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Reviewed, UniProtKB/Swiss-Prot P55884 (EIF3B_HUMAN)

Last modified November 25, 2008. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    eIF-3-eta
    eIF3 p116
    eIF3 p110
    Prt1 homolog
      Short name=hPrt1
Gene names
Name: EIF3B
Synonyms: EIF3S9
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length814 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Binds to the 40S ribosome and promotes the binding of methionyl-tRNAi and mRNA.

Subunit structure

eIF-3 is composed of at least 13 different subunits. Interacts with EIF3A.

Sequence similarities

Belongs to the eIF-3 subunit B family.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords

   Biological processProtein biosynthesis
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processtranslational initiation Ref.2

Traceable author statement. Source: ProtInc

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

eukaryotic translation initiation factor 3 complex Ref.2

Traceable author statement. Source: ProtInc

   Molecular functionRNA binding

Inferred from electronic annotation. Source: InterPro

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding Ref.4

Inferred from physical interaction. Source: IntAct

translation initiation factor activity Ref.2

Traceable author statement. Source: ProtInc

Complete GO annotation...

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
PRO_0000123531

Regions

Domain185 – 26884RRM

Amino acid modifications

Modified residue781Phosphoserine
Modified residue811Phosphoserine
Modified residue831Phosphoserine
Modified residue851Phosphoserine
Modified residue1251Phosphoserine
Modified residue1521Phosphoserine
Modified residue1541Phosphoserine
Modified residue1641Phosphoserine
Modified residue2391Phosphoserine
Modified residue4511Phosphothreonine By similarity
Modified residue5251Phosphotyrosine

Natural variations

Alternative sequence812 – 8143NQE → IRSDLEHCAQPCVLWSRGRP AGSRVTPASSLCSLALDCDC AWILPLRHIFVPFSPWCLQW GI in isoform 2.
VSP_017274

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 July 15, 1998. Version 2.
Checksum: 9EC5E0C4687562C3

FASTA81492,492
        10         20         30         40         50         60 
MQDAENVAVP EAAEERAEPG QQQPAAEPPP AEGLLRPAGP GAPEAAGTEA SSEEVGIAEA 

        70         80         90        100        110        120 
GPEPEVRTEP 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: 30C4A9A6723F4996
Show »

87399,039

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: 9388245] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
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: 8995410] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Uterus.
[4]"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: 11169732] [Abstract]
Cited for: INTERACTION WITH EIF3A.
[5]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND SER-125, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-525, MASS SPECTROMETRY.
[7]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND SER-164, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY.
[9]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-81; SER-83; SER-85; SER-125 AND SER-239, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U78525 mRNA. Translation: AAC99479.1.
U62583 mRNA. Translation: AAB42010.1.
BC001173 mRNA. Translation: AAH01173.1.
BC110865 mRNA. Translation: AAI10866.1.
PIRT09582.
RefSeqNP_001032360.1.
NP_003742.2.
UniGeneHs.371001

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2NLWNMR-A170-274[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP55884.

PTM databases

PhosphoSiteP55884.

Genome annotation databases

EnsemblENSG00000106263. Homo sapiens. [Contig view]
GeneID8662.
KEGGhsa:8662.

Organism-specific databases

H-InvDBHIX0006430.
HGNCHGNC:3280. EIF3B.
HPACAB017562.
MIM603917. gene.
PharmGKBPA27709.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP55884.

Enzyme and pathway databases

ReactomeREACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP55884.
CleanExHS_EIF3B.
GermOnlineENSG00000106263. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR013979. eIF2A_central-region.
IPR011400. eIF3b.
IPR000504. RRM_RNP1.
IPR015943. WD40/YVTN_repeat-like.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PANTHERPTHR14068. eIF3b. 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 Resources

NextBio32487.
SOURCESearch...

Entry information

Entry nameEIF3B_HUMAN
AccessionPrimary (citable) accession number: P55884
Secondary accession number(s): Q2NL77, Q9UMF9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: November 25, 2008
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 7

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

Translation initiation factors

List of translation initiation factor entries

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents