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Q9Y262

- EIF3L_HUMAN

UniProt

Q9Y262 - EIF3L_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit L

Gene

EIF3L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. 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

    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: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:18138. EIF3L.

    Subcellular locationi

    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. fibrillar center Source: Ensembl
    5. membrane Source: UniProtKB
    6. nucleoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27706.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 PublicationsUniRule annotation
    Chaini2 – 564563Eukaryotic translation initiation factor 3 subunit LPRO_0000084162Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 PublicationsUniRule annotation
    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.UniRule annotation

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti353 – 3531T → I in AAQ13507. 1 PublicationCurated
    Sequence conflicti377 – 3771M → V in BAD96249. 1 PublicationCurated
    Sequence conflicti432 – 4321H → Y in BAD96216. 1 PublicationCurated
    Sequence conflicti434 – 4341N → D in BAD96249. 1 PublicationCurated
    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:
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 124 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