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O15372

- EIF3H_HUMAN

UniProt

O15372 - EIF3H_HUMAN

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Protein
Eukaryotic translation initiation factor 3 subunit H
Gene
EIF3H, EIF3S3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. 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 H
Short name:
eIF3h
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 3
eIF-3-gamma
eIF3 p40 subunit
Gene namesi
Name:EIF3H
Synonyms:EIF3S3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3273. EIF3H.

Subcellular locationi

Cytoplasm By similarity 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. extracellular vesicular exosome Source: UniProt
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 HUniRule annotation
PRO_0000213961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO15372.
PaxDbiO15372.
PRIDEiO15372.

PTM databases

PhosphoSiteiO15372.

Expressioni

Gene expression databases

ArrayExpressiO15372.
BgeeiO15372.
CleanExiHS_EIF3H.
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.5 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. 56 interactions.
DIPiDIP-33689N.
IntActiO15372. 46 interactions.
MINTiMINT-5000446.
STRINGi9606.ENSP00000276682.

Structurei

3D structure databases

ProteinModelPortaliO15372.
SMRiO15372. Positions 36-219.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 146113MPN
Add
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit H family.

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

MASRKEGTGS TATSSSSTAG AAGKGKGKGG SGDSAVKQVQ IDGLVVLKII    50
KHYQEEGQGT EVVQGVLLGL VVEDRLEITN CFPFPQHTED DADFDEVQYQ 100
MEMMRSLRHV NIDHLHVGWY QSTYYGSFVT RALLDSQFSY QHAIEESVVL 150
IYDPIKTAQG SLSLKAYRLT PKLMEVCKEK DFSPEALKKA NITFEYMFEE 200
VPIVIKNSHL INVLMWELEK KSAVADKHEL LSLASSNHLG KNLQLLMDRV 250
DEMSQDIVKY NTYMRNTSKQ QQQKHQYQQR RQQENMQRQS RGEPPLPEED 300
LSKLFKPPQP PARMDSLLIA GQINTYCQNI KEFTAQNLGK LFMAQALQEY 350
NN 352
Length:352
Mass (Da):39,930
Last modified:January 1, 1998 - v1
Checksum:iF3A6EFA0CEF587D0
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731E → K in AAC84044. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6319.1.
RefSeqi NP_003747.1. NM_003756.2.
UniGenei Hs.492599.

3D structure databases

ProteinModelPortali O15372.
SMRi O15372. Positions 36-219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114216. 56 interactions.
DIPi DIP-33689N.
IntActi O15372. 46 interactions.
MINTi MINT-5000446.
STRINGi 9606.ENSP00000276682.

Protein family/group databases

MEROPSi M67.971.

PTM databases

PhosphoSitei O15372.

Proteomic databases

MaxQBi O15372.
PaxDbi O15372.
PRIDEi O15372.

Protocols and materials databases

DNASUi 8667.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000521861 ; ENSP00000429931 ; ENSG00000147677 .
GeneIDi 8667.
KEGGi hsa:8667.
UCSCi uc003yoa.3. human.

Organism-specific databases

CTDi 8667.
GeneCardsi GC08M117727.
HGNCi HGNC:3273. EIF3H.
HPAi HPA023117.
HPA023553.
MIMi 603912. gene.
neXtProti NX_O15372.
PharmGKBi PA162384854.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG314046.
HOVERGENi HBG000883.
InParanoidi O15372.
KOi K03247.
OrthoDBi EOG7992RH.
PhylomeDBi O15372.
TreeFami TF101504.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi EIF3H. human.
GeneWikii EIF3H.
GenomeRNAii 8667.
NextBioi 32511.
PROi O15372.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15372.
Bgeei O15372.
CleanExi HS_EIF3H.
Genevestigatori O15372.

Family and domain databases

HAMAPi MF_03007. eIF3h.
InterProi IPR027524. eIF3h.
IPR000555. JAMM/MPN+_dom.
[Graphical view ]
PANTHERi PTHR10410:SF3. PTHR10410:SF3. 1 hit.
Pfami PF01398. JAB. 1 hit.
[Graphical view ]
SMARTi SM00232. JAB_MPN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1997) [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 (SEP-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(2004) [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(2005) [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(2005) [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(2010) [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(2006) [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(2007) [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(2007) [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(2008) [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(2010) [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. "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(2005) [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: September 3, 2014
This is version 131 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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