Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 180 (16 Oct 2019)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Eukaryotic translation initiation factor 5B

Gene

FUN12

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

Plays a role in translation initiation (PubMed:9624054). Translational GTPase that catalyzes the joining of the 40S and 60S subunits to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon (PubMed:12507428, PubMed:12471154, PubMed:12008673). GTP binding and hydrolysis induces conformational changes in the enzyme that renders it active for productive interactions with the ribosome (PubMed:25478828). The release of the enzyme after formation of the initiation complex is a prerequisite to form elongation-competent ribosomes (PubMed:12507428, PubMed:18976658, PubMed:19029250). Stimulates 20S pre-rRNA cleavage to mature 18S rRNA by PIN-domain endonuclease NOB1 (PubMed:22751017).8 Publications

Miscellaneous

Present with 13400 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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

a monovalent cation1 PublicationNote: Binds 1 monovalent cation per monomer. Structural cofactor stabilizing the GTP-bound 'on' state. May also act as a transition state stabilizer of the hydrolysis reaction.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi415Monovalent cationBy similarity1
Metal bindingi419MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei431GTPBy similarity1
Metal bindingi437Monovalent cation; via carbonyl oxygenBy similarity1
Metal bindingi439MagnesiumBy similarity1

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 bindingi415 – 420GTP1 Publication6
Nucleotide bindingi437 – 439GTPBy similarity3
Nucleotide bindingi530 – 533GTP1 Publication4
Nucleotide bindingi599 – 600GTP1 Publication2

<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 functionHydrolase, Initiation factor
Biological processProtein biosynthesis
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-28845-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.5.3 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-72706 GTP hydrolysis and joining of the 60S ribosomal subunit

<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:
Eukaryotic translation initiation factor 5B1 Publication (EC:3.6.5.32 Publications)
Short name:
eIF-5B1 Publication
Alternative name(s):
Translation initiation factor IF-21 Publication
<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:FUN121 Publication
Ordered Locus Names:YAL035WImported
<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> Componenti: Chromosome I

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YAL035W

Saccharomyces Genome Database

More...
SGDi
S000000033 FUN12

<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>Mutagenesisi439T → A: Impairs the GTPase activity, but not the ribosome joining function. 1 Publication1
Mutagenesisi479G → A: Reduces GTP binding and impairs subunit joining and ribosome-dependent GTP hydrolysis. 1 Publication1
Mutagenesisi480H → E: Impairs the GTPase activity, but not the ribosome joining function. 2 Publications1

<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 ‘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_00001372961 – 1002Eukaryotic translation initiation factor 5BAdd BLAST1002

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 residuei405PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P39730

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

More...
PaxDbi
P39730

PRoteomics IDEntifications database

More...
PRIDEi
P39730

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P39730

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P39730

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31730, 103 interactors

Database of interacting proteins

More...
DIPi
DIP-3790N

Protein interaction database and analysis system

More...
IntActi
P39730, 58 interactors

Molecular INTeraction database

More...
MINTi
P39730

STRING: functional protein association networks

More...
STRINGi
4932.YAL035W

<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

11002
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
P39730

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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>Domaini403 – 621tr-type GPROSITE-ProRule annotationAdd BLAST219

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni412 – 419G1PROSITE-ProRule annotation8
Regioni437 – 441G2PROSITE-ProRule annotation5
Regioni476 – 479G3PROSITE-ProRule annotation4
Regioni530 – 533G4PROSITE-ProRule annotation4
Regioni598 – 600G5PROSITE-ProRule annotation3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi361 – 371Poly-GluAdd BLAST11

<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
HOG000105770

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P39730

KEGG Orthology (KO)

More...
KOi
K03243

Identification of Orthologs from Complete Genome Data

More...
OMAi
SMDDWKL

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.10050, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004161 EFTu-like_2
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR000795 TF_GTP-bd_dom
IPR015760 TIF_IF2
IPR023115 TIF_IF2_dom3
IPR036925 TIF_IF2_dom3_sf
IPR009000 Transl_B-barrel_sf

The PANTHER Classification System

More...
PANTHERi
PTHR43381 PTHR43381, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit
PF11987 IF-2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00315 ELONGATNFCT

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50447 SSF50447, 1 hit
SSF52156 SSF52156, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51722 G_TR_2, 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.

P39730-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKKSKKNQQ NYWDEEFEED AAQNEEISAT PTPNPESSAG ADDTSREASA
60 70 80 90 100
SAEGAEAIEG DFMSTLKQSK KKQEKKVIEE KKDGKPILKS KKEKEKEKKE
110 120 130 140 150
KEKQKKKEQA ARKKAQQQAQ KEKNKELNKQ NVEKAAAEKA AAEKSQKSKG
160 170 180 190 200
ESDKPSASAK KPAKKVPAGL AALRRQLELK KQLEEQEKLE REEEERLEKE
210 220 230 240 250
EEERLANEEK MKEEAKAAKK EKEKAKREKR KAEGKLLTRK QKEEKKLLER
260 270 280 290 300
RRAALLSSGN VKVAGLAKKD GEENKPKKVV YSKKKKRTTQ ENASEAIKSD
310 320 330 340 350
SKKDSEVVPD DELKESEDVL IDDWENLALG DDDEEGTNEE TQESTASHEN
360 370 380 390 400
EDQNQGEEEE EGEEEEEEEE ERAHVHEVAK STPAATPAAT PTPSSASPNK
410 420 430 440 450
KDLRSPICCI LGHVDTGKTK LLDKIRQTNV QGGEAGGITQ QIGATYFPID
460 470 480 490 500
AIKAKTKVMA EYEKQTFDVP GLLVIDTPGH ESFSNLRSRG SSLCNIAILV
510 520 530 540 550
IDIMHGLEQQ TIESIKLLRD RKAPFVVALN KIDRLYDWKA IPNNSFRDSF
560 570 580 590 600
AKQSRAVQEE FQSRYSKIQL ELAEQGLNSE LYFQNKNMSK YVSIVPTSAV
610 620 630 640 650
TGEGVPDLLW LLLELTQKRM SKQLMYLSHV EATILEVKVV EGFGTTIDVI
660 670 680 690 700
LSNGYLREGD RIVLCGMNGP IVTNIRALLT PQPLRELRLK SEYVHHKEVK
710 720 730 740 750
AALGVKIAAN DLEKAVSGSR LLVVGPEDDE DELMDDVMDD LTGLLDSVDT
760 770 780 790 800
TGKGVVVQAS TLGSLEALLD FLKDMKIPVM SIGLGPVYKR DVMKASTMLE
810 820 830 840 850
KAPEYAVMLC FDVKVDKEAE QYAEQEGIKI FNADVIYHLF DSFTAYQEKL
860 870 880 890 900
LEERRKDFLD YAIFPCVLQT LQIINKRGPM IIGVDVLEGT LRVGTPICAV
910 920 930 940 950
KTDPTTKERQ TLILGKVISL EINHQPVQEV KKGQTAAGVA VRLEDPSGQQ
960 970 980 990 1000
PIWGRHVDEN DTLYSLVSRR SIDTLKDKAF RDQVARSDWL LLKKLKVVFG

IE
Length:1,002
Mass (Da):112,268
Last modified:October 1, 1996 - v2
<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:i1A496195DAE1C283
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA57228 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti266L → V in AAA57228 (PubMed:8076820).Curated1
Sequence conflicti293A → S in AAA57228 (PubMed:8076820).Curated1
Sequence conflicti460A → D in AAA57228 (PubMed:8076820).Curated1
Sequence conflicti471G → R in AAA57228 (PubMed:8076820).Curated1
Sequence conflicti641E → Q in AAA57228 (PubMed:8076820).Curated1
Sequence conflicti722L → H in AAA57228 (PubMed:8076820).Curated1
Sequence conflicti970R → T in AAA57228 (PubMed:8076820).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U12980 Genomic DNA Translation: AAC04996.1
L29389 Genomic DNA Translation: AAA57228.1 Frameshift.
BK006935 Genomic DNA Translation: DAA06952.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S70292

NCBI Reference Sequences

More...
RefSeqi
NP_009365.1, NM_001178180.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YAL035W_mRNA; YAL035W; YAL035W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851196

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YAL035W

<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
U12980 Genomic DNA Translation: AAC04996.1
L29389 Genomic DNA Translation: AAA57228.1 Frameshift.
BK006935 Genomic DNA Translation: DAA06952.1
PIRiS70292
RefSeqiNP_009365.1, NM_001178180.1

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
3WBIX-ray2.35A401-1002[»]
3WBJX-ray2.50A401-855[»]
3WBKX-ray3.30A/B401-1002[»]
4N3SX-ray1.83A/B399-852[»]
4NCFX-ray3.02A/B399-852[»]
4V8Yelectron microscopy4.30CP401-739[»]
4V8Zelectron microscopy6.60CV401-739[»]
SMRiP39730
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31730, 103 interactors
DIPiDIP-3790N
IntActiP39730, 58 interactors
MINTiP39730
STRINGi4932.YAL035W

PTM databases

CarbonylDBiP39730
iPTMnetiP39730

Proteomic databases

MaxQBiP39730
PaxDbiP39730
PRIDEiP39730

Genome annotation databases

EnsemblFungiiYAL035W_mRNA; YAL035W; YAL035W
GeneIDi851196
KEGGisce:YAL035W

Organism-specific databases

EuPathDBiFungiDB:YAL035W
SGDiS000000033 FUN12

Phylogenomic databases

HOGENOMiHOG000105770
InParanoidiP39730
KOiK03243
OMAiSMDDWKL

Enzyme and pathway databases

BioCyciYEAST:G3O-28845-MONOMER
BRENDAi3.6.5.3 984
ReactomeiR-SCE-72706 GTP hydrolysis and joining of the 60S ribosomal subunit

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P39730

Family and domain databases

Gene3Di3.40.50.10050, 1 hit
InterProiView protein in InterPro
IPR004161 EFTu-like_2
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR000795 TF_GTP-bd_dom
IPR015760 TIF_IF2
IPR023115 TIF_IF2_dom3
IPR036925 TIF_IF2_dom3_sf
IPR009000 Transl_B-barrel_sf
PANTHERiPTHR43381 PTHR43381, 1 hit
PfamiView protein in Pfam
PF00009 GTP_EFTU, 1 hit
PF03144 GTP_EFTU_D2, 1 hit
PF11987 IF-2, 1 hit
PRINTSiPR00315 ELONGATNFCT
SUPFAMiSSF50447 SSF50447, 1 hit
SSF52156 SSF52156, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51722 G_TR_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiIF2P_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: P39730
Secondary accession number(s): D6VPI2
<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: February 1, 1995
Last sequence update: October 1, 1996
Last modified: October 16, 2019
This is version 180 of the entry and version 2 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, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again