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P55884 (EIF3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EIF3B
Synonyms:EIF3S9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length814 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16 Ref.17 Ref.20 Ref.30

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03001.

Domain

The RRM domain mediates interaction with EIF3J. HAMAP-Rule MF_03001

Post-translational modification

Phosphorylated. Phosphorylation is enhanced upon serum stimulation. Ref.17

Sequence similarities

Belongs to the eIF-3 subunit B family.

Contains 1 RRM (RNA recognition motif) domain.

Contains 5 WD repeats.

Mass spectrometry

Molecular mass is 93093.7 Da from positions 1 - 814. Ref.17

Molecular mass is 92561±43.5 Da from positions 1 - 814. Determined by MALDI. Ref.20

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55884-1)

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.
Isoform 2 (identifier: P55884-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 814814Eukaryotic translation initiation factor 3 subunit B HAMAP-Rule MF_03001
PRO_0000123531

Regions

Domain185 – 26884RRM
Repeat332 – 37039WD 1 HAMAP-Rule MF_03001
Repeat372 – 41746WD 2 HAMAP-Rule MF_03001
Repeat421 – 45939WD 3 HAMAP-Rule MF_03001
Repeat560 – 60142WD 4 HAMAP-Rule MF_03001
Repeat649 – 69446WD 5 HAMAP-Rule MF_03001
Region124 – 413290Sufficient for interaction with EIF3E HAMAP-Rule MF_03001
Region170 – 274105Sufficient for interaction with EIF3J HAMAP-Rule MF_03001

Amino acid modifications

Modified residue11N-acetylmethionine Ref.17 Ref.28
Modified residue781Phosphoserine Ref.19
Modified residue811Phosphoserine Ref.19
Modified residue831Phosphoserine Ref.17 Ref.19
Modified residue851Phosphoserine Ref.17 Ref.19
Modified residue1191Phosphoserine Ref.17
Modified residue1251Phosphoserine Ref.17 Ref.26
Modified residue1521Phosphoserine Ref.13 Ref.17 Ref.22 Ref.24
Modified residue1541Phosphoserine Ref.13 Ref.17 Ref.22 Ref.24 Ref.26
Modified residue1641Phosphoserine Ref.13 Ref.17 Ref.22 Ref.24
Modified residue2091N6-acetyllysine Ref.23
Modified residue2391Phosphoserine Ref.19 Ref.24
Modified residue2881N6-acetyllysine Ref.23
Modified residue3641N6-acetyllysine Ref.23

Natural variations

Alternative sequence812 – 8143NQE → IRSDLEHCAQPCVLWSRGRP AGSRVTPASSLCSLALDCDC AWILPLRHIFVPFSPWCLQW GI in isoform 2.
VSP_017274
Natural variant641S → P. Ref.1 Ref.2 Ref.6
Corresponds to variant rs9690787 [ dbSNP | Ensembl ].
VAR_047972
Natural variant7931D → E.
Corresponds to variant rs1063257 [ dbSNP | Ensembl ].
VAR_047973

Experimental info

Sequence conflict115 – 1162ER → AG in AAB42010. Ref.2

Secondary structure

................ 814
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 16, 2008. Version 3.
Checksum: C687A986EDAE0F5E

FASTA81492,482
        10         20         30         40         50         60 
MQDAENVAVP EAAEERAEPG QQQPAAEPPP AEGLLRPAGP GAPEAAGTEA SSEEVGIAEA 

        70         80         90        100        110        120 
GPESEVRTEP AAEAEAASGP SESPSPPAAE ELPGSHAEPP VPAQGEAPGE QARDERSDSR 

       130        140        150        160        170        180 
AQAVSEDAGG NEGRAAEAEP RALENGDADE PSFSDPEDFV DDVSEEELLG DVLKDRPQEA 

       190        200        210        220        230        240 
DGIDSVIVVD NVPQVGPDRL EKLKNVIHKI FSKFGKITND FYPEEDGKTK GYIFLEYASP 

       250        260        270        280        290        300 
AHAVDAVKNA DGYKLDKQHT FRVNLFTDFD KYMTISDEWD IPEKQPFKDL GNLRYWLEEA 

       310        320        330        340        350        360 
ECRDQYSVIF ESGDRTSIFW NDVKDPVSIE ERARWTETYV RWSPKGTYLA TFHQRGIALW 

       370        380        390        400        410        420 
GGEKFKQIQR FSHQGVQLID FSPCERYLVT FSPLMDTQDD PQAIIIWDIL TGHKKRGFHC 

       430        440        450        460        470        480 
ESSAHWPIFK WSHDGKFFAR MTLDTLSIYE TPSMGLLDKK SLKISGIKDF SWSPGGNIIA 

       490        500        510        520        530        540 
FWVPEDKDIP ARVTLMQLPT RQEIRVRNLF NVVDCKLHWQ KNGDYLCVKV DRTPKGTQGV 

       550        560        570        580        590        600 
VTNFEIFRMR EKQVPVDVVE MKETIIAFAW EPNGSKFAVL HGEAPRISVS FYHVKNNGKI 

       610        620        630        640        650        660 
ELIKMFDKQQ ANTIFWSPQG QFVVLAGLRS MNGALAFVDT SDCTVMNIAE HYMASDVEWD 

       670        680        690        700        710        720 
PTGRYVVTSV SWWSHKVDNA YWLWTFQGRL LQKNNKDRFC QLLWRPRPPT LLSQEQIKQI 

       730        740        750        760        770        780 
KKDLKKYSKI FEQKDRLSQS KASKELVERR RTMMEDFRKY RKMAQELYME QKNERLELRG 

       790        800        810 
GVDTDELDSN VDDWEEETIE FFVTEEIIPL GNQE 

« Hide

Isoform 2 [UniParc].

Checksum: D5799E065B3C35D7
Show »

FASTA87399,029

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"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.
[30]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT09582.
RefSeqNP_001032360.1. NM_001037283.1.
NP_003742.2. NM_003751.3.
UniGeneHs.371001.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KRBNMR-A184-264[»]
2NLWNMR-A170-274[»]
ProteinModelPortalP55884.
SMRP55884. Positions 170-274, 340-454, 632-670.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114211. 53 interactions.
DIPDIP-31113N.
IntActP55884. 38 interactions.
MINTMINT-4999648.
STRING9606.ENSP00000354125.

PTM databases

PhosphoSiteP55884.

Polymorphism databases

DMDM218512094.

Proteomic databases

PaxDbP55884.
PRIDEP55884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360876; ENSP00000354125; ENSG00000106263. [P55884-1]
ENST00000397011; ENSP00000380206; ENSG00000106263. [P55884-1]
GeneID8662.
KEGGhsa:8662.
UCSCuc003slx.3. human. [P55884-1]

Organism-specific databases

CTD8662.
GeneCardsGC07P002362.
H-InvDBHIX0006430.
HGNCHGNC:3280. EIF3B.
HPACAB017562.
HPA048983.
MIM603917. gene.
neXtProtNX_P55884.
PharmGKBPA162384603.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5354.
HOGENOMHOG000265546.
HOVERGENHBG006127.
KOK03253.
OMAHTLRVNK.
OrthoDBEOG7KM5S6.
PhylomeDBP55884.
TreeFamTF101521.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP55884.
BgeeP55884.
CleanExHS_EIF3B.
GenevestigatorP55884.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
3.30.70.330. 1 hit.
HAMAPMF_03001. eIF3b.
InterProIPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERPTHR14068. PTHR14068. 1 hit.
PfamPF08662. eIF2A. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFPIRSF036424. eIF3b. 1 hit.
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3B. human.
EvolutionaryTraceP55884.
GeneWikiEIF3B.
GenomeRNAi8662.
NextBio32487.
PROP55884.
SOURCESearch...

Entry information

Entry nameEIF3B_HUMAN
AccessionPrimary (citable) accession number: P55884
Secondary accession number(s): A4D208, Q2NL77, Q9UMF9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 16, 2008
Last modified: March 19, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM