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Protein

Eukaryotic translation initiation factor 3 subunit M

Gene

EIF3M

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionInitiation factor
Biological processProtein 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

EuPathDBiHostDB:ENSG00000149100.12
HGNCiHGNC:24460 EIF3M
MIMi609641 gene
neXtProtiNX_Q7L2H7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi115743, 49 interactors
CORUMiQ7L2H7
DIPiDIP-31256N
IntActiQ7L2H7, 28 interactors
MINTiQ7L2H7
STRINGi9606.ENSP00000436049

Structurei

Secondary structure

1374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi189 – 196Combined sources8
Helixi201 – 203Combined sources3
Helixi204 – 213Combined sources10
Helixi221 – 224Combined sources4
Helixi227 – 230Combined sources4
Helixi235 – 245Combined sources11
Helixi249 – 255Combined sources7
Helixi256 – 258Combined sources3
Helixi261 – 267Combined sources7
Helixi269 – 288Combined sources20
Beta strandi290 – 293Combined sources4
Helixi294 – 301Combined sources8
Helixi305 – 313Combined sources9
Helixi315 – 320Combined sources6
Beta strandi324 – 326Combined sources3
Turni327 – 330Combined sources4
Beta strandi331 – 333Combined sources3

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[»]
6FECelectron microscopy6.3081-374[»]
ProteinModelPortaliQ7L2H7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini180 – 339PCIPROSITE-ProRule annotationAdd BLAST160

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

Phylogenomic databases

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

Family and domain databases

HAMAPiMF_03012 eIF3m, 1 hit
InterProiView protein in InterPro
IPR016024 ARM-type_fold
IPR027528 eIF3m
IPR000717 PCI_dom
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF01399 PCI, 1 hit
SMARTiView protein in SMART
SM00088 PINT, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50250 PCI, 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 dbSNP:rs11557143Ensembl.1
Natural variantiVAR_03675380E → G in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_036754346Q → R1 PublicationCorresponds to variant dbSNP:rs1802363Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiEIF3M_HUMAN
AccessioniPrimary (citable) accession number: Q7L2H7
Secondary accession number(s): A8K7X4
, B4E2Q4, O60735, Q2F836, Q53HL6, Q9BXW1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 5, 2005
Last modified: May 23, 2018
This is version 129 of the entry and version 1 of the sequence. See 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

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