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Q41969 (IF2B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 2 subunit beta

Short name=eIF-2-beta
Alternative name(s):
Protein EMBRYO DEFECTIVE 1401
Gene names
Name:EMB1401
Ordered Locus Names:At5g20920
ORF Names:F22D1.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B By similarity.

Subunit structure

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

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionInitiation factor
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentplasma membrane

Inferred from direct assay PubMed 17317660. Source: TAIR

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 19452453. Source: TAIR

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q41969-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 268267Eukaryotic translation initiation factor 2 subunit beta
PRO_0000137411

Regions

Zinc finger222 – 24625C4-type Potential
Compositional bias22 – 287Poly-Lys
Compositional bias64 – 696Poly-Lys

Amino acid modifications

Modified residue21N-acetylalanine Ref.7

Experimental info

Sequence conflict711T → A in AAK29672. Ref.1
Sequence conflict711T → A in AAM65346. Ref.5

Sequences

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

Last modified January 10, 2003. Version 3.
Checksum: E1C17373472F4DEB

FASTA26830,663
        10         20         30         40         50         60 
MADEINEIRE EQEQLAPFDP SKKKKKKKVV IQEPVEDLAE SSQTEKSDSL PVNDGLESSF 

        70         80         90        100        110        120 
TGMKKKKKKP TESSLLNNES VDAGEDLDEI ANDEQEGEEG IVLQQRYPWE GSERDYIYDE 

       130        140        150        160        170        180 
LLGRVFNILR ENNPELAGDR RRTVMRPPQV LREGTKKTVF VNFMDLCKTM HRQPDHVMQY 

       190        200        210        220        230        240 
LLAELGTSGS LDGQQRLVVK GRFAPKNFEG ILRRYITDYV ICLGCKSPDT ILSKENRLFF 

       250        260 
LRCEKCGSQR SVAPIKTGFV ARVSRRKT 

« Hide

References

« Hide 'large scale' references
[1]Browning K.S., Chen R.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana."
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., Cooke R. expand/collapse author list , Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.
Plant J. 4:1051-1061(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-252.
Strain: cv. Columbia.
Tissue: Seedling.
[7]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF353095 mRNA. Translation: AAK29672.1.
AF296834 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92904.1.
CP002688 Genomic DNA. Translation: AED92906.1.
AY128324 mRNA. Translation: AAM91527.1.
BT000056 mRNA. Translation: AAN15375.1.
AY087810 mRNA. Translation: AAM65346.1.
Z18133 mRNA. Translation: CAA79110.1.
RefSeqNP_001078610.1. NM_001085141.1. [Q41969-1]
NP_197592.1. NM_122100.3. [Q41969-1]
UniGeneAt.21465.

3D structure databases

ProteinModelPortalQ41969.
SMRQ41969. Positions 116-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17491. 25 interactions.
IntActQ41969. 32 interactions.

Proteomic databases

PaxDbQ41969.
PRIDEQ41969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G20920.1; AT5G20920.1; AT5G20920. [Q41969-1]
AT5G20920.3; AT5G20920.3; AT5G20920. [Q41969-1]
GeneID832216.
KEGGath:AT5G20920.

Organism-specific databases

TAIRAT5G20920.

Phylogenomic databases

eggNOGCOG1601.
HOGENOMHOG000107197.
InParanoidQ41969.
KOK03238.
OMAWEGSERD.
PhylomeDBQ41969.

Gene expression databases

GenevestigatorQ41969.

Family and domain databases

Gene3D3.30.30.50. 1 hit.
InterProIPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SMARTSM00653. eIF2B_5. 1 hit.
[Graphical view]
SUPFAMSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.
ProtoNetSearch...

Other

PROQ41969.

Entry information

Entry nameIF2B_ARATH
AccessionPrimary (citable) accession number: Q41969
Secondary accession number(s): Q8L7Q3, Q9C5N7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 10, 2003
Last modified: June 11, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Translation initiation factors

List of translation initiation factor entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names