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Q9Y262

- EIF3L_HUMAN

UniProt

Q9Y262 - EIF3L_HUMAN

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Protein
Eukaryotic translation initiation factor 3 subunit L
Gene
EIF3L, EIF3EIP, EIF3S6IP, HSPC021, HSPC025, MSTP005
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. translation initiation factor activity Source: UniProtKB-HAMAP
Complete GO annotation...

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 L
Short name:
eIF3l
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 6-interacting protein
Eukaryotic translation initiation factor 3 subunit E-interacting protein
Gene namesi
Name:EIF3L
Synonyms:EIF3EIP, EIF3S6IP
ORF Names:HSPC021, HSPC025, MSTP005
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:18138. EIF3L.

Subcellular locationi

Cytoplasm By similarity 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. fibrillar center Source: Ensembl
  5. nucleoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27706.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 564563Eukaryotic translation initiation factor 3 subunit LUniRule annotation
PRO_0000084162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei465 – 4651N6-acetyllysine1 Publication
Modified residuei549 – 5491N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y262.
PaxDbiQ9Y262.
PRIDEiQ9Y262.

PTM databases

PhosphoSiteiQ9Y262.

Expressioni

Gene expression databases

ArrayExpressiQ9Y262.
BgeeiQ9Y262.
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 By similarity.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi119516. 50 interactions.
DIPiDIP-31172N.
IntActiQ9Y262. 16 interactions.
MINTiMINT-216779.
STRINGi9606.ENSP00000416892.

Structurei

3D structure databases

ProteinModelPortaliQ9Y262.

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-3 subunit L family.

Phylogenomic databases

eggNOGiNOG251364.
HOVERGENiHBG001289.
InParanoidiQ9Y262.
KOiK15029.
OMAiLCFKHKM.
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. Align

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

MSYPADDYES EAAYDPYAYP SDYDMHTGDP KQDLAYERQY EQQTYQVIPE    50
VIKNFIQYFH KTVSDLIDQK VYELQASRVS SDVIDQKVYE IQDIYENSWT 100
KLTERFFKNT PWPEAEAIAP QVGNDAVFLI LYKELYYRHI YAKVSGGPSL 150
EQRFESYYNY CNLFNYILNA DGPAPLELPN QWLWDIIDEF IYQFQSFSQY 200
RCKTAKKSEE EIDFLRSNPK IWNVHSVLNV LHSLVDKSNI NRQLEVYTSG 250
GDPESVAGEY GRHSLYKMLG YFSLVGLLRL HSLLGDYYQA IKVLENIELN 300
KKSMYSRVPE CQVTTYYYVG FAYLMMRRYQ DAIRVFANIL LYIQRTKSMF 350
QRTTYKYEMI NKQNEQMHAL LAIALTMYPM RIDESIHLQL REKYGDKMLR 400
MQKGDPQVYE ELFSYSCPKF LSPVVPNYDN VHPNYHKEPF LQQLKVFSDE 450
VQQQAQLSTI RSFLKLYTTM PVAKLAGFLD LTEQEFRIQL LVFKHKMKNL 500
VWTSGISALD GEFQSASEVD FYIDKDMIHI ADTKVARRYG DFFIRQIHKF 550
EELNRTLKKM GQRP 564
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.
The sequence CAX14899.1 differs from that shown. Reason: Erroneous initiation.

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.
VSP_045881Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti353 – 3531T → I in AAQ13507. 1 Publication
Sequence conflicti377 – 3771M → V in BAD96249. 1 Publication
Sequence conflicti432 – 4321H → Y in BAD96216. 1 Publication
Sequence conflicti434 – 4341N → D in BAD96249. 1 Publication
Sequence conflicti513 – 5131F → L in BAG63674. 1 Publication
Sequence conflicti528 – 5281I → T in BAG63674. 1 Publication
Sequence conflicti558 – 5581K → R in BAG63674. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000412331; ENSP00000416892; ENSG00000100129. [Q9Y262-1]
GeneIDi51386.
KEGGihsa:51386.
UCSCiuc003auf.3. human. [Q9Y262-1]

Polymorphism databases

DMDMi23396631.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13960.1. [Q9Y262-1 ]
CCDS56230.1. [Q9Y262-2 ]
RefSeqi NP_001229852.1. NM_001242923.1. [Q9Y262-2 ]
NP_057175.1. NM_016091.3. [Q9Y262-1 ]
UniGenei Hs.446852.

3D structure databases

ProteinModelPortali Q9Y262.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119516. 50 interactions.
DIPi DIP-31172N.
IntActi Q9Y262. 16 interactions.
MINTi MINT-216779.
STRINGi 9606.ENSP00000416892.

PTM databases

PhosphoSitei Q9Y262.

Polymorphism databases

DMDMi 23396631.

Proteomic databases

MaxQBi Q9Y262.
PaxDbi Q9Y262.
PRIDEi Q9Y262.

Protocols and materials databases

DNASUi 51386.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381683 ; ENSP00000371099 ; ENSG00000100129 . [Q9Y262-2 ]
ENST00000412331 ; ENSP00000416892 ; ENSG00000100129 . [Q9Y262-1 ]
GeneIDi 51386.
KEGGi hsa:51386.
UCSCi uc003auf.3. human. [Q9Y262-1 ]

Organism-specific databases

CTDi 51386.
GeneCardsi GC22P038244.
HGNCi HGNC:18138. EIF3L.
HPAi HPA003028.
neXtProti NX_Q9Y262.
PharmGKBi PA27706.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG251364.
HOVERGENi HBG001289.
InParanoidi Q9Y262.
KOi K15029.
OMAi LCFKHKM.
OrthoDBi EOG7XDBFF.
PhylomeDBi Q9Y262.
TreeFami TF101523.

Miscellaneous databases

ChiTaRSi EIF3L. human.
GeneWikii EIF3EIP.
GenomeRNAii 51386.
NextBioi 54905.
PROi Q9Y262.

Gene expression databases

ArrayExpressi Q9Y262.
Bgeei Q9Y262.
Genevestigatori Q9Y262.

Family and domain databases

HAMAPi MF_03011. eIF3l.
InterProi IPR019382. eIF3l.
[Graphical view ]
PANTHERi PTHR13242. PTHR13242. 1 hit.
Pfami PF10255. Paf67. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
  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].
  20. "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: September 3, 2014
This is version 123 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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