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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-Experimental evidence at protein leveli

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

Catalytic activityi

GTP + H2O = GDP + phosphate.2 Publications

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
Metal bindingi415Monovalent cationBy similarity1
Metal bindingi419MagnesiumBy similarity1
Binding sitei431GTPBy similarity1
Metal bindingi437Monovalent cation; via carboxylate oxygenBy similarity1
Metal bindingi439MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi415 – 420GTP1 Publication6
Nucleotide bindingi437 – 439GTPBy similarity3
Nucleotide bindingi530 – 533GTP1 Publication4
Nucleotide bindingi599 – 600GTP1 Publication2

GO - Molecular functioni

  • GTPase activity Source: SGD
  • GTP binding Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • ribosome binding Source: SGD
  • translation initiation factor activity Source: SGD
  • translation initiation factor binding Source: SGD

GO - Biological processi

  • formation of cytoplasmic translation initiation complex Source: SGD
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • regulation of translational initiation Source: SGD
  • ribosome assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

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.

Names & Taxonomyi

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
Gene namesi
Name:FUN121 Publication
Ordered Locus Names:YAL035WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL035W.
SGDiS000000033. FUN12.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic stress granule Source: SGD
  • cytosolic small ribosomal subunit Source: SGD
  • eukaryotic 48S preinitiation complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001372961 – 1002Eukaryotic translation initiation factor 5BAdd BLAST1002

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei405PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39730.
PRIDEiP39730.

PTM databases

iPTMnetiP39730.

Interactioni

GO - Molecular functioni

  • translation initiation factor binding Source: SGD

Protein-protein interaction databases

BioGridi31730. 82 interactors.
DIPiDIP-3790N.
IntActiP39730. 51 interactors.
MINTiMINT-508011.

Structurei

Secondary structure

11002
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi407 – 411Combined sources5
Helixi414 – 416Combined sources3
Helixi421 – 425Combined sources5
Beta strandi428 – 430Combined sources3
Beta strandi439 – 441Combined sources3
Beta strandi442 – 448Combined sources7
Helixi449 – 456Combined sources8
Helixi457 – 461Combined sources5
Beta strandi469 – 475Combined sources7
Beta strandi478 – 480Combined sources3
Helixi481 – 483Combined sources3
Helixi487 – 489Combined sources3
Helixi490 – 493Combined sources4
Beta strandi495 – 502Combined sources8
Turni503 – 505Combined sources3
Helixi509 – 521Combined sources13
Beta strandi525 – 530Combined sources6
Helixi532 – 534Combined sources3
Helixi546 – 551Combined sources6
Helixi555 – 573Combined sources19
Turni574 – 576Combined sources3
Beta strandi578 – 581Combined sources4
Helixi582 – 584Combined sources3
Turni588 – 590Combined sources3
Beta strandi591 – 596Combined sources6
Turni599 – 601Combined sources3
Helixi605 – 619Combined sources15
Turni621 – 624Combined sources4
Beta strandi631 – 640Combined sources10
Turni641 – 643Combined sources3
Beta strandi644 – 657Combined sources14
Beta strandi661 – 666Combined sources6
Beta strandi669 – 681Combined sources13
Helixi685 – 688Combined sources4
Beta strandi692 – 709Combined sources18
Beta strandi720 – 723Combined sources4
Beta strandi726 – 728Combined sources3
Helixi730 – 746Combined sources17
Beta strandi750 – 752Combined sources3
Beta strandi755 – 761Combined sources7
Helixi762 – 774Combined sources13
Beta strandi779 – 781Combined sources3
Beta strandi784 – 787Combined sources4
Helixi789 – 796Combined sources8
Helixi798 – 801Combined sources4
Helixi803 – 805Combined sources3
Beta strandi807 – 812Combined sources6
Helixi817 – 826Combined sources10
Beta strandi829 – 835Combined sources7
Helixi836 – 851Combined sources16
Beta strandi866 – 879Combined sources14
Beta strandi881 – 892Combined sources12
Beta strandi896 – 903Combined sources8
Turni904 – 907Combined sources4
Beta strandi908 – 922Combined sources15
Beta strandi925 – 931Combined sources7
Beta strandi939 – 944Combined sources6
Turni954 – 956Combined sources3
Beta strandi963 – 965Combined sources3
Helixi969 – 974Combined sources6
Helixi978 – 981Combined sources4
Helixi986 – 999Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP39730.
SMRiP39730.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini403 – 621tr-type GPROSITE-ProRule annotationAdd BLAST219

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Compositional biasi361 – 371Poly-GluAdd BLAST11

Sequence similaritiesi

Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00730000111064.
HOGENOMiHOG000105770.
InParanoidiP39730.
KOiK03243.
OMAiRQQNEDV.
OrthoDBiEOG092C11L7.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i1A496195DAE1C283
GO

Sequence cautioni

The sequence AAA57228 differs from that shown. Reason: Frameshift at positions 29, 167, 176, 449, 470 and 1001.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
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.

Genome annotation databases

EnsemblFungiiYAL035W; YAL035W; YAL035W.
GeneIDi851196.
KEGGisce:YAL035W.

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:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP39730.
SMRiP39730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31730. 82 interactors.
DIPiDIP-3790N.
IntActiP39730. 51 interactors.
MINTiMINT-508011.

PTM databases

iPTMnetiP39730.

Proteomic databases

MaxQBiP39730.
PRIDEiP39730.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL035W; YAL035W; YAL035W.
GeneIDi851196.
KEGGisce:YAL035W.

Organism-specific databases

EuPathDBiFungiDB:YAL035W.
SGDiS000000033. FUN12.

Phylogenomic databases

GeneTreeiENSGT00730000111064.
HOGENOMiHOG000105770.
InParanoidiP39730.
KOiK03243.
OMAiRQQNEDV.
OrthoDBiEOG092C11L7.

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

PROiP39730.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIF2P_YEAST
AccessioniPrimary (citable) accession number: P39730
Secondary accession number(s): D6VPI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 13400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: 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.