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Protein

Eukaryotic translation initiation factor 3 subunit M

Gene

EIF3M

Organism
Homo sapiens (Human)
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 (PubMed:17403899, PubMed:25849773, PubMed:27462815). 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 (PubMed:17403899). 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 (PubMed:25849773).UniRule annotation3 Publications
(Microbial infection) May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-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):
Fetal lung protein B5
Short name:
hFL-B5
PCI domain-containing protein 1
Gene namesi
Name:EIF3MUniRule annotation
Synonyms:HFLB5, PCID1
ORF Names:GA17, PNAS-125
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:24460. EIF3M.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi350L → P: Reduces HSV binding and entry. 1 Publication1
Mutagenesisi354L → P: Reduces HSV binding and entry. 1 Publication1
Mutagenesisi361L → P: Reduces HSV binding and entry. 1 Publication1
Mutagenesisi364V → P: Reduces HSV binding and entry. 1 Publication1

Organism-specific databases

DisGeNETi10480.
OpenTargetsiENSG00000149100.
PharmGKBiPA162384944.

Polymorphism and mutation databases

BioMutaiEIF3M.
DMDMi74754296.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotationCombined sources2 Publications
ChainiPRO_00003081952 – 374Eukaryotic translation initiation factor 3 subunit MAdd BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineUniRule annotationCombined sources2 Publications1
Modified residuei2PhosphoserineCombined sources1
Modified residuei152PhosphoserineCombined sources1
Modified residuei254N6-acetyllysineCombined sources1
Modified residuei367PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ7L2H7.
MaxQBiQ7L2H7.
PaxDbiQ7L2H7.
PeptideAtlasiQ7L2H7.
PRIDEiQ7L2H7.

PTM databases

iPTMnetiQ7L2H7.
PhosphoSitePlusiQ7L2H7.
SwissPalmiQ7L2H7.

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Inductioni

By glucose deprivation in neuroblastoma cells.1 Publication

Gene expression databases

BgeeiENSG00000149100.
CleanExiHS_EIF3M.
ExpressionAtlasiQ7L2H7. baseline and differential.
GenevisibleiQ7L2H7. HS.

Organism-specific databases

HPAiHPA031063.

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 annotation5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3FO003036EBI-353901,EBI-711990
ORFQ9Q2G42EBI-353901,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi115743. 42 interactors.
DIPiDIP-31256N.
IntActiQ7L2H7. 18 interactors.
MINTiMINT-4915331.
STRINGi9606.ENSP00000436049.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-M1-335[»]
3J8Celectron microscopy-M1-335[»]
ProteinModelPortaliQ7L2H7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini235 – 336PCIUniRule annotationAdd BLAST102

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni344 – 374Interaction with HSV-1 and HSV-2Add BLAST31

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.
InParanoidiQ7L2H7.
KOiK15030.
OMAiFHGMDEN.
OrthoDBiEOG091G0H3D.
PhylomeDBiQ7L2H7.
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.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7L2H7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSVPAFIDIS EEDQAAELRA YLKSKGAEIS 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
ISDWNLTTEK 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):42,503
Last modified:July 5, 2005 - v1
Checksum:i63736CA2B093D794
GO
Isoform 2 (identifier: Q7L2H7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     13-144: Missing.

Note: No experimental confirmation available.
Show »
Length:242
Mass (Da):27,865
Checksum:i4B68135F65422425
GO

Sequence cautioni

The sequence AAK07542 differs from that shown. Reason: Frameshift at position 371.Curated
The sequence AAK07542 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64M → V in AAC17108 (Ref. 2) Curated1
Sequence conflicti121Y → C in ABD14422 (PubMed:17719568).Curated1
Sequence conflicti129 – 131KVA → EVV in AAC17108 (Ref. 2) Curated3
Sequence conflicti173V → A in AAC17108 (Ref. 2) Curated1
Sequence conflicti210 – 211RA → EP in AAC17108 (Ref. 2) Curated2
Sequence conflicti287V → I in AAC17108 (Ref. 2) Curated1
Sequence conflicti297M → V in BAD96284 (Ref. 5) Curated1

Mass spectrometryi

Molecular mass is 42413.8 Da from positions 1 - 374. 1 Publication
Molecular mass is 42414.7±0.2 Da from positions 1 - 374. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03675237G → R.Corresponds to variant rs11557143dbSNPEnsembl.1
Natural variantiVAR_03675380E → G in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_036754346Q → R.1 PublicationCorresponds to variant rs1802363dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05691113 – 144Missing in isoform 2. 1 PublicationAdd BLAST132

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY769947 mRNA. Translation: AAX12524.1.
AF064603 mRNA. Translation: AAC17108.1.
CR450300 mRNA. Translation: CAG29296.1.
AK292139 mRNA. Translation: BAF84828.1.
AK304378 mRNA. Translation: BAG65216.1.
AK312512 mRNA. Translation: BAG35413.1.
AK222564 mRNA. Translation: BAD96284.1.
AL078477 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68217.1.
BC019103 mRNA. Translation: AAH19103.1.
BC051292 mRNA. Translation: AAH51292.1.
DQ185042 mRNA. Translation: ABD14422.1.
AF277183 mRNA. Translation: AAK07542.1. Sequence problems.
CCDSiCCDS76392.1. [Q7L2H7-2]
CCDS7880.1. [Q7L2H7-1]
RefSeqiNP_001294858.1. NM_001307929.1. [Q7L2H7-2]
NP_006351.2. NM_006360.5. [Q7L2H7-1]
UniGeneiHs.502244.

Genome annotation databases

EnsembliENST00000524896; ENSP00000436787; ENSG00000149100. [Q7L2H7-2]
ENST00000531120; ENSP00000436049; ENSG00000149100. [Q7L2H7-1]
GeneIDi10480.
KEGGihsa:10480.
UCSCiuc001mtu.5. human. [Q7L2H7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY769947 mRNA. Translation: AAX12524.1.
AF064603 mRNA. Translation: AAC17108.1.
CR450300 mRNA. Translation: CAG29296.1.
AK292139 mRNA. Translation: BAF84828.1.
AK304378 mRNA. Translation: BAG65216.1.
AK312512 mRNA. Translation: BAG35413.1.
AK222564 mRNA. Translation: BAD96284.1.
AL078477 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68217.1.
BC019103 mRNA. Translation: AAH19103.1.
BC051292 mRNA. Translation: AAH51292.1.
DQ185042 mRNA. Translation: ABD14422.1.
AF277183 mRNA. Translation: AAK07542.1. Sequence problems.
CCDSiCCDS76392.1. [Q7L2H7-2]
CCDS7880.1. [Q7L2H7-1]
RefSeqiNP_001294858.1. NM_001307929.1. [Q7L2H7-2]
NP_006351.2. NM_006360.5. [Q7L2H7-1]
UniGeneiHs.502244.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-M1-335[»]
3J8Celectron microscopy-M1-335[»]
ProteinModelPortaliQ7L2H7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115743. 42 interactors.
DIPiDIP-31256N.
IntActiQ7L2H7. 18 interactors.
MINTiMINT-4915331.
STRINGi9606.ENSP00000436049.

PTM databases

iPTMnetiQ7L2H7.
PhosphoSitePlusiQ7L2H7.
SwissPalmiQ7L2H7.

Polymorphism and mutation databases

BioMutaiEIF3M.
DMDMi74754296.

Proteomic databases

EPDiQ7L2H7.
MaxQBiQ7L2H7.
PaxDbiQ7L2H7.
PeptideAtlasiQ7L2H7.
PRIDEiQ7L2H7.

Protocols and materials databases

DNASUi10480.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000524896; ENSP00000436787; ENSG00000149100. [Q7L2H7-2]
ENST00000531120; ENSP00000436049; ENSG00000149100. [Q7L2H7-1]
GeneIDi10480.
KEGGihsa:10480.
UCSCiuc001mtu.5. human. [Q7L2H7-1]

Organism-specific databases

CTDi10480.
DisGeNETi10480.
GeneCardsiEIF3M.
HGNCiHGNC:24460. EIF3M.
HPAiHPA031063.
MIMi609641. gene.
neXtProtiNX_Q7L2H7.
OpenTargetsiENSG00000149100.
PharmGKBiPA162384944.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2753. Eukaryota.
ENOG410XNP7. LUCA.
GeneTreeiENSGT00390000004456.
HOGENOMiHOG000112351.
HOVERGENiHBG107844.
InParanoidiQ7L2H7.
KOiK15030.
OMAiFHGMDEN.
OrthoDBiEOG091G0H3D.
PhylomeDBiQ7L2H7.
TreeFamiTF106148.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiEIF3M. human.
GeneWikiiEIF3M.
GenomeRNAii10480.
PROiQ7L2H7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149100.
CleanExiHS_EIF3M.
ExpressionAtlasiQ7L2H7. baseline and differential.
GenevisibleiQ7L2H7. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q7L2H7
Secondary accession number(s): A8K7X4
, B4E2Q4, O60735, Q2F836, Q53HL6, Q9BXW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 5, 2005
Last modified: November 30, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.