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Q5U0F4

- Q5U0F4_HUMAN

UniProt

Q5U0F4 - Q5U0F4_HUMAN

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Protein

Eukaryotic translation initiation factor 3 subunit I

Gene

EIF3I

Organism
Homo sapiens (Human)
Status
Unreviewed - 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.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

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit IUniRule annotation
Short name:
eIF3iUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 2UniRule annotation
eIF-3-betaUniRule annotation
eIF3 p36UniRule annotation
Gene namesi
Name:EIF3IUniRule annotation
Synonyms:EIF3S2UniRule 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

Expressioni

Gene expression databases

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BT019597 mRNA. Translation: AAV38404.1 .
AK289356 mRNA. Translation: BAF82045.1 .
AK289882 mRNA. Translation: BAF82571.1 .
CH471059 Genomic DNA. Translation: EAX07553.1 .
RefSeqi NP_003748.1. NM_003757.2.
UniGenei Hs.530096.

3D structure databases

ProteinModelPortali Q5U0F4.
SMRi Q5U0F4. Positions 1-324.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

DNASUi 8668.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 8668.
KEGGi hsa:8668.

Organism-specific databases

CTDi 8668.
PharmGKBi PA162384875.

Phylogenomic databases

GeneTreei ENSGT00630000089849.
HOVERGENi HBG000900.
KOi K03246.
OMAi KATVCAF.
PhylomeDBi Q5U0F4.

Miscellaneous databases

ChiTaRSi EIF3I. human.
GenomeRNAii 8668.
NextBioi 32515.

Gene expression databases

ExpressionAtlasi Q5U0F4. baseline and differential.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
HAMAPi MF_03008. eIF3i.
InterProi IPR027525. eIF3i.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00400. WD40. 4 hits.
[Graphical view ]
SMARTi SM00320. WD40. 5 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view ]
ProtoNeti Search...

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(2001) [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 (OCT-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: October 29, 2014
This is version 68 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.