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Q2VIR3

- IF2GL_HUMAN

UniProt

Q2VIR3 - IF2GL_HUMAN

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Protein
Putative eukaryotic translation initiation factor 2 subunit 3-like protein
Gene
EIF2S3L
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5 - Protein uncertaini

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 By similarity.

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: InterPro
  3. translation initiation factor activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative eukaryotic translation initiation factor 2 subunit 3-like protein
    Alternative name(s):
    Eukaryotic translation initiation factor 2 subunit gamma A
    Short name:
    eIF-2-gamma A
    Short name:
    eIF-2gA
    Gene namesi
    Name:EIF2S3L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed By similarity
    Chaini2 – 472471Putative eukaryotic translation initiation factor 2 subunit 3-like protein
    PRO_0000343941Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ2VIR3.
    PaxDbiQ2VIR3.
    PRIDEiQ2VIR3.

    PTM databases

    PhosphoSiteiQ2VIR3.

    Expressioni

    Gene expression databases

    BgeeiQ2VIR3.
    GenevestigatoriQ2VIR3.

    Organism-specific databases

    HPAiCAB012471.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiQ2VIR3. 2 interactions.
    STRINGi9606.ENSP00000323063.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2VIR3.
    SMRiQ2VIR3. Positions 37-460.

    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.
    HOGENOMiHOG000229292.
    HOVERGENiHBG006123.
    InParanoidiQ2VIR3.
    OMAiTEQHEAI.
    PhylomeDBiQ2VIR3.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q2VIR3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV    50
    AHGKSTVVKA ISGVHTVRFK NELERNITIK LGYANAKIYQ LDDPSCPRPE 100
    CYRSCGSSMP DEFPTDIPGT KGNFRLVRHV SFVDCPGHDI LMATMLNGAA 150
    VMDAALLLIA GNESCPQPQT SEHLAAIEIM KLKHILILQN KIDLVKERQA 200
    KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV KKIPVPPRDF 250
    TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQETEVRPGI 300
    VSKDSEGKLM CKSIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA 350
    DRMVGQILGA VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK 400
    NEVLMVNIGS LSTGGRVSAV KADLGKIVLT NPVCTEVGEK IALSRRVEKH 450
    WRLIGWGQIR RGVTIKPTVD DD 472

    Note: No experimental confirmation available.

    Length:472
    Mass (Da):51,229
    Last modified:July 22, 2008 - v2
    Checksum:i6ECFD47900903ED9
    GO
    Isoform 2 (identifier: Q2VIR3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         437-472: VGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD → IHLIHLDLIKELEWGPLLTNETQRKSAANF

    Note: No experimental confirmation available.

    Show »
    Length:466
    Mass (Da):50,544
    Checksum:i8B418E91C29E7045
    GO

    Sequence cautioni

    The sequence CAA07331.1 differs from that shown. Reason: Frameshift at position 304.
    The sequence ABB92405.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei437 – 47236VGEKI…TVDDD → IHLIHLDLIKELEWGPLLTN ETQRKSAANF in isoform 2.
    VSP_034711Add
    BLAST

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 2431I → F in ABB92405. 1 Publication
    Sequence conflicti258 – 2581V → G in CAA07331. 1 Publication
    Sequence conflicti279 – 2791A → T in CAA07331. 1 Publication
    Sequence conflicti292 – 2921Q → H in CAA07331. 1 Publication
    Sequence conflicti300 – 3001I → L in CAA07331. 1 Publication
    Sequence conflicti313 – 3131S → P in ABB92405. 1 Publication
    Sequence conflicti313 – 3131S → P in AAH87847. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ120619 Genomic DNA. Translation: ABB92405.1. Sequence problems.
    AC068775 Genomic DNA. No translation available.
    BC087847 mRNA. Translation: AAH87847.1.
    AJ006932 Genomic DNA. Translation: CAA07331.1. Frameshift.
    UniGeneiHs.539684.

    Polymorphism databases

    DMDMi205830883.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ120619 Genomic DNA. Translation: ABB92405.1 . Sequence problems.
    AC068775 Genomic DNA. No translation available.
    BC087847 mRNA. Translation: AAH87847.1 .
    AJ006932 Genomic DNA. Translation: CAA07331.1 . Frameshift.
    UniGenei Hs.539684.

    3D structure databases

    ProteinModelPortali Q2VIR3.
    SMRi Q2VIR3. Positions 37-460.
    ModBasei Search...

    Protein-protein interaction databases

    IntActi Q2VIR3. 2 interactions.
    STRINGi 9606.ENSP00000323063.

    PTM databases

    PhosphoSitei Q2VIR3.

    Polymorphism databases

    DMDMi 205830883.

    Proteomic databases

    MaxQBi Q2VIR3.
    PaxDbi Q2VIR3.
    PRIDEi Q2VIR3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    GeneCardsi GC12P010558.
    H-InvDB HIX0036834.
    HPAi CAB012471.
    neXtProti NX_Q2VIR3.

    Phylogenomic databases

    eggNOGi COG5257.
    HOGENOMi HOG000229292.
    HOVERGENi HBG006123.
    InParanoidi Q2VIR3.
    OMAi TEQHEAI.
    PhylomeDBi Q2VIR3.

    Gene expression databases

    Bgeei Q2VIR3.
    Genevestigatori Q2VIR3.

    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. "Emergence of young human genes after a burst of retroposition in primates."
      Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.
      PLoS Biol. 3:E357-E357(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EVOLUTIONARY ANALYSIS.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] OF 2-471 (ISOFORM 2).
      Tissue: Testis.
    4. "Characterization of genes encoding translation initiation factor eIF-2gamma in mouse and human: sex chromosome localization, escape from X-inactivation and evolution."
      Ehrmann I.E., Ellis P.S., Mazeyrat S., Duthie S., Brockdorff N., Mattei M.-G., Gavin M.A., Affara N.A., Brown G.M., Simpson E., Mitchell M.J., Scott D.M.
      Hum. Mol. Genet. 7:1725-1737(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-309.

    Entry informationi

    Entry nameiIF2GL_HUMAN
    AccessioniPrimary (citable) accession number: Q2VIR3
    Secondary accession number(s): Q5I0X0, Q6KF84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: July 22, 2008
    Last modified: September 3, 2014
    This is version 71 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Translation initiation factors
      List of translation initiation factor entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi