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Protein

Eukaryotic translation initiation factor 3 subunit H

Gene

EIF3H

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

  • poly(A) RNA binding Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  • formation of translation preinitiation complex Source: UniProtKB-HAMAP
  • regulation of translational initiation Source: UniProtKB
  • translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147677-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.

Protein family/group databases

MEROPSiM67.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit HUniRule annotation
Short name:
eIF3hUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 3UniRule annotation
eIF-3-gamma
eIF3 p40 subunitUniRule annotation
Gene namesi
Name:EIF3HUniRule annotation
Synonyms:EIF3S3UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3273. EIF3H.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi8667.
OpenTargetsiENSG00000147677.
PharmGKBiPA162384854.

Polymorphism and mutation databases

BioMutaiEIF3H.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002139611 – 352Eukaryotic translation initiation factor 3 subunit HAdd BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineCombined sources1
Modified residuei183PhosphoserineUniRule annotationCombined sources1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO15372.
PaxDbiO15372.
PeptideAtlasiO15372.
PRIDEiO15372.

PTM databases

iPTMnetiO15372.
PhosphoSitePlusiO15372.
SwissPalmiO15372.

Expressioni

Gene expression databases

BgeeiENSG00000147677.
CleanExiHS_EIF3H.
ExpressionAtlasiO15372. baseline and differential.
GenevisibleiO15372. HS.

Organism-specific databases

HPAiHPA023117.
HPA023553.

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 RNF139; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner.UniRule annotation6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI3Q9P2A43EBI-709735,EBI-742038
DISC1Q9NRI58EBI-709735,EBI-529989
ORFQ9Q2G43EBI-709735,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi114216. 81 interactors.
DIPiDIP-33689N.
IntActiO15372. 54 interactors.
MINTiMINT-5000446.
STRINGi9606.ENSP00000429931.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-H1-221[»]
3J8Celectron microscopy-H1-221[»]
ProteinModelPortaliO15372.
SMRiO15372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 146MPNUniRule annotationAdd BLAST113

Sequence similaritiesi

Belongs to the eIF-3 subunit H family.UniRule annotation
Contains 1 MPN (JAB/Mov34) domain.UniRule annotation

Phylogenomic databases

eggNOGiKOG1560. Eukaryota.
ENOG410XSR9. LUCA.
GeneTreeiENSGT00730000111042.
HOVERGENiHBG000883.
InParanoidiO15372.
KOiK03247.
PhylomeDBiO15372.
TreeFamiTF101504.

Family and domain databases

CDDicd08065. MPN_eIF3h. 1 hit.
HAMAPiMF_03007. eIF3h. 1 hit.
InterProiIPR027524. eIF3h.
IPR000555. JAMM/MPN+_dom.
[Graphical view]
PANTHERiPTHR10410:SF3. PTHR10410:SF3. 2 hits.
PfamiPF01398. JAB. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRKEGTGS TATSSSSTAG AAGKGKGKGG SGDSAVKQVQ IDGLVVLKII
60 70 80 90 100
KHYQEEGQGT EVVQGVLLGL VVEDRLEITN CFPFPQHTED DADFDEVQYQ
110 120 130 140 150
MEMMRSLRHV NIDHLHVGWY QSTYYGSFVT RALLDSQFSY QHAIEESVVL
160 170 180 190 200
IYDPIKTAQG SLSLKAYRLT PKLMEVCKEK DFSPEALKKA NITFEYMFEE
210 220 230 240 250
VPIVIKNSHL INVLMWELEK KSAVADKHEL LSLASSNHLG KNLQLLMDRV
260 270 280 290 300
DEMSQDIVKY NTYMRNTSKQ QQQKHQYQQR RQQENMQRQS RGEPPLPEED
310 320 330 340 350
LSKLFKPPQP PARMDSLLIA GQINTYCQNI KEFTAQNLGK LFMAQALQEY

NN
Length:352
Mass (Da):39,930
Last modified:January 1, 1998 - v1
Checksum:iF3A6EFA0CEF587D0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73E → K in AAC84044 (Ref. 2) Curated1

Mass spectrometryi

Molecular mass is 40010.4 Da from positions 1 - 352. 1 Publication
Molecular mass is 39842.6±0.4 Da from positions 1 - 352. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54559 mRNA. Translation: AAD03465.1.
AF092576
, AF092569, AF092570, AF092571, AF092572, AF092573, AF092574, AF092575 Genomic DNA. Translation: AAC84044.1.
BC000386 mRNA. Translation: AAH00386.1.
CCDSiCCDS6319.1.
RefSeqiNP_003747.1. NM_003756.2.
UniGeneiHs.492599.

Genome annotation databases

EnsembliENST00000521861; ENSP00000429931; ENSG00000147677.
GeneIDi8667.
KEGGihsa:8667.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54559 mRNA. Translation: AAD03465.1.
AF092576
, AF092569, AF092570, AF092571, AF092572, AF092573, AF092574, AF092575 Genomic DNA. Translation: AAC84044.1.
BC000386 mRNA. Translation: AAH00386.1.
CCDSiCCDS6319.1.
RefSeqiNP_003747.1. NM_003756.2.
UniGeneiHs.492599.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-H1-221[»]
3J8Celectron microscopy-H1-221[»]
ProteinModelPortaliO15372.
SMRiO15372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114216. 81 interactors.
DIPiDIP-33689N.
IntActiO15372. 54 interactors.
MINTiMINT-5000446.
STRINGi9606.ENSP00000429931.

Protein family/group databases

MEROPSiM67.971.

PTM databases

iPTMnetiO15372.
PhosphoSitePlusiO15372.
SwissPalmiO15372.

Polymorphism and mutation databases

BioMutaiEIF3H.

Proteomic databases

EPDiO15372.
PaxDbiO15372.
PeptideAtlasiO15372.
PRIDEiO15372.

Protocols and materials databases

DNASUi8667.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000521861; ENSP00000429931; ENSG00000147677.
GeneIDi8667.
KEGGihsa:8667.

Organism-specific databases

CTDi8667.
DisGeNETi8667.
GeneCardsiEIF3H.
HGNCiHGNC:3273. EIF3H.
HPAiHPA023117.
HPA023553.
MIMi603912. gene.
neXtProtiNX_O15372.
OpenTargetsiENSG00000147677.
PharmGKBiPA162384854.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1560. Eukaryota.
ENOG410XSR9. LUCA.
GeneTreeiENSGT00730000111042.
HOVERGENiHBG000883.
InParanoidiO15372.
KOiK03247.
PhylomeDBiO15372.
TreeFamiTF101504.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147677-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

ChiTaRSiEIF3H. human.
GeneWikiiEIF3H.
GenomeRNAii8667.
PROiO15372.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147677.
CleanExiHS_EIF3H.
ExpressionAtlasiO15372. baseline and differential.
GenevisibleiO15372. HS.

Family and domain databases

CDDicd08065. MPN_eIF3h. 1 hit.
HAMAPiMF_03007. eIF3h. 1 hit.
InterProiIPR027524. eIF3h.
IPR000555. JAMM/MPN+_dom.
[Graphical view]
PANTHERiPTHR10410:SF3. PTHR10410:SF3. 2 hits.
PfamiPF01398. JAB. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3H_HUMAN
AccessioniPrimary (citable) accession number: O15372
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 156 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, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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.