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Entry version 226 (18 Sep 2019)
Sequence version 3 (23 Jan 2007)
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Protein

ATP-dependent RNA helicase eIF4A

Gene

TIF1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.6 Publications

Miscellaneous

TIF1 and TIF2 code for the same protein.
Present with 106000 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=470 µM for ATP2 Publications
  1. Vmax=2.6 pmol/sec/µg enzyme for ATP2 Publications

pH dependencei

Optimum pH is 6.0.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi66 – 73ATP8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, Initiation factor, RNA-binding
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31584-MONOMER
YEAST:G3O-32027-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-72662 Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S
R-SCE-72702 Ribosomal scanning and start codon recognition

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P10081

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ATP-dependent RNA helicase eIF4A (EC:3.6.4.132 Publications)
Alternative name(s):
Eukaryotic initiation factor 4A
Short name:
eIF-4A
Stimulator factor I 37 kDa component
Translation initiation factor 1/22 Publications
p37
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TIF12 Publications
Synonyms:TIF41A
Ordered Locus Names:YKR059W
AND
Name:TIF22 Publications
Synonyms:TIF41B
Ordered Locus Names:YJL138C
ORF Names:J0660
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome X, Chromosome XI

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000001767 TIF1
S000003674 TIF2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi24F → A: Lethal in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi42F → A: Slow growth in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi46S → A: Reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi49Q → A: Reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi49Q → E: Increases about 3-fold ATP binding but reduces about 2-fold ATPase activity in vitro. 1 Publication1
Mutagenesisi66A → D: Slow growth. 2 Publications1
Mutagenesisi66A → V: Lethal and dominant negative if overexpressed in vivo. Impairs ATP hydrolysis, RNA-helicase and translation activity in vitro. 2 Publications1
Mutagenesisi72K → A: Lethal in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi79A → V in TIF1-1; no growth at 36 degrees Celsius. 1 Publication1
Mutagenesisi126G → D: Lethal. 1 Publication1
Mutagenesisi127G → D: Slow growth. 1 Publication1
Mutagenesisi145G → D: Lethal. 1 Publication1
Mutagenesisi145G → S: Slow growth. 1 Publication1
Mutagenesisi170D → E: Lethal. 1 Publication1
Mutagenesisi173D → H: Lethal. 1 Publication1
Mutagenesisi311S → F: Slow growth. 1 Publication1
Mutagenesisi347R → E, G, I, S or T: Lethal and dominant negative if overexpressed. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000549682 – 395ATP-dependent RNA helicase eIF4AAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei73PhosphothreonineCombined sources1
Modified residuei77PhosphoserineCombined sources1
Modified residuei129PhosphoserineCombined sources1
Modified residuei146PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P10081

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P10081

PRoteomics IDEntifications database

More...
PRIDEi
P10081

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P10081

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P10081

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P10081

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) (By similarity).

Interacts with eIF4G1/TIF4631 and eIF4G2/TIF4632.

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
TIF4631P3993510EBI-9017,EBI-9002

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33619, 351 interactors
34190, 268 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-430 Eukaryotic translation initiation factor 4F complex, variant TIF4631
CPX-431 Eukaryotic translation initiation factor 4F complex, variant TIF4632

Database of interacting proteins

More...
DIPi
DIP-4571N

Protein interaction database and analysis system

More...
IntActi
P10081, 87 interactors

Molecular INTeraction database

More...
MINTi
P10081

STRING: functional protein association networks

More...
STRINGi
4932.YKR059W

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1395
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P10081

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P10081

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini53 – 222Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST170
Domaini233 – 394Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi22 – 50Q motifAdd BLAST29
Motifi170 – 173DEAD box4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000268797

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10081

KEGG Orthology (KO)

More...
KOi
K03257

Identification of Orthologs from Complete Genome Data

More...
OMAi
RNPIRIL

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR000629 RNA-helicase_DEAD-box_CS
IPR014014 RNA_helicase_DEAD_Q_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00270 DEAD, 1 hit
PF00271 Helicase_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00039 DEAD_ATP_HELICASE, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51195 Q_MOTIF, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P10081-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEGITDIEE SQIQTNYDKV VYKFDDMELD ENLLRGVFGY GFEEPSAIQQ
60 70 80 90 100
RAIMPIIEGH DVLAQAQSGT GKTGTFSIAA LQRIDTSVKA PQALMLAPTR
110 120 130 140 150
ELALQIQKVV MALAFHMDIK VHACIGGTSF VEDAEGLRDA QIVVGTPGRV
160 170 180 190 200
FDNIQRRRFR TDKIKMFILD EADEMLSSGF KEQIYQIFTL LPPTTQVVLL
210 220 230 240 250
SATMPNDVLE VTTKFMRNPV RILVKKDELT LEGIKQFYVN VEEEEYKYEC
260 270 280 290 300
LTDLYDSISV TQAVIFCNTR RKVEELTTKL RNDKFTVSAI YSDLPQQERD
310 320 330 340 350
TIMKEFRSGS SRILISTDLL ARGIDVQQVS LVINYDLPAN KENYIHRIGR
360 370 380 390
GGRFGRKGVA INFVTNEDVG AMRELEKFYS TQIEELPSDI ATLLN
Length:395
Mass (Da):44,697
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i19D8C133C815DD48
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X12813 Genomic DNA Translation: CAA31301.1
X12814 Genomic DNA Translation: CAA31302.1
X58099 Genomic DNA Translation: CAA41110.1
X87371 Genomic DNA Translation: CAA60817.1
Z49413 Genomic DNA Translation: CAA89433.1
U25436 Genomic DNA Translation: AAA91645.1
Z28284 Genomic DNA Translation: CAA82138.1
BK006943 Genomic DNA Translation: DAA08662.1
BK006944 Genomic DNA Translation: DAA09210.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S05835 FIBY1

NCBI Reference Sequences

More...
RefSeqi
NP_012397.1, NM_001181571.1
NP_012985.3, NM_001179849.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJL138C_mRNA; YJL138C; YJL138C
YKR059W_mRNA; YKR059W; YKR059W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853303
853933

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJL138C
sce:YKR059W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12813 Genomic DNA Translation: CAA31301.1
X12814 Genomic DNA Translation: CAA31302.1
X58099 Genomic DNA Translation: CAA41110.1
X87371 Genomic DNA Translation: CAA60817.1
Z49413 Genomic DNA Translation: CAA89433.1
U25436 Genomic DNA Translation: AAA91645.1
Z28284 Genomic DNA Translation: CAA82138.1
BK006943 Genomic DNA Translation: DAA08662.1
BK006944 Genomic DNA Translation: DAA09210.1
PIRiS05835 FIBY1
RefSeqiNP_012397.1, NM_001181571.1
NP_012985.3, NM_001179849.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FUKX-ray1.75A231-395[»]
1FUUX-ray2.50A/B2-395[»]
1QDEX-ray2.00A9-232[»]
1QVAX-ray2.50A2-224[»]
2VSOX-ray2.60A/B1-395[»]
2VSXX-ray2.80A/B1-395[»]
SMRiP10081
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi33619, 351 interactors
34190, 268 interactors
ComplexPortaliCPX-430 Eukaryotic translation initiation factor 4F complex, variant TIF4631
CPX-431 Eukaryotic translation initiation factor 4F complex, variant TIF4632
DIPiDIP-4571N
IntActiP10081, 87 interactors
MINTiP10081
STRINGi4932.YKR059W

PTM databases

CarbonylDBiP10081
iPTMnetiP10081

2D gel databases

SWISS-2DPAGEiP10081

Proteomic databases

MaxQBiP10081
PaxDbiP10081
PRIDEiP10081

Genome annotation databases

EnsemblFungiiYJL138C_mRNA; YJL138C; YJL138C
YKR059W_mRNA; YKR059W; YKR059W
GeneIDi853303
853933
KEGGisce:YJL138C
sce:YKR059W

Organism-specific databases

SGDiS000001767 TIF1
S000003674 TIF2

Phylogenomic databases

HOGENOMiHOG000268797
InParanoidiP10081
KOiK03257
OMAiRNPIRIL

Enzyme and pathway databases

BioCyciYEAST:G3O-31584-MONOMER
YEAST:G3O-32027-MONOMER
ReactomeiR-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-72662 Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S
R-SCE-72702 Ribosomal scanning and start codon recognition
SABIO-RKiP10081

Miscellaneous databases

EvolutionaryTraceiP10081

Protein Ontology

More...
PROi
PR:P10081

Family and domain databases

InterProiView protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR000629 RNA-helicase_DEAD-box_CS
IPR014014 RNA_helicase_DEAD_Q_motif
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF00271 Helicase_C, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS00039 DEAD_ATP_HELICASE, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51195 Q_MOTIF, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIF4A_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P10081
Secondary accession number(s): D6VW46
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 18, 2019
This is version 226 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
  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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
  6. Translation initiation factors
    List of translation initiation factor entries
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