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Protein

Eukaryotic translation initiation factor 3 subunit J

Gene

EIF3J

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 (PubMed:25849773, PubMed:27462815). 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 (PubMed:25849773).2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104131-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit JUniRule annotation
Short name:
eIF3jUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 1UniRule annotation
eIF-3-alphaUniRule annotation
eIF3 p35UniRule annotation
Gene namesi
Name:EIF3JUniRule annotation
Synonyms:EIF3S1UniRule annotation
ORF Names:PRO0391
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:3270. EIF3J.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi8669.
OpenTargetsiENSG00000104131.
PharmGKBiPA162384902.

Polymorphism and mutation databases

BioMutaiEIF3J.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotationCombined sources2 Publications
ChainiPRO_00001235062 – 258Eukaryotic translation initiation factor 3 subunit JAdd BLAST257

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineUniRule annotationCombined sources2 Publications1
Modified residuei11PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei13PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei20PhosphoserineUniRule annotation1 Publication1
Modified residuei109PhosphothreonineUniRule annotationCombined sources1 Publication1
Modified residuei127PhosphoserineCombined sources1
Modified residuei254PhosphotyrosineCombined sources1

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO75822.
MaxQBiO75822.
PaxDbiO75822.
PeptideAtlasiO75822.
PRIDEiO75822.

PTM databases

iPTMnetiO75822.
PhosphoSitePlusiO75822.
SwissPalmiO75822.

Miscellaneous databases

PMAP-CutDBO75822.

Expressioni

Gene expression databases

BgeeiENSG00000104131.
CleanExiHS_EIF3J.
ExpressionAtlasiO75822. baseline and differential.
GenevisibleiO75822. HS.

Organism-specific databases

HPAiHPA050977.

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 annotation8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSNK2A1P684002EBI-366647,EBI-347804
EIF3BP558845EBI-366647,EBI-366696
EIF4G1Q046372EBI-366647,EBI-73711

Protein-protein interaction databases

BioGridi114218. 34 interactors.
DIPiDIP-31117N.
IntActiO75822. 19 interactors.
MINTiMINT-5003918.
STRINGi9606.ENSP00000261868.

Structurei

Secondary structure

1258
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni145 – 147Combined sources3
Helixi153 – 167Combined sources15
Helixi168 – 170Combined sources3
Helixi176 – 188Combined sources13
Helixi193 – 212Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KRBNMR-B45-55[»]
3BPJX-ray1.85A/B/C/D141-220[»]
ProteinModelPortaliO75822.
SMRiO75822.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75822.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 69Sufficient for interaction with EIF3BAdd BLAST68
Regioni243 – 258Promotes stable association with the 40S ribosomeAdd BLAST16

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili70 – 135UniRule annotationAdd BLAST66

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 8Poly-Ala7
Compositional biasi29 – 32Poly-Gly4
Compositional biasi53 – 57Poly-Asp5
Compositional biasi218 – 224Poly-Lys7

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4813. Eukaryota.
ENOG4111U5G. LUCA.
GeneTreeiENSGT00390000018400.
HOGENOMiHOG000048982.
InParanoidiO75822.
KOiK03245.
OMAiSSREDFT.
OrthoDBiEOG091G141O.
PhylomeDBiO75822.
TreeFamiTF101514.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75822-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAAAAGD SDSWDADAFS VEDPVRKVGG GGTAGGDRWE GEDEDEDVKD
60 70 80 90 100
NWDDDDDEKK EEAEVKPEVK ISEKKKIAEK IKEKERQQKK RQEEIKKRLE
110 120 130 140 150
EPEEPKVLTP EEQLADKLRL KKLQEESDLE LAKETFGVNN AVYGIDAMNP
160 170 180 190 200
SSRDDFTEFG KLLKDKITQY EKSLYYASFL EVLVRDVCIS LEIDDLKKIT
210 220 230 240 250
NSLTVLCSEK QKQEKQSKAK KKKKGVVPGG GLKATMKDDL ADYGGYDGGY

VQDYEDFM
Length:258
Mass (Da):29,062
Last modified:September 19, 2002 - v2
Checksum:i83624235424445AA
GO
Isoform 2 (identifier: O75822-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     137-191: GVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISL → V

Note: No experimental confirmation available.
Show »
Length:204
Mass (Da):22,941
Checksum:iB2F463EE48927284
GO
Isoform 3 (identifier: O75822-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-98: Missing.

Note: No experimental confirmation available.
Show »
Length:209
Mass (Da):23,027
Checksum:iCA7D79180C47F1A0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40E → G in AAC78729 (PubMed:9822659).Curated1

Mass spectrometryi

Molecular mass is 29293.2 Da from positions 1 - 258. 1 Publication
Molecular mass is 28974.2±0.3 Da from positions 1 - 258. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034007141A → T.1 PublicationCorresponds to variant rs2303578dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05477650 – 98Missing in isoform 3. 1 PublicationAdd BLAST49
Alternative sequenceiVSP_054593137 – 191GVNNA…VCISL → V in isoform 2. 1 PublicationAdd BLAST55

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97670 mRNA. Translation: AAC78729.1.
AK023388 mRNA. Translation: BAB14555.1.
AK300659 mRNA. Translation: BAG62345.1.
CR606839 mRNA. No translation available.
AC009996 Genomic DNA. No translation available.
BC002719 mRNA. Translation: AAH02719.1.
AF090923 mRNA. Translation: AAF24039.1.
CCDSiCCDS10111.1. [O75822-1]
CCDS61612.1. [O75822-2]
CCDS61613.1. [O75822-3]
RefSeqiNP_001271264.1. NM_001284335.1. [O75822-2]
NP_001271265.1. NM_001284336.1. [O75822-3]
NP_003749.2. NM_003758.3. [O75822-1]
UniGeneiHs.404056.

Genome annotation databases

EnsembliENST00000261868; ENSP00000261868; ENSG00000104131. [O75822-1]
ENST00000424492; ENSP00000414548; ENSG00000104131. [O75822-3]
ENST00000535391; ENSP00000440221; ENSG00000104131. [O75822-2]
GeneIDi8669.
KEGGihsa:8669.
UCSCiuc001ztv.4. human. [O75822-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97670 mRNA. Translation: AAC78729.1.
AK023388 mRNA. Translation: BAB14555.1.
AK300659 mRNA. Translation: BAG62345.1.
CR606839 mRNA. No translation available.
AC009996 Genomic DNA. No translation available.
BC002719 mRNA. Translation: AAH02719.1.
AF090923 mRNA. Translation: AAF24039.1.
CCDSiCCDS10111.1. [O75822-1]
CCDS61612.1. [O75822-2]
CCDS61613.1. [O75822-3]
RefSeqiNP_001271264.1. NM_001284335.1. [O75822-2]
NP_001271265.1. NM_001284336.1. [O75822-3]
NP_003749.2. NM_003758.3. [O75822-1]
UniGeneiHs.404056.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KRBNMR-B45-55[»]
3BPJX-ray1.85A/B/C/D141-220[»]
ProteinModelPortaliO75822.
SMRiO75822.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114218. 34 interactors.
DIPiDIP-31117N.
IntActiO75822. 19 interactors.
MINTiMINT-5003918.
STRINGi9606.ENSP00000261868.

PTM databases

iPTMnetiO75822.
PhosphoSitePlusiO75822.
SwissPalmiO75822.

Polymorphism and mutation databases

BioMutaiEIF3J.

Proteomic databases

EPDiO75822.
MaxQBiO75822.
PaxDbiO75822.
PeptideAtlasiO75822.
PRIDEiO75822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261868; ENSP00000261868; ENSG00000104131. [O75822-1]
ENST00000424492; ENSP00000414548; ENSG00000104131. [O75822-3]
ENST00000535391; ENSP00000440221; ENSG00000104131. [O75822-2]
GeneIDi8669.
KEGGihsa:8669.
UCSCiuc001ztv.4. human. [O75822-1]

Organism-specific databases

CTDi8669.
DisGeNETi8669.
GeneCardsiEIF3J.
HGNCiHGNC:3270. EIF3J.
HPAiHPA050977.
MIMi603910. gene.
neXtProtiNX_O75822.
OpenTargetsiENSG00000104131.
PharmGKBiPA162384902.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4813. Eukaryota.
ENOG4111U5G. LUCA.
GeneTreeiENSGT00390000018400.
HOGENOMiHOG000048982.
InParanoidiO75822.
KOiK03245.
OMAiSSREDFT.
OrthoDBiEOG091G141O.
PhylomeDBiO75822.
TreeFamiTF101514.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104131-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEIF3J. human.
EvolutionaryTraceiO75822.
GeneWikiiEIF3J.
GenomeRNAii8669.
PMAP-CutDBO75822.
PROiO75822.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104131.
CleanExiHS_EIF3J.
ExpressionAtlasiO75822. baseline and differential.
GenevisibleiO75822. HS.

Family and domain databases

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

Entry informationi

Entry nameiEIF3J_HUMAN
AccessioniPrimary (citable) accession number: O75822
Secondary accession number(s): B4DUI3
, F5H425, Q9BUD2, Q9H8Q2, Q9UI65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 19, 2002
Last modified: November 30, 2016
This is version 168 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.