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Entry version 129 (08 May 2019)
Sequence version 2 (27 Jul 2011)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 pre-initiation 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. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.UniRule annotation
Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling.UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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). EC:3.4.19.12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Initiation factor, Protease, Thiol protease
Biological processProtein biosynthesis, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M67.974

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Eif3f
Synonyms:Eif3s5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1913335 Eif3f

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedUniRule annotation
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002139652 – 361Eukaryotic translation initiation factor 3 subunit FAdd BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineUniRule annotationBy similarity1
Modified residuei52Phosphoserine; by CDK11; in vitroUniRule annotationBy similarity1
Modified residuei242N6-acetyllysineBy similarity1
Modified residuei262PhosphoserineUniRule annotationBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9DCH4

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9DCH4

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9DCH4

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9DCH4

PRoteomics IDEntifications database

More...
PRIDEi
Q9DCH4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9DCH4

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9DCH4

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9DCH4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000031029 Expressed in 283 organ(s), highest expression level in urinary bladder urothelium

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9DCH4 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
211203, 6 interactors

Database of interacting proteins

More...
DIPi
DIP-42766N

Protein interaction database and analysis system

More...
IntActi
Q9DCH4, 12 interactors

Molecular INTeraction database

More...
MINTi
Q9DCH4

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000033342

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9DCH4

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini96 – 226MPNPROSITE-ProRule annotationAdd BLAST131

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The MPN domain mediates deubiquitinating activity.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2975 Eukaryota
COG1310 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183073

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000241154

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9DCH4

KEGG Orthology (KO)

More...
KOi
K03249

Identification of Orthologs from Complete Genome Data

More...
OMAi
AVDMEYH

Database of Orthologous Groups

More...
OrthoDBi
1038775at2759

TreeFam database of animal gene trees

More...
TreeFami
TF101517

Family and domain databases

Conserved Domains Database

More...
CDDi
cd08064 MPN_eIF3f, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_03005 eIF3f, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027531 eIF3f
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR024969 Rpn11/EIF3F_C

The PANTHER Classification System

More...
PANTHERi
PTHR10540:SF16 PTHR10540:SF16, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01398 JAB, 1 hit
PF13012 MitMem_reg, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00232 JAB_MPN, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50249 MPN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD0BE3309F9141E40
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti198A → S in BAB22352 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK002778 mRNA Translation: BAB22352.1
CH466531 Genomic DNA Translation: EDL16920.1
BC083190 mRNA Translation: AAH83190.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS21731.1

NCBI Reference Sequences

More...
RefSeqi
NP_079620.2, NM_025344.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000033342; ENSMUSP00000033342; ENSMUSG00000031029

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
66085

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:66085

UCSC genome browser

More...
UCSCi
uc009jdc.2 mouse

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

SMRiQ9DCH4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211203, 6 interactors
DIPiDIP-42766N
IntActiQ9DCH4, 12 interactors
MINTiQ9DCH4
STRINGi10090.ENSMUSP00000033342

Protein family/group databases

MEROPSiM67.974

PTM databases

iPTMnetiQ9DCH4
PhosphoSitePlusiQ9DCH4
SwissPalmiQ9DCH4

Proteomic databases

EPDiQ9DCH4
jPOSTiQ9DCH4
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

Comparative Toxicogenomics Database

More...
CTDi
8665
MGIiMGI:1913335 Eif3f

Phylogenomic databases

eggNOGiKOG2975 Eukaryota
COG1310 LUCA
GeneTreeiENSGT00950000183073
HOGENOMiHOG000241154
InParanoidiQ9DCH4
KOiK03249
OMAiAVDMEYH
OrthoDBi1038775at2759
TreeFamiTF101517

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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Eif3f mouse

Protein Ontology

More...
PROi
PR:Q9DCH4

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000031029 Expressed in 283 organ(s), highest expression level in urinary bladder urothelium
GenevisibleiQ9DCH4 MM

Family and domain databases

CDDicd08064 MPN_eIF3f, 1 hit
HAMAPiMF_03005 eIF3f, 1 hit
InterProiView protein in InterPro
IPR027531 eIF3f
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR024969 Rpn11/EIF3F_C
PANTHERiPTHR10540:SF16 PTHR10540:SF16, 1 hit
PfamiView protein in Pfam
PF01398 JAB, 1 hit
PF13012 MitMem_reg, 1 hit
SMARTiView protein in SMART
SM00232 JAB_MPN, 1 hit
PROSITEiView protein in PROSITE
PS50249 MPN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEIF3F_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9DCH4
Secondary accession number(s): Q5XJV3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: July 27, 2011
Last modified: May 8, 2019
This is version 129 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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