O15372 (EIF3H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EIF3H
Synonyms:	EIF3S3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Protein existence	Evidence 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 posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.
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.13
Subcellular location	Cytoplasm Probable.
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.11 Molecular mass is 39842.6±0.4 Da from positions 1 - 352. Determined by MALDI. Ref.13

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of translational initiation Traceable author statement Ref.1. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 3 complex Inferred from direct assay Ref.11Ref.9Ref.13. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.13. Source: UniProtKB translation initiation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABI3	Q9P2A4	3	EBI-709735,EBI-742038
DISC1	Q9NRI5	8	EBI-709735,EBI-529989

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 352	352	Eukaryotic translation initiation factor 3 subunit H		PRO_0000213961
Regions
	Domain	34 – 146	113	MPN
Amino acid modifications
	Modified residue	8	1	Phosphothreonine Ref.10
	Modified residue	10	1	Phosphoserine Ref.10
	Modified residue	11	1	Phosphothreonine Ref.10
	Modified residue	183	1	Phosphoserine Ref.7 Ref.11 Ref.12
Experimental info
	Sequence conflict	73	1	E → K in AAC84044. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O15372 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: F3A6EFA0CEF587D0	FASTA	352	39,930
	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

References

	« Hide 'large scale' referencesShow '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: 9341143] [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: 15489334] [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: 16286006] [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: 15703437] [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: 20068067] [Abstract] Cited for: INTERACTION WITH RNF139.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 16766523] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[9]	"Reconstitution reveals the functional core of mammalian eIF3." Masutani M., Sonenberg N., Yokoyama S., Imataka H. EMBO J. 26:3373-3383(2007) [PubMed: 17581632] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[10]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-10 AND THR-11, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 17322308] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, PHOSPHORYLATION AT SER-183, MASS SPECTROMETRY.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 18599441] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY, INTERACTION WITH EIF3B; EIF3F AND EIF3M.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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: 16322461] [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 , AF092569, AF092570, AF092571, AF092572, AF092573, AF092574, AF092575 Genomic DNA. Translation: AAC84044.1. BC000386 mRNA. Translation: AAH00386.1.
IPI	IPI00977658.
RefSeq	NP_003747.1. NM_003756.2.
UniGene	Hs.492599.
3D structure databases
ProteinModelPortal	O15372.
SMR	O15372. Positions 33-218.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33689N.
IntAct	O15372. 43 interactions.
MINT	MINT-5000446.
STRING	O15372.
Protein family/group databases
MEROPS	M67.971.
PTM databases
PhosphoSite	O15372.
Proteomic databases
PRIDE	O15372.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000276682; ENSP00000276682; ENSG00000147677. ENST00000411422; ENSP00000394044; ENSG00000147677.
GeneID	8667.
KEGG	hsa:8667.
UCSC	uc003yoa.1. human.
Organism-specific databases
CTD	8667.
GeneCards	GC08M117727.
H-InvDB	HIX0007736.
HGNC	HGNC:3273. EIF3H.
HPA	HPA023117. HPA023553.
MIM	603912. gene.
neXtProt	NX_O15372.
PharmGKB	PA162384854.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG000883.
InParanoid	O15372.
OrthoDB	EOG4SJ5FF.
PhylomeDB	O15372.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	O15372.
Bgee	O15372.
CleanEx	HS_EIF3H.
Genevestigator	O15372.
GermOnline	ENSG00000147677. Homo sapiens.
Family and domain databases
InterPro	IPR000555. Mov34_MPN_PAD1. [Graphical view]
KO	K03247.
Pfam	PF01398. Mov34. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	32511.
SOURCE	Search...

Entry information

Entry name

EIF3H_HUMAN

Accession

Primary (citable) accession number: O15372

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.