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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. 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.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  3. gene expression Source: Reactome
  4. regulation of translational initiation Source: UniProtKB
  5. translation Source: Reactome
  6. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

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
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3273. EIF3H.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  3. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  4. eukaryotic translation initiation factor 3 complex Source: UniProtKB
  5. eukaryotic translation initiation factor 3 complex, eIF3m Source: Ensembl
  6. extracellular vesicular exosome Source: UniProtKB
  7. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384854.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Eukaryotic translation initiation factor 3 subunit HPRO_0000213961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831PhosphoserineUniRule annotation2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO15372.
PaxDbiO15372.
PRIDEiO15372.

PTM databases

PhosphoSiteiO15372.

Expressioni

Gene expression databases

BgeeiO15372.
CleanExiHS_EIF3H.
ExpressionAtlasiO15372. baseline and differential.
GenevestigatoriO15372.

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 annotation5 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. 61 interactions.
DIPiDIP-33689N.
IntActiO15372. 46 interactions.
MINTiMINT-5000446.
STRINGi9606.ENSP00000276682.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-H1-221[»]
3J8Celectron microscopy-H1-221[»]
ProteinModelPortaliO15372.
SMRiO15372. Positions 37-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 146113MPNUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG314046.
HOVERGENiHBG000883.
InParanoidiO15372.
KOiK03247.
OrthoDBiEOG7992RH.
PhylomeDBiO15372.
TreeFamiTF101504.

Family and domain databases

HAMAPiMF_03007. eIF3h.
InterProiIPR027524. eIF3h.
IPR000555. JAMM/MPN+_dom.
[Graphical view]
PANTHERiPTHR10410:SF3. PTHR10410:SF3. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731E → K in AAC84044 (Ref. 2) Curated

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.
UCSCiuc003yoa.3. human.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-H1-221[»]
3J8Celectron microscopy-H1-221[»]
ProteinModelPortaliO15372.
SMRiO15372. Positions 37-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114216. 61 interactions.
DIPiDIP-33689N.
IntActiO15372. 46 interactions.
MINTiMINT-5000446.
STRINGi9606.ENSP00000276682.

Protein family/group databases

MEROPSiM67.971.

PTM databases

PhosphoSiteiO15372.

Proteomic databases

MaxQBiO15372.
PaxDbiO15372.
PRIDEiO15372.

Protocols and materials databases

DNASUi8667.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000521861; ENSP00000429931; ENSG00000147677.
GeneIDi8667.
KEGGihsa:8667.
UCSCiuc003yoa.3. human.

Organism-specific databases

CTDi8667.
GeneCardsiGC08M117654.
HGNCiHGNC:3273. EIF3H.
HPAiHPA023117.
HPA023553.
MIMi603912. gene.
neXtProtiNX_O15372.
PharmGKBiPA162384854.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG314046.
HOVERGENiHBG000883.
InParanoidiO15372.
KOiK03247.
OrthoDBiEOG7992RH.
PhylomeDBiO15372.
TreeFamiTF101504.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSiEIF3H. human.
GeneWikiiEIF3H.
GenomeRNAii8667.
NextBioi32511.
PROiO15372.
SOURCEiSearch...

Gene expression databases

BgeeiO15372.
CleanExiHS_EIF3H.
ExpressionAtlasiO15372. baseline and differential.
GenevestigatoriO15372.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly."
    Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C., Hinnebusch A.G., Hershey J.W.B.
    J. Biol. Chem. 272:27042-27052(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The gene encoding the p40 subunit of the translation initiation factor eIF3 has 8 exons, maps to the Langer-Giedion syndrome region on chromosome 8q24, but is not the TRPS gene."
    Schmidt O.G., von Holtum D., Gross S., Horsthemke B., Luedecke H.-J.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. "mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events."
    Holz M.K., Ballif B.A., Gygi S.P., Blenis J.
    Cell 123:569-580(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS6KB1, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association."
    Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.
    RNA 11:470-486(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
  6. "The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways."
    Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A., Gemmill R.M.
    Mol. Cancer Res. 8:93-106(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF139.
  7. "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit."
    LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E.
    J. Biol. Chem. 281:22917-22932(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Reconstitution reveals the functional core of mammalian eIF3."
    Masutani M., Sonenberg N., Yokoyama S., Imataka H.
    EMBO J. 26:3373-3383(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
  9. "Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry."
    Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.
    Mol. Cell. Proteomics 6:1135-1146(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, PHOSPHORYLATION AT SER-183, MASS SPECTROMETRY.
  10. "Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
    Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V.
    Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY, INTERACTION WITH EIF3B; EIF3F AND EIF3M.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Structural roles for human translation factor eIF3 in initiation of protein synthesis."
    Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.
    Science 310:1513-1515(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.

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: March 4, 2015
This is version 137 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

External Data

Dasty 3

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 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.