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Q7L2H7

- EIF3M_HUMAN

UniProt

Q7L2H7 - EIF3M_HUMAN

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
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    2. 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

    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

    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

    ArrayExpressiQ7L2H7.
    BgeeiQ7L2H7.
    CleanExiHS_EIF3M.
    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. 24 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.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q7L2H7-1 [UniParc]FASTAAdd to Basket

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    MSVPAFIDIS EEDQAAELRA YLKSKGAEIS EENSEGGLHV DLAQIIEACD    50
    VCLKEDDKDV ESVMNSVVSL LLILEPDKQE ALIESLCEKL VKFREGERPS 100
    LRLQLLSNLF HGMDKNTPVR YTVYCSLIKV AASCGAIQYI PTELDQVRKW 150
    ISDWNLTTEK KHTLLRLLYE ALVDCKKSDA ASKVMVELLG SYTEDNASQA 200
    RVDAHRCIVR ALKDPNAFLF DHLLTLKPVK FLEGELIHDL LTIFVSAKLA 250
    SYVKFYQNNK DFIDSLGLLH EQNMAKMRLL TFMGMAVENK EISFDTMQQE 300
    LQIGADDVEA FVIDAVRTKM VYCKIDQTQR KVVVSHSTHR TFGKQQWQQL 350
    YDTLNAWKQN LNKVKNSLLS LSDT 374
    Length:374
    Mass (Da):42,503
    Last modified:July 5, 2005 - v1
    Checksum:i63736CA2B093D794
    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

    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.
    AK222564 mRNA. Translation: BAD96284.1.
    AK292139 mRNA. Translation: BAF84828.1.
    AK312512 mRNA. Translation: BAG35413.1.
    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

    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 .
    AK222564 mRNA. Translation: BAD96284.1 .
    AK292139 mRNA. Translation: BAF84828.1 .
    AK312512 mRNA. Translation: BAG35413.1 .
    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. 24 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.
    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

    ArrayExpressi Q7L2H7.
    Bgeei Q7L2H7.
    CleanExi HS_EIF3M.
    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

    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], 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], 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].
    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].
      Tissue: Synovium and Thalamus.
    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].
      Tissue: Coronary arterial endothelium.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Muscle and Uterus.
    8. 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.
    9. "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, INDUCTION.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. "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].
    15. "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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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].
    21. "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].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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].
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-80.

    Entry informationi

    Entry nameiEIF3M_HUMAN
    AccessioniPrimary (citable) accession number: Q7L2H7
    Secondary accession number(s): A8K7X4
    , O60735, Q2F836, Q53HL6, Q9BXW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 93 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