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O15372 (EIF3H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EIF3H
Synonyms:EIF3S3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03007

Subunit structure

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. Ref.4 Ref.6 Ref.7 Ref.9 Ref.10

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03007.

Sequence similarities

Belongs to the eIF-3 subunit H family.

Contains 1 MPN (JAB/Mov34) domain.

Mass spectrometry

Molecular mass is 40010.4 Da from positions 1 - 352. Ref.9

Molecular mass is 39842.6±0.4 Da from positions 1 - 352. Determined by MALDI. Ref.10

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABI3Q9P2A43EBI-709735,EBI-742038
DISC1Q9NRI58EBI-709735,EBI-529989
ORFQ9Q2G43EBI-709735,EBI-6248094From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Eukaryotic translation initiation factor 3 subunit H HAMAP-Rule MF_03007
PRO_0000213961

Regions

Domain34 – 146113MPN

Amino acid modifications

Modified residue1831Phosphoserine Ref.9 Ref.11

Experimental info

Sequence conflict731E → K in AAC84044. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O15372 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F3A6EFA0CEF587D0

FASTA35239,930
        10         20         30         40         50         60 
MASRKEGTGS TATSSSSTAG AAGKGKGKGG SGDSAVKQVQ IDGLVVLKII KHYQEEGQGT 

        70         80         90        100        110        120 
EVVQGVLLGL VVEDRLEITN CFPFPQHTED DADFDEVQYQ MEMMRSLRHV NIDHLHVGWY 

       130        140        150        160        170        180 
QSTYYGSFVT RALLDSQFSY QHAIEESVVL IYDPIKTAQG SLSLKAYRLT PKLMEVCKEK 

       190        200        210        220        230        240 
DFSPEALKKA NITFEYMFEE VPIVIKNSHL INVLMWELEK KSAVADKHEL LSLASSNHLG 

       250        260        270        280        290        300 
KNLQLLMDRV DEMSQDIVKY NTYMRNTSKQ QQQKHQYQQR RQQENMQRQS RGEPPLPEED 

       310        320        330        340        350 
LSKLFKPPQP PARMDSLLIA GQINTYCQNI KEFTAQNLGK LFMAQALQEY NN 

« Hide

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U54559 mRNA. Translation: AAD03465.1.
AF092576 expand/collapse EMBL AC list , AF092569, AF092570, AF092571, AF092572, AF092573, AF092574, AF092575 Genomic DNA. Translation: AAC84044.1.
BC000386 mRNA. Translation: AAH00386.1.
CCDSCCDS6319.1.
RefSeqNP_003747.1. NM_003756.2.
UniGeneHs.492599.

3D structure databases

ProteinModelPortalO15372.
SMRO15372. Positions 36-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114216. 57 interactions.
DIPDIP-33689N.
IntActO15372. 46 interactions.
MINTMINT-5000446.
STRING9606.ENSP00000276682.

Protein family/group databases

MEROPSM67.971.

PTM databases

PhosphoSiteO15372.

Proteomic databases

MaxQBO15372.
PaxDbO15372.
PRIDEO15372.

Protocols and materials databases

DNASU8667.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000521861; ENSP00000429931; ENSG00000147677.
GeneID8667.
KEGGhsa:8667.
UCSCuc003yoa.3. human.

Organism-specific databases

CTD8667.
GeneCardsGC08M117727.
HGNCHGNC:3273. EIF3H.
HPAHPA023117.
HPA023553.
MIM603912. gene.
neXtProtNX_O15372.
PharmGKBPA162384854.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314046.
HOVERGENHBG000883.
InParanoidO15372.
KOK03247.
OrthoDBEOG7992RH.
PhylomeDBO15372.
TreeFamTF101504.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO15372.
BgeeO15372.
CleanExHS_EIF3H.
GenevestigatorO15372.

Family and domain databases

HAMAPMF_03007. eIF3h.
InterProIPR027524. eIF3h.
IPR000555. JAMM/MPN+_dom.
[Graphical view]
PANTHERPTHR10410:SF3. PTHR10410:SF3. 1 hit.
PfamPF01398. JAB. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3H. human.
GeneWikiEIF3H.
GenomeRNAi8667.
NextBio32511.
PROO15372.
SOURCESearch...

Entry information

Entry nameEIF3H_HUMAN
AccessionPrimary (citable) accession number: O15372
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM