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P23301

- IF5A1_YEAST

UniProt

P23301 - IF5A1_YEAST

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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

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. ribosome binding Source: SGD
  2. RNA binding Source: SGD
  3. translation elongation factor activity Source: SGD
  4. translation initiation factor activity Source: SGD

GO - Biological processi

  1. peptidyl-lysine modification to peptidyl-hypusine Source: InterPro
  2. positive regulation of cytoplasmic translational elongation through polyproline stretches Source: SGD
  3. positive regulation of translational elongation Source: SGD
  4. positive regulation of translational initiation Source: SGD
  5. positive regulation of translational termination Source: SGD
  6. translational frameshifting Source: SGD
  7. translational initiation Source: GOC
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP23301.
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

        10         20         30         40         50
MSDEEHTFET ADAGSSATYP MQCSALRKNG FVVIKSRPCK IVDMSTSKTG
60 70 80 90 100
KHGHAKVHLV AIDIFTGKKL EDLSPSTHNM EVPVVKRNEY QLLDIDDGFL
110 120 130 140 150
SLMNMDGDTK DDVKAPEGEL GDSLQTAFDE GKDLMVTIIS AMGEEAAISF

KEAARTD
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.
InParanoidi P23301.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 146 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