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O00303

- EIF3F_HUMAN

UniProt

O00303 - EIF3F_HUMAN

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Protein

Eukaryotic translation initiation factor 3 subunit F

Gene
EIF3F, EIF3S5
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.1 Publication
Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling.1 Publication

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).1 Publication

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. translation initiation factor activity Source: UniProtKB
  3. ubiquitin-specific protease activity Source: FlyBase

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. protein deubiquitination Source: FlyBase
  5. regulation of translational initiation Source: UniProtKB-HAMAP
  6. translation Source: Reactome
  7. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Initiation factor, Protease, Thiol protease

Keywords - Biological processi

Protein biosynthesis, Ubl conjugation pathway

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.

Protein family/group databases

MEROPSiM67.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit F
Short name:
eIF3f
Alternative name(s):
Deubiquitinating enzyme eIF3f (EC:3.4.19.12)
Eukaryotic translation initiation factor 3 subunit 5
eIF-3-epsilon
eIF3 p47
Gene namesi
Name:EIF3F
Synonyms:EIF3S5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3275. EIF3F.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384806.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 357356Eukaryotic translation initiation factor 3 subunit FUniRule annotationPRO_0000213964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei46 – 461Phosphoserine; by CDK11; in vitro1 Publication
Modified residuei238 – 2381N6-acetyllysine1 Publication
Modified residuei258 – 2581Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO00303.
PaxDbiO00303.
PRIDEiO00303.

PTM databases

PhosphoSiteiO00303.

Expressioni

Gene expression databases

ArrayExpressiO00303.
BgeeiO00303.
CleanExiHS_EIF3F.
GenevestigatoriO00303.

Organism-specific databases

HPAiHPA049250.

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 RNF139; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner. Interacts with DTX1, the interaction is required for deubiquitinating activity towards NOTCH1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK11BP211273EBI-711990,EBI-1298
EIF3BP558843EBI-711990,EBI-366696
FBXO32Q969P57EBI-711990,EBI-2932534
GLE1Q53GS72EBI-711990,EBI-1955541
MSH4O154576EBI-711990,EBI-6092777
ORFQ9Q2G43EBI-711990,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi114214. 66 interactions.
DIPiDIP-35580N.
IntActiO00303. 23 interactions.
MINTiMINT-5000761.
STRINGi9606.ENSP00000310040.

Structurei

3D structure databases

ProteinModelPortaliO00303.
SMRiO00303. Positions 90-356.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 196110MPNAdd
BLAST

Domaini

The MPN domain mediates deubiquitinating activity.UniRule annotation

Sequence similaritiesi

Belongs to the eIF-3 subunit F family.

Phylogenomic databases

eggNOGiCOG1310.
HOGENOMiHOG000241154.
HOVERGENiHBG107843.
InParanoidiO00303.
KOiK03249.
OrthoDBiEOG77T152.
PhylomeDBiO00303.
TreeFamiTF101517.

Family and domain databases

HAMAPiMF_03005. eIF3f.
InterProiIPR027531. eIF3f.
IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O00303-1 [UniParc]FASTAAdd to Basket

« Hide

MATPAVPVSA PPATPTPVPA AAPASVPAPT PAPAAAPVPA AAPASSSDPA    50
AAAAATAAPG QTPASAQAPA QTPAPALPGP ALPGPFPGGR VVRLHPVILA 100
SIVDSYERRN EGAARVIGTL LGTVDKHSVE VTNCFSVPHN ESEDEVAVDM 150
EFAKNMYELH KKVSPNELIL GWYATGHDIT EHSVLIHEYY SREAPNPIHL 200
TVDTSLQNGR MSIKAYVSTL MGVPGRTMGV MFTPLTVKYA YYDTERIGVD 250
LIMKTCFSPN RVIGLSSDLQ QVGGASARIQ DALSTVLQYA EDVLSGKVSA 300
DNTVGRFLMS LVNQVPKIVP DDFETMLNSN INDLLMVTYL ANLTQSQIAL 350
NEKLVNL 357
Length:357
Mass (Da):37,564
Last modified:July 1, 1997 - v1
Checksum:i8A70FC6E2BF07737
GO

Mass spectrometryi

Molecular mass is 37554.8 Da from positions 1 - 357. 1 Publication
Molecular mass is 37475.6±0.2 Da from positions 1 - 357. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391P → L.
Corresponds to variant rs1043738 [ dbSNP | Ensembl ].
VAR_029267
Natural varianti172 – 1721W → L.
Corresponds to variant rs1044058 [ dbSNP | Ensembl ].
VAR_014452

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 567Missing in BAC04577. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U94855 mRNA. Translation: AAD03467.1.
AK095574 mRNA. Translation: BAC04577.1.
AK289637 mRNA. Translation: BAF82326.1.
AK291354 mRNA. Translation: BAF84043.1.
BT006894 mRNA. Translation: AAP35540.1.
CR456959 mRNA. Translation: CAG33240.1.
BC000490 mRNA. Translation: AAH00490.1.
CCDSiCCDS7785.1.
RefSeqiNP_003745.1. NM_003754.2.
UniGeneiHs.516023.

Genome annotation databases

EnsembliENST00000309828; ENSP00000310040; ENSG00000175390.
ENST00000533626; ENSP00000431800; ENSG00000175390.
GeneIDi8665.
KEGGihsa:8665.
UCSCiuc001mfw.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U94855 mRNA. Translation: AAD03467.1 .
AK095574 mRNA. Translation: BAC04577.1 .
AK289637 mRNA. Translation: BAF82326.1 .
AK291354 mRNA. Translation: BAF84043.1 .
BT006894 mRNA. Translation: AAP35540.1 .
CR456959 mRNA. Translation: CAG33240.1 .
BC000490 mRNA. Translation: AAH00490.1 .
CCDSi CCDS7785.1.
RefSeqi NP_003745.1. NM_003754.2.
UniGenei Hs.516023.

3D structure databases

ProteinModelPortali O00303.
SMRi O00303. Positions 90-356.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114214. 66 interactions.
DIPi DIP-35580N.
IntActi O00303. 23 interactions.
MINTi MINT-5000761.
STRINGi 9606.ENSP00000310040.

Chemistry

ChEMBLi CHEMBL2062352.

Protein family/group databases

MEROPSi M67.974.

PTM databases

PhosphoSitei O00303.

Proteomic databases

MaxQBi O00303.
PaxDbi O00303.
PRIDEi O00303.

Protocols and materials databases

DNASUi 8665.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309828 ; ENSP00000310040 ; ENSG00000175390 .
ENST00000533626 ; ENSP00000431800 ; ENSG00000175390 .
GeneIDi 8665.
KEGGi hsa:8665.
UCSCi uc001mfw.3. human.

Organism-specific databases

CTDi 8665.
GeneCardsi GC11P007966.
HGNCi HGNC:3275. EIF3F.
HPAi HPA049250.
MIMi 603914. gene.
neXtProti NX_O00303.
PharmGKBi PA162384806.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1310.
HOGENOMi HOG000241154.
HOVERGENi HBG107843.
InParanoidi O00303.
KOi K03249.
OrthoDBi EOG77T152.
PhylomeDBi O00303.
TreeFami TF101517.

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

GeneWikii EIF3F.
GenomeRNAii 8665.
NextBioi 32503.
PROi O00303.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00303.
Bgeei O00303.
CleanExi HS_EIF3F.
Genevestigatori O00303.

Family and domain databases

HAMAPi MF_03005. eIF3f.
InterProi IPR027531. eIF3f.
IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view ]
Pfami PF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view ]
SMARTi SM00232. JAB_MPN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly."
    Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C., Hinnebusch A.G., Hershey J.W.B.
    J. Biol. Chem. 272:27042-27052(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "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].
    Tissue: Amygdala and Brain.
  3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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].
    Tissue: Lung.
  6. "The p34cdc2-related cyclin-dependent kinase 11 interacts with the p47 subunit of eukaryotic initiation factor 3 during apoptosis."
    Shi J., Feng Y., Goulet A.C., Vaillancourt R.R., Sachs N.A., Hershey J.W., Nelson M.A.
    J. Biol. Chem. 278:5062-5071(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-46.
  7. "mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events."
    Holz M.K., Ballif B.A., Gygi S.P., Blenis J.
    Cell 123:569-580(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS6KB1, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "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.
  9. "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.
  10. "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.
  11. "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, PHOSPHORYLATION AT SER-258, MASS SPECTROMETRY.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways."
    Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A., Gemmill R.M.
    Mol. Cancer Res. 8:93-106(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF139.
  16. "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, INTERACTION WITH EIF3B; EIF3H AND EIF3M.
  17. "The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation."
    Moretti J., Chastagner P., Gastaldello S., Heuss S.F., Dirac A.M., Bernards R., Masucci M.G., Israel A., Brou C.
    PLoS Biol. 8:E1000545-E1000545(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A DEUBIQUITINATING ENZYME, CATALYTIC ACTIVITY, INTERACTION WITH DTX1.
  18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Structural roles for human translation factor eIF3 in initiation of protein synthesis."
    Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.
    Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.

Entry informationi

Entry nameiEIF3F_HUMAN
AccessioniPrimary (citable) accession number: O00303
Secondary accession number(s): A8K0S2, Q6IB45, Q8N978
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 140 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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