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P20042

- IF2B_HUMAN

UniProt

P20042 - IF2B_HUMAN

Protein

Eukaryotic translation initiation factor 2 subunit 2

Gene

EIF2S2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      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
    Zinc fingeri281 – 30525C4-typeSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. RNA binding Source: ProtInc
    5. translation factor activity, nucleic acid binding Source: ProtInc
    6. translation initiation factor activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. in utero embryonic development Source: Ensembl
    4. male germ cell proliferation Source: Ensembl
    5. male gonad development Source: Ensembl
    6. translation Source: Reactome
    7. translational initiation Source: Reactome

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    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 2
    Alternative name(s):
    Eukaryotic translation initiation factor 2 subunit beta
    Short name:
    eIF-2-beta
    Gene namesi
    Name:EIF2S2
    Synonyms:EIF2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:3266. EIF2S2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic translation initiation factor 2 complex Source: ProtInc

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27696.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 333332Eukaryotic translation initiation factor 2 subunit 2PRO_0000137406Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei2 – 21Phosphoserine3 Publications
    Modified residuei13 – 131PhosphoserineBy similarity
    Modified residuei67 – 671Phosphoserine2 Publications
    Modified residuei105 – 1051Phosphoserine2 Publications
    Modified residuei111 – 1111Phosphothreonine2 Publications
    Modified residuei158 – 1581Phosphoserine1 Publication
    Modified residuei218 – 2181PhosphoserineBy similarity
    Modified residuei265 – 2651N6-acetyllysine1 Publication
    Modified residuei293 – 2931N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP20042.
    PRIDEiP20042.

    PTM databases

    PhosphoSiteiP20042.

    Expressioni

    Gene expression databases

    ArrayExpressiP20042.
    BgeeiP20042.
    CleanExiHS_EIF2S2.
    GenevestigatoriP20042.

    Organism-specific databases

    HPAiCAB034415.
    HPA041262.

    Interactioni

    Subunit structurei

    Heterotrimer composed of an alpha, a beta and a gamma chain. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF2S1P051986EBI-711977,EBI-1056162
    EIF2S3P410913EBI-711977,EBI-1054228
    EIF4G2P783444EBI-711977,EBI-296519

    Protein-protein interaction databases

    BioGridi114411. 33 interactions.
    IntActiP20042. 22 interactions.
    MINTiMINT-5004121.
    STRINGi9606.ENSP00000364119.

    Structurei

    3D structure databases

    ProteinModelPortaliP20042.
    SMRiP20042. Positions 174-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi14 – 218Poly-Lys
    Compositional biasi79 – 879Poly-Lys
    Compositional biasi124 – 1296Poly-Lys

    Sequence similaritiesi

    Belongs to the eIF-2-beta/eIF-5 family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri281 – 30525C4-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    HOGENOMiHOG000107198.
    HOVERGENiHBG000927.
    InParanoidiP20042.
    KOiK03238.
    OMAiPTEDKDM.
    OrthoDBiEOG71ZP2X.
    PhylomeDBiP20042.
    TreeFamiTF101503.

    Family and domain databases

    Gene3Di3.30.30.50. 1 hit.
    InterProiIPR002735. Transl_init_fac_IF2/IF5.
    IPR016189. Transl_init_fac_IF2/IF5_N.
    IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
    [Graphical view]
    PfamiPF01873. eIF-5_eIF-2B. 1 hit.
    [Graphical view]
    SMARTiSM00653. eIF2B_5. 1 hit.
    [Graphical view]
    SUPFAMiSSF100966. SSF100966. 1 hit.
    SSF75689. SSF75689. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P20042-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE    50
    DKDLEADEED TRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD 100
    LKIESDVQEP TEPEDDLDIM LGNKKKKKKN VKFPDEDEIL EKDEALEDED 150
    NKKDDGISFS NQTGPAWAGS ERDYTYEELL NRVFNIMREK NPDMVAGEKR 200
    KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL LAELGTSGSI 250
    DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL 300
    QCETCHSRCS VASIKTGFQA VTGKRAQLRA KAN 333
    Length:333
    Mass (Da):38,388
    Last modified:December 1, 2000 - v2
    Checksum:i3E9FD4B48AA61A51
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti295 – 2951T → I in AAA52383. (PubMed:3044606)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti177 – 1771E → D.1 Publication
    Corresponds to variant rs17856024 [ dbSNP | Ensembl ].
    VAR_048909

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29536 mRNA. Translation: AAA52383.1.
    AL031668 Genomic DNA. Translation: CAB43741.1.
    BC000461 mRNA. Translation: AAH00461.1.
    BC000934 mRNA. Translation: AAH00934.1.
    CCDSiCCDS13231.1.
    PIRiA31226.
    RefSeqiNP_003899.2. NM_003908.3.
    UniGeneiHs.429180.

    Genome annotation databases

    EnsembliENST00000374980; ENSP00000364119; ENSG00000125977.
    GeneIDi8894.
    KEGGihsa:8894.
    UCSCiuc002xaf.3. human.

    Polymorphism databases

    DMDMi12644154.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29536 mRNA. Translation: AAA52383.1 .
    AL031668 Genomic DNA. Translation: CAB43741.1 .
    BC000461 mRNA. Translation: AAH00461.1 .
    BC000934 mRNA. Translation: AAH00934.1 .
    CCDSi CCDS13231.1.
    PIRi A31226.
    RefSeqi NP_003899.2. NM_003908.3.
    UniGenei Hs.429180.

    3D structure databases

    ProteinModelPortali P20042.
    SMRi P20042. Positions 174-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114411. 33 interactions.
    IntActi P20042. 22 interactions.
    MINTi MINT-5004121.
    STRINGi 9606.ENSP00000364119.

    PTM databases

    PhosphoSitei P20042.

    Polymorphism databases

    DMDMi 12644154.

    Proteomic databases

    MaxQBi P20042.
    PRIDEi P20042.

    Protocols and materials databases

    DNASUi 8894.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374980 ; ENSP00000364119 ; ENSG00000125977 .
    GeneIDi 8894.
    KEGGi hsa:8894.
    UCSCi uc002xaf.3. human.

    Organism-specific databases

    CTDi 8894.
    GeneCardsi GC20M032676.
    HGNCi HGNC:3266. EIF2S2.
    HPAi CAB034415.
    HPA041262.
    MIMi 603908. gene.
    neXtProti NX_P20042.
    PharmGKBi PA27696.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000107198.
    HOVERGENi HBG000927.
    InParanoidi P20042.
    KOi K03238.
    OMAi PTEDKDM.
    OrthoDBi EOG71ZP2X.
    PhylomeDBi P20042.
    TreeFami TF101503.

    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 EIF2S2. human.
    GeneWikii EIF2S2.
    GenomeRNAii 8894.
    NextBioi 33403.
    PROi P20042.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20042.
    Bgeei P20042.
    CleanExi HS_EIF2S2.
    Genevestigatori P20042.

    Family and domain databases

    Gene3Di 3.30.30.50. 1 hit.
    InterProi IPR002735. Transl_init_fac_IF2/IF5.
    IPR016189. Transl_init_fac_IF2/IF5_N.
    IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
    [Graphical view ]
    Pfami PF01873. eIF-5_eIF-2B. 1 hit.
    [Graphical view ]
    SMARTi SM00653. eIF2B_5. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100966. SSF100966. 1 hit.
    SSF75689. SSF75689. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the beta subunit of translational initiation factor eIF-2."
      Pathak V.K., Nielsen P.J., Trachsel H., Hershey J.W.B.
      Cell 54:633-639(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [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], VARIANT ASP-177.
      Tissue: Lung and Placenta.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND THR-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67 AND SER-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67; SER-105 AND THR-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIF2B_HUMAN
    AccessioniPrimary (citable) accession number: P20042
    Secondary accession number(s): Q9BVU0, Q9UJE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 155 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 20
      Human chromosome 20: 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