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Q3UGC7

- EI3JA_MOUSE

UniProt

Q3UGC7 - EI3JA_MOUSE

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Protein

Eukaryotic translation initiation factor 3 subunit J-A

Gene
Eif3j1, Eif3s1-1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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. This subunit binds directly within the mRNA entry channel of the 40S ribosome to the aminoacyl (A) site. It may regulate the interaction between the 43S PIC and mRNA By similarity.UniRule annotation

GO - Molecular functioni

  1. translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  2. regulation of translational initiation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit J-A
Short name:
eIF3j-A
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 1-A
eIF-3-alpha-A
eIF3 p35
Gene namesi
Name:Eif3j1
Synonyms:Eif3s1-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1925905. Eif3j1.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  2. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  3. eukaryotic translation initiation factor 3 complex Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Eukaryotic translation initiation factor 3 subunit J-AUniRule annotationPRO_0000419334Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine By similarity
Modified residuei16 – 161Phosphoserine By similarity
Modified residuei23 – 231Phosphoserine By similarity
Modified residuei112 – 1121Phosphothreonine By similarity
Modified residuei130 – 1301Phosphoserine By similarity
Modified residuei257 – 2571Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation By similarity.UniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3UGC7.
PaxDbiQ3UGC7.
PRIDEiQ3UGC7.

Expressioni

Gene expression databases

BgeeiQ3UGC7.
GenevestigatoriQ3UGC7.

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 By similarity.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028668.

Structurei

3D structure databases

ProteinModelPortaliQ3UGC7.
SMRiQ3UGC7. Positions 145-214.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 7269Sufficient for interaction with EIF3B By similarityAdd
BLAST
Regioni246 – 26116Promotes stable association with the 40S ribosome By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili73 – 13866 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit J family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG247523.
GeneTreeiENSGT00390000018400.
HOGENOMiHOG000238746.
HOVERGENiHBG066230.
InParanoidiQ3UGC7.
KOiK03245.
OMAiSTCGIDA.
OrthoDBiEOG7J70H8.
PhylomeDBiQ3UGC7.
TreeFamiTF101514.

Family and domain databases

Gene3Di1.10.246.60. 1 hit.
HAMAPiMF_03009. eIF3j.
InterProiIPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view]
PANTHERiPTHR21681. PTHR21681. 1 hit.
PfamiPF08597. eIF3_subunit. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UGC7-1 [UniParc]FASTAAdd to Basket

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MAAAAAAAAA AGDSDSWDAD TFSMEDPVRK VAGGGTAGGD RWEGEDEDED    50
VKDNWDDDDD ENKEEAEVKP EVKISEKKKI AEKIKEKERQ QKKRQEEIKK 100
RLEEPEESKV LTPEEQLADK LRLKKLQEES DLELAKETFG VNNTVYGIDA 150
MNPSSRDDFT EFGKLLKDKI TQYEKSLYYA SFLEALVRDV CISLEIDDLK 200
KITNSLTVLC SEKQKQEKQS KAKKKKKGVV PGGGLKATMK DDLADYGGYE 250
GGYVQDYEDF M 261
Length:261
Mass (Da):29,344
Last modified:October 11, 2005 - v1
Checksum:i5BED22967289E651
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK147154 mRNA. Translation: BAE27721.1.
AK148004 mRNA. Translation: BAE28282.1.
AK154934 mRNA. Translation: BAE32935.1.
AK161038 mRNA. Translation: BAE36162.1.
AL845457 Genomic DNA. Translation: CAM21780.1.
CH466519 Genomic DNA. Translation: EDL28081.1.
CCDSiCCDS38219.1.
RefSeqiNP_653128.2. NM_144545.4.
XP_006500478.1. XM_006500415.1.
UniGeneiMm.458184.

Genome annotation databases

EnsembliENSMUST00000028668; ENSMUSP00000028668; ENSMUSG00000027236.
GeneIDi78655.
KEGGimmu:78655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK147154 mRNA. Translation: BAE27721.1 .
AK148004 mRNA. Translation: BAE28282.1 .
AK154934 mRNA. Translation: BAE32935.1 .
AK161038 mRNA. Translation: BAE36162.1 .
AL845457 Genomic DNA. Translation: CAM21780.1 .
CH466519 Genomic DNA. Translation: EDL28081.1 .
CCDSi CCDS38219.1.
RefSeqi NP_653128.2. NM_144545.4.
XP_006500478.1. XM_006500415.1.
UniGenei Mm.458184.

3D structure databases

ProteinModelPortali Q3UGC7.
SMRi Q3UGC7. Positions 145-214.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000028668.

Proteomic databases

MaxQBi Q3UGC7.
PaxDbi Q3UGC7.
PRIDEi Q3UGC7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028668 ; ENSMUSP00000028668 ; ENSMUSG00000027236 .
GeneIDi 78655.
KEGGi mmu:78655.

Organism-specific databases

CTDi 78655.
MGIi MGI:1925905. Eif3j1.

Phylogenomic databases

eggNOGi NOG247523.
GeneTreei ENSGT00390000018400.
HOGENOMi HOG000238746.
HOVERGENi HBG066230.
InParanoidi Q3UGC7.
KOi K03245.
OMAi STCGIDA.
OrthoDBi EOG7J70H8.
PhylomeDBi Q3UGC7.
TreeFami TF101514.

Miscellaneous databases

NextBioi 349286.
PROi Q3UGC7.
SOURCEi Search...

Gene expression databases

Bgeei Q3UGC7.
Genevestigatori Q3UGC7.

Family and domain databases

Gene3Di 1.10.246.60. 1 hit.
HAMAPi MF_03009. eIF3j.
InterProi IPR023194. eIF3-like_dom.
IPR013906. eIF3j.
[Graphical view ]
PANTHERi PTHR21681. PTHR21681. 1 hit.
Pfami PF08597. eIF3_subunit. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].
    Strain: C57BL/6J and NOD.
    Tissue: Amnion, Dendritic cell, Embryonic liver and Melanocyte.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiEI3JA_MOUSE
AccessioniPrimary (citable) accession number: Q3UGC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 78 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi