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P55884

- EIF3B_HUMAN

UniProt

P55884 - EIF3B_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit B

Gene

EIF3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (16 Dec 2008)
      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 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.1 Publication

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. protein complex scaffold Source: UniProtKB
    4. translation initiation factor activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. formation of translation preinitiation complex Source: UniProtKB-HAMAP
    3. gene expression Source: Reactome
    4. regulation of translational initiation Source: UniProtKB
    5. translation Source: Reactome
    6. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 3 subunit BUniRule annotation
    Short name:
    eIF3bUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 9UniRule annotation
    Prt1 homolog
    Short name:
    hPrt1
    eIF-3-etaUniRule annotation
    eIF3 p110UniRule annotation
    eIF3 p116
    Gene namesi
    Name:EIF3BUniRule annotation
    Synonyms:EIF3S9UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:3280. EIF3B.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
    3. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
    4. eukaryotic translation initiation factor 3 complex Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162384603.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 814814Eukaryotic translation initiation factor 3 subunit BPRO_0000123531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 PublicationsUniRule annotation
    Modified residuei78 – 781Phosphoserine1 PublicationUniRule annotation
    Modified residuei81 – 811Phosphoserine1 PublicationUniRule annotation
    Modified residuei83 – 831Phosphoserine2 PublicationsUniRule annotation
    Modified residuei85 – 851Phosphoserine2 PublicationsUniRule annotation
    Modified residuei119 – 1191Phosphoserine1 PublicationUniRule annotation
    Modified residuei125 – 1251Phosphoserine2 PublicationsUniRule annotation
    Modified residuei152 – 1521Phosphoserine4 PublicationsUniRule annotation
    Modified residuei154 – 1541Phosphoserine5 PublicationsUniRule annotation
    Modified residuei164 – 1641Phosphoserine4 PublicationsUniRule annotation
    Modified residuei209 – 2091N6-acetyllysine1 Publication
    Modified residuei239 – 2391Phosphoserine2 PublicationsUniRule annotation
    Modified residuei288 – 2881N6-acetyllysine1 Publication
    Modified residuei364 – 3641N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated. Phosphorylation is enhanced upon serum stimulation.6 PublicationsUniRule annotation

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP55884.
    PaxDbiP55884.
    PRIDEiP55884.

    PTM databases

    PhosphoSiteiP55884.

    Expressioni

    Gene expression databases

    ArrayExpressiP55884.
    BgeeiP55884.
    CleanExiHS_EIF3B.
    GenevestigatoriP55884.

    Organism-specific databases

    HPAiCAB017562.
    HPA048983.

    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. Also interacts with UPF2 and HNRPD.11 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX3XO005715EBI-366696,EBI-353779
    EIF3AQ141526EBI-366696,EBI-366617
    EIF3FO003033EBI-366696,EBI-711990
    EIF3GO758214EBI-366696,EBI-366632
    EIF3IQ133474EBI-366696,EBI-354047
    EIF3JO758225EBI-366696,EBI-366647

    Protein-protein interaction databases

    BioGridi114211. 54 interactions.
    DIPiDIP-31113N.
    IntActiP55884. 38 interactions.
    MINTiMINT-4999648.
    STRINGi9606.ENSP00000354125.

    Structurei

    Secondary structure

    1
    814
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi186 – 1916
    Turni197 – 1993
    Helixi200 – 21213
    Beta strandi217 – 2215
    Beta strandi232 – 2398
    Helixi240 – 2478
    Beta strandi250 – 2523
    Beta strandi256 – 2594
    Beta strandi260 – 2645

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KRBNMR-A184-264[»]
    2NLWNMR-A170-274[»]
    ProteinModelPortaliP55884.
    SMRiP55884. Positions 170-274, 342-708.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55884.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini185 – 26884RRMUniRule annotationAdd
    BLAST
    Repeati332 – 37039WD 1Add
    BLAST
    Repeati372 – 41746WD 2Add
    BLAST
    Repeati421 – 45939WD 3Add
    BLAST
    Repeati560 – 60142WD 4Add
    BLAST
    Repeati649 – 69446WD 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni124 – 413290Sufficient for interaction with EIF3EAdd
    BLAST
    Regioni170 – 274105Sufficient for interaction with EIF3JAdd
    BLAST

    Domaini

    The RRM domain mediates interaction with EIF3J.

    Sequence similaritiesi

    Belongs to the eIF-3 subunit B family.UniRule annotation
    Contains 1 RRM (RNA recognition motif) domain.UniRule annotation
    Contains 5 WD repeats.UniRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG5354.
    HOGENOMiHOG000265546.
    HOVERGENiHBG006127.
    KOiK03253.
    OMAiHTLRVNK.
    OrthoDBiEOG7KM5S6.
    PhylomeDBiP55884.
    TreeFamiTF101521.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    3.30.70.330. 1 hit.
    HAMAPiMF_03001. eIF3b.
    InterProiIPR011400. EIF3B.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR013979. TIF_beta_prop-like.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PANTHERiPTHR14068. PTHR14068. 1 hit.
    PfamiPF08662. eIF2A. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036424. eIF3b. 1 hit.
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P55884-1) [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

    MQDAENVAVP EAAEERAEPG QQQPAAEPPP AEGLLRPAGP GAPEAAGTEA    50
    SSEEVGIAEA GPESEVRTEP AAEAEAASGP SESPSPPAAE ELPGSHAEPP 100
    VPAQGEAPGE QARDERSDSR AQAVSEDAGG NEGRAAEAEP RALENGDADE 150
    PSFSDPEDFV DDVSEEELLG DVLKDRPQEA DGIDSVIVVD NVPQVGPDRL 200
    EKLKNVIHKI FSKFGKITND FYPEEDGKTK GYIFLEYASP AHAVDAVKNA 250
    DGYKLDKQHT FRVNLFTDFD KYMTISDEWD IPEKQPFKDL GNLRYWLEEA 300
    ECRDQYSVIF ESGDRTSIFW NDVKDPVSIE ERARWTETYV RWSPKGTYLA 350
    TFHQRGIALW GGEKFKQIQR FSHQGVQLID FSPCERYLVT FSPLMDTQDD 400
    PQAIIIWDIL TGHKKRGFHC ESSAHWPIFK WSHDGKFFAR MTLDTLSIYE 450
    TPSMGLLDKK SLKISGIKDF SWSPGGNIIA FWVPEDKDIP ARVTLMQLPT 500
    RQEIRVRNLF NVVDCKLHWQ KNGDYLCVKV DRTPKGTQGV VTNFEIFRMR 550
    EKQVPVDVVE MKETIIAFAW EPNGSKFAVL HGEAPRISVS FYHVKNNGKI 600
    ELIKMFDKQQ ANTIFWSPQG QFVVLAGLRS MNGALAFVDT SDCTVMNIAE 650
    HYMASDVEWD PTGRYVVTSV SWWSHKVDNA YWLWTFQGRL LQKNNKDRFC 700
    QLLWRPRPPT LLSQEQIKQI KKDLKKYSKI FEQKDRLSQS KASKELVERR 750
    RTMMEDFRKY RKMAQELYME QKNERLELRG GVDTDELDSN VDDWEEETIE 800
    FFVTEEIIPL GNQE 814
    Length:814
    Mass (Da):92,482
    Last modified:December 16, 2008 - v3
    Checksum:iC687A986EDAE0F5E
    GO
    Isoform 2 (identifier: P55884-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         812-814: NQE → IRSDLEHCAQPCVLWSRGRPAGSRVTPASSLCSLALDCDCAWILPLRHIFVPFSPWCLQWGI

    Show »
    Length:873
    Mass (Da):99,029
    Checksum:iD5799E065B3C35D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1162ER → AG in AAB42010. (PubMed:8995410)Curated

    Mass spectrometryi

    Molecular mass is 93093.7 Da from positions 1 - 814. 1 Publication
    Molecular mass is 92561±43.5 Da from positions 1 - 814. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641S → P.3 Publications
    Corresponds to variant rs9690787 [ dbSNP | Ensembl ].
    VAR_047972
    Natural varianti793 – 7931D → E.
    Corresponds to variant rs1063257 [ dbSNP | Ensembl ].
    VAR_047973

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei812 – 8143NQE → IRSDLEHCAQPCVLWSRGRP AGSRVTPASSLCSLALDCDC AWILPLRHIFVPFSPWCLQW GI in isoform 2. 1 PublicationVSP_017274

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78525 mRNA. Translation: AAC99479.1.
    U62583 mRNA. Translation: AAB42010.1.
    AC004971 Genomic DNA. No translation available.
    AC004840 Genomic DNA. No translation available.
    CH236953 Genomic DNA. Translation: EAL23951.1.
    CH471144 Genomic DNA. Translation: EAW87237.1.
    BC001173 mRNA. Translation: AAH01173.1.
    BC110865 mRNA. Translation: AAI10866.1.
    CCDSiCCDS5332.1. [P55884-1]
    PIRiT09582.
    RefSeqiNP_001032360.1. NM_001037283.1. [P55884-1]
    NP_003742.2. NM_003751.3. [P55884-1]
    UniGeneiHs.371001.

    Genome annotation databases

    EnsembliENST00000360876; ENSP00000354125; ENSG00000106263. [P55884-1]
    ENST00000397011; ENSP00000380206; ENSG00000106263. [P55884-1]
    GeneIDi8662.
    KEGGihsa:8662.
    UCSCiuc003slx.3. human. [P55884-1]

    Polymorphism databases

    DMDMi218512094.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78525 mRNA. Translation: AAC99479.1 .
    U62583 mRNA. Translation: AAB42010.1 .
    AC004971 Genomic DNA. No translation available.
    AC004840 Genomic DNA. No translation available.
    CH236953 Genomic DNA. Translation: EAL23951.1 .
    CH471144 Genomic DNA. Translation: EAW87237.1 .
    BC001173 mRNA. Translation: AAH01173.1 .
    BC110865 mRNA. Translation: AAI10866.1 .
    CCDSi CCDS5332.1. [P55884-1 ]
    PIRi T09582.
    RefSeqi NP_001032360.1. NM_001037283.1. [P55884-1 ]
    NP_003742.2. NM_003751.3. [P55884-1 ]
    UniGenei Hs.371001.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KRB NMR - A 184-264 [» ]
    2NLW NMR - A 170-274 [» ]
    ProteinModelPortali P55884.
    SMRi P55884. Positions 170-274, 342-708.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114211. 54 interactions.
    DIPi DIP-31113N.
    IntActi P55884. 38 interactions.
    MINTi MINT-4999648.
    STRINGi 9606.ENSP00000354125.

    PTM databases

    PhosphoSitei P55884.

    Polymorphism databases

    DMDMi 218512094.

    Proteomic databases

    MaxQBi P55884.
    PaxDbi P55884.
    PRIDEi P55884.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360876 ; ENSP00000354125 ; ENSG00000106263 . [P55884-1 ]
    ENST00000397011 ; ENSP00000380206 ; ENSG00000106263 . [P55884-1 ]
    GeneIDi 8662.
    KEGGi hsa:8662.
    UCSCi uc003slx.3. human. [P55884-1 ]

    Organism-specific databases

    CTDi 8662.
    GeneCardsi GC07P002362.
    H-InvDB HIX0006430.
    HGNCi HGNC:3280. EIF3B.
    HPAi CAB017562.
    HPA048983.
    MIMi 603917. gene.
    neXtProti NX_P55884.
    PharmGKBi PA162384603.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5354.
    HOGENOMi HOG000265546.
    HOVERGENi HBG006127.
    KOi K03253.
    OMAi HTLRVNK.
    OrthoDBi EOG7KM5S6.
    PhylomeDBi P55884.
    TreeFami TF101521.

    Enzyme and pathway databases

    Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Miscellaneous databases

    ChiTaRSi EIF3B. human.
    EvolutionaryTracei P55884.
    GeneWikii EIF3B.
    GenomeRNAii 8662.
    NextBioi 32487.
    PROi P55884.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55884.
    Bgeei P55884.
    CleanExi HS_EIF3B.
    Genevestigatori P55884.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    3.30.70.330. 1 hit.
    HAMAPi MF_03001. eIF3b.
    InterProi IPR011400. EIF3B.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR013979. TIF_beta_prop-like.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    PANTHERi PTHR14068. PTHR14068. 1 hit.
    Pfami PF08662. eIF2A. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036424. eIF3b. 1 hit.
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Biochemical characterization of mammalian translation initiation factor 3 (eIF3). Molecular cloning reveals that p110 subunit is the mammalian homologue of Saccharomyces cerevisiae protein Prt1."
      Chaudhuri J., Chakrabarti A., Maitra U.
      J. Biol. Chem. 272:30975-30983(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT PRO-64.
      Tissue: Skeletal muscle.
    2. "The human homologue of the yeast Prt1 protein is an integral part of the eukaryotic initiation factor 3 complex and interacts with p170."
      Methot N., Rom E., Olsen H., Sonenberg N.
      J. Biol. Chem. 272:1110-1116(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT PRO-64.
      Tissue: Placenta.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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), VARIANT PRO-64.
      Tissue: Brain and Uterus.
    7. "Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6 interact with the eIF3 core complex by binding to cognate eIF3b subunits."
      Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L., Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.
      J. Biol. Chem. 276:34948-34957(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3E.
    8. "Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7."
      Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.
      J. Cell. Biochem. 80:483-490(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3A.
    9. "Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3."
      Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.
      Eur. J. Biochem. 270:4133-4139(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3A; EIF3C; EIF3G; EIF3I AND EIF3K.
    10. "The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro."
      Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A., Hershey J.W.B.
      J. Biol. Chem. 279:8946-8956(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3A; EIF3G; EIF3I AND EIF3J.
    11. "mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events."
      Holz M.K., Ballif B.A., Gygi S.P., Blenis J.
      Cell 123:569-580(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4B; MTOR; RPTOR AND RPS6KB1.
    12. "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.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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.
    15. "Reconstitution reveals the functional core of mammalian eIF3."
      Masutani M., Sonenberg N., Yokoyama S., Imataka H.
      EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
    16. "Human INT6/eIF3e is required for nonsense-mediated mRNA decay."
      Morris C., Wittmann J., Jaeck H.-M., Jalinot P.
      EMBO Rep. 8:596-602(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3A; EIF3C; EIF3E AND UPF2.
    17. "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, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-83; SER-85; SER-119; SER-125; SER-152; SER-154 AND SER-164, MASS SPECTROMETRY.
    18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-81; SER-83; SER-85 AND SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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, INTERACTION WITH EIF3E; EIF3F; EIF3H; EIF3L AND EIF3M, MASS SPECTROMETRY.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "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-209; LYS-288 AND LYS-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154; SER-164 AND SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation."
      Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H., Hong K.Y., Jang S.K., Kim K.T.
      Nucleic Acids Res. 42:3590-3606(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRPD, RNA-BINDING.
    30. "Structural roles for human translation factor eIF3 in initiation of protein synthesis."
      Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.
      Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
    31. "Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit."
      ElAntak L., Tzakos A.G., Locker N., Lukavsky P.J.
      J. Biol. Chem. 282:8165-8174(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 170-274, INTERACTION WITH EIF3J.

    Entry informationi

    Entry nameiEIF3B_HUMAN
    AccessioniPrimary (citable) accession number: P55884
    Secondary accession number(s): A4D208, Q2NL77, Q9UMF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. Translation initiation factors
      List of translation initiation factor entries
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3