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Protein

Eukaryotic translation initiation factor 3 subunit L

Gene

Eif3l

Organism
Mus musculus (Mouse)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit LUniRule annotation
Short name:
eIF3lUniRule annotation
Alternative name(s):
66 kDa tyrosine-rich heat shock protein
67 kDa polymerase-associated factor
Eukaryotic translation initiation factor 3 subunit 6-interacting proteinUniRule annotation
Eukaryotic translation initiation factor 3 subunit E-interacting proteinUniRule annotation
HSP-66Y
PAF67
Gene namesi
Name:Eif3l
Synonyms:Eif3eip, Eif3s6ip, Paf67
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2386251. Eif3l.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic translation initiation factor 3 complex Source: UniProtKB
  • fibrillar center Source: MGI
  • membrane Source: MGI
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedUniRule annotation
Chaini2 – 564563Eukaryotic translation initiation factor 3 subunit LPRO_0000297498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineUniRule annotationBy similarity
Modified residuei465 – 4651N6-acetyllysineCombined sources
Modified residuei549 – 5491N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8QZY1.
MaxQBiQ8QZY1.
PaxDbiQ8QZY1.
PRIDEiQ8QZY1.

PTM databases

iPTMnetiQ8QZY1.
PhosphoSiteiQ8QZY1.
SwissPalmiQ8QZY1.

Expressioni

Gene expression databases

BgeeiQ8QZY1.
GenevisibleiQ8QZY1. MM.

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 may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead 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 annotation2 Publications

Protein-protein interaction databases

BioGridi230176. 4 interactions.
IntActiQ8QZY1. 3 interactions.
MINTiMINT-249281.
STRINGi10090.ENSMUSP00000038839.

Structurei

3D structure databases

ProteinModelPortaliQ8QZY1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3677. Eukaryota.
ENOG410XPJT. LUCA.
GeneTreeiENSGT00390000000411.
HOGENOMiHOG000265377.
HOVERGENiHBG001289.
InParanoidiQ8QZY1.
KOiK15029.
OMAiDVYENSW.
OrthoDBiEOG7XDBFF.
PhylomeDBiQ8QZY1.
TreeFamiTF101523.

Family and domain databases

HAMAPiMF_03011. eIF3l.
InterProiIPR019382. eIF3l.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13242. PTHR13242. 2 hits.
PfamiPF10255. Paf67. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q8QZY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYPADDYES EAAYDPYAYP GDYDMHTGDP 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
RCKTAKKSEG EMDFLRSNPK VWNVHSVLNV 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 ELFSYACPKF 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):66,613
Last modified:June 1, 2002 - v1
Checksum:i914324CB5046763D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491S → P in BAE39691 (PubMed:16141072).Curated
Sequence conflicti215 – 2151L → F in CAC84554 (Ref. 1) Curated
Sequence conflicti253 – 2531P → Q in BAE40238 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ310346 mRNA. Translation: CAC84554.1.
AB066095 Genomic DNA. Translation: BAB85122.1.
AK032936 mRNA. Translation: BAC28090.1.
AK075584 mRNA. Translation: BAC35837.1.
AK150895 mRNA. Translation: BAE29941.1.
AK151175 mRNA. Translation: BAE30177.1.
AK167640 mRNA. Translation: BAE39691.1.
AK168009 mRNA. Translation: BAE39996.1.
AK168295 mRNA. Translation: BAE40238.1.
BC024463 mRNA. Translation: AAH24463.1.
CCDSiCCDS27632.1.
RefSeqiNP_660121.2. NM_145139.2.
UniGeneiMm.206404.

Genome annotation databases

EnsembliENSMUST00000040518; ENSMUSP00000038839; ENSMUSG00000033047.
GeneIDi223691.
KEGGimmu:223691.
UCSCiuc007wsk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ310346 mRNA. Translation: CAC84554.1.
AB066095 Genomic DNA. Translation: BAB85122.1.
AK032936 mRNA. Translation: BAC28090.1.
AK075584 mRNA. Translation: BAC35837.1.
AK150895 mRNA. Translation: BAE29941.1.
AK151175 mRNA. Translation: BAE30177.1.
AK167640 mRNA. Translation: BAE39691.1.
AK168009 mRNA. Translation: BAE39996.1.
AK168295 mRNA. Translation: BAE40238.1.
BC024463 mRNA. Translation: AAH24463.1.
CCDSiCCDS27632.1.
RefSeqiNP_660121.2. NM_145139.2.
UniGeneiMm.206404.

3D structure databases

ProteinModelPortaliQ8QZY1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230176. 4 interactions.
IntActiQ8QZY1. 3 interactions.
MINTiMINT-249281.
STRINGi10090.ENSMUSP00000038839.

PTM databases

iPTMnetiQ8QZY1.
PhosphoSiteiQ8QZY1.
SwissPalmiQ8QZY1.

Proteomic databases

EPDiQ8QZY1.
MaxQBiQ8QZY1.
PaxDbiQ8QZY1.
PRIDEiQ8QZY1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040518; ENSMUSP00000038839; ENSMUSG00000033047.
GeneIDi223691.
KEGGimmu:223691.
UCSCiuc007wsk.1. mouse.

Organism-specific databases

CTDi51386.
MGIiMGI:2386251. Eif3l.

Phylogenomic databases

eggNOGiKOG3677. Eukaryota.
ENOG410XPJT. LUCA.
GeneTreeiENSGT00390000000411.
HOGENOMiHOG000265377.
HOVERGENiHBG001289.
InParanoidiQ8QZY1.
KOiK15029.
OMAiDVYENSW.
OrthoDBiEOG7XDBFF.
PhylomeDBiQ8QZY1.
TreeFamiTF101523.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEif3l. mouse.
PROiQ8QZY1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8QZY1.
GenevisibleiQ8QZY1. MM.

Family and domain databases

HAMAPiMF_03011. eIF3l.
InterProiIPR019382. eIF3l.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13242. PTHR13242. 2 hits.
PfamiPF10255. Paf67. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterisation of PAF67, a novel protein that is associated with RNA polymerase I."
    Seither P., Iben S., Thiry M., Grummt I.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A novel tyrosine-rich heat shock protein (HSP-66Y): molecular cloning and characterization."
    Muramatsu H., Salama R., Zou K., Ikematsu S., Fan Q., Sakuma S., Muramatsu T.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ, C57BL/6J and DBA/2.
    Tissue: Bone marrow, Kidney, Liver and Wolffian duct.
  4. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  5. "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.
  6. "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, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiEIF3L_MOUSE
AccessioniPrimary (citable) accession number: Q8QZY1
Secondary accession number(s): Q3THF8, Q3TJ04, Q91YE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.