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Protein

Eukaryotic translation initiation factor 3 subunit K

Gene

Eif3k

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit KUniRule annotation
Short name:
eIF3kUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 12UniRule annotation
eIF-3 p25UniRule annotation
Gene namesi
Name:Eif3k
Synonyms:Eif3s12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1921080. Eif3k.

Subcellular locationi

  • Nucleus UniRule annotation
  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedUniRule annotation
Chaini2 – 218217Eukaryotic translation initiation factor 3 subunit KPRO_0000123547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineUniRule annotationBy similarity
Modified residuei28 – 281PhosphothreonineBy similarity
Modified residuei217 – 2171PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DBZ5.
MaxQBiQ9DBZ5.
PaxDbiQ9DBZ5.
PeptideAtlasiQ9DBZ5.
PRIDEiQ9DBZ5.
TopDownProteomicsiQ9DBZ5-1. [Q9DBZ5-1]

PTM databases

iPTMnetiQ9DBZ5.
PhosphoSiteiQ9DBZ5.
SwissPalmiQ9DBZ5.

Expressioni

Gene expression databases

BgeeiQ9DBZ5.
ExpressionAtlasiQ9DBZ5. baseline and differential.
GenevisibleiQ9DBZ5. MM.

Interactioni

Subunit structurei

Interacts with CCND3, but not with CCND1 and CCND2 (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 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.By similarity1 Publication

Protein-protein interaction databases

BioGridi216289. 3 interactions.
IntActiQ9DBZ5. 2 interactions.
MINTiMINT-4098437.
STRINGi10090.ENSMUSP00000066038.

Structurei

3D structure databases

ProteinModelPortaliQ9DBZ5.
SMRiQ9DBZ5. Positions 2-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-3 subunit K family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3252. Eukaryota.
ENOG410ZSE4. LUCA.
GeneTreeiENSGT00390000009409.
HOGENOMiHOG000008222.
HOVERGENiHBG052081.
InParanoidiQ9DBZ5.
KOiK15028.
OMAiYVQDQAK.
OrthoDBiEOG7N37DN.
PhylomeDBiQ9DBZ5.
TreeFamiTF314893.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.250. 1 hit.
HAMAPiMF_03010. eIF3k.
InterProiIPR016024. ARM-type_fold.
IPR033464. CSN8_PSD8_EIF3K.
IPR009374. eIF3k.
IPR016020. Transl_init_fac_sub12_N_euk.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR13022. PTHR13022. 1 hit.
PfamiPF10075. CSN8_PSD8_EIF3K. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48371. 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. AlignAdd to basket

Isoform 1 (identifier: Q9DBZ5-1) [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

        10         20         30         40         50
MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV
60 70 80 90 100
LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR
110 120 130 140 150
QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY
160 170 180 190 200
QHIDRWLLAE MLGDLTDNQL KVWMSKYGWS ADESGQVFIC SQEESIKPKN
210
IVEKIDFDSV SSIMASSQ
Length:218
Mass (Da):25,087
Last modified:June 1, 2001 - v1
Checksum:i84173F6E77F8C294
GO
Isoform 2 (identifier: Q9DBZ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     21-53: Missing.

Note: No experimental confirmation available.
Show »
Length:185
Mass (Da):21,307
Checksum:i509E5FB991EAAEB9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei21 – 5333Missing in isoform 2. 1 PublicationVSP_013425Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004664 mRNA. Translation: BAB23454.1.
BC027638 mRNA. Translation: AAH27638.1.
BC091749 mRNA. Translation: AAH91749.1.
CCDSiCCDS21062.1. [Q9DBZ5-1]
RefSeqiNP_001272871.1. NM_001285942.1. [Q9DBZ5-2]
NP_082935.1. NM_028659.3. [Q9DBZ5-1]
UniGeneiMm.29714.

Genome annotation databases

EnsembliENSMUST00000066070; ENSMUSP00000066038; ENSMUSG00000053565. [Q9DBZ5-1]
ENSMUST00000207683; ENSMUSP00000146940; ENSMUSG00000053565. [Q9DBZ5-2]
GeneIDi73830.
KEGGimmu:73830.
UCSCiuc009gai.2. mouse. [Q9DBZ5-1]
uc009gaj.2. mouse. [Q9DBZ5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004664 mRNA. Translation: BAB23454.1.
BC027638 mRNA. Translation: AAH27638.1.
BC091749 mRNA. Translation: AAH91749.1.
CCDSiCCDS21062.1. [Q9DBZ5-1]
RefSeqiNP_001272871.1. NM_001285942.1. [Q9DBZ5-2]
NP_082935.1. NM_028659.3. [Q9DBZ5-1]
UniGeneiMm.29714.

3D structure databases

ProteinModelPortaliQ9DBZ5.
SMRiQ9DBZ5. Positions 2-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216289. 3 interactions.
IntActiQ9DBZ5. 2 interactions.
MINTiMINT-4098437.
STRINGi10090.ENSMUSP00000066038.

PTM databases

iPTMnetiQ9DBZ5.
PhosphoSiteiQ9DBZ5.
SwissPalmiQ9DBZ5.

Proteomic databases

EPDiQ9DBZ5.
MaxQBiQ9DBZ5.
PaxDbiQ9DBZ5.
PeptideAtlasiQ9DBZ5.
PRIDEiQ9DBZ5.
TopDownProteomicsiQ9DBZ5-1. [Q9DBZ5-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066070; ENSMUSP00000066038; ENSMUSG00000053565. [Q9DBZ5-1]
ENSMUST00000207683; ENSMUSP00000146940; ENSMUSG00000053565. [Q9DBZ5-2]
GeneIDi73830.
KEGGimmu:73830.
UCSCiuc009gai.2. mouse. [Q9DBZ5-1]
uc009gaj.2. mouse. [Q9DBZ5-2]

Organism-specific databases

CTDi27335.
MGIiMGI:1921080. Eif3k.

Phylogenomic databases

eggNOGiKOG3252. Eukaryota.
ENOG410ZSE4. LUCA.
GeneTreeiENSGT00390000009409.
HOGENOMiHOG000008222.
HOVERGENiHBG052081.
InParanoidiQ9DBZ5.
KOiK15028.
OMAiYVQDQAK.
OrthoDBiEOG7N37DN.
PhylomeDBiQ9DBZ5.
TreeFamiTF314893.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

PROiQ9DBZ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBZ5.
ExpressionAtlasiQ9DBZ5. baseline and differential.
GenevisibleiQ9DBZ5. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.250. 1 hit.
HAMAPiMF_03010. eIF3k.
InterProiIPR016024. ARM-type_fold.
IPR033464. CSN8_PSD8_EIF3K.
IPR009374. eIF3k.
IPR016020. Transl_init_fac_sub12_N_euk.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR13022. PTHR13022. 1 hit.
PfamiPF10075. CSN8_PSD8_EIF3K. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Lung.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and Czech II.
    Tissue: Mammary gland.
  3. "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.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiEIF3K_MOUSE
AccessioniPrimary (citable) accession number: Q9DBZ5
Secondary accession number(s): Q58EU9, Q8K3A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.