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Protein

Eukaryotic translation initiation factor 3 subunit D

Gene

EIF3D

Organism
Homo sapiens (Human)
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 pre-initiation 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. In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426).1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit DUniRule annotation
Short name:
eIF3dUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 7UniRule annotation
eIF-3-zetaUniRule annotation
eIF3 p66
Gene namesi
Name:EIF3DUniRule annotation
Synonyms:EIF3S7UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:3278. EIF3D.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384740.

Polymorphism and mutation databases

BioMutaiEIF3D.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Eukaryotic translation initiation factor 3 subunit DPRO_0000123520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei161 – 1611PhosphoserineCombined sources
Modified residuei528 – 5281PhosphoserineCombined sources
Modified residuei529 – 5291PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO15371.
MaxQBiO15371.
PaxDbiO15371.
PeptideAtlasiO15371.
PRIDEiO15371.

PTM databases

iPTMnetiO15371.
PhosphoSiteiO15371.
SwissPalmiO15371.

Expressioni

Gene expression databases

BgeeiO15371.
CleanExiHS_EIF3D.
ExpressionAtlasiO15371. baseline and differential.
GenevisibleiO15371. HS.

Organism-specific databases

HPAiHPA045882.
HPA063330.
HPA066216.

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 annotation3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BEND5Q7L4P63EBI-353818,EBI-724373
HOMER3B2RA103EBI-353818,EBI-10175777
LZTS2Q9BRK43EBI-353818,EBI-741037
ORFQ9Q2G45EBI-353818,EBI-6248094From a different organism.
PHLDA1Q8WV242EBI-353818,EBI-738731
RELQ048643EBI-353818,EBI-307352
SATQ6ICU93EBI-353818,EBI-10178867
TRIM27P143733EBI-353818,EBI-719493

Protein-protein interaction databases

BioGridi114213. 64 interactions.
DIPiDIP-32870N.
IntActiO15371. 32 interactions.
MINTiMINT-5003799.
STRINGi9606.ENSP00000216190.

Structurei

3D structure databases

ProteinModelPortaliO15371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi530 – 54718Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2479. Eukaryota.
ENOG410XP1E. LUCA.
GeneTreeiENSGT00390000002667.
HOGENOMiHOG000241593.
HOVERGENiHBG000849.
InParanoidiO15371.
KOiK03251.
OMAiYHVKDSA.
OrthoDBiEOG74XS6H.
PhylomeDBiO15371.
TreeFamiTF101519.

Family and domain databases

HAMAPiMF_03003. eIF3d.
InterProiIPR007783. eIF3d.
[Graphical view]
PANTHERiPTHR12399. PTHR12399. 1 hit.
PfamiPF05091. eIF-3_zeta. 1 hit.
[Graphical view]
PIRSFiPIRSF016281. EIF-3_zeta. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15371-1) [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
MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY
60 70 80 90 100
QDKRYTNKYS SQFGGGSQYA YFHEEDESSF QLVDTARTQK TAYQRNRMRF
110 120 130 140 150
AQRNLRRDKD RRNMLQFNLQ ILPKSAKQKE RERIRLQKKF QKQFGVRQKW
160 170 180 190 200
DQKSQKPRDS SVEVRSDWEV KEEMDFPQLM KMRYLEVSEP QDIECCGALE
210 220 230 240 250
YYDKAFDRIT TRSEKPLRSI KRIFHTVTTT DDPVIRKLAK TQGNVFATDA
260 270 280 290 300
ILATLMSCTR SVYSWDIVVQ RVGSKLFFDK RDNSDFDLLT VSETANEPPQ
310 320 330 340 350
DEGNSFNSPR NLAMEATYIN HNFSQQCLRM GKERYNFPNP NPFVEDDMDK
360 370 380 390 400
NEIASVAYRY RRWKLGDDID LIVRCEHDGV MTGANGEVSF INIKTLNEWD
410 420 430 440 450
SRHCNGVDWR QKLDSQRGAV IATELKNNSY KLARWTCCAL LAGSEYLKLG
460 470 480 490 500
YVSRYHVKDS SRHVILGTQQ FKPNEFASQI NLSVENAWGI LRCVIDICMK
510 520 530 540
LEEGKYLILK DPNKQVIRVY SLPDGTFSSD EDEEEEEEEE EEEEEEET
Length:548
Mass (Da):63,973
Last modified:January 1, 1998 - v1
Checksum:i7FE0448EC3BE1711
GO
Isoform 2 (identifier: O15371-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     54-102: Missing.

Note: No experimental confirmation available.
Show »
Length:499
Mass (Da):58,140
Checksum:iE6E9019C723159C2
GO
Isoform 3 (identifier: O15371-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     137-151: Missing.

Note: No experimental confirmation available.
Show »
Length:533
Mass (Da):62,040
Checksum:i32AA0A0A31EEF2CD
GO

Mass spectrometryi

Molecular mass is 63972.9 Da from positions 1 - 548. 1 Publication
Molecular mass is 64046.7±1.4 Da from positions 1 - 548. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti310 – 3101R → C.1 Publication
VAR_074184

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei54 – 10249Missing in isoform 2. 1 PublicationVSP_055473Add
BLAST
Alternative sequencei137 – 15115Missing in isoform 3. 1 PublicationVSP_055474Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54558 mRNA. Translation: AAD03466.1.
BT007381 mRNA. Translation: AAP36045.1.
CR456489 mRNA. Translation: CAG30375.1.
AK300199 mRNA. Translation: BAG61970.1.
AK301284 mRNA. Translation: BAG62843.1.
AK312939 mRNA. Translation: BAG35781.1.
AL022313 Genomic DNA. Translation: CAA18440.1.
CH471095 Genomic DNA. Translation: EAW60109.1.
BC000328 mRNA. Translation: AAH00328.1.
BC000469 mRNA. Translation: AAH00469.1.
BC014912 mRNA. Translation: AAH14912.1.
BC080515 mRNA. Translation: AAH80515.1.
BC093100 mRNA. Translation: AAH93100.1.
BC093686 mRNA. Translation: AAH93686.1.
BC101477 mRNA. Translation: AAI01478.1.
CCDSiCCDS13930.1. [O15371-1]
RefSeqiNP_003744.1. NM_003753.3. [O15371-1]
XP_011528781.1. XM_011530479.1. [O15371-1]
UniGeneiHs.55682.

Genome annotation databases

EnsembliENST00000216190; ENSP00000216190; ENSG00000100353. [O15371-1]
ENST00000405442; ENSP00000385812; ENSG00000100353. [O15371-1]
GeneIDi8664.
KEGGihsa:8664.
UCSCiuc003apr.4. human. [O15371-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54558 mRNA. Translation: AAD03466.1.
BT007381 mRNA. Translation: AAP36045.1.
CR456489 mRNA. Translation: CAG30375.1.
AK300199 mRNA. Translation: BAG61970.1.
AK301284 mRNA. Translation: BAG62843.1.
AK312939 mRNA. Translation: BAG35781.1.
AL022313 Genomic DNA. Translation: CAA18440.1.
CH471095 Genomic DNA. Translation: EAW60109.1.
BC000328 mRNA. Translation: AAH00328.1.
BC000469 mRNA. Translation: AAH00469.1.
BC014912 mRNA. Translation: AAH14912.1.
BC080515 mRNA. Translation: AAH80515.1.
BC093100 mRNA. Translation: AAH93100.1.
BC093686 mRNA. Translation: AAH93686.1.
BC101477 mRNA. Translation: AAI01478.1.
CCDSiCCDS13930.1. [O15371-1]
RefSeqiNP_003744.1. NM_003753.3. [O15371-1]
XP_011528781.1. XM_011530479.1. [O15371-1]
UniGeneiHs.55682.

3D structure databases

ProteinModelPortaliO15371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114213. 64 interactions.
DIPiDIP-32870N.
IntActiO15371. 32 interactions.
MINTiMINT-5003799.
STRINGi9606.ENSP00000216190.

PTM databases

iPTMnetiO15371.
PhosphoSiteiO15371.
SwissPalmiO15371.

Polymorphism and mutation databases

BioMutaiEIF3D.

Proteomic databases

EPDiO15371.
MaxQBiO15371.
PaxDbiO15371.
PeptideAtlasiO15371.
PRIDEiO15371.

Protocols and materials databases

DNASUi8664.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216190; ENSP00000216190; ENSG00000100353. [O15371-1]
ENST00000405442; ENSP00000385812; ENSG00000100353. [O15371-1]
GeneIDi8664.
KEGGihsa:8664.
UCSCiuc003apr.4. human. [O15371-1]

Organism-specific databases

CTDi8664.
GeneCardsiEIF3D.
HGNCiHGNC:3278. EIF3D.
HPAiHPA045882.
HPA063330.
HPA066216.
MIMi603915. gene.
neXtProtiNX_O15371.
PharmGKBiPA162384740.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2479. Eukaryota.
ENOG410XP1E. LUCA.
GeneTreeiENSGT00390000002667.
HOGENOMiHOG000241593.
HOVERGENiHBG000849.
InParanoidiO15371.
KOiK03251.
OMAiYHVKDSA.
OrthoDBiEOG74XS6H.
PhylomeDBiO15371.
TreeFamiTF101519.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiEIF3D. human.
GeneWikiiEIF3D.
GenomeRNAii8664.
NextBioi32499.
PROiO15371.
SOURCEiSearch...

Gene expression databases

BgeeiO15371.
CleanExiHS_EIF3D.
ExpressionAtlasiO15371. baseline and differential.
GenevisibleiO15371. HS.

Family and domain databases

HAMAPiMF_03003. eIF3d.
InterProiIPR007783. eIF3d.
[Graphical view]
PANTHERiPTHR12399. PTHR12399. 1 hit.
PfamiPF05091. eIF-3_zeta. 1 hit.
[Graphical view]
PIRSFiPIRSF016281. EIF-3_zeta. 1 hit.
ProtoNetiSearch...

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] (ISOFORM 1).
    Tissue: Liver.
  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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Placenta and Stomach.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Brain, Lung, Muscle, Skin and Uterus.
  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. "The mechanism of an exceptional case of reinitiation after translation of a long ORF reveals why such events do not generally occur in mammalian mRNA translation."
    Poyry T.A., Kaminski A., Connell E.J., Fraser C.S., Jackson R.J.
    Genes Dev. 21:3149-3162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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, MASS SPECTROMETRY.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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.
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "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.
  23. Cited for: VARIANT CYS-310.

Entry informationi

Entry nameiEIF3D_HUMAN
AccessioniPrimary (citable) accession number: O15371
Secondary accession number(s): A8MWD3
, B2R7D4, B4DTF8, B4DVY1, Q3MJD9, Q5M9Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 153 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 22
    Human chromosome 22: 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

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.