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.