Reviewed, UniProtKB/Swiss-Prot O75822 (EIF3J_HUMAN)

Names and origin

Protein names

Recommended name:
    Eukaryotic translation initiation factor 3 subunit J
      Short name=eIF3j
Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 1
    eIF-3-alpha
    eIF3 p35

Gene names

Name:	EIF3J
Synonyms:	EIF3S1
ORF Names:	PRO0391

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	258 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA.
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 FRAP1 and RAPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Ref.1 Ref.6 Ref.7 Ref.12 Ref.14
Subcellular location	Cytoplasm Probable.
Post-translational modification	Phosphorylated. Phosphorylation is enhanced upon serum stimulation. Ref.9 Ref.11 Ref.13 Ref.15 Ref.16
Sequence similarities	Belongs to the eIF-3 subunit J family.
Mass spectrometry	Molecular mass is 29293.2 Da from positions 1 - 258. Ref.15 Molecular mass is 28974.2±0.3 Da from positions 1 - 258. Determined by MALDI. Ref.17

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	protein binding Ref.7 Inferred from physical interaction. Source: IntAct translation initiation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF3B	P55884	1	EBI-366647,EBI-366696

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.15 Ref.4

Chain

2 – 258

257

Eukaryotic translation initiation factor 3 subunit J

PRO_0000123506

Regions

Region

2 – 69

68

Sufficient for interaction with EIF3B

Region

243 – 258

16

Promotes stable association with the 40S ribosome

Coiled coil

70 – 135

66

Potential

Compositional bias

2 – 8

7

Poly-Ala

Compositional bias

29 – 32

4

Poly-Gly

Compositional bias

53 – 57

5

Poly-Asp

Compositional bias

218 – 224

7

Poly-Lys

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.15 Ref.4

Modified residue

11

1

Phosphoserine Ref.9 Ref.15

Modified residue

13

1

Phosphoserine Ref.9 Ref.15

Modified residue

20

1

Phosphoserine Ref.15

Modified residue

109

1

Phosphothreonine Ref.11 Ref.13 Ref.15 Ref.16

Modified residue

127

1

Phosphoserine Ref.16

Natural variations

Natural variant

141

1

A → T: dbSNP rs2303578. Ref.2

VAR_034007

Experimental info

Sequence conflict

40

1

E → G in AAC78729. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

258

Helix Strand Turn

Details...

Turn

145 – 147

3

Helix

153 – 167

15

Helix

168 – 170

3

Helix

176 – 188

13

Helix

193 – 212

20

Sequences

	Sequence		Length	Mass (Da)
	O75822-1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: 83624235424445AA	FASTA	258	29,062
	10 20 30 40 50 60 MAAAAAAAGD SDSWDADAFS VEDPVRKVGG GGTAGGDRWE GEDEDEDVKD NWDDDDDEKK 70 80 90 100 110 120 EEAEVKPEVK ISEKKKIAEK IKEKERQQKK RQEEIKKRLE EPEEPKVLTP EEQLADKLRL 130 140 150 160 170 180 KKLQEESDLE LAKETFGVNN AVYGIDAMNP SSRDDFTEFG KLLKDKITQY EKSLYYASFL 190 200 210 220 230 240 EVLVRDVCIS LEIDDLKKIT NSLTVLCSEK QKQEKQSKAK KKKKGVVPGG GLKATMKDDL 250 ADYGGYDGGY VQDYEDFM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3." Block K.L., Vornlocher H.-P., Hershey J.W.B. J. Biol. Chem. 273:31901-31908(1998) [PubMed: 9822659] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH EIF3A.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-141. Tissue: Ovarian carcinoma.
[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: Uterus.
[4]	Bienvenut W.V., Vousden K.H., Lukashchuk N. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-27; 99-119; 123-133 AND 199-210, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[5]	"Functional prediction of the coding sequences of 50 new genes deduced by analysis of cDNA clones from human fetal liver." Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S., Liu M., He F. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-258. Tissue: Fetal liver.
[6]	"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 EIF3K.
[7]	"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 AND THE 40S RIBOSOMAL SUBUNIT.
[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]	"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-11 AND SER-13, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit." ElAntak L., Tzakos A.G., Locker N., Lukavsky P.J. J. Biol. Chem. 282:8165-8174(2007) [PubMed: 17190833] [Abstract] Cited for: INTERACTION WITH EIF3B AND THE 40S RIBOSOMAL SUBUNIT.
[13]	"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-109, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"eIF3j is located in the decoding center of the human 40S ribosomal subunit." Fraser C.S., Berry K.E., Hershey J.W.B., Doudna J.A. Mol. Cell 26:811-819(2007) [PubMed: 17588516] [Abstract] Cited for: INTERACTION WITH THE 40S RIBOSOMAL SUBUNIT.
[15]	"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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-11; SER-13; SER-20 AND THR-109, MASS SPECTROMETRY.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109 AND SER-127, MASS SPECTROMETRY.
[17]	"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.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"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.
[20]	"Crystal structure of human translation initiation factor 3, subunit 1 alpha." Structural genomics consortium (SGC) Submitted (JAN-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 141-220.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U97670 mRNA. Translation: AAC78729.1.
AK023388 mRNA. Translation: BAB14555.1.
BC002719 mRNA. Translation: AAH02719.1.
AF090923 mRNA. Translation: AAF24039.1.

IPI

IPI00290461.

RefSeq

NP_003749.2.

UniGene

Hs.404056

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BPJ	X-ray	1.85	A/B/C/D	141-220	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O75822. 11 interactions.

PTM databases

PhosphoSite

O75822.

Proteomic databases

PeptideAtlas

O75822.

PRIDE

O75822.

Genome annotation databases

Ensembl

ENSG00000104131. Homo sapiens. [Contig view]

GeneID

8669.

KEGG

hsa:8669.

NMPDR

fig|9606.3.peg.10639.

Organism-specific databases

GeneCards

GC15P042617.

H-InvDB

HIX0012198.

HGNC

HGNC:3270. EIF3J.

MIM

603910. gene.

PharmGKB

PA27698.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O75822.

HOVERGEN

O75822.

OMA

O75822. DSWDADA.

Enzyme and pathway databases

Reactome

REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O75822.

Bgee

O75822.

CleanEx

HS_EIF3J.

GermOnline

ENSG00000104131. Homo sapiens.

Family and domain databases

InterPro

IPR013906. eIF3_subunit.
[Graphical view]

PANTHER

PTHR21681. eIF3_subunit. 1 hit.

Pfam

PF08597. eIF3_subunit. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

32519.

PMAP-CutDB

O75822.

SOURCE

Search...

Entry information

Entry name

EIF3J_HUMAN

Accession

Primary (citable) accession number: O75822
Secondary accession number(s): Q9BUD2, Q9H8Q2, Q9UI65

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	September 19, 2002
Last modified:	June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)