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Reviewed, UniProtKB/Swiss-Prot P41091 (IF2G_HUMAN)

Last modified July 7, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

Names and origin

Protein namesRecommended name:
    Eukaryotic translation initiation factor 2 subunit 3
Alternative name(s):
    Eukaryotic translation initiation factor 2 subunit gamma
      Short name=eIF-2-gamma
Gene names
Name: EIF2S3
Synonyms: EIF2G
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length472 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.

Subunit structure

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

Sequence similarities

Belongs to the GTP-binding elongation factor family. EIF2G subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processtranslational initiation

Inferred from direct assay. Source: UniProtKB

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity Ref.1

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: IntAct

translation initiation factor activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 472471Eukaryotic translation initiation factor 2 subunit 3
PRO_0000137438

Regions

Nucleotide binding48 – 558GTP By similarity
Nucleotide binding134 – 1385GTP By similarity
Nucleotide binding190 – 1934GTP By similarity

Amino acid modifications

Modified residue21N-acetylalanine; partial Ref.4
Modified residue221Phosphothreonine By similarity

Natural variations

Natural variant1251K → R: dbSNP rs16997659.
VAR_002352

Sequences

Sequence LengthMass (Da)Tools
P41091-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7A292A6AAF6DF983

FASTA47251,109
        10         20         30         40         50         60 
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA 

        70         80         90        100        110        120 
ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE CYRSCGSSTP DEFPTDIPGT 

       130        140        150        160        170        180 
KGNFKLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM 

       190        200        210        220        230        240 
KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV 

       250        260        270        280        290        300 
KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI 

       310        320        330        340        350        360 
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA 

       370        380        390        400        410        420 
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV 

       430        440        450        460        470 
KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD 

« Hide

References

« Hide 'large scale' references
[1]"Translation initiation factor eIF-2. Cloning and expression of the human cDNA encoding the gamma-subunit."
Gaspar N.J., Kinzy T.G., Scherer B.J., Huembelin M., Hershey J.W.B., Merrick W.C.
J. Biol. Chem. 269:3415-3422(1994) [PubMed: 8106381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Leukemia.
[2]"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].
Tissue: Lymph.
[3]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-17.
Tissue: Platelet.
[4]Bienvenut W.V., Boldt K., von Kriegsheim A., Kolch W., Heiserich L., Gottlieb E., Vousden K.H., Lukashchuk N., Lilla S., Lempens A.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-54; 60-75; 182-191; 242-255; 276-285; 290-303; 318-342; 401-416; 453-460 AND 462-472, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: Colon carcinoma, Hepatoma, Lung carcinoma and Ovarian carcinoma.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

L19161 mRNA. Translation: AAA19696.1.
BC019906 mRNA. Translation: AAH19906.1.
IPIIPI00297982.
PIRA53048.
RefSeqNP_001406.1.
UniGeneHs.539684

3D structure databases

HSSPHSSP built from PDB template 1KK1 based on UniProtKB Q9V1G0.
ModBaseSearch...

Protein-protein interaction databases

IntActP41091. 11 interactions.

PTM databases

PhosphoSiteP41091.

Proteomic databases

PeptideAtlasP41091.
PRIDEP41091.

Genome annotation databases

EnsemblENSG00000130741. Homo sapiens. [Contig view]
GeneID1968.
KEGGhsa:1968.
NMPDRfig|9606.3.peg.32560.
UCSCuc004dbc.1. human.

Organism-specific databases

GeneCardsGC0XP023982.
H-InvDBHIX0016706.
HGNCHGNC:3267. EIF2S3.
MIM300161. gene.
PharmGKBPA27697.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP41091.
HOVERGENP41091.
OMAP41091. ENAPIIP.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP41091.
BgeeP41091.
CleanExHS_EIF2S3.
GermOnlineENSG00000130741. Homo sapiens.

Family and domain databases

InterProIPR015256. eIF2_C.
IPR000795. ProtSyn_GTP_bd.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamPF09173. eIF2_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
ProtoNetSearch...

Other Resources

NextBio7979.
SOURCESearch...

Entry information

Entry nameIF2G_HUMAN
AccessionPrimary (citable) accession number: P41091
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: July 7, 2009
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome X

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Translation initiation factors

List of translation initiation factor entries

MIM cross-references

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

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