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Reviewed, UniProtKB/Swiss-Prot P41375 (IF2B_DROME)

Last modified November 4, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Eukaryotic translation initiation factor 2 subunit 2
Alternative name(s):
    Eukaryotic translation initiation factor 2 subunit beta
      Short name=eIF-2-beta
Gene names
Name: eIF-2beta
Synonyms: eIF2b
ORF Names: CG4153
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This preinitiation complex mediates ribosomal recognition of a start codon during the scanning process of the leader region.

Subunit structure

Heterotrimer composed of an alpha, a beta and a gamma chain.

Sequence similarities

Belongs to the eIF-2-beta/eIF-5 family.

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Ontologies

Keywords

   Biological processProtein biosynthesis
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionInitiation factor
   PTMPhosphoprotein
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processmitotic spindle elongation

Inferred from mutant phenotype. Source: FlyBase

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9W004-11EBI-136516,EBI-218559

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Eukaryotic translation initiation factor 2 subunit 2
PRO_0000137409

Regions

Zinc finger260 – 28425C4-type Potential
Compositional bias13 – 197Poly-Lys
Compositional bias63 – 708Poly-Lys
Compositional bias93 – 997Poly-Glu
Compositional bias110 – 1189Poly-Lys

Amino acid modifications

Modified residue441Phosphoserine
Modified residue1331Phosphoserine
Modified residue1451Phosphothreonine

Experimental info

Sequence conflict601S → G in AAL48875. Ref.4
Sequence conflict641K → E in AAL48875. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
P41375-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 163B98C43A35A764

FASTA31235,218
        10         20         30         40         50         60 
MDAEDGFDPT LLKKKKKKKT TFDLDAALGL EDDTKKEDPQ DEASAEGGAA AEEDNLDLES 

        70         80         90        100        110        120 
FGKKKKKKKK PFNMDEIEAA IPSFGGDDVA ASEEPEEEEI NLDMDFSMAK KKKKSKKKEL 

       130        140        150        160        170        180 
DELFADQADD DKSEDKENDE DNSSTWFGSD RDYTYDELLK RVFEIILDKN PDMAAGRKPK 

       190        200        210        220        230        240 
FVMRPPQVLR VGTKKTSFAN FMDIAKTLHR LPKHLLDFLL AELGTSGSMD GNQQLIIKGR 

       250        260        270        280        290        300 
FQPKQIENVL RRYIKEYVTC HTCRSPETIL QKDTRLFFLQ CESCGSRCSV ASIKSGFQAV 

       310 
TGKRAAIRAK TT

« Hide

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References

« Hide 'large scale' references
[1]"Isolation and characterization of the Drosophila melanogaster gene encoding translation-initiation factor eIF-2 beta."
Ye X., Cavener D.R.
Gene 142:271-274(1994) [PubMed: 8194763] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Oregon-R.
Tissue: Embryo and Pupae.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, MASS SPECTROMETRY.
[6]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND THR-145, MASS SPECTROMETRY.
Tissue: Embryo.

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Cross-references

Sequence databases

L19197 mRNA. Translation: AAA28504.1.
AE014296 Genomic DNA. Translation: AAF49902.1.
AY071253 mRNA. Translation: AAL48875.1.
RefSeqNP_524043.1.
UniGeneDm.942

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:21095N.
IntActP41375.

Genome annotation databases

EnsemblCG4153. Drosophila melanogaster. [Contig view]
GeneID39433.
KEGGdme:Dmel_CG4153.
NMPDRfig|7227.3.peg.9557.

Organism-specific databases

FlyBaseFBgn0004926. eIF-2beta.

Phylogenomic databases

HOGENOMP41375.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-016419-MON.

Gene expression databases

GermOnlineCG4153. Drosophila melanogaster.

Family and domain databases

InterProIPR002735. Transl_init_fac_IF2/IF5.
[Graphical view]
PfamPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
ProDomPD004078. eIF5_eIF2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00653. eIF2B_5. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio813610.

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Entry information

Entry nameIF2B_DROME
AccessionPrimary (citable) accession number: P41375
Secondary accession number(s): Q8SYX9, Q9VTZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 4, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

Translation initiation factors

List of translation initiation factor entries

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

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