Q8JZQ9 (EIF3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 3 subunit B
Short name=eIF3b

Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 9
eIF-3-eta
eIF3 p116

Gene names

Name:	Eif3b
Synonyms:	Eif3s9

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. 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 preinitiation 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. Ref.1
Subunit structure	Interacts with UPF2 By similarity. 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 may also interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead 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. Ref.5 Ref.7
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Ubiquitously expressed. Ref.1
Domain	The RRM domain mediates interaction with EIF3J By similarity. HAMAP-Rule MF_03001
Post-translational modification	Phosphorylated. Phosphorylation is enhanced upon serum stimulation By similarity. HAMAP-Rule MF_03001
Disruption phenotype	Embryonic death. Ref.1
Sequence similarities	Belongs to the eIF-3 subunit B family. Contains 1 RRM (RNA recognition motif) domain. Contains 5 WD repeats.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Domain	Repeat WD repeat
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of translational initiation Inferred from electronic annotation. Source: Compara translational initiation Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	eukaryotic translation initiation factor 3 complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro translation initiation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 803	803	Eukaryotic translation initiation factor 3 subunit B HAMAP-Rule MF_03001		PRO_0000223479
Regions
	Domain	174 – 257	84	RRM
	Repeat	321 – 359	39	WD 1 HAMAP-Rule MF_03001
	Repeat	361 – 406	46	WD 2 HAMAP-Rule MF_03001
	Repeat	410 – 448	39	WD 3 HAMAP-Rule MF_03001
	Repeat	549 – 590	42	WD 4 HAMAP-Rule MF_03001
	Repeat	638 – 683	46	WD 5 HAMAP-Rule MF_03001
	Region	113 – 402	290	Sufficient for interaction with EIF3E By similarity
	Region	159 – 263	105	Sufficient for interaction with EIF3J By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	31	1	Phosphothreonine Ref.4
	Modified residue	68	1	Phosphoserine Ref.10
	Modified residue	74	1	Phosphothreonine Ref.10 Ref.14
	Modified residue	75	1	Phosphoserine Ref.10 Ref.13 Ref.14
	Modified residue	79	1	Phosphoserine Ref.10 Ref.11 Ref.13 Ref.14
	Modified residue	90	1	Phosphoserine Ref.10
	Modified residue	120	1	Phosphoserine Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14
	Modified residue	123	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12 Ref.14
	Modified residue	141	1	Phosphoserine By similarity
	Modified residue	143	1	Phosphoserine By similarity
	Modified residue	153	1	Phosphoserine By similarity
	Modified residue	198	1	N6-acetyllysine By similarity
	Modified residue	228	1	Phosphoserine By similarity
	Modified residue	277	1	N6-acetyllysine By similarity
	Modified residue	353	1	N6-acetyllysine By similarity
	Modified residue	440	1	Phosphothreonine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q8JZQ9 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: D770AC70BFE9832F	FASTA	803	91,370
	10 20 30 40 50 60 MQDAENVAVP EAAEERAEPA RQQPASESPP TDEAAGSGGS EVGQTEDAEE DAEAGPEPEV 70 80 90 100 110 120 RAKPAAQSEE ETATSPAASP TPQSAERSPS QEPSAPGKAE AVGEQARGHP SAGAEEEGGS 130 140 150 160 170 180 DGSAAEAEPR ALENGEADEP SFSDPEDFVD DVSEEELLGD VLKDRPQEAD GIDSVIVVDN 190 200 210 220 230 240 VPQVGPDRLE KLKNVIHKIF SKFGKIINDY YPEEDGKTKG YIFLEYASPA HAVDAVKNAD 250 260 270 280 290 300 GYKLDKQHTF RVNLFTDFDK YMTISDEWDI PEKQPFKDLG NLRYWLEEAE CRDQYSVIFE 310 320 330 340 350 360 SGDRTSIFWN DVKDPVSIEE RARWTETYVR WSPKGTYLAT FHQRGIALWG GDKFKQIQRF 370 380 390 400 410 420 SHQGVQLIDF SPCERYLVTF SPLMDTQDDP QAIIIWDILT GHKKRGFHCE SSAHWPIFKW 430 440 450 460 470 480 SHDGKFFARM TLDTLSIYET PSMGLLDKKS LKISGIKDFS WSPGGNIIAF WVPEDKDIPA 490 500 510 520 530 540 RVTLMQLPTR QEIRVRNLFN VVDCKLHWQK NGDYLCVKVD RTPKGTQGVV TNFEIFRMRE 550 560 570 580 590 600 KQVPVDVVEM KETIIAFAWE PNGSKFAVLH GEAPRISVSF YHVKSNGKIE LIKMFDKQQA 610 620 630 640 650 660 NTIFWSPQGQ FVVLAGLRSM NGALAFVDTS DCTVMNIAEH YMASDVEWDP TGRYVVTSVS 670 680 690 700 710 720 WWSHKVDNAY WLWTFQGRLL QKNNKDRFCQ LLWRPRPPTL LSQDQIKQIK KDLKKYSKIF 730 740 750 760 770 780 EQKDRLSQSK ASKELVERRR TMMEDFRQYR KMAQELYMKQ KNERLELRGG VDTDELDSNV 790 800 DDWEEETIEF FVTEEVIPLG SQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Embryonic lethality of mutant mice deficient in the p116 gene." Koyanagi-Katsuta R., Akimitsu N., Hamamoto H., Arimitsu N., Hatano T., Sekimizu K. J. Biochem. 131:833-837(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY. Tissue: Embryonic stem cell.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Cecum and Placenta.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II and FVB/N. Tissue: Mammary tumor.
[4]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, MASS SPECTROMETRY. Tissue: Embryonic brain.
[5]	"mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin." Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr. EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3A; EIF3F; EIF3J; EIF4A1; EIF4B; EIF4E; EIF4G1 AND RPS6.
[6]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Reconstitution reveals the functional core of mammalian eIF3." Masutani M., Sonenberg N., Yokoyama S., Imataka H. EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[8]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-440, MASS SPECTROMETRY. Tissue: Liver.
[9]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, MASS SPECTROMETRY. Tissue: Teratocarcinoma.
[10]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; THR-74; SER-75; SER-79; SER-90; SER-120 AND SER-123, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-120 AND SER-123, MASS SPECTROMETRY. Tissue: Liver.
[12]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, MASS SPECTROMETRY. Tissue: Melanoma.
[13]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-79, MASS SPECTROMETRY. Tissue: Macrophage.
[14]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-75; SER-79; SER-120 AND SER-123, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK033722 mRNA. Translation: BAC28445.1. AK167618 mRNA. Translation: BAE39671.1. AK170938 mRNA. Translation: BAE42128.1. BC007175 mRNA. Translation: AAH07175.1. BC031704 mRNA. Translation: AAH31704.1.
IPI	IPI01008667.
PIR	JC7862.
RefSeq	NP_598677.1. NM_133916.2.
UniGene	Mm.21671.
3D structure databases
ProteinModelPortal	Q8JZQ9.
SMR	Q8JZQ9. Positions 159-263, 327-486, 621-659.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8JZQ9. 1 interaction.
MINT	MINT-1899500.
STRING	10090.ENSMUSP00000075175.
PTM databases
PhosphoSite	Q8JZQ9.
Proteomic databases
PaxDb	Q8JZQ9.
PRIDE	Q8JZQ9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
GeneID	27979.
KEGG	mmu:27979.
UCSC	uc009ahr.1. mouse.
Organism-specific databases
CTD	8662.
MGI	MGI:106478. Eif3b.
Phylogenomic databases
eggNOG	COG5354.
GeneTree	ENSGT00550000074913.
HOGENOM	HOG000265546.
HOVERGEN	HBG006127.
KO	K03253.
OMA	FYPEADG.
Gene expression databases
Bgee	Q8JZQ9.
Genevestigator	Q8JZQ9.
GermOnline	ENSMUSG00000056076. Mus musculus.
Family and domain databases
Gene3D	2.120.10.30. 1 hit. 2.130.10.10. 1 hit. 3.30.70.330. 1 hit.
HAMAP	MF_03001. eIF3b.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR011400. eIF3b. IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR013979. TIF2A_beta_prop-like. IPR015943. WD40/YVTN_repeat-like_dom. [Graphical view]
PANTHER	PTHR14068. PTHR14068. 1 hit.
Pfam	PF08662. eIF2A. 1 hit. PF00076. RRM_1. 1 hit. [Graphical view]
PIRSF	PIRSF036424. eIF3b. 1 hit.
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. False negative. PS50294. WD_REPEATS_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EIF3B. mouse.
NextBio	306472.
SOURCE	Search...

Entry information

Entry name

EIF3B_MOUSE

Accession

Primary (citable) accession number: Q8JZQ9
Secondary accession number(s): Q922K2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program