Q13347 (EIF3I_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 3 subunit I
Short name=eIF3i

Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 2
TGF-beta receptor-interacting protein 1
Short name=TRIP-1
eIF-3-beta
eIF3 p36

Gene names

Name:	EIF3I
Synonyms:	EIF3S2, TRIP1

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	325 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. Ref.5 Ref.6
Subcellular location	Cytoplasm Probable.
Post-translational modification	Phosphorylated by TGF-beta type II receptor. Ref.7 Ref.10
Sequence similarities	Belongs to the eIF-3 subunit I family. Contains 5 WD repeats.
Mass spectrometry	Molecular mass is 36501.9 Da from positions 1 - 325. Ref.12 Molecular mass is 36503.2±0.4 Da from positions 1 - 325. Determined by MALDI. Ref.14

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Domain	Repeat WD repeat
Molecular function	Initiation factor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 3 complex Inferred from direct assay Ref.12Ref.11Ref.14. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.6. Source: IntAct translation initiation factor activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CLEC4G	Q6UXB4	3	EBI-354047,EBI-2114729
EIF3B	P55884	3	EBI-354047,EBI-366696

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 325	325	Eukaryotic translation initiation factor 3 subunit I		PRO_0000051036
Regions
	Repeat	8 – 47	40	WD 1
	Repeat	50 – 91	42	WD 2
	Repeat	144 – 183	40	WD 3
	Repeat	186 – 225	40	WD 4
	Repeat	283 – 324	42	WD 5
Amino acid modifications
	Modified residue	264	1	N6-acetyllysine Ref.15
	Modified residue	308	1	Phosphotyrosine Ref.7 Ref.10
	Cross-link	282		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

Sequences

	Sequence		Length	Mass (Da)
	Q13347 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 02797BB72A752A96	FASTA	325	36,502
	10 20 30 40 50 60 MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA 70 80 90 100 110 120 DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC 130 140 150 160 170 180 FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV 190 200 210 220 230 240 LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN 250 260 270 280 290 300 YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY 310 320 SSGGEDGYVR IHYFDPQYFE FEFEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation and diversity of eukaryotic translation initiation factor eIF3." Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B. J. Biol. Chem. 272:1101-1109(1997) [PubMed: 8995409] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor." Chen R.H., Miettinen P.J., Maruka E.M., Choy L., Derynck R. Nature 377:548-552(1995) [PubMed: 7566156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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 and Muscle.
[4]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 269-280 AND 283-298, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[5]	"Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3." Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B. Eur. J. Biochem. 270:4133-4139(2003) [PubMed: 14519125] [Abstract] Cited for: INTERACTION WITH EIF3B.
[6]	"The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro." Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A., Hershey J.W.B. J. Biol. Chem. 279:8946-8956(2004) [PubMed: 14688252] [Abstract] Cited for: INTERACTION WITH EIF3B.
[7]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, MASS SPECTROMETRY.
[8]	"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.
[9]	"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.
[10]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[11]	"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.
[12]	"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, MASS SPECTROMETRY.
[13]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-282, MASS SPECTROMETRY.
[14]	"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.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, MASS SPECTROMETRY.
[16]	"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].
[17]	"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	U39067 mRNA. Translation: AAC97144.1. U36764 mRNA. Translation: AAC50224.1. BC000413 mRNA. Translation: AAH00413.1. BC003140 mRNA. Translation: AAH03140.1.
IPI	IPI00012795.
PIR	S60335.
RefSeq	NP_003748.1. NM_003757.2.
UniGene	Hs.530096.
3D structure databases
ProteinModelPortal	Q13347.
SMR	Q13347. Positions 1-324.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31116N.
IntAct	Q13347. 13 interactions.
MINT	MINT-5004513.
STRING	Q13347.
PTM databases
PhosphoSite	Q13347.
Polymorphism databases
DMDM	2494895.
2D gel databases
DOSAC-COBS-2DPAGE	Q13347.
OGP	Q13347.
PHCI-2DPAGE	Q13347.
Proteomic databases
PeptideAtlas	Q13347.
PRIDE	Q13347.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000373586; ENSP00000362688; ENSG00000084623.
GeneID	8668.
KEGG	hsa:8668.
UCSC	uc001bur.2. human.
Organism-specific databases
CTD	8668.
GeneCards	GC01P032687.
H-InvDB	HIX0018823.
HGNC	HGNC:3272. EIF3I.
HPA	HPA029939. HPA029940.
MIM	603911. gene.
neXtProt	NX_Q13347.
PharmGKB	PA162384875.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG525604.
HOVERGEN	HBG000900.
InParanoid	Q13347.
OMA	ATVAGWS.
OrthoDB	EOG4HX519.
PhylomeDB	Q13347.
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	Q13347.
Bgee	Q13347.
CleanEx	HS_EIF3I.
Genevestigator	Q13347.
GermOnline	ENSG00000084623. Homo sapiens.
Family and domain databases
InterPro	IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KO	K03246.
Pfam	PF00400. WD40. 4 hits. [Graphical view]
SMART	SM00320. WD40. 5 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. 4 hits. PS50294. WD_REPEATS_REGION. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	32515.
SOURCE	Search...

Entry information

Entry name

EIF3I_HUMAN

Accession

Primary (citable) accession number: Q13347

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 120 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.