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P41091 (IF2G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 2 subunit 3
Alternative name(s):
Eukaryotic translation initiation factor 2 subunit gamma X
Short name=eIF-2-gamma X
Short name=eIF-2gX
Gene names
Name:EIF2S3
Synonyms:EIF2G
OrganismHomo sapiens (Human) [Reference 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF2S1P051984EBI-1054228,EBI-1056162
EIF2S2P200423EBI-1054228,EBI-711977

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
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.6
Modified residue161Phosphoserine By similarity

Natural variations

Natural variant1251K → R.
Corresponds to variant rs16997659 [ dbSNP | Ensembl ].
VAR_002352

Sequences

Sequence LengthMass (Da)Tools
P41091 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Leukemia.
[2]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]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].
[4]"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].
Tissue: Lymph.
[5]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-17.
Tissue: Platelet.
[6]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma, Hepatoma, Lung carcinoma and Ovarian carcinoma.
[7]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19161 mRNA. Translation: AAA19696.1.
AB451230 mRNA. Translation: BAG70044.1.
AB451353 mRNA. Translation: BAG70167.1.
CH471074 Genomic DNA. Translation: EAW99010.1.
BC019906 mRNA. Translation: AAH19906.1.
PIRA53048.
RefSeqNP_001406.1. NM_001415.3.
UniGeneHs.539684.

3D structure databases

ProteinModelPortalP41091.
SMRP41091. Positions 39-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108287. 30 interactions.
IntActP41091. 12 interactions.
MINTMINT-3015066.
STRING9606.ENSP00000253039.

PTM databases

PhosphoSiteP41091.

Polymorphism databases

DMDM729816.

Proteomic databases

PaxDbP41091.
PeptideAtlasP41091.
PRIDEP41091.

Protocols and materials databases

DNASU1968.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253039; ENSP00000253039; ENSG00000130741.
GeneID1968.
KEGGhsa:1968.
UCSCuc004dbc.3. human.

Organism-specific databases

CTD1968.
GeneCardsGC0XP024072.
HGNCHGNC:3267. EIF2S3.
HPACAB012471.
MIM300161. gene.
neXtProtNX_P41091.
PharmGKBPA27697.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5257.
HOVERGENHBG006123.
InParanoidP41091.
KOK03242.
OMACPQPQTK.
OrthoDBEOG7H1JK8.
PhylomeDBP41091.
TreeFamTF101513.

Enzyme and pathway databases

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

Gene expression databases

BgeeP41091.
CleanExHS_EIF2S3.
GenevestigatorP41091.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR015256. TIF2_gsu_C.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
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.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSEIF2S3. human.
GeneWikiEIF2S3.
GenomeRNAi1968.
NextBio7979.
PROP41091.
SOURCESearch...

Entry information

Entry nameIF2G_HUMAN
AccessionPrimary (citable) accession number: P41091
Secondary accession number(s): B5BTZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 134 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

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 X

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