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Q9DCH4 (EIF3F_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 3 subunit F

Short name=eIF3f
Alternative name(s):
Deubiquitinating enzyme eIF3f
EC=3.4.19.12
Eukaryotic translation initiation factor 3 subunit 5
eIF-3-epsilon
eIF3 p47
Gene names
Name:Eif3f
Synonyms:Eif3s5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03005

Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling By similarity. HAMAP-Rule MF_03005

Catalytic activity

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). HAMAP-Rule MF_03005

Subunit structure

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. Ref.4 Ref.5

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03005.

Domain

The MPN domain mediates deubiquitinating activity By similarity. HAMAP-Rule MF_03005

Post-translational modification

Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11 By similarity. HAMAP-Rule MF_03005

Sequence similarities

Belongs to the eIF-3 subunit F family.

Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
Ubl conjugation pathway
   Cellular componentCytoplasm
   Molecular functionHydrolase
Initiation factor
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processformation of translation preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein deubiquitination

Inferred from direct assay PubMed 21124883. Source: FlyBase

regulation of translational initiation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

translational initiation

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componenteukaryotic 43S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic 48S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic translation initiation factor 3 complex

Inferred from direct assay Ref.5. Source: UniProtKB

eukaryotic translation initiation factor 3 complex, eIF3m

Inferred from direct assay PubMed 24003236. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction Ref.4. Source: IntAct

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

translation initiation factor binding

Inferred from direct assay PubMed 24003236. Source: MGI

ubiquitin-specific protease activity

Inferred from direct assay PubMed 21124883. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MtorQ9JLN95EBI-1634316,EBI-1571628

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 361360Eukaryotic translation initiation factor 3 subunit F HAMAP-Rule MF_03005
PRO_0000213965

Regions

Domain91 – 200110MPN

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue521Phosphoserine; by CDK11; in vitro By similarity
Modified residue2421N6-acetyllysine By similarity
Modified residue2621Phosphoserine By similarity

Experimental info

Sequence conflict1981A → S in BAB22352. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9DCH4 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: D0BE3309F9141E40

FASTA36137,984
        10         20         30         40         50         60 
MASPAVPANV PPATAAAAPA PVVTAAPASA PTPSTPAPTP AATPAASPAP VSSDPAVAAP 

        70         80         90        100        110        120 
AAPGQTPASA PAPAQTPAPS QPGPALPGPF PGGRVVRLHP VILASIVDSY ERRNEGAARV 

       130        140        150        160        170        180 
IGTLLGTVDK HSVEVTNCFS VPHNESEDEV AVDMEFAKNM YELHKKVSPN ELILGWYATG 

       190        200        210        220        230        240 
HDITEHSVLI HEYYSREAPN PIHLTVDTGL QHGRMSIKAY VSTLMGVPGR TMGVMFTPLT 

       250        260        270        280        290        300 
VKYAYYDTER IGVDLIMKTC FSPNRVIGLS SDLQQVGGAS ARIQDALSTV LQYAEDVLSG 

       310        320        330        340        350        360 
KVSADNTVGR FLMSLVNQVP KIVPDDFETM LNSNINDLLM VTYLANLTQS QIALNEKLVN 


L 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002778 mRNA. Translation: BAB22352.1.
CH466531 Genomic DNA. Translation: EDL16920.1.
BC083190 mRNA. Translation: AAH83190.1.
CCDSCCDS21731.1.
RefSeqNP_079620.2. NM_025344.2.
UniGeneMm.182962.

3D structure databases

ProteinModelPortalQ9DCH4.
SMRQ9DCH4. Positions 94-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211203. 2 interactions.
DIPDIP-42766N.
IntActQ9DCH4. 8 interactions.
MINTMINT-1899046.
STRING10090.ENSMUSP00000033342.

Protein family/group databases

MEROPSM67.974.

PTM databases

PhosphoSiteQ9DCH4.

Proteomic databases

MaxQBQ9DCH4.
PaxDbQ9DCH4.
PRIDEQ9DCH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033342; ENSMUSP00000033342; ENSMUSG00000031029.
GeneID66085.
KEGGmmu:66085.
UCSCuc009jdc.2. mouse.

Organism-specific databases

CTD8665.
MGIMGI:1913335. Eif3f.

Phylogenomic databases

eggNOGCOG1310.
GeneTreeENSGT00530000063075.
HOGENOMHOG000241154.
HOVERGENHBG107843.
InParanoidQ5XJV3.
KOK03249.
OMAHPVVLFQ.
OrthoDBEOG77T152.
TreeFamTF101517.

Gene expression databases

ArrayExpressQ9DCH4.
BgeeQ9DCH4.
GenevestigatorQ9DCH4.

Family and domain databases

HAMAPMF_03005. eIF3f.
InterProIPR027531. eIF3f.
IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3F. mouse.
NextBio320584.
PROQ9DCH4.
SOURCESearch...

Entry information

Entry nameEIF3F_MOUSE
AccessionPrimary (citable) accession number: Q9DCH4
Secondary accession number(s): Q5XJV3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries