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Protein

Eukaryotic translation initiation factor 2 subunit 3

Gene

EIF2S3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 558GTPBy similarity
Nucleotide bindingi134 – 1385GTPBy similarity
Nucleotide bindingi190 – 1934GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: ProtInc
  2. GTP binding Source: UniProtKB-KW
  3. translation factor activity, nucleic acid binding Source: UniProtKB
  4. translation initiation factor activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. translation Source: Reactome
  4. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1815. Recycling of eIF2:GDP.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:EIF2S3
Synonyms:EIF2G
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3267. EIF2S3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27697.

Polymorphism and mutation databases

BioMutaiEIF2S3.
DMDMi729816.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 472471Eukaryotic translation initiation factor 2 subunit 3PRO_0000137438Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine; partial1 Publication
Modified residuei16 – 161PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41091.
PaxDbiP41091.
PeptideAtlasiP41091.
PRIDEiP41091.

PTM databases

PhosphoSiteiP41091.

Expressioni

Gene expression databases

BgeeiP41091.
CleanExiHS_EIF2S3.
ExpressionAtlasiP41091. baseline and differential.
GenevestigatoriP41091.

Organism-specific databases

HPAiCAB012471.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF2S1P051984EBI-1054228,EBI-1056162
EIF2S2P200423EBI-1054228,EBI-711977

Protein-protein interaction databases

BioGridi108287. 31 interactions.
IntActiP41091. 12 interactions.
MINTiMINT-3015066.
STRINGi9606.ENSP00000253039.

Structurei

3D structure databases

ProteinModelPortaliP41091.
SMRiP41091. Positions 39-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 248210tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 558G1PROSITE-ProRule annotation
Regioni76 – 805G2PROSITE-ProRule annotation
Regioni134 – 1374G3PROSITE-ProRule annotation
Regioni190 – 1934G4PROSITE-ProRule annotation
Regioni225 – 2273G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5257.
GeneTreeiENSGT00550000074801.
HOVERGENiHBG006123.
InParanoidiP41091.
KOiK03242.
OMAiCPQPQTK.
OrthoDBiEOG7H1JK8.
PhylomeDBiP41091.
TreeFamiTF101513.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR000795. 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]
PfamiPF09173. eIF2_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41091-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV
60 70 80 90 100
AHGKSTVVKA ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE
110 120 130 140 150
CYRSCGSSTP DEFPTDIPGT KGNFKLVRHV SFVDCPGHDI LMATMLNGAA
160 170 180 190 200
VMDAALLLIA GNESCPQPQT SEHLAAIEIM KLKHILILQN KIDLVKESQA
210 220 230 240 250
KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV KKIPVPPRDF
260 270 280 290 300
TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI
310 320 330 340 350
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA
360 370 380 390 400
DRMVGQVLGA VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK
410 420 430 440 450
NEVLMVNIGS LSTGGRVSAV KADLGKIVLT NPVCTEVGEK IALSRRVEKH
460 470
WRLIGWGQIR RGVTIKPTVD DD
Length:472
Mass (Da):51,109
Last modified:January 23, 2007 - v3
Checksum:i7A292A6AAF6DF983
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251K → R.
Corresponds to variant rs16997659 [ dbSNP | Ensembl ].
VAR_002352

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14210.1.
PIRiA53048.
RefSeqiNP_001406.1. NM_001415.3.
UniGeneiHs.539684.

Genome annotation databases

EnsembliENST00000253039; ENSP00000253039; ENSG00000130741.
GeneIDi1968.
KEGGihsa:1968.
UCSCiuc004dbc.3. human.

Polymorphism and mutation databases

BioMutaiEIF2S3.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14210.1.
PIRiA53048.
RefSeqiNP_001406.1. NM_001415.3.
UniGeneiHs.539684.

3D structure databases

ProteinModelPortaliP41091.
SMRiP41091. Positions 39-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108287. 31 interactions.
IntActiP41091. 12 interactions.
MINTiMINT-3015066.
STRINGi9606.ENSP00000253039.

PTM databases

PhosphoSiteiP41091.

Polymorphism and mutation databases

BioMutaiEIF2S3.
DMDMi729816.

Proteomic databases

MaxQBiP41091.
PaxDbiP41091.
PeptideAtlasiP41091.
PRIDEiP41091.

Protocols and materials databases

DNASUi1968.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000253039; ENSP00000253039; ENSG00000130741.
GeneIDi1968.
KEGGihsa:1968.
UCSCiuc004dbc.3. human.

Organism-specific databases

CTDi1968.
GeneCardsiGC0XP024072.
HGNCiHGNC:3267. EIF2S3.
HPAiCAB012471.
MIMi300161. gene.
neXtProtiNX_P41091.
PharmGKBiPA27697.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5257.
GeneTreeiENSGT00550000074801.
HOVERGENiHBG006123.
InParanoidiP41091.
KOiK03242.
OMAiCPQPQTK.
OrthoDBiEOG7H1JK8.
PhylomeDBiP41091.
TreeFamiTF101513.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1815. Recycling of eIF2:GDP.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSiEIF2S3. human.
GeneWikiiEIF2S3.
GenomeRNAii1968.
NextBioi7979.
PROiP41091.
SOURCEiSearch...

Gene expression databases

BgeeiP41091.
CleanExiHS_EIF2S3.
ExpressionAtlasiP41091. baseline and differential.
GenevestigatoriP41091.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR000795. 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]
PfamiPF09173. eIF2_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF2G_HUMAN
AccessioniPrimary (citable) accession number: P41091
Secondary accession number(s): B5BTZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.