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Q9UBQ5

- EIF3K_HUMAN

UniProt

Q9UBQ5 - EIF3K_HUMAN

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Protein
Eukaryotic translation initiation factor 3 subunit K
Gene
EIF3K, EIF3S12, ARG134, HSPC029, MSTP001, PTD001
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. ribosome binding Source: InterPro
  3. translation initiation factor activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  3. gene expression Source: Reactome
  4. regulation of translational initiation Source: UniProtKB-HAMAP
  5. translation Source: Reactome
  6. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
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 namesi
Name:EIF3K
Synonyms:EIF3S12
ORF Names:ARG134, HSPC029, MSTP001, PTD001
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:24656. EIF3K.

Subcellular locationi

Nucleus. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  3. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  4. eukaryotic translation initiation factor 3 complex Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384923.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 218217Eukaryotic translation initiation factor 3 subunit KUniRule annotation
PRO_0000123546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei217 – 2171Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UBQ5.
PaxDbiQ9UBQ5.
PeptideAtlasiQ9UBQ5.
PRIDEiQ9UBQ5.

PTM databases

PhosphoSiteiQ9UBQ5.

Expressioni

Tissue specificityi

Ubiquitous, with the highest levels of expression in brain, testis and kidney.1 Publication

Gene expression databases

ArrayExpressiQ9UBQ5.
BgeeiQ9UBQ5.
CleanExiHS_EIF3K.
GenevestigatoriQ9UBQ5.

Organism-specific databases

HPAiHPA045446.

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. Interacts with CCND3, but not with CCND1 and CCND2.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ORFQ9Q2G45EBI-354344,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi118148. 46 interactions.
DIPiDIP-32880N.
IntActiQ9UBQ5. 12 interactions.
MINTiMINT-5002042.
STRINGi9606.ENSP00000248342.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614
Helixi18 – 214
Helixi23 – 253
Helixi26 – 3914
Helixi44 – 5613
Helixi58 – 603
Helixi63 – 7513
Turni76 – 783
Helixi81 – 877
Helixi91 – 944
Helixi99 – 11012
Helixi114 – 1207
Helixi126 – 1294
Helixi134 – 14916
Beta strandi151 – 1533
Helixi155 – 1617
Helixi167 – 17711
Helixi192 – 1954
Helixi207 – 2148

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZ4X-ray2.10A1-218[»]
ProteinModelPortaliQ9UBQ5.
SMRiQ9UBQ5. Positions 2-216.

Miscellaneous databases

EvolutionaryTraceiQ9UBQ5.

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-3 subunit K family.

Phylogenomic databases

eggNOGiNOG311878.
HOGENOMiHOG000008222.
HOVERGENiHBG052081.
InParanoidiQ9UBQ5.
KOiK15028.
OMAiGLERYNP.
PhylomeDBiQ9UBQ5.
TreeFamiTF314893.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.250. 1 hit.
HAMAPiMF_03010. eIF3k.
InterProiIPR016024. ARM-type_fold.
IPR009374. eIF3k.
IPR016020. Transl_init_fac_sub12_N_euk.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR13022. PTHR13022. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UBQ5-1) [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

MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV    50
LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR 100
QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY 150
QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN 200
IVEKIDFDSV SSIMASSQ 218
Length:218
Mass (Da):25,060
Last modified:May 1, 2000 - v1
Checksum:i6B2CBBE8A9D1F28F
GO
Isoform 2 (identifier: Q9UBQ5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     210-218: VSSIMASSQ → EW

Note: No experimental confirmation available.

Show »
Length:211
Mass (Da):24,484
Checksum:i59CDE70AC1995450
GO

Mass spectrometryi

Molecular mass is 24970.6 Da from positions 1 - 218. 1 Publication
Molecular mass is 24971.1±0.2 Da from positions 1 - 218. Determined by MALDI. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei210 – 2189VSSIMASSQ → EW in isoform 2.
VSP_055475

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191Q → K in AAD40193. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
AK316344 mRNA. Translation: BAH14715.1.
AC008649 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56807.1.
BC001031 mRNA. Translation: AAH01031.1.
BC007335 mRNA. Translation: AAH07335.2.
BC007559 mRNA. Translation: AAH07559.1.
CCDSiCCDS12517.1.
RefSeqiNP_037366.1. NM_013234.2.
UniGeneiHs.314359.

Genome annotation databases

EnsembliENST00000248342; ENSP00000248342; ENSG00000178982.
ENST00000545173; ENSP00000438145; ENSG00000178982.
GeneIDi27335.
KEGGihsa:27335.
UCSCiuc002oiz.1. human.

Polymorphism databases

DMDMi23396628.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
AK316344 mRNA. Translation: BAH14715.1 .
AC008649 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56807.1 .
BC001031 mRNA. Translation: AAH01031.1 .
BC007335 mRNA. Translation: AAH07335.2 .
BC007559 mRNA. Translation: AAH07559.1 .
CCDSi CCDS12517.1.
RefSeqi NP_037366.1. NM_013234.2.
UniGenei Hs.314359.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RZ4 X-ray 2.10 A 1-218 [» ]
ProteinModelPortali Q9UBQ5.
SMRi Q9UBQ5. Positions 2-216.
ModBasei Search...

Protein-protein interaction databases

BioGridi 118148. 46 interactions.
DIPi DIP-32880N.
IntActi Q9UBQ5. 12 interactions.
MINTi MINT-5002042.
STRINGi 9606.ENSP00000248342.

PTM databases

PhosphoSitei Q9UBQ5.

Polymorphism databases

DMDMi 23396628.

Proteomic databases

MaxQBi Q9UBQ5.
PaxDbi Q9UBQ5.
PeptideAtlasi Q9UBQ5.
PRIDEi Q9UBQ5.

Protocols and materials databases

DNASUi 27335.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248342 ; ENSP00000248342 ; ENSG00000178982 .
ENST00000545173 ; ENSP00000438145 ; ENSG00000178982 .
GeneIDi 27335.
KEGGi hsa:27335.
UCSCi uc002oiz.1. human.

Organism-specific databases

CTDi 27335.
GeneCardsi GC19P039109.
HGNCi HGNC:24656. EIF3K.
HPAi HPA045446.
MIMi 609596. gene.
neXtProti NX_Q9UBQ5.
PharmGKBi PA162384923.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG311878.
HOGENOMi HOG000008222.
HOVERGENi HBG052081.
InParanoidi Q9UBQ5.
KOi K15028.
OMAi GLERYNP.
PhylomeDBi Q9UBQ5.
TreeFami TF314893.

Enzyme and pathway databases

Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSi EIF3K. human.
EvolutionaryTracei Q9UBQ5.
GeneWikii EIF3K.
GenomeRNAii 27335.
NextBioi 50392.
PROi Q9UBQ5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBQ5.
Bgeei Q9UBQ5.
CleanExi HS_EIF3K.
Genevestigatori Q9UBQ5.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.25.40.250. 1 hit.
HAMAPi MF_03010. eIF3k.
InterProi IPR016024. ARM-type_fold.
IPR009374. eIF3k.
IPR016020. Transl_init_fac_sub12_N_euk.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR13022. PTHR13022. 1 hit.
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 1).
    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] (ISOFORM 1).
    Tissue: Pituitary tumor.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum and Spleen.
  8. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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).
    Tissue: Placenta, Skin and Uterus.
  11. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  12. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCND3, SUBCELLULAR LOCATION.
  13. "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.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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.
  16. "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.
  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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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, MASS SPECTROMETRY.
  20. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Entry informationi

Entry nameiEIF3K_HUMAN
AccessioniPrimary (citable) accession number: Q9UBQ5
Secondary accession number(s): A8K0I9
, B7ZAM9, Q96IQ0, Q9Y6D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 138 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Translation initiation factors
    List of translation initiation factor entries
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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