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Protein

Eukaryotic translation initiation factor 3 subunit K

Gene

EIF3K

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:17581632, 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 (PubMed:17581632). 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).UniRule annotation3 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:ENSG00000178982-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 KUniRule annotation
Short name:
eIF3kUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 12UniRule annotation
Muscle-specific gene M9 protein
PLAC-24
eIF-3 p25UniRule annotation
eIF-3 p28
Gene namesi
Name:EIF3KUniRule annotation
Synonyms:EIF3S12UniRule annotation
ORF Names:ARG134, HSPC029, MSTP001, PTD001
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:24656. EIF3K.

Subcellular locationi

  • Nucleus UniRule annotation1 Publication
  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic translation initiation factor 3 complex Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi27335.
OpenTargetsiENSG00000178982.
ENSG00000282986.
PharmGKBiPA162384923.

Polymorphism and mutation databases

BioMutaiEIF3K.
DMDMi23396628.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotationCombined sources2 Publications
ChainiPRO_00001235462 – 218Eukaryotic translation initiation factor 3 subunit KAdd BLAST217

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineUniRule annotationCombined sources2 Publications1
Modified residuei28PhosphothreonineCombined sources1
Modified residuei217PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UBQ5.
PaxDbiQ9UBQ5.
PeptideAtlasiQ9UBQ5.
PRIDEiQ9UBQ5.
TopDownProteomicsiQ9UBQ5-1. [Q9UBQ5-1]

PTM databases

iPTMnetiQ9UBQ5.
PhosphoSitePlusiQ9UBQ5.
SwissPalmiQ9UBQ5.

Expressioni

Tissue specificityi

Ubiquitous, with the highest levels of expression in brain, testis and kidney.1 Publication

Gene expression databases

BgeeiENSG00000178982.
CleanExiHS_EIF3K.
ExpressionAtlasiQ9UBQ5. baseline and differential.
GenevisibleiQ9UBQ5. HS.

Organism-specific databases

HPAiHPA045446.
HPA054590.

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. Interacts with CCND3, but not with CCND1 and CCND2.UniRule annotation6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3LQ9Y2625EBI-354344,EBI-373519
ORFQ9Q2G45EBI-354344,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi118148. 53 interactors.
DIPiDIP-32880N.
IntActiQ9UBQ5. 17 interactors.
MINTiMINT-5002042.
STRINGi9606.ENSP00000248342.

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 16Combined sources14
Helixi18 – 21Combined sources4
Helixi23 – 25Combined sources3
Helixi26 – 39Combined sources14
Helixi44 – 56Combined sources13
Helixi58 – 60Combined sources3
Helixi63 – 75Combined sources13
Turni76 – 78Combined sources3
Helixi81 – 87Combined sources7
Helixi91 – 94Combined sources4
Helixi99 – 110Combined sources12
Helixi114 – 120Combined sources7
Helixi126 – 129Combined sources4
Helixi134 – 149Combined sources16
Beta strandi151 – 153Combined sources3
Helixi155 – 161Combined sources7
Helixi167 – 177Combined sources11
Helixi192 – 195Combined sources4
Helixi207 – 214Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RZ4X-ray2.10A1-218[»]
3J8Belectron microscopy-K1-190[»]
3J8Celectron microscopy-K1-190[»]
ProteinModelPortaliQ9UBQ5.
SMRiQ9UBQ5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBQ5.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3252. Eukaryota.
ENOG410ZSE4. LUCA.
GeneTreeiENSGT00390000009409.
HOGENOMiHOG000008222.
HOVERGENiHBG052081.
InParanoidiQ9UBQ5.
KOiK15028.
OMAiYVQDQAK.
OrthoDBiEOG091G0IXT.
PhylomeDBiQ9UBQ5.
TreeFamiTF314893.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.250. 1 hit.
HAMAPiMF_03010. eIF3k. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR033464. CSN8_PSD8_EIF3K.
IPR009374. eIF3k.
IPR016020. Transl_init_fac_sub12_N_euk.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR13022. PTHR13022. 1 hit.
PfamiPF10075. CSN8_PSD8_EIF3K. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48371. SSF48371. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBQ5-1) [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
MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV
60 70 80 90 100
LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR
110 120 130 140 150
QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY
160 170 180 190 200
QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN
210
IVEKIDFDSV SSIMASSQ
Length:218
Mass (Da):25,060
Last modified:May 1, 2000 - v1
Checksum:i6B2CBBE8A9D1F28F
GO
Isoform 2 (identifier: Q9UBQ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     210-218: VSSIMASSQ → EW

Note: No experimental confirmation available.
Show »
Length:211
Mass (Da):24,484
Checksum:i59CDE70AC1995450
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti119Q → K in AAD40193 (PubMed:11042152).Curated1

Mass spectrometryi

Molecular mass is 24970.6 Da from positions 1 - 218. 1 Publication
Molecular mass is 24971.1±0.2 Da from positions 1 - 218. Determined by MALDI. 1 Publication

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055475210 – 218VSSIMASSQ → EW in isoform 2. 1 Publication9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY245432 mRNA. Translation: AAP22070.1.
AB019392 mRNA. Translation: BAA76626.1.
AF077051 mRNA. Translation: AAD27784.1.
AF109355 mRNA. Translation: AAQ13503.1.
AF315506 mRNA. Translation: AAK01365.1.
AF085358 mRNA. Translation: AAD40193.1.
AK289554 mRNA. Translation: BAF82243.1.
AK316344 mRNA. Translation: BAH14715.1.
AC008649 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56807.1.
BC001031 mRNA. Translation: AAH01031.1.
BC007335 mRNA. Translation: AAH07335.2.
BC007559 mRNA. Translation: AAH07559.1.
CCDSiCCDS12517.1. [Q9UBQ5-1]
RefSeqiNP_037366.1. NM_013234.3. [Q9UBQ5-1]
UniGeneiHs.314359.

Genome annotation databases

EnsembliENST00000248342; ENSP00000248342; ENSG00000178982. [Q9UBQ5-1]
ENST00000545173; ENSP00000438145; ENSG00000178982. [Q9UBQ5-2]
ENST00000635417; ENSP00000489379; ENSG00000282986. [Q9UBQ5-2]
ENST00000635567; ENSP00000489438; ENSG00000282986. [Q9UBQ5-1]
GeneIDi27335.
KEGGihsa:27335.
UCSCiuc002oiz.2. human. [Q9UBQ5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY245432 mRNA. Translation: AAP22070.1.
AB019392 mRNA. Translation: BAA76626.1.
AF077051 mRNA. Translation: AAD27784.1.
AF109355 mRNA. Translation: AAQ13503.1.
AF315506 mRNA. Translation: AAK01365.1.
AF085358 mRNA. Translation: AAD40193.1.
AK289554 mRNA. Translation: BAF82243.1.
AK316344 mRNA. Translation: BAH14715.1.
AC008649 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56807.1.
BC001031 mRNA. Translation: AAH01031.1.
BC007335 mRNA. Translation: AAH07335.2.
BC007559 mRNA. Translation: AAH07559.1.
CCDSiCCDS12517.1. [Q9UBQ5-1]
RefSeqiNP_037366.1. NM_013234.3. [Q9UBQ5-1]
UniGeneiHs.314359.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RZ4X-ray2.10A1-218[»]
3J8Belectron microscopy-K1-190[»]
3J8Celectron microscopy-K1-190[»]
ProteinModelPortaliQ9UBQ5.
SMRiQ9UBQ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118148. 53 interactors.
DIPiDIP-32880N.
IntActiQ9UBQ5. 17 interactors.
MINTiMINT-5002042.
STRINGi9606.ENSP00000248342.

PTM databases

iPTMnetiQ9UBQ5.
PhosphoSitePlusiQ9UBQ5.
SwissPalmiQ9UBQ5.

Polymorphism and mutation databases

BioMutaiEIF3K.
DMDMi23396628.

Proteomic databases

EPDiQ9UBQ5.
PaxDbiQ9UBQ5.
PeptideAtlasiQ9UBQ5.
PRIDEiQ9UBQ5.
TopDownProteomicsiQ9UBQ5-1. [Q9UBQ5-1]

Protocols and materials databases

DNASUi27335.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248342; ENSP00000248342; ENSG00000178982. [Q9UBQ5-1]
ENST00000545173; ENSP00000438145; ENSG00000178982. [Q9UBQ5-2]
ENST00000635417; ENSP00000489379; ENSG00000282986. [Q9UBQ5-2]
ENST00000635567; ENSP00000489438; ENSG00000282986. [Q9UBQ5-1]
GeneIDi27335.
KEGGihsa:27335.
UCSCiuc002oiz.2. human. [Q9UBQ5-1]

Organism-specific databases

CTDi27335.
DisGeNETi27335.
GeneCardsiEIF3K.
HGNCiHGNC:24656. EIF3K.
HPAiHPA045446.
HPA054590.
MIMi609596. gene.
neXtProtiNX_Q9UBQ5.
OpenTargetsiENSG00000178982.
ENSG00000282986.
PharmGKBiPA162384923.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3252. Eukaryota.
ENOG410ZSE4. LUCA.
GeneTreeiENSGT00390000009409.
HOGENOMiHOG000008222.
HOVERGENiHBG052081.
InParanoidiQ9UBQ5.
KOiK15028.
OMAiYVQDQAK.
OrthoDBiEOG091G0IXT.
PhylomeDBiQ9UBQ5.
TreeFamiTF314893.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000178982-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

ChiTaRSiEIF3K. human.
EvolutionaryTraceiQ9UBQ5.
GeneWikiiEIF3K.
GenomeRNAii27335.
PROiQ9UBQ5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000178982.
CleanExiHS_EIF3K.
ExpressionAtlasiQ9UBQ5. baseline and differential.
GenevisibleiQ9UBQ5. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.250. 1 hit.
HAMAPiMF_03010. eIF3k. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR033464. CSN8_PSD8_EIF3K.
IPR009374. eIF3k.
IPR016020. Transl_init_fac_sub12_N_euk.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR13022. PTHR13022. 1 hit.
PfamiPF10075. CSN8_PSD8_EIF3K. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3K_HUMAN
AccessioniPrimary (citable) accession number: Q9UBQ5
Secondary accession number(s): A8K0I9
, B7ZAM9, Q96IQ0, Q9Y6D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 163 of the entry and version 1 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Translation initiation factors
    List of translation initiation factor entries
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.