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Protein

Eukaryotic translation initiation factor 3 subunit J

Gene

EIF3J

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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.

GO - Molecular functioni

  1. translation initiation factor activity Source: GO_Central

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cytoplasmic translation Source: GO_Central
  3. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  4. gene expression Source: Reactome
  5. regulation of translational initiation Source: UniProtKB-HAMAP
  6. translation Source: Reactome
  7. 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.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit JUniRule annotation
Short name:
eIF3jUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 1UniRule annotation
eIF-3-alphaUniRule annotation
eIF3 p35UniRule annotation
Gene namesi
Name:EIF3JUniRule annotation
Synonyms:EIF3S1UniRule annotation
ORF Names:PRO0391
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:3270. EIF3J.

Subcellular locationi

  1. Cytoplasm 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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384902.

Polymorphism and mutation databases

BioMutaiEIF3J.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation8 Publications
Chaini2 – 258257Eukaryotic translation initiation factor 3 subunit JPRO_0000123506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineUniRule annotation8 Publications
Modified residuei11 – 111PhosphoserineUniRule annotation3 Publications
Modified residuei13 – 131PhosphoserineUniRule annotation3 Publications
Modified residuei20 – 201PhosphoserineUniRule annotation1 Publication
Modified residuei109 – 1091PhosphothreonineUniRule annotation5 Publications
Modified residuei127 – 1271Phosphoserine1 Publication
Modified residuei254 – 2541Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75822.
PaxDbiO75822.
PeptideAtlasiO75822.
PRIDEiO75822.

PTM databases

PhosphoSiteiO75822.

Miscellaneous databases

PMAP-CutDBO75822.

Expressioni

Gene expression databases

BgeeiO75822.
CleanExiHS_EIF3J.
ExpressionAtlasiO75822. baseline and differential.
GenevestigatoriO75822.

Organism-specific databases

HPAiHPA050977.

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.UniRule annotation8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3BP558845EBI-366647,EBI-366696
EIF4G1Q046372EBI-366647,EBI-73711

Protein-protein interaction databases

BioGridi114218. 27 interactions.
DIPiDIP-31117N.
IntActiO75822. 15 interactions.
MINTiMINT-5003918.
STRINGi9606.ENSP00000261868.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni145 – 1473Combined sources
Helixi153 – 16715Combined sources
Helixi168 – 1703Combined sources
Helixi176 – 18813Combined sources
Helixi193 – 21220Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KRBNMR-B45-55[»]
3BPJX-ray1.85A/B/C/D141-220[»]
ProteinModelPortaliO75822.
SMRiO75822. Positions 141-211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75822.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 6968Sufficient for interaction with EIF3BAdd
BLAST
Regioni243 – 25816Promotes stable association with the 40S ribosomeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili70 – 13566UniRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 87Poly-Ala
Compositional biasi29 – 324Poly-Gly
Compositional biasi53 – 575Poly-Asp
Compositional biasi218 – 2247Poly-Lys

Sequence similaritiesi

Belongs to the eIF-3 subunit J family.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG247523.
GeneTreeiENSGT00390000018400.
HOGENOMiHOG000048982.
InParanoidiO75822.
KOiK03245.
OMAiNASRDIH.
OrthoDBiEOG7J70H8.
PhylomeDBiO75822.
TreeFamiTF101514.

Family and domain databases

Gene3Di1.10.246.60. 1 hit.
HAMAPiMF_03009. eIF3j.
InterProiIPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view]
PANTHERiPTHR21681. PTHR21681. 1 hit.
PfamiPF08597. eIF3_subunit. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75822-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAAAAGD SDSWDADAFS VEDPVRKVGG GGTAGGDRWE GEDEDEDVKD
60 70 80 90 100
NWDDDDDEKK EEAEVKPEVK ISEKKKIAEK IKEKERQQKK RQEEIKKRLE
110 120 130 140 150
EPEEPKVLTP EEQLADKLRL KKLQEESDLE LAKETFGVNN AVYGIDAMNP
160 170 180 190 200
SSRDDFTEFG KLLKDKITQY EKSLYYASFL EVLVRDVCIS LEIDDLKKIT
210 220 230 240 250
NSLTVLCSEK QKQEKQSKAK KKKKGVVPGG GLKATMKDDL ADYGGYDGGY

VQDYEDFM
Length:258
Mass (Da):29,062
Last modified:September 19, 2002 - v2
Checksum:i83624235424445AA
GO
Isoform 2 (identifier: O75822-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     137-191: GVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISL → V

Note: No experimental confirmation available.

Show »
Length:204
Mass (Da):22,941
Checksum:iB2F463EE48927284
GO
Isoform 3 (identifier: O75822-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-98: Missing.

Note: No experimental confirmation available.

Show »
Length:209
Mass (Da):23,027
Checksum:iCA7D79180C47F1A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401E → G in AAC78729 (PubMed:9822659).Curated

Mass spectrometryi

Molecular mass is 29293.2 Da from positions 1 - 258. 1 Publication
Molecular mass is 28974.2±0.3 Da from positions 1 - 258. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411A → T.1 Publication
Corresponds to variant rs2303578 [ dbSNP | Ensembl ].
VAR_034007

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei50 – 9849Missing in isoform 3. 1 PublicationVSP_054776Add
BLAST
Alternative sequencei137 – 19155GVNNA…VCISL → V in isoform 2. 1 PublicationVSP_054593Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97670 mRNA. Translation: AAC78729.1.
AK023388 mRNA. Translation: BAB14555.1.
AK300659 mRNA. Translation: BAG62345.1.
CR606839 mRNA. No translation available.
AC009996 Genomic DNA. No translation available.
BC002719 mRNA. Translation: AAH02719.1.
AF090923 mRNA. Translation: AAF24039.1.
CCDSiCCDS10111.1. [O75822-1]
CCDS61612.1. [O75822-2]
CCDS61613.1. [O75822-3]
RefSeqiNP_001271264.1. NM_001284335.1. [O75822-2]
NP_001271265.1. NM_001284336.1. [O75822-3]
NP_003749.2. NM_003758.3. [O75822-1]
UniGeneiHs.404056.

Genome annotation databases

EnsembliENST00000261868; ENSP00000261868; ENSG00000104131. [O75822-1]
ENST00000424492; ENSP00000414548; ENSG00000104131. [O75822-3]
ENST00000535391; ENSP00000440221; ENSG00000104131. [O75822-2]
GeneIDi8669.
KEGGihsa:8669.
UCSCiuc001ztv.3. human. [O75822-1]
uc010ueg.2. human.

Polymorphism and mutation databases

BioMutaiEIF3J.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97670 mRNA. Translation: AAC78729.1.
AK023388 mRNA. Translation: BAB14555.1.
AK300659 mRNA. Translation: BAG62345.1.
CR606839 mRNA. No translation available.
AC009996 Genomic DNA. No translation available.
BC002719 mRNA. Translation: AAH02719.1.
AF090923 mRNA. Translation: AAF24039.1.
CCDSiCCDS10111.1. [O75822-1]
CCDS61612.1. [O75822-2]
CCDS61613.1. [O75822-3]
RefSeqiNP_001271264.1. NM_001284335.1. [O75822-2]
NP_001271265.1. NM_001284336.1. [O75822-3]
NP_003749.2. NM_003758.3. [O75822-1]
UniGeneiHs.404056.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KRBNMR-B45-55[»]
3BPJX-ray1.85A/B/C/D141-220[»]
ProteinModelPortaliO75822.
SMRiO75822. Positions 141-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114218. 27 interactions.
DIPiDIP-31117N.
IntActiO75822. 15 interactions.
MINTiMINT-5003918.
STRINGi9606.ENSP00000261868.

PTM databases

PhosphoSiteiO75822.

Polymorphism and mutation databases

BioMutaiEIF3J.

Proteomic databases

MaxQBiO75822.
PaxDbiO75822.
PeptideAtlasiO75822.
PRIDEiO75822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261868; ENSP00000261868; ENSG00000104131. [O75822-1]
ENST00000424492; ENSP00000414548; ENSG00000104131. [O75822-3]
ENST00000535391; ENSP00000440221; ENSG00000104131. [O75822-2]
GeneIDi8669.
KEGGihsa:8669.
UCSCiuc001ztv.3. human. [O75822-1]
uc010ueg.2. human.

Organism-specific databases

CTDi8669.
GeneCardsiGC15P044829.
HGNCiHGNC:3270. EIF3J.
HPAiHPA050977.
MIMi603910. gene.
neXtProtiNX_O75822.
PharmGKBiPA162384902.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG247523.
GeneTreeiENSGT00390000018400.
HOGENOMiHOG000048982.
InParanoidiO75822.
KOiK03245.
OMAiNASRDIH.
OrthoDBiEOG7J70H8.
PhylomeDBiO75822.
TreeFamiTF101514.

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.

Miscellaneous databases

ChiTaRSiEIF3J. human.
EvolutionaryTraceiO75822.
GeneWikiiEIF3J.
GenomeRNAii8669.
NextBioi32519.
PMAP-CutDBO75822.
PROiO75822.
SOURCEiSearch...

Gene expression databases

BgeeiO75822.
CleanExiHS_EIF3J.
ExpressionAtlasiO75822. baseline and differential.
GenevestigatoriO75822.

Family and domain databases

Gene3Di1.10.246.60. 1 hit.
HAMAPiMF_03009. eIF3j.
InterProiIPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view]
PANTHERiPTHR21681. PTHR21681. 1 hit.
PfamiPF08597. eIF3_subunit. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT THR-141.
    Tissue: Ovarian carcinoma and Skeletal muscle.
  3. Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Fetal brain.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Uterus.
  6. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma.
  7. "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 (ISOFORM 1).
    Tissue: Fetal liver.
  8. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3K.
  9. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3B AND THE 40S RIBOSOMAL SUBUNIT.
  10. "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.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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.
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3B AND THE 40S RIBOSOMAL SUBUNIT.
  15. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE 40S RIBOSOMAL SUBUNIT.
  17. "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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-11; SER-13; SER-20 AND THR-109, MASS SPECTROMETRY.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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.
  20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; THR-109 AND SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13 AND THR-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  26. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  28. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  29. "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.
  30. "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.

Entry informationi

Entry nameiEIF3J_HUMAN
AccessioniPrimary (citable) accession number: O75822
Secondary accession number(s): B4DUI3
, F5H425, Q9BUD2, Q9H8Q2, Q9UI65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 19, 2002
Last modified: April 29, 2015
This is version 150 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.