UniProt Accession

 EIF3B_HUMAN; P55884; A4D208; Q2NL77; Q9UMF9 

Genbank Protein ID

 U78525; U62583; AC004971; AC004840; CH236953; CH471144; BC001173; BC110865 

Genbank Nucleotide ID

 AAC99479.1; AAB42010.1; EAL23951.1; EAW87237.1; AAH01173.1; AAI10866.1 

Protein Name

 Eukaryotic translation initiation factor 3 subunit B 

Protein Synonyms/Alias

 eIF3b; Eukaryotic translation initiation factor 3 subunit 9; Prt1 homolog; hPrt1; eIF-3-eta; eIF3 p110; eIF3 p116 

Gene Name

 EIF3B 

Gene Synonyms/Alias

 EIF3S9 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
202	VGPDRLEKLKNVIHK	ubiquitination	[1]
209	KLKNVIHKIFSKFGK	acetylation	[2]
209	KLKNVIHKIFSKFGK	ubiquitination	[1, 3]
213	VIHKIFSKFGKITND	acetylation	[2]
213	VIHKIFSKFGKITND	ubiquitination	[1, 3]
216	KIFSKFGKITNDFYP	ubiquitination	[1]
228	FYPEEDGKTKGYIFL	ubiquitination	[1]
230	PEEDGKTKGYIFLEY	ubiquitination	[3]
254	VKNADGYKLDKQHTF	ubiquitination	[1]
257	ADGYKLDKQHTFRVN	ubiquitination	[3]
284	DEWDIPEKQPFKDLG	ubiquitination	[1]
288	IPEKQPFKDLGNLRY	acetylation	[2]
288	IPEKQPFKDLGNLRY	ubiquitination	[3]
324	SIFWNDVKDPVSIEE	ubiquitination	[1]
345	TYVRWSPKGTYLATF	ubiquitination	[3]
364	IALWGGEKFKQIQRF	acetylation	[2]
364	IALWGGEKFKQIQRF	ubiquitination	[3]
436	FKWSHDGKFFARMTL	acetylation	[2]
460	SMGLLDKKSLKISGI	ubiquitination	[4]
463	LLDKKSLKISGIKDF	ubiquitination	[4, 5]
516	LFNVVDCKLHWQKNG	ubiquitination	[3, 4, 5, 6]
521	DCKLHWQKNGDYLCV	ubiquitination	[4]
529	NGDYLCVKVDRTPKG	ubiquitination	[4, 5, 7]
535	VKVDRTPKGTQGVVT	ubiquitination	[1, 3, 4, 5, 8, 9, 10]
552	EIFRMREKQVPVDVV	ubiquitination	[1, 3, 4, 5]
599	YHVKNNGKIELIKMF	ubiquitination	[1, 4]
604	NGKIELIKMFDKQQA	ubiquitination	[1, 3, 4]
608	ELIKMFDKQQANTIF	ubiquitination	[1]
718	LLSQEQIKQIKKDLK	ubiquitination	[3]
726	QIKKDLKKYSKIFEQ	ubiquitination	[4, 5]
729	KDLKKYSKIFEQKDR	ubiquitination	[3, 4, 5]
734	YSKIFEQKDRLSQSK	ubiquitination	[4, 5]
744	LSQSKASKELVERRR	acetylation	[11]
744	LSQSKASKELVERRR	ubiquitination	[3, 4, 5]
762	EDFRKYRKMAQELYM	ubiquitination	[1, 4, 5]
772	QELYMEQKNERLELR	ubiquitination	[1]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [10] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [11] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 185 268 RRM.
 REPEAT 332 370 WD 1.
 REPEAT 372 417 WD 2.
 REPEAT 421 459 WD 3.
 REPEAT 560 601 WD 4.
 REPEAT 649 694 WD 5.
 REGION 124 413 Sufficient for interaction with EIF3E.
 REGION 170 274 Sufficient for interaction with EIF3J.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 78 78 Phosphoserine.
 MOD_RES 81 81 Phosphoserine.
 MOD_RES 83 83 Phosphoserine.
 MOD_RES 85 85 Phosphoserine.
 MOD_RES 119 119 Phosphoserine.
 MOD_RES 125 125 Phosphoserine.
 MOD_RES 152 152 Phosphoserine.
 MOD_RES 154 154 Phosphoserine.
 MOD_RES 164 164 Phosphoserine.
 MOD_RES 209 209 N6-acetyllysine.
 MOD_RES 239 239 Phosphoserine.
 MOD_RES 288 288 N6-acetyllysine.
 MOD_RES 364 364 N6-acetyllysine.
 MOD_RES 451 451 Phosphothreonine (By similarity).  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Initiation factor; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome; Repeat; RNA-binding; WD repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 814 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:HAMAP.
 GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:HAMAP.
 GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0032947; F:protein complex scaffold; TAS:UniProtKB.
 GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
 GO:0001731; P:formation of translation preinitiation complex; IEA:HAMAP.
 GO:0006446; P:regulation of translational initiation; IDA:UniProtKB. 

Interpro

 IPR011400; EIF3B.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR013979; TIF_beta_prop-like.
 IPR015943; WD40/YVTN_repeat-like_dom. 

Pfam

 PF08662; eIF2A
 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 

PRINTS