Q9UBQ5 (EIF3K_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 3 subunit K
Short name=eIF3k

Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 12
Muscle-specific gene M9 protein
PLAC-24
eIF-3 p25
eIF-3 p28

Gene names

Name:	EIF3K
Synonyms:	EIF3S12
ORF Names:	ARG134, HSPC029, MSTP001, PTD001

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.
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. Interacts with CCND3, but not with CCND1 and CCND2. Ref.1 Ref.11
Subcellular location	Nucleus. Cytoplasm Ref.11.
Tissue specificity	Ubiquitous, with the highest levels of expression in brain, testis and kidney. Ref.1
Sequence similarities	Belongs to the eIF-3 subunit K family.
Mass spectrometry	Molecular mass is 24970.6 Da from positions 1 - 218. Ref.16 Molecular mass is 24971.1±0.2 Da from positions 1 - 218. Determined by MALDI. Ref.18

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Nucleus
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	regulation of translational initiation Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 3 complex Inferred from direct assay Ref.16Ref.15Ref.18. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA
Molecular function	ribosome 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

Initiator methionine

1

1

Removed Ref.10 Ref.16

Chain

2 – 218

217

Eukaryotic translation initiation factor 3 subunit K

PRO_0000123546

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10 Ref.16 Ref.19

Modified residue

217

1

Phosphoserine Ref.13 Ref.17 Ref.19 Ref.20

Experimental info

Sequence conflict

119

1

Q → K in AAD40193. Ref.6

Secondary structure

1

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218

Helix Strand Turn

Details...

Helix

3 – 16

14

Helix

18 – 21

4

Helix

23 – 25

3

Helix

26 – 39

14

Helix

44 – 56

13

Helix

58 – 60

3

Helix

63 – 75

13

Turn

76 – 78

3

Helix

81 – 87

7

Helix

91 – 94

4

Helix

99 – 110

12

Helix

114 – 120

7

Helix

126 – 129

4

Helix

134 – 149

16

Beta strand

151 – 153

3

Helix

155 – 161

7

Helix

167 – 177

11

Helix

192 – 195

4

Helix

207 – 214

8

Sequences

	Sequence		Length	Mass (Da)
	Q9UBQ5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6B2CBBE8A9D1F28F	FASTA	218	25,060
	10 20 30 40 50 60 MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF 70 80 90 100 110 120 FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR QILYLGDLLE TCHFQAFWQA 130 140 150 160 170 180 LDENMDLLEG ITGFEDSVRK FICHVVGITY QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS 190 200 210 ADESGQIFIC SQEESIKPKN IVEKIDFDSV SSIMASSQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 14519125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-31, IDENTIFICATION IN THE EIF-3 COMPLEX, INTERACTION WITH EIF3B; EIF3C; EIF3G AND EIF3J, TISSUE SPECIFICITY, BLOCKAGE OF N-TERMINUS. Tissue: Cervix carcinoma.
[2]	"Muscle specific gene M9." Nawa G., Miyoshi Y., Nakamura Y. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[3]	Ye M., Song H., Peng Y., Huang Q., Dai M., Mao Y., Zhu H., Li G., Luo M., Hu R., Chen J. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary tumor.
[4]	Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y., Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J., Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L. , Jiang Y.X., Zhao X.W., Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Aorta.
[5]	"Gene cloning of human adenocarcinoma cell line." Yanqiu Z., Huazhang A., Fei L., Baojun C., Taidong Q., Kaichun W., Jie D., Daiming F. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Stomach cancer.
[6]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[8]	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].
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta, Skin and Uterus.
[10]	Bienvenut W.V., Zebisch A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-8; 21-31 AND 39-52, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[11]	"Identification of the p28 subunit of eukaryotic initiation factor 3(eIF3k) as a new interaction partner of cyclin D3." Shen X., Yang Y., Liu W., Sun M., Jiang J., Zong H., Gu J. FEBS Lett. 573:139-146(2004) [PubMed: 15327989] [Abstract] Cited for: INTERACTION WITH CCND3, SUBCELLULAR LOCATION.
[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: 15703437] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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: 16766523] [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: 17581632] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[16]	"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: 17322308] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
[17]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 18599441] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY.
[19]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"Crystal structure of human eIF3k, the first structure of eIF3 subunits." Wei Z., Zhang P., Zhou Z., Cheng Z., Wan M., Gong W. J. Biol. Chem. 279:34983-34990(2004) [PubMed: 15180986] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY245432 mRNA. Translation: AAP22070.1.
AB019392 mRNA. Translation: BAA76626.1.
AF077051 mRNA. Translation: AAD27784.1.
AF109355 mRNA. Translation: AAQ13503.1.
AF315506 mRNA. Translation: AAK01365.1.
AF085358 mRNA. Translation: AAD40193.1.
AK289554 mRNA. Translation: BAF82243.1.
CH471126 Genomic DNA. Translation: EAW56807.1.
BC001031 mRNA. Translation: AAH01031.1.
BC007335 mRNA. Translation: AAH07335.2.
BC007559 mRNA. Translation: AAH07559.1.

IPI

IPI00033143.

RefSeq

NP_037366.1. NM_013234.2.

UniGene

Hs.314359.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RZ4	X-ray	2.10	A	1-218	[»]

ProteinModelPortal

Q9UBQ5.

SMR

Q9UBQ5. Positions 2-216.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32880N.

IntAct

Q9UBQ5. 6 interactions.

MINT

MINT-5002042.

STRING

Q9UBQ5.

PTM databases

PhosphoSite

Q9UBQ5.

Polymorphism databases

DMDM

23396628.

Proteomic databases

PeptideAtlas

Q9UBQ5.

PRIDE

Q9UBQ5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000248342; ENSP00000248342; ENSG00000178982.

GeneID

27335.

KEGG

hsa:27335.

UCSC

uc002oiz.1. human.

Organism-specific databases

CTD

27335.

GeneCards

GC19P039109.

H-InvDB

HIX0015096.

HGNC

HGNC:24656. EIF3K.

HPA

HPA045446.

MIM

609596. gene.

neXtProt

NX_Q9UBQ5.

PharmGKB

PA162384923.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10558.

GeneTree

ENSGT00390000009409.

HOGENOM

HBG385843.

HOVERGEN

HBG052081.

InParanoid

Q9UBQ5.

OMA

HVADLLT.

OrthoDB

EOG4N30PT.

PhylomeDB

Q9UBQ5.

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

Q9UBQ5.

Bgee

Q9UBQ5.

CleanEx

HS_EIF3K.

Genevestigator

Q9UBQ5.

GermOnline

ENSG00000178982. Homo sapiens.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR019280. COP9_signalosome_subunit_CSN8.
IPR009374. Transl_init_fac_sub12_euk.
IPR016020. Transl_init_fac_sub12_N_euk.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.25.40.250. Transl_init_fac_sub12_N_euk. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K15028.

PANTHER

PTHR13022. EIF-3_p25. 1 hit.

Pfam

PF10075. PCI_Csn8. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

ProtoNet

Search...

Other

NextBio

50392.

SOURCE

Search...

Entry information

Entry name

EIF3K_HUMAN

Accession

Primary (citable) accession number: Q9UBQ5
Secondary accession number(s): A8K0I9, Q96IQ0, Q9Y6D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 111 of the entry and version 1 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.