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P41091

- IF2G_HUMAN

UniProt

P41091 - IF2G_HUMAN

Protein

Eukaryotic translation initiation factor 2 subunit 3

Gene

EIF2S3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. translation factor activity, nucleic acid binding Source: UniProtKB
    5. translation initiation factor activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. GTP catabolic process Source: GOC
    4. translation Source: Reactome
    5. translational initiation Source: UniProtKB

    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

    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 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.
    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.
    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.
    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

    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: October 1, 2014
    This is version 139 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