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P55884

- EIF3B_HUMAN

UniProt

P55884 - EIF3B_HUMAN

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Protein
Eukaryotic translation initiation factor 3 subunit B
Gene
EIF3B, EIF3S9
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 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
Complete GO annotation...

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 B
Short name:
eIF3b
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 9
Prt1 homolog
Short name:
hPrt1
eIF-3-eta
eIF3 p110
eIF3 p116
Gene namesi
Name:EIF3B
Synonyms:EIF3S9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:3280. EIF3B.

Subcellular locationi

Cytoplasm By similarity 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
Complete GO annotation...

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 BUniRule annotation
PRO_0000123531Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.1 Publication

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 Publications

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

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.

Miscellaneous databases

EvolutionaryTraceiP55884.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 413290Sufficient for interaction with EIF3EUniRule annotation
Add
BLAST
Regioni170 – 274105Sufficient for interaction with EIF3JUniRule annotation
Add
BLAST

Domaini

The RRM domain mediates interaction with EIF3J.UniRule annotation

Sequence similaritiesi

Belongs to the eIF-3 subunit B family.
Contains 5 WD repeats.

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

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.
VSP_017274

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1162ER → AG in AAB42010. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 147 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

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