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P23301

- IF5A1_YEAST

UniProt

P23301 - IF5A1_YEAST

Protein

Eukaryotic translation initiation factor 5A-1

Gene

HYP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Essential for polarized growth, a process necessary for G1/S transition. May mediate large range of effects of the polyamine spermidine in the cell.9 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ribosome binding Source: SGD
    3. RNA binding Source: SGD
    4. translation elongation factor activity Source: SGD
    5. translation initiation factor activity Source: SGD

    GO - Biological processi

    1. peptidyl-lysine modification to peptidyl-hypusine Source: InterPro
    2. positive regulation of translational elongation Source: SGD
    3. positive regulation of translational initiation Source: SGD
    4. positive regulation of translational termination Source: SGD
    5. translational frameshifting Source: SGD
    6. translational initiation Source: GOC

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30156-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 5A-1
    Short name:
    eIF-5A-1
    Alternative name(s):
    Hypusine-containing protein HP2
    eIF-4D
    Gene namesi
    Name:HYP2
    Synonyms:TIF51A
    Ordered Locus Names:YEL034W
    ORF Names:SYGP-ORF21
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    SGDiS000000760. HYP2.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Concentrates in the perinuclear region.

    GO - Cellular componenti

    1. cytosolic ribosome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi22 – 221Q → H: Temperature-sensitive growth phenotype; when associated with F-93. 1 Publication
    Mutagenesisi24 – 241S → P: Temperature-sensitive growth phenotype. 1 Publication
    Mutagenesisi39 – 391C → Y: Temperature-sensitive growth phenotype. Lethal; when associated with L-83 and D-118 or with I-66 and D-118 or with D-118 and I-142 or with L-116 and D-118. 2 Publications
    Mutagenesisi50 – 501G → A or P: Lethal. 1 Publication
    Mutagenesisi51 – 511K → R: Impairs association to the ribosome and cell growth. 5 Publications
    Mutagenesisi52 – 521H → A or D: Lethal. 1 Publication
    Mutagenesisi53 – 531G → A or D: Lethal. 1 Publication
    Mutagenesisi54 – 541H → D: Lethal. 1 Publication
    Mutagenesisi56 – 561K → A: Temperature-sensitive growth phenotype. 1 Publication
    Mutagenesisi56 – 561K → D: Lethal. 1 Publication
    Mutagenesisi57 – 571V → D: Temperature-sensitive growth phenotype. 1 Publication
    Mutagenesisi63 – 631D → V: Impairs programmed ribosomal frameshifting. 1 Publication
    Mutagenesisi66 – 661T → I: Temperature-sensitive growth phenotype. Lethal; when associated with Y-39 and D-118. 1 Publication
    Mutagenesisi83 – 831P → S or L: Temperature-sensitive growth phenotype. Lethal; when associated with Y-39 and D-118. 2 Publications
    Mutagenesisi93 – 931L → F: Lethal. 1 Publication
    Mutagenesisi102 – 1021L → A: Temperature-sensitive growth phenotype. 1 Publication
    Mutagenesisi116 – 1161P → L: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. 1 Publication
    Mutagenesisi118 – 1181G → D: Temperature-sensitive growth phenotype; when associated with L-116 or W-122 or F-140 or I-142. Lethal; when associated with Y-39 and I-66 or with Y-39 and L-83 or with Y-39 and L-116 or with Y-39 and F-140 or with Y-39 and I-142 or with N-120 and D-124. 1 Publication
    Mutagenesisi118 – 1181G → V: Temperature-sensitive growth phenotype; when associated with W-122. 1 Publication
    Mutagenesisi120 – 1201L → N: Lethal; when associated with D-118 and D-124. 1 Publication
    Mutagenesisi122 – 1221D → W: Temperature-sensitive growth phenotype; when associated with V-118. 1 Publication
    Mutagenesisi124 – 1241L → D: Lethal; when associated with D-118 and N-120. 1 Publication
    Mutagenesisi140 – 1401S → F: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. 1 Publication
    Mutagenesisi142 – 1421M → I: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. 1 Publication
    Mutagenesisi149 – 1491S → P in ts1159; temperature-sensitive growth phenotype and impairs programmed ribosomal frameshifting. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 157156Eukaryotic translation initiation factor 5A-1PRO_0000142488Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei2 – 21Phosphoserine6 Publications
    Modified residuei7 – 71PhosphothreonineBy similarity
    Modified residuei10 – 101Phosphothreonine1 Publication
    Modified residuei51 – 511Hypusine
    Modified residuei74 – 741Phosphoserine2 Publications

    Post-translational modificationi

    eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine).

    Keywords - PTMi

    Acetylation, Hypusine, Phosphoprotein

    Proteomic databases

    MaxQBiP23301.
    PaxDbiP23301.
    PeptideAtlasiP23301.
    PRIDEiP23301.

    2D gel databases

    SWISS-2DPAGEP23301.

    Expressioni

    Inductioni

    Expressed in aerobic conditions.1 Publication

    Gene expression databases

    GenevestigatoriP23301.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DYS1 and LIA1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DYS1P387914EBI-9033,EBI-5871
    LIA1P471202EBI-9033,EBI-25526

    Protein-protein interaction databases

    BioGridi36695. 155 interactions.
    DIPiDIP-4230N.
    IntActiP23301. 8 interactions.
    MINTiMINT-545311.
    STRINGi4932.YEL034W.

    Structurei

    Secondary structure

    1
    157
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 224
    Turni23 – 253
    Beta strandi31 – 344
    Beta strandi37 – 4711
    Beta strandi50 – 534
    Beta strandi56 – 6611
    Beta strandi70 – 8213
    Beta strandi87 – 915
    Turni96 – 994
    Beta strandi105 – 1073
    Helixi120 – 1267
    Beta strandi135 – 1417
    Beta strandi144 – 1507

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ER0X-ray3.35A/B1-157[»]
    ProteinModelPortaliP23301.
    SMRiP23301. Positions 12-157.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23301.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eIF-5A family.Curated

    Phylogenomic databases

    eggNOGiCOG0231.
    GeneTreeiENSGT00390000003738.
    HOGENOMiHOG000106270.
    KOiK03263.
    OrthoDBiEOG7WMCWW.

    Family and domain databases

    Gene3Di2.30.30.30. 1 hit.
    2.40.50.140. 1 hit.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR014722. Rib_L2_dom2.
    IPR019769. Trans_elong_IF5A_hypusine_site.
    IPR001884. Transl_elong_IF5A.
    IPR020189. Transl_elong_IF5A_C.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view]
    PANTHERiPTHR11673. PTHR11673. 1 hit.
    PfamiPF01287. eIF-5a. 1 hit.
    [Graphical view]
    PIRSFiPIRSF003025. eIF5A. 1 hit.
    SUPFAMiSSF50104. SSF50104. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00037. eIF_5A. 1 hit.
    PROSITEiPS00302. IF5A_HYPUSINE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23301-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDEEHTFET ADAGSSATYP MQCSALRKNG FVVIKSRPCK IVDMSTSKTG    50
    KHGHAKVHLV AIDIFTGKKL EDLSPSTHNM EVPVVKRNEY QLLDIDDGFL 100
    SLMNMDGDTK DDVKAPEGEL GDSLQTAFDE GKDLMVTIIS AMGEEAAISF 150
    KEAARTD 157
    Length:157
    Mass (Da):17,114
    Last modified:January 23, 2007 - v3
    Checksum:i738F29CCC7820C47
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63541 Genomic DNA. Translation: AAA35155.1.
    X56236 Genomic DNA. Translation: CAA39693.1.
    D83166 mRNA. Translation: BAA11826.1.
    U18779 Genomic DNA. Translation: AAB65008.1.
    BK006939 Genomic DNA. Translation: DAA07619.1.
    PIRiA40259. FIBYA1.
    RefSeqiNP_010880.3. NM_001178849.3.

    Genome annotation databases

    EnsemblFungiiYEL034W; YEL034W; YEL034W.
    GeneIDi856677.
    KEGGisce:YEL034W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63541 Genomic DNA. Translation: AAA35155.1 .
    X56236 Genomic DNA. Translation: CAA39693.1 .
    D83166 mRNA. Translation: BAA11826.1 .
    U18779 Genomic DNA. Translation: AAB65008.1 .
    BK006939 Genomic DNA. Translation: DAA07619.1 .
    PIRi A40259. FIBYA1.
    RefSeqi NP_010880.3. NM_001178849.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ER0 X-ray 3.35 A/B 1-157 [» ]
    ProteinModelPortali P23301.
    SMRi P23301. Positions 12-157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36695. 155 interactions.
    DIPi DIP-4230N.
    IntActi P23301. 8 interactions.
    MINTi MINT-545311.
    STRINGi 4932.YEL034W.

    2D gel databases

    SWISS-2DPAGE P23301.

    Proteomic databases

    MaxQBi P23301.
    PaxDbi P23301.
    PeptideAtlasi P23301.
    PRIDEi P23301.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YEL034W ; YEL034W ; YEL034W .
    GeneIDi 856677.
    KEGGi sce:YEL034W.

    Organism-specific databases

    SGDi S000000760. HYP2.

    Phylogenomic databases

    eggNOGi COG0231.
    GeneTreei ENSGT00390000003738.
    HOGENOMi HOG000106270.
    KOi K03263.
    OrthoDBi EOG7WMCWW.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30156-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P23301.
    NextBioi 982702.

    Gene expression databases

    Genevestigatori P23301.

    Family and domain databases

    Gene3Di 2.30.30.30. 1 hit.
    2.40.50.140. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR014722. Rib_L2_dom2.
    IPR019769. Trans_elong_IF5A_hypusine_site.
    IPR001884. Transl_elong_IF5A.
    IPR020189. Transl_elong_IF5A_C.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view ]
    PANTHERi PTHR11673. PTHR11673. 1 hit.
    Pfami PF01287. eIF-5a. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003025. eIF5A. 1 hit.
    SUPFAMi SSF50104. SSF50104. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00037. eIF_5A. 1 hit.
    PROSITEi PS00302. IF5A_HYPUSINE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae."
      Schnier J., Schwelberger H.G., Smit-Mcbride Z., Kang H.A., Hershey J.W.B.
      Mol. Cell. Biol. 11:3105-3114(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Sandholzer U.R.
      Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DBY874.
    3. "Sequence determination of cDNA encoding yeast cycloheximide sensitivity factor (CH-SF) and its plausible role at a first peptide bond formation step in the initiation process of protein synthesis."
      Kitaoka Y., Miyazaki M.
      Nucleic Acids Symp. Ser. 22:69-70(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Determination and mutational analysis of the phosphorylation site in the hypusine-containing protein Hyp2p."
      Klier H., Woehl T., Eckerskorn C., Magdolen V., Lottspeich F.
      FEBS Lett. 334:360-364(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-2.
    7. "The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes."
      Benne R., Hershey J.W.B.
      J. Biol. Chem. 253:3078-3087(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Hypusine formation in eukaryotic initiation factor 4D is not reversed when rates or specificity of protein synthesis is altered."
      Gordon E.D., Mora R., Meredith S.C., Lindquist S.L.
      J. Biol. Chem. 262:16590-16595(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: HYPUSINE FORMATION.
    9. "Translation initiation factor eIF-5A expressed from either of two yeast genes or from human cDNA. Functional identity under aerobic and anaerobic conditions."
      Schwelberger H.G., Kang H.A., Hershey J.W.B.
      J. Biol. Chem. 268:14018-14025(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Translation initiation factor eIF-5A, the hypusine-containing protein, is phosphorylated on serine in Saccharomyces cerevisiae."
      Kang H.A., Schwelberger H.G., Hershey J.W.B.
      J. Biol. Chem. 268:14750-14756(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-2.
    11. "Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae."
      Kang H.A., Hershey J.W.B.
      J. Biol. Chem. 269:3934-3940(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "A single amino acid substitution in yeast eIF-5A results in mRNA stabilization."
      Zuk D., Jacobson A.
      EMBO J. 17:2914-2925(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-149, FUNCTION.
    13. "Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor."
      Lee Y.B., Joe Y.A., Wolff E.C., Dimitriadis E.K., Park M.H.
      Biochem. J. 340:273-281(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-39 AND PRO-83.
    14. "Mapping eIF5A binding sites for Dys1 and Lia1: in vivo evidence for regulation of eIF5A hypusination."
      Thompson G.M., Cano V.S.P., Valentini S.R.
      FEBS Lett. 555:464-468(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYS1 AND LIA1.
    15. "Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity defects of a yeast eIF5A mutant."
      Zanelli C.F., Valentini S.R.
      Genetics 171:1571-1581(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    17. Cited for: FUNCTION, ASSOCIATION WITH THE 80S RIBOSOME, MUTAGENESIS OF LYS-51.
    18. "Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex."
      Jao D.L., Chen K.Y.
      J. Cell. Biochem. 97:583-598(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYS1, ASSOCIATION WITH THE 80S RIBOSOME, MUTAGENESIS OF LYS-51.
    19. "Rapid depletion of mutant eukaryotic initiation factor 5A at restrictive temperature reveals connections to actin cytoskeleton and cell cycle progression."
      Chatterjee I., Gross S.R., Kinzy T.G., Chen K.Y.
      Mol. Genet. Genomics 275:264-276(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-102, FUNCTION.
    20. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    21. "Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis."
      Dias C.A.O., Cano V.S.P., Rangel S.M., Apponi L.H., Frigieri M.C., Muniz J.R.C., Garcia W., Park M.H., Garratt R.C., Zanelli C.F., Valentini S.R.
      FEBS J. 275:1874-1888(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLN-22; SER-24; CYS-39; GLY-50; LYS-51; HIS-52; GLY-53; HIS-54; LYS-56; VAL-57; THR-66; PRO-83; LEU-93; PRO-116; GLY-118; LEU-120; ASP-122; LEU-124; SER-140; MET-142; SER-149 AND 116-PRO--ASP-157.
    22. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: FUNCTION.
    24. "Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent."
      Gentz P.M., Blatch G.L., Dorrington R.A.
      FEBS J. 276:695-706(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, MUTAGENESIS OF LYS-51.
    25. "Hypusine-containing protein eIF5A promotes translation elongation."
      Saini P., Eyler D.E., Green R., Dever T.E.
      Nature 459:118-121(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-51; ASP-63 AND SER-149.
    26. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIF5A1_YEAST
    AccessioniPrimary (citable) accession number: P23301
    Secondary accession number(s): D3DLL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two genes for eIF-5A in yeast.

    Caution

    Was originally thought (PubMed:641056) to be a translation initiation factor but further analysis (PubMed:19424157 and PubMed:19338753) clearly suggests that it is involved in translation elongation and not translation initiation. subclass.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Translation initiation factors
      List of translation initiation factor entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3