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Protein

Eukaryotic translation initiation factor 3 subunit L

Gene

EIF3L

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.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  2. regulation of translational initiation Source: UniProtKB-HAMAP
  3. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit LUniRule annotation
Short name:
eIF3lUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 6-interacting proteinUniRule annotation
Eukaryotic translation initiation factor 3 subunit E-interacting proteinUniRule annotation
Gene namesi
Name:EIF3LUniRule annotation
Synonyms:EIF3EIPUniRule annotation, EIF3S6IPUniRule annotation
ORF Names:HSPC021, HSPC025, MSTP005
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:18138. EIF3L.

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  2. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  3. eukaryotic translation initiation factor 3 complex Source: UniProtKB
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27706.

Polymorphism and mutation databases

BioMutaiEIF3L.
DMDMi23396631.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation3 Publications
Chaini2 – 564563Eukaryotic translation initiation factor 3 subunit LPRO_0000084162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineUniRule annotation3 Publications
Modified residuei21 – 211Phosphoserine1 Publication
Modified residuei465 – 4651N6-acetyllysine1 Publication
Modified residuei549 – 5491N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y262.
PaxDbiQ9Y262.
PRIDEiQ9Y262.

PTM databases

PhosphoSiteiQ9Y262.

Expressioni

Gene expression databases

BgeeiQ9Y262.
ExpressionAtlasiQ9Y262. baseline and differential.
GenevestigatoriQ9Y262.

Organism-specific databases

HPAiHPA003028.

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. Interacts with RRN3.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3KQ9UBQ55EBI-373519,EBI-354344
ORFQ9Q2G45EBI-373519,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi119516. 49 interactions.
DIPiDIP-31172N.
IntActiQ9Y262. 16 interactions.
MINTiMINT-216779.
STRINGi9606.ENSP00000416892.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-L1-515[»]
3J8Celectron microscopy-L1-515[»]
ProteinModelPortaliQ9Y262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG251364.
GeneTreeiENSGT00390000000411.
HOVERGENiHBG001289.
InParanoidiQ9Y262.
KOiK15029.
OMAiDVYENSW.
OrthoDBiEOG7XDBFF.
PhylomeDBiQ9Y262.
TreeFamiTF101523.

Family and domain databases

HAMAPiMF_03011. eIF3l.
InterProiIPR019382. eIF3l.
[Graphical view]
PANTHERiPTHR13242. PTHR13242. 1 hit.
PfamiPF10255. Paf67. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y262-1) [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
MSYPADDYES EAAYDPYAYP SDYDMHTGDP KQDLAYERQY EQQTYQVIPE
60 70 80 90 100
VIKNFIQYFH KTVSDLIDQK VYELQASRVS SDVIDQKVYE IQDIYENSWT
110 120 130 140 150
KLTERFFKNT PWPEAEAIAP QVGNDAVFLI LYKELYYRHI YAKVSGGPSL
160 170 180 190 200
EQRFESYYNY CNLFNYILNA DGPAPLELPN QWLWDIIDEF IYQFQSFSQY
210 220 230 240 250
RCKTAKKSEE EIDFLRSNPK IWNVHSVLNV LHSLVDKSNI NRQLEVYTSG
260 270 280 290 300
GDPESVAGEY GRHSLYKMLG YFSLVGLLRL HSLLGDYYQA IKVLENIELN
310 320 330 340 350
KKSMYSRVPE CQVTTYYYVG FAYLMMRRYQ DAIRVFANIL LYIQRTKSMF
360 370 380 390 400
QRTTYKYEMI NKQNEQMHAL LAIALTMYPM RIDESIHLQL REKYGDKMLR
410 420 430 440 450
MQKGDPQVYE ELFSYSCPKF LSPVVPNYDN VHPNYHKEPF LQQLKVFSDE
460 470 480 490 500
VQQQAQLSTI RSFLKLYTTM PVAKLAGFLD LTEQEFRIQL LVFKHKMKNL
510 520 530 540 550
VWTSGISALD GEFQSASEVD FYIDKDMIHI ADTKVARRYG DFFIRQIHKF
560
EELNRTLKKM GQRP
Length:564
Mass (Da):66,727
Last modified:November 1, 1999 - v1
Checksum:iECBD32192D96E3FE
GO
Isoform 2 (identifier: Q9Y262-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     146-193: Missing.

Note: No experimental confirmation available.

Show »
Length:516
Mass (Da):61,014
Checksum:i677BF3B55FF29FAF
GO

Sequence cautioni

The sequence CAG30322.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAX14899.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti353 – 3531T → I in AAQ13507 (Ref. 2) Curated
Sequence conflicti377 – 3771M → V in BAD96249 (Ref. 5) Curated
Sequence conflicti432 – 4321H → Y in BAD96216 (Ref. 5) Curated
Sequence conflicti434 – 4341N → D in BAD96249 (Ref. 5) Curated
Sequence conflicti513 – 5131F → L in BAG63674 (PubMed:14702039).Curated
Sequence conflicti528 – 5281I → T in BAG63674 (PubMed:14702039).Curated
Sequence conflicti558 – 5581K → R in BAG63674 (PubMed:14702039).Curated

Mass spectrometryi

Molecular mass is 66637.9 Da from positions 1 - 564. 1 Publication
Molecular mass is 66640.2±0.5 Da from positions 1 - 564. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti239 – 2391N → S.
Corresponds to variant rs11551387 [ dbSNP | Ensembl ].
VAR_053937

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei146 – 19348Missing in isoform 2. 1 PublicationVSP_045881Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077207 mRNA. Translation: AAD27002.1.
AF083243 mRNA. Translation: AAD39841.1.
AF109359 mRNA. Translation: AAQ13507.1.
CR456436 mRNA. Translation: CAG30322.1. Different initiation.
AK302346 mRNA. Translation: BAG63674.1.
AK315533 mRNA. Translation: BAG37913.1.
AK222496 mRNA. Translation: BAD96216.1.
AK222529 mRNA. Translation: BAD96249.1.
Z97630, AL022311 Genomic DNA. Translation: CAX14899.1. Different initiation.
CH471095 Genomic DNA. Translation: EAW60198.1.
BC001101 mRNA. Translation: AAH01101.1.
BC007510 mRNA. Translation: AAH07510.1.
BC029265 mRNA. Translation: AAH29265.1.
CCDSiCCDS13960.1. [Q9Y262-1]
CCDS56230.1. [Q9Y262-2]
RefSeqiNP_001229852.1. NM_001242923.1. [Q9Y262-2]
NP_057175.1. NM_016091.3. [Q9Y262-1]
UniGeneiHs.446852.

Genome annotation databases

EnsembliENST00000381683; ENSP00000371099; ENSG00000100129. [Q9Y262-2]
ENST00000624234; ENSP00000485663; ENSG00000100129. [Q9Y262-1]
GeneIDi51386.
KEGGihsa:51386.
UCSCiuc003auf.3. human. [Q9Y262-1]

Polymorphism and mutation databases

BioMutaiEIF3L.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077207 mRNA. Translation: AAD27002.1.
AF083243 mRNA. Translation: AAD39841.1.
AF109359 mRNA. Translation: AAQ13507.1.
CR456436 mRNA. Translation: CAG30322.1. Different initiation.
AK302346 mRNA. Translation: BAG63674.1.
AK315533 mRNA. Translation: BAG37913.1.
AK222496 mRNA. Translation: BAD96216.1.
AK222529 mRNA. Translation: BAD96249.1.
Z97630, AL022311 Genomic DNA. Translation: CAX14899.1. Different initiation.
CH471095 Genomic DNA. Translation: EAW60198.1.
BC001101 mRNA. Translation: AAH01101.1.
BC007510 mRNA. Translation: AAH07510.1.
BC029265 mRNA. Translation: AAH29265.1.
CCDSiCCDS13960.1. [Q9Y262-1]
CCDS56230.1. [Q9Y262-2]
RefSeqiNP_001229852.1. NM_001242923.1. [Q9Y262-2]
NP_057175.1. NM_016091.3. [Q9Y262-1]
UniGeneiHs.446852.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-L1-515[»]
3J8Celectron microscopy-L1-515[»]
ProteinModelPortaliQ9Y262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119516. 49 interactions.
DIPiDIP-31172N.
IntActiQ9Y262. 16 interactions.
MINTiMINT-216779.
STRINGi9606.ENSP00000416892.

PTM databases

PhosphoSiteiQ9Y262.

Polymorphism and mutation databases

BioMutaiEIF3L.
DMDMi23396631.

Proteomic databases

MaxQBiQ9Y262.
PaxDbiQ9Y262.
PRIDEiQ9Y262.

Protocols and materials databases

DNASUi51386.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381683; ENSP00000371099; ENSG00000100129. [Q9Y262-2]
ENST00000624234; ENSP00000485663; ENSG00000100129. [Q9Y262-1]
GeneIDi51386.
KEGGihsa:51386.
UCSCiuc003auf.3. human. [Q9Y262-1]

Organism-specific databases

CTDi51386.
GeneCardsiGC22P038244.
HGNCiHGNC:18138. EIF3L.
HPAiHPA003028.
neXtProtiNX_Q9Y262.
PharmGKBiPA27706.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG251364.
GeneTreeiENSGT00390000000411.
HOVERGENiHBG001289.
InParanoidiQ9Y262.
KOiK15029.
OMAiDVYENSW.
OrthoDBiEOG7XDBFF.
PhylomeDBiQ9Y262.
TreeFamiTF101523.

Miscellaneous databases

ChiTaRSiEIF3L. human.
GeneWikiiEIF3EIP.
GenomeRNAii51386.
NextBioi54905.
PROiQ9Y262.

Gene expression databases

BgeeiQ9Y262.
ExpressionAtlasiQ9Y262. baseline and differential.
GenevestigatoriQ9Y262.

Family and domain databases

HAMAPiMF_03011. eIF3l.
InterProiIPR019382. eIF3l.
[Graphical view]
PANTHERiPTHR13242. PTHR13242. 1 hit.
PfamiPF10255. Paf67. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Aorta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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).
    Tissue: Testis.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adipose tissue.
  6. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Brain, Cervix and Colon.
  9. "The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3."
    Morris-Desbois C., Rety S., Ferro M., Garin J., Jalinot P.
    J. Biol. Chem. 276:45988-45995(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3E.
  10. "Multiple interactions between RNA polymerase I, TIF-IA and TAF(I) subunits regulate preinitiation complex assembly at the ribosomal gene promoter."
    Yuan X., Zhao J., Zentgraf H., Hoffmann-Rohrer U., Grummt I.
    EMBO Rep. 3:1082-1087(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RRN3.
  11. "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.
  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. "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.
  14. "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 SER-2, MASS SPECTROMETRY.
  15. "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.
  16. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-465 AND LYS-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "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.

Entry informationi

Entry nameiEIF3L_HUMAN
AccessioniPrimary (citable) accession number: Q9Y262
Secondary accession number(s): B2RDG6
, B4DYB2, G8JLH4, Q53HQ1, Q53HT4, Q5QTR1, Q5TI15, Q6ICD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1999
Last modified: April 29, 2015
This is version 129 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.