P55884 (EIF3B_HUMAN) 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
Prt1 homolog
Short name=hPrt1
eIF-3-eta
eIF3 p110
eIF3 p116

Gene names

Name:	EIF3B
Synonyms:	EIF3S9

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	814 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	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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.16 Ref.17 Ref.20 Ref.27
Subcellular location	Cytoplasm By similarity.
Domain	The RRM domain mediates interaction with EIF3J. HAMAP-Rule MF_03001
Post-translational modification	Phosphorylated. Phosphorylation is enhanced upon serum stimulation. Ref.17
Sequence similarities	Belongs to the eIF-3 subunit B family. Contains 1 RRM (RNA recognition motif) domain. Contains 5 WD repeats.
Mass spectrometry	Molecular mass is 93093.7 Da from positions 1 - 814. Ref.17 Molecular mass is 92561±43.5 Da from positions 1 - 814. Determined by MALDI. Ref.20

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat WD repeat
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of translational initiation Inferred from direct assay Ref.2. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 3 complex Inferred from direct assay Ref.17Ref.15Ref.20Ref.2. Source: UniProtKB
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro protein complex scaffold Traceable author statement Ref.17. Source: UniProtKB translation initiation factor activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX3X	O00571	5	EBI-366696,EBI-353779
EIF3A	Q14152	5	EBI-366696,EBI-366617
EIF3G	O75821	4	EBI-366696,EBI-366632
EIF3I	Q13347	4	EBI-366696,EBI-354047
EIF3J	O75822	5	EBI-366696,EBI-366647

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P55884-1)

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.

Isoform 2 (identifier: P55884-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 814

814

Eukaryotic translation initiation factor 3 subunit B HAMAP-Rule MF_03001

PRO_0000123531

Regions

Domain

185 – 268

84

RRM

Repeat

332 – 370

39

WD 1 HAMAP-Rule MF_03001

Repeat

372 – 417

46

WD 2 HAMAP-Rule MF_03001

Repeat

421 – 459

39

WD 3 HAMAP-Rule MF_03001

Repeat

560 – 601

42

WD 4 HAMAP-Rule MF_03001

Repeat

649 – 694

46

WD 5 HAMAP-Rule MF_03001

Region

124 – 413

290

Sufficient for interaction with EIF3E HAMAP-Rule MF_03001

Region

170 – 274

105

Sufficient for interaction with EIF3J HAMAP-Rule MF_03001

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.17

Modified residue

78

1

Phosphoserine Ref.19

Modified residue

81

1

Phosphoserine Ref.19

Modified residue

83

1

Phosphoserine Ref.17 Ref.19

Modified residue

85

1

Phosphoserine Ref.17 Ref.19

Modified residue

119

1

Phosphoserine Ref.17

Modified residue

125

1

Phosphoserine Ref.17 Ref.25

Modified residue

152

1

Phosphoserine Ref.13 Ref.17 Ref.21 Ref.23

Modified residue

154

1

Phosphoserine Ref.13 Ref.17 Ref.21 Ref.23 Ref.25

Modified residue

164

1

Phosphoserine Ref.13 Ref.17 Ref.21 Ref.23

Modified residue

209

1

N6-acetyllysine Ref.22

Modified residue

239

1

Phosphoserine Ref.19 Ref.23

Modified residue

288

1

N6-acetyllysine Ref.22

Modified residue

364

1

N6-acetyllysine Ref.22

Modified residue

451

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

812 – 814

3

NQE → IRSDLEHCAQPCVLWSRGRP AGSRVTPASSLCSLALDCDC AWILPLRHIFVPFSPWCLQW GI in isoform 2.

VSP_017274

Natural variant

64

1

S → P. Ref.1 Ref.2 Ref.6
Corresponds to variant rs9690787 [ dbSNP | Ensembl ].

VAR_047972

Natural variant

793

1

D → E.
Corresponds to variant rs1063257 [ dbSNP | Ensembl ].

VAR_047973

Experimental info

Sequence conflict

115 – 116

2

ER → AG in AAB42010. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

814

Helix Strand Turn

Details...

Beta strand

186 – 191

6

Turn

197 – 199

3

Helix

200 – 212

13

Beta strand

217 – 221

5

Beta strand

232 – 239

8

Helix

240 – 247

8

Beta strand

250 – 252

3

Beta strand

256 – 259

4

Beta strand

260 – 264

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 3. Checksum: C687A986EDAE0F5E	FASTA	814	92,482
	10 20 30 40 50 60 MQDAENVAVP EAAEERAEPG QQQPAAEPPP AEGLLRPAGP GAPEAAGTEA SSEEVGIAEA 70 80 90 100 110 120 GPESEVRTEP AAEAEAASGP SESPSPPAAE ELPGSHAEPP VPAQGEAPGE QARDERSDSR 130 140 150 160 170 180 AQAVSEDAGG NEGRAAEAEP RALENGDADE PSFSDPEDFV DDVSEEELLG DVLKDRPQEA 190 200 210 220 230 240 DGIDSVIVVD NVPQVGPDRL EKLKNVIHKI FSKFGKITND FYPEEDGKTK GYIFLEYASP 250 260 270 280 290 300 AHAVDAVKNA DGYKLDKQHT FRVNLFTDFD KYMTISDEWD IPEKQPFKDL GNLRYWLEEA 310 320 330 340 350 360 ECRDQYSVIF ESGDRTSIFW NDVKDPVSIE ERARWTETYV RWSPKGTYLA TFHQRGIALW 370 380 390 400 410 420 GGEKFKQIQR FSHQGVQLID FSPCERYLVT FSPLMDTQDD PQAIIIWDIL TGHKKRGFHC 430 440 450 460 470 480 ESSAHWPIFK WSHDGKFFAR MTLDTLSIYE TPSMGLLDKK SLKISGIKDF SWSPGGNIIA 490 500 510 520 530 540 FWVPEDKDIP ARVTLMQLPT RQEIRVRNLF NVVDCKLHWQ KNGDYLCVKV DRTPKGTQGV 550 560 570 580 590 600 VTNFEIFRMR EKQVPVDVVE MKETIIAFAW EPNGSKFAVL HGEAPRISVS FYHVKNNGKI 610 620 630 640 650 660 ELIKMFDKQQ ANTIFWSPQG QFVVLAGLRS MNGALAFVDT SDCTVMNIAE HYMASDVEWD 670 680 690 700 710 720 PTGRYVVTSV SWWSHKVDNA YWLWTFQGRL LQKNNKDRFC QLLWRPRPPT LLSQEQIKQI 730 740 750 760 770 780 KKDLKKYSKI FEQKDRLSQS KASKELVERR RTMMEDFRKY RKMAQELYME QKNERLELRG 790 800 810 GVDTDELDSN VDDWEEETIE FFVTEEIIPL GNQE
	Isoform 2 [UniParc]. Checksum: D5799E065B3C35D7	FASTA	873	99,029
	10 20 30 40 50 60 MQDAENVAVP EAAEERAEPG QQQPAAEPPP AEGLLRPAGP GAPEAAGTEA SSEEVGIAEA 70 80 90 100 110 120 GPESEVRTEP AAEAEAASGP SESPSPPAAE ELPGSHAEPP VPAQGEAPGE QARDERSDSR 130 140 150 160 170 180 AQAVSEDAGG NEGRAAEAEP RALENGDADE PSFSDPEDFV DDVSEEELLG DVLKDRPQEA 190 200 210 220 230 240 DGIDSVIVVD NVPQVGPDRL EKLKNVIHKI FSKFGKITND FYPEEDGKTK GYIFLEYASP 250 260 270 280 290 300 AHAVDAVKNA DGYKLDKQHT FRVNLFTDFD KYMTISDEWD IPEKQPFKDL GNLRYWLEEA 310 320 330 340 350 360 ECRDQYSVIF ESGDRTSIFW NDVKDPVSIE ERARWTETYV RWSPKGTYLA TFHQRGIALW 370 380 390 400 410 420 GGEKFKQIQR FSHQGVQLID FSPCERYLVT FSPLMDTQDD PQAIIIWDIL TGHKKRGFHC 430 440 450 460 470 480 ESSAHWPIFK WSHDGKFFAR MTLDTLSIYE TPSMGLLDKK SLKISGIKDF SWSPGGNIIA 490 500 510 520 530 540 FWVPEDKDIP ARVTLMQLPT RQEIRVRNLF NVVDCKLHWQ KNGDYLCVKV DRTPKGTQGV 550 560 570 580 590 600 VTNFEIFRMR EKQVPVDVVE MKETIIAFAW EPNGSKFAVL HGEAPRISVS FYHVKNNGKI 610 620 630 640 650 660 ELIKMFDKQQ ANTIFWSPQG QFVVLAGLRS MNGALAFVDT SDCTVMNIAE HYMASDVEWD 670 680 690 700 710 720 PTGRYVVTSV SWWSHKVDNA YWLWTFQGRL LQKNNKDRFC QLLWRPRPPT LLSQEQIKQI 730 740 750 760 770 780 KKDLKKYSKI FEQKDRLSQS KASKELVERR RTMMEDFRKY RKMAQELYME QKNERLELRG 790 800 810 820 830 840 GVDTDELDSN VDDWEEETIE FFVTEEIIPL GIRSDLEHCA QPCVLWSRGR PAGSRVTPAS 850 860 870 SLCSLALDCD CAWILPLRHI FVPFSPWCLQ WGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Biochemical characterization of mammalian translation initiation factor 3 (eIF3). Molecular cloning reveals that p110 subunit is the mammalian homologue of Saccharomyces cerevisiae protein Prt1." Chaudhuri J., Chakrabarti A., Maitra U. J. Biol. Chem. 272:30975-30983(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT PRO-64. Tissue: Skeletal muscle.
[2]	"The human homologue of the yeast Prt1 protein is an integral part of the eukaryotic initiation factor 3 complex and interacts with p170." Methot N., Rom E., Olsen H., Sonenberg N. J. Biol. Chem. 272:1110-1116(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT PRO-64. Tissue: Placenta.
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORM 1), VARIANT PRO-64. Tissue: Brain and Uterus.
[7]	"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 EIF3E.
[8]	"Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7." Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M. J. Cell. Biochem. 80:483-490(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3A.
[9]	"Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3." Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B. Eur. J. Biochem. 270:4133-4139(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3A; EIF3C; EIF3G; EIF3I AND EIF3K.
[10]	"The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro." Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A., Hershey J.W.B. J. Biol. Chem. 279:8946-8956(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3A; EIF3G; EIF3I AND EIF3J.
[11]	"mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events." Holz M.K., Ballif B.A., Gygi S.P., Blenis J. Cell 123:569-580(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF4B; MTOR; RPTOR AND RPS6KB1.
[12]	"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association." Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V. RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND SER-164, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit." LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E. J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[15]	"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.
[16]	"Human INT6/eIF3e is required for nonsense-mediated mRNA decay." Morris C., Wittmann J., Jaeck H.-M., Jalinot P. EMBO Rep. 8:596-602(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3A; EIF3C; EIF3E AND UPF2.
[17]	"Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry." Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A. Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-83; SER-85; SER-119; SER-125; SER-152; SER-154 AND SER-164, MASS SPECTROMETRY.
[18]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-81; SER-83; SER-85 AND SER-239, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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, CHARACTERIZATION OF THE EIF-3 COMPLEX, INTERACTION WITH EIF3E; EIF3F; EIF3H; EIF3L AND EIF3M, MASS SPECTROMETRY.
[21]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154 AND SER-164, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209; LYS-288 AND LYS-364, MASS SPECTROMETRY.
[23]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154; SER-164 AND SER-239, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-154, MASS SPECTROMETRY.
[26]	"Structural roles for human translation factor eIF3 in initiation of protein synthesis." Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E. Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
[27]	"Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit." ElAntak L., Tzakos A.G., Locker N., Lukavsky P.J. J. Biol. Chem. 282:8165-8174(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 170-274, INTERACTION WITH EIF3J.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00396370.
IPI00719752.

PIR

T09582.

RefSeq

NP_001032360.1. NM_001037283.1.
NP_003742.2. NM_003751.3.

UniGene

Hs.371001.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KRB	NMR	-	A	184-264	[»]
2NLW	NMR	-	A	170-274	[»]

ProteinModelPortal

P55884.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31113N.

IntAct

P55884. 29 interactions.

MINT

MINT-4999648.

STRING

9606.ENSP00000354125.

PTM databases

PhosphoSite

P55884.

Polymorphism databases

DMDM

218512094.

Proteomic databases

PaxDb

P55884.

PRIDE

P55884.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360876; ENSP00000354125; ENSG00000106263.
ENST00000397011; ENSP00000380206; ENSG00000106263.

GeneID

8662.

KEGG

hsa:8662.

UCSC

uc003slx.3. human.

Organism-specific databases

CTD

8662.

GeneCards

GC07P002362.

H-InvDB

HIX0006430.

HGNC

HGNC:3280. EIF3B.

HPA

CAB017562.

MIM

603917. gene.

neXtProt

NX_P55884.

PharmGKB

PA162384603.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5354.

HOGENOM

HOG000265546.

HOVERGEN

HBG006127.

KO

K03253.

OrthoDB

EOG42JNQZ.

PhylomeDB

P55884.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P55884.

Bgee

P55884.

CleanEx

HS_EIF3B.

Genevestigator

P55884.

GermOnline

ENSG00000106263. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 2 hits.
3.30.70.330. 1 hit.

HAMAP

MF_03001. eIF3b.

InterPro

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. human.

EvolutionaryTrace

P55884.

GenomeRNAi

8662.

NextBio

32487.

SOURCE

Search...

Entry information

Entry name

EIF3B_HUMAN

Accession

Primary (citable) accession number: P55884
Secondary accession number(s): A4D208, Q2NL77, Q9UMF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.