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Protein
Submitted name:

Eukaryotic translation initiation factor 3, subunit 2 beta, 36kDa

Gene

EIF3S2

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 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.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 factorUniRule annotationSAAS annotation

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

SignaLinkiQ5U0F4.

Names & Taxonomyi

Protein namesi
Submitted name:
Eukaryotic translation initiation factor 3, subunit 2 beta, 36kDaImported
Submitted name:
Eukaryotic translation initiation factor 3, subunit 2 beta, 36kDa, isoform CRA_bImported
Submitted name:
cDNA FLJ77665, highly similar to Homo sapiens eukaryotic translation initiation factor 3, subunit 2 beta, 36kDa (EIF3S2), mRNAImported
Submitted name:
cDNA FLJ78316, highly similar to Homo sapiens eukaryotic translation initiation factor 3, subunit 2 beta, 36kDa (EIF3S2), mRNAImported
Gene namesi
Name:EIF3S2UniRule annotationImported
Synonyms:EIF3IUniRule annotation
ORF Names:hCG_41608Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

Cytoplasm 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, eIF3m Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384875.

PTM / Processingi

Post-translational modificationi

Phosphorylated by TGF-beta type II receptor.UniRule annotation

Keywords - PTMi

PhosphoproteinUniRule annotation

Proteomic databases

PRIDEiQ5U0F4.

Expressioni

Gene expression databases

BgeeiQ5U0F4.
ExpressionAtlasiQ5U0F4. baseline and differential.

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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5U0F4.
SMRiQ5U0F4. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati8 – 4740WD 1UniRule annotationAdd
BLAST
Repeati50 – 9142WD 2UniRule annotationAdd
BLAST
Repeati144 – 18340WD 3UniRule annotationAdd
BLAST
Repeati186 – 22540WD 4UniRule annotationAdd
BLAST
Repeati283 – 32442WD 5UniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit I family.UniRule annotation
Contains 5 WD repeats.UniRule annotation

Keywords - Domaini

RepeatUniRule annotation, WD repeatUniRule annotation

Phylogenomic databases

GeneTreeiENSGT00630000089849.
HOVERGENiHBG000900.
KOiK03246.
OMAiKATVCAF.
PhylomeDBiQ5U0F4.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03008. eIF3i.
InterProiIPR027525. eIF3i.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5U0F4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG
60 70 80 90 100
HTGAVWCVDA DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG
110 120 130 140 150
FDFGGNIIMF STDKQMGYQC FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT
160 170 180 190 200
SAVWGPLGEC IIAGHESGEL NQYSAKSGEV LVNVKEHSRQ INDIQLSRDM
210 220 230 240 250
TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN YDHVVLGGGQ
260 270 280 290 300
EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY
310 320
SSGGEDGYVR IHYFDPQYFE FEFEA
Length:325
Mass (Da):36,502
Last modified:February 5, 2008 - v1
Checksum:i02797BB72A752A96
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT019597 mRNA. Translation: AAV38404.1.
AK289356 mRNA. Translation: BAF82045.1.
AK289882 mRNA. Translation: BAF82571.1.
CH471059 Genomic DNA. Translation: EAX07553.1.
RefSeqiNP_003748.1. NM_003757.2.
UniGeneiHs.530096.

Genome annotation databases

GeneIDi8668.
KEGGihsa:8668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT019597 mRNA. Translation: AAV38404.1.
AK289356 mRNA. Translation: BAF82045.1.
AK289882 mRNA. Translation: BAF82571.1.
CH471059 Genomic DNA. Translation: EAX07553.1.
RefSeqiNP_003748.1. NM_003757.2.
UniGeneiHs.530096.

3D structure databases

ProteinModelPortaliQ5U0F4.
SMRiQ5U0F4. Positions 1-324.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5U0F4.

Protocols and materials databases

DNASUi8668.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8668.
KEGGihsa:8668.

Organism-specific databases

CTDi8668.
PharmGKBiPA162384875.

Phylogenomic databases

GeneTreeiENSGT00630000089849.
HOVERGENiHBG000900.
KOiK03246.
OMAiKATVCAF.
PhylomeDBiQ5U0F4.

Enzyme and pathway databases

SignaLinkiQ5U0F4.

Miscellaneous databases

ChiTaRSiEIF3I. human.
GenomeRNAii8668.
NextBioi32515.

Gene expression databases

BgeeiQ5U0F4.
ExpressionAtlasiQ5U0F4. baseline and differential.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03008. eIF3i.
InterProiIPR027525. eIF3i.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Cloning of human full-length CDSs in BD Creator(TM) System Donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Caudate nucleusImported.

Entry informationi

Entry nameiQ5U0F4_HUMAN
AccessioniPrimary (citable) accession number: Q5U0F4
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: April 1, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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 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.