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O43432

- IF4G3_HUMAN

UniProt

O43432 - IF4G3_HUMAN

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Protein
Eukaryotic translation initiation factor 4 gamma 3
Gene
EIF4G3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei699 – 7002Cleavage; by enterovirus/rhinovirus protease 2A
Sitei700 – 7012Cleavage; by foot-and-mouth disease virus leader protease

GO - Molecular functioni

  1. RNA cap binding Source: ProtInc
  2. poly(A) RNA binding Source: UniProtKB
  3. translation factor activity, nucleic acid binding Source: ProtInc
  4. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: Reactome
  2. positive regulation of meiosis I Source: Ensembl
  3. positive regulation of protein phosphorylation Source: Ensembl
  4. positive regulation of translation Source: Ensembl
  5. regulation of translational initiation Source: ProtInc
  6. spermatogenesis Source: Ensembl
  7. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Host-virus interaction, Protein biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4 gamma 3
Short name:
eIF-4-gamma 3
Short name:
eIF-4G 3
Short name:
eIF4G 3
Alternative name(s):
eIF-4-gamma II
Short name:
eIF4GII
Gene namesi
Name:EIF4G3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3298. EIF4G3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic translation initiation factor 4F complex Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi756 – 7561R → D: Reduces binding to EIF4A; when associated with D-759 and D-764. 1 Publication
Mutagenesisi759 – 7591R → D: Reduces binding to EIF4A; when associated with D-756 and D-764. 1 Publication
Mutagenesisi764 – 7641K → D: Reduces binding to EIF4A; when associated with D-756 and D-759. 1 Publication
Mutagenesisi814 – 8141R → D: Reduces binding to EIF4A; when associated with D-820. 1 Publication
Mutagenesisi820 – 8201K → D: Reduces binding to EIF4A; when associated with D-814. 1 Publication
Mutagenesisi834 – 8352RK → DD: Reduces binding to IRES.

Organism-specific databases

PharmGKBiPA27724.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15851585Eukaryotic translation initiation factor 4 gamma 3
PRO_0000213329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681Phosphothreonine By similarity
Modified residuei230 – 2301Phosphoserine2 Publications
Modified residuei232 – 2321Phosphoserine2 Publications
Modified residuei267 – 2671Phosphoserine By similarity
Modified residuei495 – 4951Phosphoserine7 Publications
Modified residuei1156 – 11561Phosphoserine; by CaMK11 Publication

Post-translational modificationi

Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43432.
PaxDbiO43432.
PRIDEiO43432.

PTM databases

PhosphoSiteiO43432.

Miscellaneous databases

PMAP-CutDBO43432.

Expressioni

Gene expression databases

ArrayExpressiO43432.
BgeeiO43432.
CleanExiHS_EIF4G3.
GenevestigatoriO43432.

Organism-specific databases

HPAiHPA025031.
HPA025039.
HPA025041.

Interactioni

Subunit structurei

Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a complex with EIF4E. eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4G1/EIF4G3 interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate eIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIFG3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA By similarity.2 Publications

Protein-protein interaction databases

BioGridi114220. 16 interactions.
DIPiDIP-33245N.
IntActiO43432. 11 interactions.
MINTiMINT-85560.
STRINGi9606.ENSP00000264211.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi746 – 76217
Helixi770 – 7778
Helixi785 – 80117
Helixi803 – 8053
Helixi806 – 81611
Helixi833 – 84816
Helixi885 – 90016
Turni901 – 9033
Helixi907 – 91913
Helixi923 – 94018
Turni943 – 9453
Helixi946 – 96116
Helixi967 – 98115
Turni982 – 9843

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HU3X-ray2.37A745-1003[»]
ProteinModelPortaliO43432.
SMRiO43432. Positions 136-161, 745-986, 1214-1551.

Miscellaneous databases

EvolutionaryTraceiO43432.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati745 – 78339HEAT 1
Add
BLAST
Domaini755 – 983229MIF4G
Add
BLAST
Repeati784 – 83148HEAT 2
Add
BLAST
Repeati832 – 90574HEAT 3
Add
BLAST
Repeati906 – 94439HEAT 4
Add
BLAST
Repeati945 – 98440HEAT 5
Add
BLAST
Domaini1221 – 1343123MI
Add
BLAST
Domaini1416 – 1585170W2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 16229PABPC1-binding
Add
BLAST
Regioni619 – 63012EIF4E-binding By similarity
Add
BLAST
Regioni699 – 1019321eIF3/EIF4A-binding By similarity
Add
BLAST
Regioni1433 – 1585153EIF4A-binding By similarity
Add
BLAST
Regioni1571 – 158515Necessary but not sufficient for MKNK1-binding By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili447 – 47529 Reviewed prediction
Add
BLAST
Coiled coili994 – 102330 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 5 HEAT repeats.
Contains 1 MI domain.
Contains 1 MIF4G domain.
Contains 1 W2 domain.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG301289.
HOVERGENiHBG052083.
InParanoidiO43432.
KOiK03260.
OMAiICKKSCS.
OrthoDBiEOG7D59N2.
PhylomeDBiO43432.
TreeFamiTF101527.

Family and domain databases

Gene3Di1.25.40.180. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
IPR003307. W2_domain.
[Graphical view]
PfamiPF02847. MA3. 1 hit.
PF02854. MIF4G. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00515. eIF5C. 1 hit.
SM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43432-1) [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

MNSQPQTRSP FFQRPQIQPP RATIPNSSPS IRPGAQTPTA VYQANQHIMM     50
VNHLPMPYPV PQGPQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG 100
PGDFPNAYGT PFYPSQPVYQ SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG 150
GKDITEEIMS GGGSRNPTPP IGRPTSTPTP PQQLPSQVPE HSPVVYGTVE 200
SAHLAASTPV TAASDQKQEE KPKPDPVLKS PSPVLRLVLS GEKKEQEGQT 250
SETTAIVSIA ELPLPPSPTT VSSVARSTIA APTSSALSSQ PIFTTAIDDR 300
CELSSPREDT IPIPSLTSCT ETSDPLPTNE NDDDICKKPC SVAPNDIPLV 350
SSTNLINEIN GVSEKLSATE SIVEIVKQEV LPLTLELEIL ENPPEEMKLE 400
CIPAPITPST VPSFPPTPPT PPASPPHTPV IVPAAATTVS SPSAAITVQR 450
VLEEDESIRT CLSEDAKEIQ NKIEVEADGQ TEEILDSQNL NSRRSPVPAQ 500
IAITVPKTWK KPKDRTRTTE EMLEAELELK AEEELSIDKV LESEQDKMSQ 550
GFHPERDPSD LKKVKAVEEN GEEAEPVRNG AESVSEGEGI DANSGSTDSS 600
GDGVTFPFKP ESWKPTDTEG KKQYDREFLL DFQFMPACIQ KPEGLPPISD 650
VVLDKINQPK LPMRTLDPRI LPRGPDFTPA FADFGRQTPG GRGVPLLNVG 700
SRRSQPGQRR EPRKIITVSV KEDVHLKKAE NAWKPSQKRD SQADDPENIK 750
TQELFRKVRS ILNKLTPQMF NQLMKQVSGL TVDTEERLKG VIDLVFEKAI 800
DEPSFSVAYA NMCRCLVTLK VPMADKPGNT VNFRKLLLNR CQKEFEKDKA 850
DDDVFEKKQK ELEAASAPEE RTRLHDELEE AKDKARRRSI GNIKFIGELF 900
KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFEKAKPRMD 950
QYFNQMEKIV KERKTSSRIR FMLQDVIDLR LCNWVSRRAD QGPKTIEQIH 1000
KEAKIEEQEE QRKVQQLMTK EKRRPGVQRV DEGGWNTVQG AKNSRVLDPS 1050
KFLKITKPTI DEKIQLVPKA QLGSWGKGSS GGAKASETDA LRSSASSLNR 1100
FSALQPPAPS GSTPSTPVEF DSRRTLTSRG SMGREKNDKP LPSATARPNT 1150
FMRGGSSKDL LDNQSQEEQR REMLETVKQL TGGVDVERNS TEAERNKTRE 1200
SAKPEISAMS AHDKAALSEE ELERKSKSII DEFLHINDFK EAMQCVEELN 1250
AQGLLHVFVR VGVESTLERS QITRDHMGQL LYQLVQSEKL SKQDFFKGFS 1300
ETLELADDMA IDIPHIWLYL AELVTPMLKE GGISMRELTI EFSKPLLPVG 1350
RAGVLLSEIL HLLCKQMSHK KVGALWREAD LSWKDFLPEG EDVHNFLLEQ 1400
KLDFIESDSP CSSEALSKKE LSAEELYKRL EKLIIEDKAN DEQIFDWVEA 1450
NLDEIQMSSP TFLRALMTAV CKAAIIADSS TFRVDTAVIK QRVPILLKYL 1500
DSDTEKELQA LYALQASIVK LDQPANLLRM FFDCLYDEEV ISEDAFYKWE 1550
SSKDPAEQNG KGVALKSVTA FFTWLREAEE ESEDN 1585
Length:1,585
Mass (Da):176,652
Last modified:March 1, 2001 - v2
Checksum:iEA483139373DCA5C
GO
Isoform 2 (identifier: O43432-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     11-11: F → FAAGPRPPHHQF
     499-504: AQIAIT → ETSNEC
     505-1585: Missing.

Note: No experimental confirmation available.

Show »
Length:515
Mass (Da):55,227
Checksum:i0B4E961F10F62EA0
GO
Isoform 3 (identifier: O43432-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: P → PGGFRPIQ
     182-182: Missing.

Note: No experimental confirmation available.

Show »
Length:1,591
Mass (Da):177,280
Checksum:iA6A4BEC78E05CC92
GO
Isoform 4 (identifier: O43432-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-498: Missing.

Note: No experimental confirmation available.

Show »
Length:1,305
Mass (Da):146,871
Checksum:iEDF74715CD55642D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti378 – 3781Q → R.
Corresponds to variant rs35731992 [ dbSNP | Ensembl ].
VAR_048924
Natural varianti496 – 4961P → A.
Corresponds to variant rs35176330 [ dbSNP | Ensembl ].
VAR_034009
Natural varianti1185 – 11851D → E.
Corresponds to variant rs2230572 [ dbSNP | Ensembl ].
VAR_048925

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei10 – 101P → PGGFRPIQ in isoform 3.
VSP_043447
Alternative sequencei11 – 111F → FAAGPRPPHHQF in isoform 2.
VSP_010487
Alternative sequencei182 – 1821Missing in isoform 3.
VSP_043448
Alternative sequencei219 – 498280Missing in isoform 4.
VSP_054502Add
BLAST
Alternative sequencei499 – 5046AQIAIT → ETSNEC in isoform 2.
VSP_010488
Alternative sequencei505 – 15851081Missing in isoform 2.
VSP_010489Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591M → I in AAH30578. 1 Publication
Sequence conflicti333 – 3331D → G in AAH30578. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF012072 mRNA. Translation: AAC02903.2.
AL031005 Genomic DNA. No translation available.
AL358392, AL606477, AL627311 Genomic DNA. Translation: CAI12155.1.
AL606477, AL358392, AL627311 Genomic DNA. Translation: CAI12534.1.
AL627311, AL358392, AL606477 Genomic DNA. Translation: CAI14553.1.
AL672037 Genomic DNA. No translation available.
CH471134 Genomic DNA. Translation: EAW94956.1.
BC030578 mRNA. Translation: AAH30578.1.
BC094683 mRNA. Translation: AAH94683.1.
BC136643 mRNA. Translation: AAI36644.1.
Z34918 mRNA. Translation: CAA84397.1.
CCDSiCCDS214.1. [O43432-1]
CCDS55580.1. [O43432-3]
CCDS59192.1. [O43432-2]
PIRiS49172.
RefSeqiNP_001185730.1. NM_001198801.1.
NP_001185731.1. NM_001198802.1. [O43432-3]
NP_001185732.1. NM_001198803.1. [O43432-2]
NP_003751.2. NM_003760.4. [O43432-1]
UniGeneiHs.467084.
Hs.732241.

Genome annotation databases

EnsembliENST00000264211; ENSP00000264211; ENSG00000075151. [O43432-1]
ENST00000356916; ENSP00000349386; ENSG00000075151. [O43432-2]
ENST00000374935; ENSP00000364071; ENSG00000075151.
ENST00000374937; ENSP00000364073; ENSG00000075151. [O43432-3]
ENST00000400422; ENSP00000383274; ENSG00000075151. [O43432-1]
ENST00000602326; ENSP00000473510; ENSG00000075151. [O43432-3]
GeneIDi8672.
KEGGihsa:8672.
UCSCiuc001bec.3. human. [O43432-1]
uc001bee.3. human. [O43432-3]
uc001beh.3. human. [O43432-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF012072 mRNA. Translation: AAC02903.2 .
AL031005 Genomic DNA. No translation available.
AL358392 , AL606477 , AL627311 Genomic DNA. Translation: CAI12155.1 .
AL606477 , AL358392 , AL627311 Genomic DNA. Translation: CAI12534.1 .
AL627311 , AL358392 , AL606477 Genomic DNA. Translation: CAI14553.1 .
AL672037 Genomic DNA. No translation available.
CH471134 Genomic DNA. Translation: EAW94956.1 .
BC030578 mRNA. Translation: AAH30578.1 .
BC094683 mRNA. Translation: AAH94683.1 .
BC136643 mRNA. Translation: AAI36644.1 .
Z34918 mRNA. Translation: CAA84397.1 .
CCDSi CCDS214.1. [O43432-1 ]
CCDS55580.1. [O43432-3 ]
CCDS59192.1. [O43432-2 ]
PIRi S49172.
RefSeqi NP_001185730.1. NM_001198801.1.
NP_001185731.1. NM_001198802.1. [O43432-3 ]
NP_001185732.1. NM_001198803.1. [O43432-2 ]
NP_003751.2. NM_003760.4. [O43432-1 ]
UniGenei Hs.467084.
Hs.732241.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HU3 X-ray 2.37 A 745-1003 [» ]
ProteinModelPortali O43432.
SMRi O43432. Positions 136-161, 745-986, 1214-1551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114220. 16 interactions.
DIPi DIP-33245N.
IntActi O43432. 11 interactions.
MINTi MINT-85560.
STRINGi 9606.ENSP00000264211.

PTM databases

PhosphoSitei O43432.

Proteomic databases

MaxQBi O43432.
PaxDbi O43432.
PRIDEi O43432.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264211 ; ENSP00000264211 ; ENSG00000075151 . [O43432-1 ]
ENST00000356916 ; ENSP00000349386 ; ENSG00000075151 . [O43432-2 ]
ENST00000374935 ; ENSP00000364071 ; ENSG00000075151 .
ENST00000374937 ; ENSP00000364073 ; ENSG00000075151 . [O43432-3 ]
ENST00000400422 ; ENSP00000383274 ; ENSG00000075151 . [O43432-1 ]
ENST00000602326 ; ENSP00000473510 ; ENSG00000075151 . [O43432-3 ]
GeneIDi 8672.
KEGGi hsa:8672.
UCSCi uc001bec.3. human. [O43432-1 ]
uc001bee.3. human. [O43432-3 ]
uc001beh.3. human. [O43432-2 ]

Organism-specific databases

CTDi 8672.
GeneCardsi GC01M021132.
HGNCi HGNC:3298. EIF4G3.
HPAi HPA025031.
HPA025039.
HPA025041.
MIMi 603929. gene.
neXtProti NX_O43432.
PharmGKBi PA27724.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301289.
HOVERGENi HBG052083.
InParanoidi O43432.
KOi K03260.
OMAi ICKKSCS.
OrthoDBi EOG7D59N2.
PhylomeDBi O43432.
TreeFami TF101527.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.

Miscellaneous databases

ChiTaRSi EIF4G3. human.
EvolutionaryTracei O43432.
GeneWikii EIF4G3.
GenomeRNAii 8672.
NextBioi 32529.
PMAP-CutDB O43432.
PROi O43432.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43432.
Bgeei O43432.
CleanExi HS_EIF4G3.
Genevestigatori O43432.

Family and domain databases

Gene3Di 1.25.40.180. 3 hits.
InterProi IPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
IPR003307. W2_domain.
[Graphical view ]
Pfami PF02847. MA3. 1 hit.
PF02854. MIF4G. 1 hit.
PF02020. W2. 1 hit.
[Graphical view ]
SMARTi SM00515. eIF5C. 1 hit.
SM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
PROSITEi PS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel functional human eukaryotic translation initiation factor 4G."
    Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S., Sonenberg N.
    Mol. Cell. Biol. 18:334-342(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EIF4A; EIF4E AND EIF3.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 2; 3 AND 4).
    Tissue: PNS and Testis.
  5. "Characterization of secretory proteins of human ovarian follicle cells by cDNA cloning."
    Klaudiny J.J., von der Kammer H.H., Scheit K.K.
    Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 887-1585 (ISOFORM 1).
    Tissue: Ovary.
  6. "A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation."
    Imataka H., Gradi A., Sonenberg N.
    EMBO J. 17:7480-7489(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PABPC1.
  7. "Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I."
    Qin H., Raught B., Sonenberg N., Goldstein E.G., Edelman A.M.
    J. Biol. Chem. 278:48570-48579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1156 BY CAMK1.
  8. "Human rhin4ovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different."
    Gradi A., Svitkin Y.V., Sommergruber W., Imataka H., Morino S., Skern T., Sonenberg N.
    J. Virol. 77:5026-5029(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY RHINOVIRUS PROTEASE.
  9. "Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro."
    Gradi A., Foeger N., Strong R., Svitkin Y.V., Sonenberg N., Skern T., Belsham G.J.
    J. Virol. 78:3271-3278(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY FOOT-AND-MOUTH DISEASE VIRUS PROTEASE.
  10. "eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation."
    Gingras A.-C., Raught B., Sonenberg N.
    Annu. Rev. Biochem. 68:913-963(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-230; SER-232 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-230; SER-232 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Backbone resonance assignment of human eukaryotic translation initiation factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and a 17-amino acid peptide derived from human eIF4GII."
    Miura T., Shiratori Y., Shimma N.
    J. Biomol. NMR 27:279-280(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 621-637 IN COMPLEX WITH EIF4E.
  21. "A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery."
    Marcotrigiano J., Lomakin I.B., Sonenberg N., Pestova T.V., Hellen C.U.T., Burley S.K.
    Mol. Cell 7:193-203(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 745-986, MUTAGENESIS OF ARG-756; ARG-759; LYS-764; ARG-814; LYS-820 AND 834-ARG-LYS-835.

Entry informationi

Entry nameiIF4G3_HUMAN
AccessioniPrimary (citable) accession number: O43432
Secondary accession number(s): B9EGQ7
, Q15597, Q504Z1, Q5SWC3, Q8NEN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 135 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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