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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: 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

  • ribosome binding Source: SGD
  • RNA binding Source: SGD
  • translation elongation factor activity Source: SGD
  • translation initiation factor activity Source: SGD

GO - Biological processi

  • positive regulation of cytoplasmic translational elongation through polyproline stretches Source: SGD
  • positive regulation of translational elongation Source: SGD
  • positive regulation of translational initiation Source: SGD
  • positive regulation of translational termination Source: SGD
  • translational frameshifting Source: SGD
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.
ReactomeiR-SCE-204626. Hypusine synthesis from eIF5A-lysine.

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
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL034W.
SGDiS000000760. HYP2.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Concentrates in the perinuclear region.

GO - Cellular componenti

  • cytosolic ribosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22Q → H: Temperature-sensitive growth phenotype; when associated with F-93. 1 Publication1
Mutagenesisi24S → P: Temperature-sensitive growth phenotype. 1 Publication1
Mutagenesisi39C → 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 Publications1
Mutagenesisi50G → A or P: Lethal. 1 Publication1
Mutagenesisi51K → R: Impairs association to the ribosome and cell growth. 5 Publications1
Mutagenesisi52H → A or D: Lethal. 1 Publication1
Mutagenesisi53G → A or D: Lethal. 1 Publication1
Mutagenesisi54H → D: Lethal. 1 Publication1
Mutagenesisi56K → A: Temperature-sensitive growth phenotype. 1 Publication1
Mutagenesisi56K → D: Lethal. 1 Publication1
Mutagenesisi57V → D: Temperature-sensitive growth phenotype. 1 Publication1
Mutagenesisi63D → V: Impairs programmed ribosomal frameshifting. 1 Publication1
Mutagenesisi66T → I: Temperature-sensitive growth phenotype. Lethal; when associated with Y-39 and D-118. 1 Publication1
Mutagenesisi83P → S or L: Temperature-sensitive growth phenotype. Lethal; when associated with Y-39 and D-118. 2 Publications1
Mutagenesisi93L → F: Lethal. 1 Publication1
Mutagenesisi102L → A: Temperature-sensitive growth phenotype. 1 Publication1
Mutagenesisi116P → L: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. 1 Publication1
Mutagenesisi118G → 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 Publication1
Mutagenesisi118G → V: Temperature-sensitive growth phenotype; when associated with W-122. 1 Publication1
Mutagenesisi120L → N: Lethal; when associated with D-118 and D-124. 1 Publication1
Mutagenesisi122D → W: Temperature-sensitive growth phenotype; when associated with V-118. 1 Publication1
Mutagenesisi124L → D: Lethal; when associated with D-118 and N-120. 1 Publication1
Mutagenesisi140S → F: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. 1 Publication1
Mutagenesisi142M → I: Temperature-sensitive growth phenotype; when associated with D-118. Lethal; when associated with Y-39 and D-118. 1 Publication1
Mutagenesisi149S → P in ts1159; temperature-sensitive growth phenotype and impairs programmed ribosomal frameshifting. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001424882 – 157Eukaryotic translation initiation factor 5A-1Add BLAST156

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources2 Publications1
Modified residuei7PhosphothreonineBy similarity1
Modified residuei10PhosphothreonineCombined sources1
Modified residuei51Hypusine1 Publication1
Modified residuei74PhosphoserineCombined sources1
Cross-linki86Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

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, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP23301.
PRIDEiP23301.
TopDownProteomicsiP23301.

2D gel databases

SWISS-2DPAGEP23301.

PTM databases

iPTMnetiP23301.

Expressioni

Inductioni

Expressed in aerobic conditions.1 Publication

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. 164 interactors.
DIPiDIP-4230N.
IntActiP23301. 8 interactors.
MINTiMINT-545311.

Structurei

Secondary structure

1157
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 22Combined sources4
Turni23 – 25Combined sources3
Beta strandi31 – 34Combined sources4
Beta strandi37 – 47Combined sources11
Beta strandi50 – 53Combined sources4
Beta strandi56 – 66Combined sources11
Beta strandi70 – 82Combined sources13
Beta strandi87 – 91Combined sources5
Turni96 – 99Combined sources4
Beta strandi105 – 107Combined sources3
Helixi120 – 126Combined sources7
Beta strandi135 – 141Combined sources7
Beta strandi144 – 150Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ER0X-ray3.35A/B1-157[»]
5DATX-ray3.15f1-157[»]
5DC3X-ray3.25f1-157[»]
5GAKelectron microscopy3.88q1-157[»]
ProteinModelPortaliP23301.
SMRiP23301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23301.

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-5A family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003738.
HOGENOMiHOG000106270.
InParanoidiP23301.
KOiK03263.
OrthoDBiEOG092C4XQW.

Family and domain databases

Gene3Di2.30.30.30. 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.
SMARTiSM01376. eIF-5a. 1 hit.
[Graphical view]
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ER0X-ray3.35A/B1-157[»]
5DATX-ray3.15f1-157[»]
5DC3X-ray3.25f1-157[»]
5GAKelectron microscopy3.88q1-157[»]
ProteinModelPortaliP23301.
SMRiP23301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36695. 164 interactors.
DIPiDIP-4230N.
IntActiP23301. 8 interactors.
MINTiMINT-545311.

PTM databases

iPTMnetiP23301.

2D gel databases

SWISS-2DPAGEP23301.

Proteomic databases

MaxQBiP23301.
PRIDEiP23301.
TopDownProteomicsiP23301.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YEL034W.
SGDiS000000760. HYP2.

Phylogenomic databases

GeneTreeiENSGT00390000003738.
HOGENOMiHOG000106270.
InParanoidiP23301.
KOiK03263.
OrthoDBiEOG092C4XQW.

Enzyme and pathway databases

BioCyciYEAST:G3O-30156-MONOMER.
ReactomeiR-SCE-204626. Hypusine synthesis from eIF5A-lysine.

Miscellaneous databases

EvolutionaryTraceiP23301.
PROiP23301.

Family and domain databases

Gene3Di2.30.30.30. 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.
SMARTiSM01376. eIF-5a. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00037. eIF_5A. 1 hit.
PROSITEiPS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 167 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.