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Protein

Eukaryotic translation initiation factor 3 subunit B

Gene

EIF3B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:9388245, PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:9388245, PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773).UniRule annotation4 Publications
(Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426).1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • protein complex scaffold Source: UniProtKB
  • RNA binding Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB

GO - Biological processi

  • formation of translation preinitiation complex Source: UniProtKB-HAMAP
  • IRES-dependent viral translational initiation Source: UniProtKB
  • regulation of translational initiation Source: UniProtKB
  • translational initiation Source: UniProtKB
  • viral translational termination-reinitiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000084623-MONOMER.
ZFISH:ENSG00000106263-MONOMER.
ZFISH:ENSG00000132361-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit BUniRule annotation
Short name:
eIF3bUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 9UniRule annotation
Prt1 homolog
Short name:
hPrt1
eIF-3-etaUniRule annotation
eIF3 p110UniRule annotation
eIF3 p116
Gene namesi
Name:EIF3BUniRule annotation
Synonyms:EIF3S9UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:3280. EIF3B.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi8662.
OpenTargetsiENSG00000106263.
PharmGKBiPA162384603.

Polymorphism and mutation databases

BioMutaiEIF3B.
DMDMi218512094.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001235311 – 814Eukaryotic translation initiation factor 3 subunit BAdd BLAST814

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineUniRule annotationCombined sources1 Publication1
Modified residuei78PhosphoserineCombined sources1
Modified residuei81PhosphoserineCombined sources1
Modified residuei83PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei85PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei119PhosphoserineUniRule annotation1 Publication1
Modified residuei125PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei152PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei154PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei164PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei209N6-acetyllysineCombined sources1
Modified residuei239PhosphoserineCombined sources1
Modified residuei288N6-acetyllysineCombined sources1
Modified residuei364N6-acetyllysineCombined sources1

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP55884.
MaxQBiP55884.
PaxDbiP55884.
PeptideAtlasiP55884.
PRIDEiP55884.

PTM databases

iPTMnetiP55884.
PhosphoSitePlusiP55884.
SwissPalmiP55884.

Expressioni

Gene expression databases

BgeeiENSG00000106263.
CleanExiHS_EIF3B.
ExpressionAtlasiP55884. baseline and differential.
GenevisibleiP55884. HS.

Organism-specific databases

HPAiCAB017562.
HPA048983.

Interactioni

Subunit structurei

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with UPF2 and HNRPD. Interacts with METTL3 (PubMed:27117702).UniRule annotation13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX3XO005715EBI-366696,EBI-353779
EIF3AQ141526EBI-366696,EBI-366617
EIF3FO003034EBI-366696,EBI-711990
EIF3GO758215EBI-366696,EBI-366632
EIF3IQ133474EBI-366696,EBI-354047
EIF3JO758225EBI-366696,EBI-366647
RPS6KB1P234433EBI-366696,EBI-1775921
UL54Q9J0X94EBI-366696,EBI-7967856From a different organism.

GO - Molecular functioni

  • protein complex scaffold Source: UniProtKB

Protein-protein interaction databases

BioGridi114211. 79 interactors.
DIPiDIP-31113N.
IntActiP55884. 50 interactors.
MINTiMINT-4999648.
STRINGi9606.ENSP00000354125.

Structurei

Secondary structure

1814
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi186 – 191Combined sources6
Turni197 – 199Combined sources3
Helixi200 – 212Combined sources13
Beta strandi217 – 221Combined sources5
Beta strandi232 – 239Combined sources8
Helixi240 – 247Combined sources8
Beta strandi250 – 252Combined sources3
Beta strandi256 – 259Combined sources4
Beta strandi260 – 264Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KRBNMR-A184-264[»]
2NLWNMR-A170-274[»]
5K1Helectron microscopy4.90B170-745[»]
ProteinModelPortaliP55884.
SMRiP55884.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55884.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini185 – 268RRMUniRule annotationAdd BLAST84
Repeati285 – 324WD 1Add BLAST40
Repeati325 – 365WD 2Add BLAST41
Repeati366 – 425WD 3Add BLAST60
Repeati426 – 489WD 4Add BLAST64
Repeati490 – 553WD 5Add BLAST64
Repeati554 – 598WD 6Add BLAST45
Repeati599 – 642WD 7Add BLAST44
Repeati643 – 685WD 8Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni124 – 413Sufficient for interaction with EIF3EAdd BLAST290
Regioni170 – 274Sufficient for interaction with EIF3JAdd BLAST105

Domaini

The RRM domain mediates interaction with EIF3J.

Sequence similaritiesi

Belongs to the eIF-3 subunit B family.UniRule annotation
Contains 1 RRM (RNA recognition motif) domain.UniRule annotation
Contains 8 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG2314. Eukaryota.
COG5354. LUCA.
GeneTreeiENSGT00550000074913.
HOGENOMiHOG000265546.
HOVERGENiHBG006127.
InParanoidiP55884.
KOiK03253.
OMAiAFMEYKQ.
OrthoDBiEOG091G02V5.
PhylomeDBiP55884.
TreeFamiTF101521.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
3.30.70.330. 1 hit.
HAMAPiMF_03001. eIF3b. 1 hit.
InterProiIPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR14068. PTHR14068. 1 hit.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55884-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQDAENVAVP EAAEERAEPG QQQPAAEPPP AEGLLRPAGP GAPEAAGTEA
60 70 80 90 100
SSEEVGIAEA GPESEVRTEP AAEAEAASGP SESPSPPAAE ELPGSHAEPP
110 120 130 140 150
VPAQGEAPGE QARDERSDSR AQAVSEDAGG NEGRAAEAEP RALENGDADE
160 170 180 190 200
PSFSDPEDFV DDVSEEELLG DVLKDRPQEA DGIDSVIVVD NVPQVGPDRL
210 220 230 240 250
EKLKNVIHKI FSKFGKITND FYPEEDGKTK GYIFLEYASP AHAVDAVKNA
260 270 280 290 300
DGYKLDKQHT FRVNLFTDFD KYMTISDEWD IPEKQPFKDL GNLRYWLEEA
310 320 330 340 350
ECRDQYSVIF ESGDRTSIFW NDVKDPVSIE ERARWTETYV RWSPKGTYLA
360 370 380 390 400
TFHQRGIALW GGEKFKQIQR FSHQGVQLID FSPCERYLVT FSPLMDTQDD
410 420 430 440 450
PQAIIIWDIL TGHKKRGFHC ESSAHWPIFK WSHDGKFFAR MTLDTLSIYE
460 470 480 490 500
TPSMGLLDKK SLKISGIKDF SWSPGGNIIA FWVPEDKDIP ARVTLMQLPT
510 520 530 540 550
RQEIRVRNLF NVVDCKLHWQ KNGDYLCVKV DRTPKGTQGV VTNFEIFRMR
560 570 580 590 600
EKQVPVDVVE MKETIIAFAW EPNGSKFAVL HGEAPRISVS FYHVKNNGKI
610 620 630 640 650
ELIKMFDKQQ ANTIFWSPQG QFVVLAGLRS MNGALAFVDT SDCTVMNIAE
660 670 680 690 700
HYMASDVEWD PTGRYVVTSV SWWSHKVDNA YWLWTFQGRL LQKNNKDRFC
710 720 730 740 750
QLLWRPRPPT LLSQEQIKQI KKDLKKYSKI FEQKDRLSQS KASKELVERR
760 770 780 790 800
RTMMEDFRKY RKMAQELYME QKNERLELRG GVDTDELDSN VDDWEEETIE
810
FFVTEEIIPL GNQE
Length:814
Mass (Da):92,482
Last modified:December 16, 2008 - v3
Checksum:iC687A986EDAE0F5E
GO
Isoform 2 (identifier: P55884-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     812-814: NQE → IRSDLEHCAQPCVLWSRGRPAGSRVTPASSLCSLALDCDCAWILPLRHIFVPFSPWCLQWGI

Show »
Length:873
Mass (Da):99,029
Checksum:iD5799E065B3C35D7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115 – 116ER → AG in AAB42010 (PubMed:8995410).Curated2

Mass spectrometryi

Molecular mass is 93093.7 Da from positions 1 - 814. 1 Publication
Molecular mass is 92561±43.5 Da from positions 1 - 814. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04797264S → P.3 PublicationsCorresponds to variant rs9690787dbSNPEnsembl.1
Natural variantiVAR_047973793D → E.Corresponds to variant rs1063257dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_017274812 – 814NQE → IRSDLEHCAQPCVLWSRGRP AGSRVTPASSLCSLALDCDC AWILPLRHIFVPFSPWCLQW GI in isoform 2. 1 Publication3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78525 mRNA. Translation: AAC99479.1.
U62583 mRNA. Translation: AAB42010.1.
AC004971 Genomic DNA. No translation available.
AC004840 Genomic DNA. No translation available.
CH236953 Genomic DNA. Translation: EAL23951.1.
CH471144 Genomic DNA. Translation: EAW87237.1.
BC001173 mRNA. Translation: AAH01173.1.
BC110865 mRNA. Translation: AAI10866.1.
CCDSiCCDS5332.1. [P55884-1]
PIRiT09582.
RefSeqiNP_001032360.1. NM_001037283.1. [P55884-1]
NP_003742.2. NM_003751.3. [P55884-1]
XP_011513901.1. XM_011515599.1. [P55884-1]
XP_011513902.1. XM_011515600.1. [P55884-1]
XP_016868241.1. XM_017012752.1. [P55884-1]
UniGeneiHs.371001.

Genome annotation databases

EnsembliENST00000360876; ENSP00000354125; ENSG00000106263. [P55884-1]
ENST00000397011; ENSP00000380206; ENSG00000106263. [P55884-1]
GeneIDi8662.
KEGGihsa:8662.
UCSCiuc003slx.4. human. [P55884-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78525 mRNA. Translation: AAC99479.1.
U62583 mRNA. Translation: AAB42010.1.
AC004971 Genomic DNA. No translation available.
AC004840 Genomic DNA. No translation available.
CH236953 Genomic DNA. Translation: EAL23951.1.
CH471144 Genomic DNA. Translation: EAW87237.1.
BC001173 mRNA. Translation: AAH01173.1.
BC110865 mRNA. Translation: AAI10866.1.
CCDSiCCDS5332.1. [P55884-1]
PIRiT09582.
RefSeqiNP_001032360.1. NM_001037283.1. [P55884-1]
NP_003742.2. NM_003751.3. [P55884-1]
XP_011513901.1. XM_011515599.1. [P55884-1]
XP_011513902.1. XM_011515600.1. [P55884-1]
XP_016868241.1. XM_017012752.1. [P55884-1]
UniGeneiHs.371001.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KRBNMR-A184-264[»]
2NLWNMR-A170-274[»]
5K1Helectron microscopy4.90B170-745[»]
ProteinModelPortaliP55884.
SMRiP55884.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114211. 79 interactors.
DIPiDIP-31113N.
IntActiP55884. 50 interactors.
MINTiMINT-4999648.
STRINGi9606.ENSP00000354125.

PTM databases

iPTMnetiP55884.
PhosphoSitePlusiP55884.
SwissPalmiP55884.

Polymorphism and mutation databases

BioMutaiEIF3B.
DMDMi218512094.

Proteomic databases

EPDiP55884.
MaxQBiP55884.
PaxDbiP55884.
PeptideAtlasiP55884.
PRIDEiP55884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360876; ENSP00000354125; ENSG00000106263. [P55884-1]
ENST00000397011; ENSP00000380206; ENSG00000106263. [P55884-1]
GeneIDi8662.
KEGGihsa:8662.
UCSCiuc003slx.4. human. [P55884-1]

Organism-specific databases

CTDi8662.
DisGeNETi8662.
GeneCardsiEIF3B.
H-InvDBHIX0006430.
HGNCiHGNC:3280. EIF3B.
HPAiCAB017562.
HPA048983.
MIMi603917. gene.
neXtProtiNX_P55884.
OpenTargetsiENSG00000106263.
PharmGKBiPA162384603.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2314. Eukaryota.
COG5354. LUCA.
GeneTreeiENSGT00550000074913.
HOGENOMiHOG000265546.
HOVERGENiHBG006127.
InParanoidiP55884.
KOiK03253.
OMAiAFMEYKQ.
OrthoDBiEOG091G02V5.
PhylomeDBiP55884.
TreeFamiTF101521.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000084623-MONOMER.
ZFISH:ENSG00000106263-MONOMER.
ZFISH:ENSG00000132361-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiEIF3B. human.
EvolutionaryTraceiP55884.
GeneWikiiEIF3B.
GenomeRNAii8662.
PROiP55884.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106263.
CleanExiHS_EIF3B.
ExpressionAtlasiP55884. baseline and differential.
GenevisibleiP55884. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
3.30.70.330. 1 hit.
HAMAPiMF_03001. eIF3b. 1 hit.
InterProiIPR011400. EIF3B.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR013979. TIF_beta_prop-like.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR14068. PTHR14068. 1 hit.
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...

Entry informationi

Entry nameiEIF3B_HUMAN
AccessioniPrimary (citable) accession number: P55884
Secondary accession number(s): A4D208, Q2NL77, Q9UMF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 16, 2008
Last modified: November 30, 2016
This is version 172 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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.