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Protein

Eukaryotic translation initiation factor 3 subunit F

Gene

Eif3f

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.
Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling.By similarity

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

GO - Molecular functioni

  1. translation initiation factor activity Source: UniProtKB-HAMAP
  2. translation initiation factor binding Source: MGI
  3. ubiquitin-specific protease activity Source: FlyBase

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Initiation factor, Protease, Thiol protease

Keywords - Biological processi

Protein biosynthesis, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_236458. Ribosomal scanning and start codon recognition.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_249316. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_256488. Translation initiation complex formation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Protein family/group databases

MEROPSiM67.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit FUniRule annotation
Short name:
eIF3fUniRule annotation
Alternative name(s):
Deubiquitinating enzyme eIF3f (EC:3.4.19.12)
Eukaryotic translation initiation factor 3 subunit 5UniRule annotation
eIF-3-epsilonUniRule annotation
eIF3 p47UniRule annotation
Gene namesi
Name:Eif3f
Synonyms:Eif3s5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1913335. Eif3f.

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. eukaryotic translation initiation factor 3 complex, eIF3m Source: MGI
  5. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 361360Eukaryotic translation initiation factor 3 subunit FPRO_0000213965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineUniRule annotation
Modified residuei52 – 521Phosphoserine; by CDK11; in vitroUniRule annotation
Modified residuei242 – 2421N6-acetyllysineBy similarity
Modified residuei262 – 2621PhosphoserineUniRule annotation

Post-translational modificationi

Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9DCH4.
PaxDbiQ9DCH4.
PRIDEiQ9DCH4.

PTM databases

PhosphoSiteiQ9DCH4.

Expressioni

Gene expression databases

BgeeiQ9DCH4.
ExpressionAtlasiQ9DCH4. baseline and differential.
GenevestigatoriQ9DCH4.

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 RNF139; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner. Interacts with DTX1, the interaction is required for deubiquitinating activity towards NOTCH1 (By similarity).UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
MtorQ9JLN95EBI-1634316,EBI-1571628

Protein-protein interaction databases

BioGridi211203. 3 interactions.
DIPiDIP-42766N.
IntActiQ9DCH4. 8 interactions.
MINTiMINT-1899046.
STRINGi10090.ENSMUSP00000033342.

Structurei

3D structure databases

ProteinModelPortaliQ9DCH4.
SMRiQ9DCH4. Positions 96-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 200110MPNUniRule annotationAdd
BLAST

Domaini

The MPN domain mediates deubiquitinating activity.By similarity

Sequence similaritiesi

Belongs to the eIF-3 subunit F family.UniRule annotation
Contains 1 MPN (JAB/Mov34) domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG1310.
GeneTreeiENSGT00530000063075.
HOGENOMiHOG000241154.
HOVERGENiHBG107843.
InParanoidiQ9DCH4.
KOiK03249.
OMAiVGVMFTP.
OrthoDBiEOG77T152.
TreeFamiTF101517.

Family and domain databases

HAMAPiMF_03005. eIF3f.
InterProiIPR027531. eIF3f.
IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9DCH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPAVPANV PPATAAAAPA PVVTAAPASA PTPSTPAPTP AATPAASPAP
60 70 80 90 100
VSSDPAVAAP AAPGQTPASA PAPAQTPAPS QPGPALPGPF PGGRVVRLHP
110 120 130 140 150
VILASIVDSY ERRNEGAARV IGTLLGTVDK HSVEVTNCFS VPHNESEDEV
160 170 180 190 200
AVDMEFAKNM YELHKKVSPN ELILGWYATG HDITEHSVLI HEYYSREAPN
210 220 230 240 250
PIHLTVDTGL QHGRMSIKAY VSTLMGVPGR TMGVMFTPLT VKYAYYDTER
260 270 280 290 300
IGVDLIMKTC FSPNRVIGLS SDLQQVGGAS ARIQDALSTV LQYAEDVLSG
310 320 330 340 350
KVSADNTVGR FLMSLVNQVP KIVPDDFETM LNSNINDLLM VTYLANLTQS
360
QIALNEKLVN L
Length:361
Mass (Da):37,984
Last modified:July 27, 2011 - v2
Checksum:iD0BE3309F9141E40
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti198 – 1981A → S in BAB22352 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002778 mRNA. Translation: BAB22352.1.
CH466531 Genomic DNA. Translation: EDL16920.1.
BC083190 mRNA. Translation: AAH83190.1.
CCDSiCCDS21731.1.
RefSeqiNP_079620.2. NM_025344.2.
UniGeneiMm.182962.

Genome annotation databases

EnsembliENSMUST00000033342; ENSMUSP00000033342; ENSMUSG00000031029.
GeneIDi66085.
KEGGimmu:66085.
UCSCiuc009jdc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002778 mRNA. Translation: BAB22352.1.
CH466531 Genomic DNA. Translation: EDL16920.1.
BC083190 mRNA. Translation: AAH83190.1.
CCDSiCCDS21731.1.
RefSeqiNP_079620.2. NM_025344.2.
UniGeneiMm.182962.

3D structure databases

ProteinModelPortaliQ9DCH4.
SMRiQ9DCH4. Positions 96-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211203. 3 interactions.
DIPiDIP-42766N.
IntActiQ9DCH4. 8 interactions.
MINTiMINT-1899046.
STRINGi10090.ENSMUSP00000033342.

Protein family/group databases

MEROPSiM67.974.

PTM databases

PhosphoSiteiQ9DCH4.

Proteomic databases

MaxQBiQ9DCH4.
PaxDbiQ9DCH4.
PRIDEiQ9DCH4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033342; ENSMUSP00000033342; ENSMUSG00000031029.
GeneIDi66085.
KEGGimmu:66085.
UCSCiuc009jdc.2. mouse.

Organism-specific databases

CTDi8665.
MGIiMGI:1913335. Eif3f.

Phylogenomic databases

eggNOGiCOG1310.
GeneTreeiENSGT00530000063075.
HOGENOMiHOG000241154.
HOVERGENiHBG107843.
InParanoidiQ9DCH4.
KOiK03249.
OMAiVGVMFTP.
OrthoDBiEOG77T152.
TreeFamiTF101517.

Enzyme and pathway databases

ReactomeiREACT_236458. Ribosomal scanning and start codon recognition.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_249316. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_256488. Translation initiation complex formation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEif3f. mouse.
NextBioi320584.
PROiQ9DCH4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCH4.
ExpressionAtlasiQ9DCH4. baseline and differential.
GenevestigatoriQ9DCH4.

Family and domain databases

HAMAPiMF_03005. eIF3f.
InterProiIPR027531. eIF3f.
IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: C57BL/6J.
    Tissue: Kidney.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: C57BL/6.
    Tissue: Brain.
  4. "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin."
    Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr.
    EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF3B AND MTOR.
  5. "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.

Entry informationi

Entry nameiEIF3F_MOUSE
AccessioniPrimary (citable) accession number: Q9DCH4
Secondary accession number(s): Q5XJV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 98 of the entry and version 2 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. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.