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Protein

Eukaryotic translation initiation factor 3 subunit M

Gene

Eif3m

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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.UniRule annotation

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 MUniRule annotation
Short name:
eIF3mUniRule annotation
Alternative name(s):
PCI domain-containing protein 1
Gene namesi
Name:Eif3m
Synonyms:Pcid1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1351744. Eif3m.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedUniRule annotation
Chaini2 – 374373Eukaryotic translation initiation factor 3 subunit MPRO_0000308196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineUniRule annotationBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei152 – 1521PhosphoserineBy similarity
Modified residuei254 – 2541N6-acetyllysineBy similarity
Modified residuei367 – 3671PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99JX4.
MaxQBiQ99JX4.
PaxDbiQ99JX4.
PeptideAtlasiQ99JX4.
PRIDEiQ99JX4.

PTM databases

iPTMnetiQ99JX4.
PhosphoSiteiQ99JX4.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027170.
ExpressionAtlasiQ99JX4. baseline and differential.
GenevisibleiQ99JX4. 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 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.UniRule annotation

GO - Molecular functioni

  • translation initiation factor binding Source: MGI

Protein-protein interaction databases

BioGridi221017. 3 interactions.
DIPiDIP-59784N.
IntActiQ99JX4. 1 interaction.
MINTiMINT-1869888.
STRINGi10090.ENSMUSP00000028592.

Structurei

3D structure databases

ProteinModelPortaliQ99JX4.
SMRiQ99JX4. Positions 6-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini235 – 336102PCIUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit M family.UniRule annotation
Contains 1 PCI domain.UniRule annotation

Phylogenomic databases

eggNOGiKOG2753. Eukaryota.
ENOG410XNP7. LUCA.
GeneTreeiENSGT00390000004456.
HOGENOMiHOG000112351.
HOVERGENiHBG107844.
InParanoidiQ99JX4.
KOiK15030.
OMAiFHGMDEN.
OrthoDBiEOG091G0H3D.
PhylomeDBiQ99JX4.
TreeFamiTF106148.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03012. eIF3m. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR027528. eIF3m.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q99JX4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVPAFIDIS EEDQAAELRA YLKSKGAELS EENSEGGLHV DLAQIIEACD
60 70 80 90 100
VCLKEDDKDV ESVMNSVVSL LLILEPDKQE ALIESLCEKL VKFREGERPS
110 120 130 140 150
LRLQLLSNLF HGMDKNTPVR YTVYCSLIKV AASCGAIQYI PTELDQVRKW
160 170 180 190 200
ISDWKLTTEK KHTLLRLLYE ALVDCKKSDA ASKVMVELLG SYTEDNASQA
210 220 230 240 250
RVDAHRCIVR ALKDPNAFLF DHLLTLKPVK FLEGELIHDL LTIFVSAKLA
260 270 280 290 300
SYVKFYQNNK DFIDSLGLLH EQNMAKMRLL TFMGMAVENK EISFDTMQQE
310 320 330 340 350
LQIGADDVEA FVIDAVRTKM VYCKIDQTQR KVVVSHSTHR TFGKQQWQQL
360 370
YDTLNAWKQN LNKVKNSLLS LSDT
Length:374
Mass (Da):42,517
Last modified:June 1, 2001 - v1
Checksum:i09845D87E792B783
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291L → I in AAH89568 (PubMed:15489334).Curated
Sequence conflicti141 – 1411P → Q in BAE40042 (PubMed:16141072).Curated
Sequence conflicti155 – 1551K → N in AAH89568 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077480 mRNA. Translation: BAC36821.1.
AK084738 mRNA. Translation: BAC39270.1.
AK146222 mRNA. Translation: BAE26990.1.
AK168066 mRNA. Translation: BAE40042.1.
AL606494 Genomic DNA. Translation: CAM17236.1.
BC005598 mRNA. Translation: AAH05598.1.
BC089568 mRNA. Translation: AAH89568.1.
BC103795 mRNA. Translation: AAI03796.1.
BC116787 mRNA. Translation: AAI16788.1.
BC116789 mRNA. Translation: AAI16790.1.
CCDSiCCDS16495.1.
RefSeqiNP_663355.1. NM_145380.2.
UniGeneiMm.379278.

Genome annotation databases

EnsembliENSMUST00000028592; ENSMUSP00000028592; ENSMUSG00000027170.
GeneIDi98221.
KEGGimmu:98221.
UCSCiuc008lkl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077480 mRNA. Translation: BAC36821.1.
AK084738 mRNA. Translation: BAC39270.1.
AK146222 mRNA. Translation: BAE26990.1.
AK168066 mRNA. Translation: BAE40042.1.
AL606494 Genomic DNA. Translation: CAM17236.1.
BC005598 mRNA. Translation: AAH05598.1.
BC089568 mRNA. Translation: AAH89568.1.
BC103795 mRNA. Translation: AAI03796.1.
BC116787 mRNA. Translation: AAI16788.1.
BC116789 mRNA. Translation: AAI16790.1.
CCDSiCCDS16495.1.
RefSeqiNP_663355.1. NM_145380.2.
UniGeneiMm.379278.

3D structure databases

ProteinModelPortaliQ99JX4.
SMRiQ99JX4. Positions 6-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221017. 3 interactions.
DIPiDIP-59784N.
IntActiQ99JX4. 1 interaction.
MINTiMINT-1869888.
STRINGi10090.ENSMUSP00000028592.

PTM databases

iPTMnetiQ99JX4.
PhosphoSiteiQ99JX4.

Proteomic databases

EPDiQ99JX4.
MaxQBiQ99JX4.
PaxDbiQ99JX4.
PeptideAtlasiQ99JX4.
PRIDEiQ99JX4.

Protocols and materials databases

DNASUi98221.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028592; ENSMUSP00000028592; ENSMUSG00000027170.
GeneIDi98221.
KEGGimmu:98221.
UCSCiuc008lkl.1. mouse.

Organism-specific databases

CTDi10480.
MGIiMGI:1351744. Eif3m.

Phylogenomic databases

eggNOGiKOG2753. Eukaryota.
ENOG410XNP7. LUCA.
GeneTreeiENSGT00390000004456.
HOGENOMiHOG000112351.
HOVERGENiHBG107844.
InParanoidiQ99JX4.
KOiK15030.
OMAiFHGMDEN.
OrthoDBiEOG091G0H3D.
PhylomeDBiQ99JX4.
TreeFamiTF106148.

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

PROiQ99JX4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027170.
ExpressionAtlasiQ99JX4. baseline and differential.
GenevisibleiQ99JX4. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03012. eIF3m. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR027528. eIF3m.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3M_MOUSE
AccessioniPrimary (citable) accession number: Q99JX4
Secondary accession number(s): Q3TI04, Q5EBI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 123 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.