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Protein

Eukaryotic translation initiation factor 3 subunit B

Gene

PRT1

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

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.UniRule annotation1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • nucleotide binding Source: InterPro
  • translation initiation factor activity Source: SGD

GO - Biological processi

  • cytoplasmic translational initiation Source: SGD
  • formation of translation preinitiation complex Source: UniProtKB-HAMAP
  • regulation of translational initiation Source: UniProtKB-HAMAP
  • translational initiation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33831-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit BUniRule annotation
Short name:
eIF3bUniRule annotation
Alternative name(s):
Cell cycle regulation and translation initiation protein
Eukaryotic translation initiation factor 3 90 kDa subunit
Short name:
eIF3 p90UniRule annotation
Translation initiation factor eIF3 p90 subunit
Gene namesi
Name:PRT1UniRule annotation
Synonyms:CDC63
Ordered Locus Names:YOR361C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR361C.
SGDiS000005888. PRT1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic stress granule Source: SGD
  • eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic 48S preinitiation complex Source: SGD
  • eukaryotic translation initiation factor 3 complex Source: SGD
  • multi-eIF complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi124 – 1307KGFLFVE → AAAAAAA: Impairs interaction with HCR1 and TIF32, impairs interaction of the eIF-3 complex with eIF-1, eIF-2 and the 40S ribosome, and impairs initiation of translation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 763763Eukaryotic translation initiation factor 3 subunit BPRO_0000123535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611PhosphoserineCombined sources
Modified residuei67 – 671PhosphotyrosineCombined sources
Modified residuei669 – 6691PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06103.
PeptideAtlasiP06103.

PTM databases

iPTMnetiP06103.

Interactioni

Subunit structurei

The eukaryotic translation initiation factor 3 (eIF-3) core complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5 and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex (MFC) that may bind to the 40S ribosome.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NIP1P324979EBI-8973,EBI-8965
RPG1P3824911EBI-8973,EBI-8981
TIF34P4021714EBI-8973,EBI-8951
TIF35Q0406710EBI-8973,EBI-8958

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi34746. 117 interactions.
DIPiDIP-2519N.
IntActiP06103. 44 interactions.
MINTiMINT-578476.

Structurei

Secondary structure

1
763
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi78 – 836Combined sources
Helixi89 – 913Combined sources
Helixi92 – 10413Combined sources
Beta strandi109 – 1135Combined sources
Turni118 – 1214Combined sources
Beta strandi125 – 1339Combined sources
Helixi134 – 14411Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi156 – 1605Combined sources
Helixi161 – 1688Combined sources
Helixi186 – 1894Combined sources
Helixi191 – 1944Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi207 – 2148Combined sources
Beta strandi224 – 23411Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi245 – 2484Combined sources
Beta strandi250 – 2578Combined sources
Turni258 – 2614Combined sources
Beta strandi262 – 2687Combined sources
Beta strandi272 – 2776Combined sources
Beta strandi283 – 2908Combined sources
Helixi305 – 3073Combined sources
Beta strandi312 – 3165Combined sources
Turni317 – 3193Combined sources
Beta strandi322 – 3265Combined sources
Beta strandi338 – 3414Combined sources
Beta strandi345 – 3528Combined sources
Beta strandi355 – 3606Combined sources
Helixi361 – 3633Combined sources
Helixi371 – 3733Combined sources
Beta strandi380 – 3834Combined sources
Beta strandi395 – 3973Combined sources
Beta strandi400 – 4078Combined sources
Beta strandi411 – 4133Combined sources
Beta strandi416 – 4227Combined sources
Beta strandi427 – 4326Combined sources
Beta strandi435 – 4439Combined sources
Beta strandi447 – 45711Combined sources
Beta strandi464 – 4729Combined sources
Beta strandi480 – 4845Combined sources
Beta strandi486 – 4949Combined sources
Beta strandi501 – 5066Combined sources
Beta strandi519 – 5279Combined sources
Beta strandi538 – 54710Combined sources
Beta strandi551 – 5544Combined sources
Beta strandi558 – 5658Combined sources
Beta strandi571 – 5733Combined sources
Beta strandi575 – 5806Combined sources
Beta strandi593 – 5964Combined sources
Beta strandi600 – 6034Combined sources
Beta strandi611 – 6155Combined sources
Beta strandi622 – 6265Combined sources
Turni628 – 6303Combined sources
Beta strandi636 – 6416Combined sources
Beta strandi646 – 6516Combined sources
Beta strandi657 – 6604Combined sources
Helixi694 – 72835Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JAPelectron microscopy4.90r704-734[»]
3JAQelectron microscopy6.00r704-737[»]
3NS5X-ray2.60A/B76-161[»]
3NS6X-ray1.25A/B76-170[»]
3ZWLX-ray2.20E/F693-739[»]
4U1EX-ray2.00B694-737[»]
4U1FX-ray2.20A/B172-665[»]
ProteinModelPortaliP06103.
SMRiP06103. Positions 76-169, 185-664, 694-737.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06103.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 16286RRMUniRule annotationAdd
BLAST
Repeati228 – 26639WD 1Add
BLAST
Repeati277 – 32549WD 2Add
BLAST
Repeati373 – 41644WD 3Add
BLAST
Repeati484 – 52441WD 4Add
BLAST
Repeati544 – 58946WD 5Add
BLAST
Repeati605 – 65046WD 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 136136Sufficient for interaction with HCR1 and TIF32Add
BLAST
Regioni28 – 261234Sufficient for interaction with PIC8Add
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit B family.UniRule annotation
Contains 1 RRM (RNA recognition motif) domain.UniRule annotation
Contains 6 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00550000074913.
HOGENOMiHOG000265546.
InParanoidiP06103.
KOiK03253.
OMAiRTTNTIR.
OrthoDBiEOG7QG4CT.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
3.30.70.330. 1 hit.
HAMAPiMF_03001. eIF3b.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
[Graphical view]
PANTHERiPTHR14068. PTHR14068. 2 hits.
PfamiPF08662. eIF2A. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF036424. eIF3b. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNFLPRTLK NIYELYFNNI SVHSIVSRNT QLKRSKIIQM TTETFEDIKL
60 70 80 90 100
EDIPVDDIDF SDLEEQYKVT EEFNFDQYIV VNGAPVIPSA KVPVLKKALT
110 120 130 140 150
SLFSKAGKVV NMEFPIDEAT GKTKGFLFVE CGSMNDAKKI IKSFHGKRLD
160 170 180 190 200
LKHRLFLYTM KDVERYNSDD FDTEFREPDM PTFVPSSSLK SWLMDDKVRD
210 220 230 240 250
QFVLQDDVKT SVFWNSMFNE EDSLVESREN WSTNYVRFSP KGTYLFSYHQ
260 270 280 290 300
QGVTAWGGPN FDRLRRFYHP DVRNSSVSPN EKYLVTFSTE PIIVEEDNEF
310 320 330 340 350
SPFTKKNEGH QLCIWDIASG LLMATFPVIK SPYLKWPLVR WSYNDKYCAR
360 370 380 390 400
MVGDSLIVHD ATKNFMPLEA KALKPSGIRD FSFAPEGVKL QPFRNGDEPS
410 420 430 440 450
VLLAYWTPET NNSACTATIA EVPRGRVLKT VNLVQVSNVT LHWQNQAEFL
460 470 480 490 500
CFNVERHTKS GKTQFSNLQI CRLTERDIPV EKVELKDSVF EFGWEPHGNR
510 520 530 540 550
FVTISVHEVA DMNYAIPANT IRFYAPETKE KTDVIKRWSL VKEIPKTFAN
560 570 580 590 600
TVSWSPAGRF VVVGALVGPN MRRSDLQFYD MDYPGEKNIN DNNDVSASLK
610 620 630 640 650
DVAHPTYSAA TNITWDPSGR YVTAWSSSLK HKVEHGYKIF NIAGNLVKED
660 670 680 690 700
IIAGFKNFAW RPRPASILSN AERKKVRKNL REWSAQFEEQ DAMEADTAMR
710 720 730 740 750
DLILHQRELL KQWTEYREKI GQEMEKSMNF KIFDVQPEDA SDDFTTIEEI
760
VEEVLEETKE KVE
Length:763
Mass (Da):88,130
Last modified:January 1, 1988 - v1
Checksum:iF5E4E783408EE948
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02674 Genomic DNA. Translation: AAA34917.1.
Z75269 Genomic DNA. Translation: CAA99690.1.
BK006948 Genomic DNA. Translation: DAA11122.1.
PIRiA29562.
RefSeqiNP_015006.3. NM_001183781.3.

Genome annotation databases

EnsemblFungiiYOR361C; YOR361C; YOR361C.
GeneIDi854543.
KEGGisce:YOR361C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02674 Genomic DNA. Translation: AAA34917.1.
Z75269 Genomic DNA. Translation: CAA99690.1.
BK006948 Genomic DNA. Translation: DAA11122.1.
PIRiA29562.
RefSeqiNP_015006.3. NM_001183781.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JAPelectron microscopy4.90r704-734[»]
3JAQelectron microscopy6.00r704-737[»]
3NS5X-ray2.60A/B76-161[»]
3NS6X-ray1.25A/B76-170[»]
3ZWLX-ray2.20E/F693-739[»]
4U1EX-ray2.00B694-737[»]
4U1FX-ray2.20A/B172-665[»]
ProteinModelPortaliP06103.
SMRiP06103. Positions 76-169, 185-664, 694-737.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34746. 117 interactions.
DIPiDIP-2519N.
IntActiP06103. 44 interactions.
MINTiMINT-578476.

PTM databases

iPTMnetiP06103.

Proteomic databases

MaxQBiP06103.
PeptideAtlasiP06103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR361C; YOR361C; YOR361C.
GeneIDi854543.
KEGGisce:YOR361C.

Organism-specific databases

EuPathDBiFungiDB:YOR361C.
SGDiS000005888. PRT1.

Phylogenomic databases

GeneTreeiENSGT00550000074913.
HOGENOMiHOG000265546.
InParanoidiP06103.
KOiK03253.
OMAiRTTNTIR.
OrthoDBiEOG7QG4CT.

Enzyme and pathway databases

BioCyciYEAST:G3O-33831-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.

Miscellaneous databases

EvolutionaryTraceiP06103.
NextBioi976952.
PROiP06103.

Family and domain databases

Gene3Di2.120.10.30. 2 hits.
3.30.70.330. 1 hit.
HAMAPiMF_03001. eIF3b.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
[Graphical view]
PANTHERiPTHR14068. PTHR14068. 2 hits.
PfamiPF08662. eIF2A. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF036424. eIF3b. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the yeast PRT1 gene in which mutations affect translation initiation and regulation of cell proliferation."
    Hanic-Joyce P.J., Singer R.A., Johnston G.C.
    J. Biol. Chem. 262:2845-2851(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5."
    Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R., Qin J., Hinnebusch A.G.
    Mol. Cell. Biol. 18:4935-4946(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 CORE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)Met."
    Phan L., Schoenfeld L.W., Valasek L., Nielsen K.H., Hinnebusch A.G.
    EMBO J. 20:2954-2965(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6 interact with the eIF3 core complex by binding to cognate eIF3b subunits."
    Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L., Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.
    J. Biol. Chem. 276:34948-34957(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCI8.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast."
    Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.
    Mol. Cell. Biol. 26:2984-2998(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCR1; NIP1; TIF32; TIF34; TIF35; EIF-1; EIF-2 AND EIF-5, ASSOCIATION WITH THE 40S RIBOSOME, MUTAGENESIS OF 124-LYS--GLU-130.
  10. "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-61 AND SER-669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
    Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V.
    Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX WITH NIP1; TIF32; TIF34 AND TIF35.
  12. "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-61 AND TYR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEIF3B_YEAST
AccessioniPrimary (citable) accession number: P06103
Secondary accession number(s): D6W356
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 11, 2016
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 47500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.