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Q7L2H7

- EIF3M_HUMAN

UniProt

Q7L2H7 - EIF3M_HUMAN

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Protein

Eukaryotic translation initiation factor 3 subunit M

Gene

EIF3M

Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).2 PublicationsUniRule annotation

GO - Molecular functioni

  1. translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cytoplasmic translational initiation Source: RefGenome
  2. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  3. regulation of translational initiation Source: UniProtKB-HAMAP
  4. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:24460. EIF3M.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  2. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  3. eukaryotic translation initiation factor 3 complex Source: UniProtKB
  4. eukaryotic translation initiation factor 3 complex, eIF3m Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi350 – 3501L → P: Reduces HSV binding and entry. 1 Publication
Mutagenesisi354 – 3541L → P: Reduces HSV binding and entry. 1 Publication
Mutagenesisi361 – 3611L → P: Reduces HSV binding and entry. 1 Publication
Mutagenesisi364 – 3641V → P: Reduces HSV binding and entry. 1 Publication

Organism-specific databases

PharmGKBiPA162384944.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 PublicationsUniRule annotation
Chaini2 – 374373Eukaryotic translation initiation factor 3 subunit MPRO_0000308195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine5 PublicationsUniRule annotation
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei254 – 2541N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7L2H7.
PaxDbiQ7L2H7.
PeptideAtlasiQ7L2H7.
PRIDEiQ7L2H7.

PTM databases

PhosphoSiteiQ7L2H7.

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Inductioni

By glucose deprivation in neuroblastoma cells.1 Publication

Gene expression databases

BgeeiQ7L2H7.
CleanExiHS_EIF3M.
ExpressionAtlasiQ7L2H7. baseline and differential.
GenevestigatoriQ7L2H7.

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-3.5 PublicationsUniRule annotation

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115743. 27 interactions.
DIPiDIP-31256N.
IntActiQ7L2H7. 12 interactions.
MINTiMINT-4915331.
STRINGi9606.ENSP00000319910.

Structurei

3D structure databases

ProteinModelPortaliQ7L2H7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni344 – 37431Interaction with HSV-1 and HSV-2Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG253821.
GeneTreeiENSGT00390000004456.
HOGENOMiHOG000112351.
HOVERGENiHBG107844.
InParanoidiQ7L2H7.
KOiK15030.
OMAiAQIIEVC.
PhylomeDBiQ7L2H7.
TreeFamiTF106148.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03012. eIF3m.
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]
SUPFAMiSSF48371. 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. Align

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 AAK07542.1 differs from that shown. Reason: Frameshift at position 371.
The sequence AAK07542.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641M → V in AAC17108. 1 PublicationCurated
Sequence conflicti121 – 1211Y → C in ABD14422. (PubMed:17719568)Curated
Sequence conflicti129 – 1313KVA → EVV in AAC17108. 1 PublicationCurated
Sequence conflicti173 – 1731V → A in AAC17108. 1 PublicationCurated
Sequence conflicti210 – 2112RA → EP in AAC17108. 1 PublicationCurated
Sequence conflicti287 – 2871V → I in AAC17108. 1 PublicationCurated
Sequence conflicti297 – 2971M → V in BAD96284. 1 PublicationCurated

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371G → R.
Corresponds to variant rs11557143 [ dbSNP | Ensembl ].
VAR_036752
Natural varianti80 – 801E → G in a breast cancer sample; somatic mutation. 1 Publication
VAR_036753
Natural varianti346 – 3461Q → R.1 Publication
Corresponds to variant rs1802363 [ dbSNP | Ensembl ].
VAR_036754

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei13 – 144132Missing in isoform 2. 1 PublicationVSP_056911Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS7880.1.
RefSeqiNP_006351.2. NM_006360.4.
UniGeneiHs.502244.

Genome annotation databases

EnsembliENST00000531120; ENSP00000436049; ENSG00000149100.
GeneIDi10480.
KEGGihsa:10480.
UCSCiuc001mtu.4. human.

Polymorphism databases

DMDMi74754296.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS7880.1.
RefSeqi NP_006351.2. NM_006360.4.
UniGenei Hs.502244.

3D structure databases

ProteinModelPortali Q7L2H7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115743. 27 interactions.
DIPi DIP-31256N.
IntActi Q7L2H7. 12 interactions.
MINTi MINT-4915331.
STRINGi 9606.ENSP00000319910.

PTM databases

PhosphoSitei Q7L2H7.

Polymorphism databases

DMDMi 74754296.

Proteomic databases

MaxQBi Q7L2H7.
PaxDbi Q7L2H7.
PeptideAtlasi Q7L2H7.
PRIDEi Q7L2H7.

Protocols and materials databases

DNASUi 10480.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000531120 ; ENSP00000436049 ; ENSG00000149100 .
GeneIDi 10480.
KEGGi hsa:10480.
UCSCi uc001mtu.4. human.

Organism-specific databases

CTDi 10480.
GeneCardsi GC11P032564.
HGNCi HGNC:24460. EIF3M.
HPAi HPA031063.
MIMi 609641. gene.
neXtProti NX_Q7L2H7.
PharmGKBi PA162384944.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253821.
GeneTreei ENSGT00390000004456.
HOGENOMi HOG000112351.
HOVERGENi HBG107844.
InParanoidi Q7L2H7.
KOi K15030.
OMAi AQIIEVC.
PhylomeDBi Q7L2H7.
TreeFami TF106148.

Miscellaneous databases

ChiTaRSi EIF3M. human.
GeneWikii EIF3M.
GenomeRNAii 10480.
NextBioi 39758.
PROi Q7L2H7.
SOURCEi Search...

Gene expression databases

Bgeei Q7L2H7.
CleanExi HS_EIF3M.
ExpressionAtlasi Q7L2H7. baseline and differential.
Genevestigatori Q7L2H7.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
HAMAPi MF_03012. eIF3m.
InterProi IPR016024. ARM-type_fold.
IPR027528. eIF3m.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF01399. PCI. 1 hit.
[Graphical view ]
SMARTi SM00088. PINT. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A new class of receptor for herpes simplex virus has heptad repeat motifs that are common to membrane fusion proteins."
    Perez A., Li Q.-X., Perez-Romero P., DeLassus G., Lopez S.R., Sutter S., McLaren N., Fuller A.O.
    J. Virol. 79:7419-7430(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Fetal lung.
  2. "A novel gene from human dendritic cell."
    Zhao Z., Huang X., Li N., Zhu X., Cao X.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-346.
    Tissue: Dendritic cell.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Synovium, Thalamus and Trachea.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Coronary arterial endothelium.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Muscle and Uterus.
  9. Cited for: PROTEIN SEQUENCE OF 2-19; 103-115; 184-201; 261-276 AND 279-290, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma and Lung carcinoma.
  10. "Subtractive hybridisation screen identifies genes regulated by glucose deprivation in human neuroblastoma cells."
    Kobayashi K., Xin Y., Ymer S.I., Werther G.A., Russo V.C.
    Brain Res. 1170:129-139(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-139 (ISOFORM 1), INDUCTION.
  11. "Human acute promyelocytic leukemia cell line NB4's apoptosis/differentiation related genes."
    Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-374 (ISOFORM 1/2).
  12. "Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP."
    Unbehaun A., Borukhov S.I., Hellen C.U.T., Pestova T.V.
    Genes Dev. 18:3078-3093(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes."
    Zhou C., Arslan F., Wee S., Krishnan S., Ivanov A.R., Oliva A., Leatherwood J., Wolf D.A.
    BMC Biol. 3:14-14(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  14. "The C-terminus of the B5 receptor for herpes simplex virus contains a functional region important for infection."
    Perez-Romero P., Fuller A.O.
    J. Virol. 79:7431-7437(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-350; LEU-354; LEU-361 AND VAL-364.
  15. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association."
    Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.
    RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
  17. "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit."
    LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E.
    J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "CIF-1, a shared subunit of the COP9/signalosome and eukaryotic initiation factor 3 complexes, regulates MEL-26 levels in the Caenorhabditis elegans embryo."
    Luke-Glaser S., Roy M., Larsen B., Le Bihan T., Metalnikov P., Tyers M., Peter M., Pintard L.
    Mol. Cell. Biol. 27:4526-4540(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX.
  19. "Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry."
    Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.
    Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
  20. "Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
    Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V.
    Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY, INTERACTION WITH EIF3B; EIF3F AND EIF3H.
  21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-80.

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: October 29, 2014
This is version 94 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3