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P41091

- IF2G_HUMAN

UniProt

P41091 - IF2G_HUMAN

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Protein
Eukaryotic translation initiation factor 2 subunit 3
Gene
EIF2S3, EIF2G
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 558GTP By similarity
Nucleotide bindingi134 – 1385GTP By similarity
Nucleotide bindingi190 – 1934GTP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. cellular protein metabolic process Source: Reactome
  3. gene expression Source: Reactome
  4. translation Source: Reactome
  5. 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: Chromosome X

Organism-specific databases

HGNCiHGNC:3267. EIF2S3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27697.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41091.
PaxDbiP41091.
PeptideAtlasiP41091.
PRIDEiP41091.

PTM databases

PhosphoSiteiP41091.

Expressioni

Gene expression databases

BgeeiP41091.
CleanExiHS_EIF2S3.
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. 30 interactions.
IntActiP41091. 12 interactions.
MINTiMINT-3015066.
STRINGi9606.ENSP00000253039.

Structurei

3D structure databases

ProteinModelPortaliP41091.
SMRiP41091. Positions 39-459.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 248210tr-type G
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 558G1 By similarity
Regioni76 – 805G2 By similarity
Regioni134 – 1374G3 By similarity
Regioni190 – 1934G4 By similarity
Regioni225 – 2273G5 By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5257.
HOVERGENiHBG006123.
InParanoidiP41091.
KOiK03242.
OMAiYRSDKED.
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

MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV    50
AHGKSTVVKA ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE 100
CYRSCGSSTP DEFPTDIPGT KGNFKLVRHV SFVDCPGHDI LMATMLNGAA 150
VMDAALLLIA GNESCPQPQT SEHLAAIEIM KLKHILILQN KIDLVKESQA 200
KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV KKIPVPPRDF 250
TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI 300
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA 350
DRMVGQVLGA VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK 400
NEVLMVNIGS LSTGGRVSAV KADLGKIVLT NPVCTEVGEK IALSRRVEKH 450
WRLIGWGQIR RGVTIKPTVD DD 472
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:
EMBL
GenBank
DDBJ
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 databases

DMDMi729816.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14210.1.
PIRi A53048.
RefSeqi NP_001406.1. NM_001415.3.
UniGenei Hs.539684.

3D structure databases

ProteinModelPortali P41091.
SMRi P41091. Positions 39-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108287. 30 interactions.
IntActi P41091. 12 interactions.
MINTi MINT-3015066.
STRINGi 9606.ENSP00000253039.

PTM databases

PhosphoSitei P41091.

Polymorphism databases

DMDMi 729816.

Proteomic databases

MaxQBi P41091.
PaxDbi P41091.
PeptideAtlasi P41091.
PRIDEi P41091.

Protocols and materials databases

DNASUi 1968.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253039 ; ENSP00000253039 ; ENSG00000130741 .
GeneIDi 1968.
KEGGi hsa:1968.
UCSCi uc004dbc.3. human.

Organism-specific databases

CTDi 1968.
GeneCardsi GC0XP024072.
HGNCi HGNC:3267. EIF2S3.
HPAi CAB012471.
MIMi 300161. gene.
neXtProti NX_P41091.
PharmGKBi PA27697.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5257.
HOVERGENi HBG006123.
InParanoidi P41091.
KOi K03242.
OMAi YRSDKED.
OrthoDBi EOG7H1JK8.
PhylomeDBi P41091.
TreeFami TF101513.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi EIF2S3. human.
GeneWikii EIF2S3.
GenomeRNAii 1968.
NextBioi 7979.
PROi P41091.
SOURCEi Search...

Gene expression databases

Bgeei P41091.
CleanExi HS_EIF2S3.
Genevestigatori P41091.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR000795. 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 ]
Pfami PF09173. eIF2_C. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 138 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

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