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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. poly(A) RNA binding Source: UniProtKB
  2. RNA cap binding Source: ProtInc
  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. 1 Publication

Organism-specific databases

PharmGKBiPA27724.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681PhosphothreonineBy similarity
Modified residuei230 – 2301Phosphoserine2 Publications
Modified residuei232 – 2321Phosphoserine2 Publications
Modified residuei267 – 2671PhosphoserineBy 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

BgeeiO43432.
CleanExiHS_EIF4G3.
ExpressionAtlasiO43432. baseline and differential.
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).By similarity

Protein-protein interaction databases

BioGridi114220. 25 interactions.
DIPiDIP-33245N.
IntActiO43432. 13 interactions.
MINTiMINT-85560.
STRINGi9606.ENSP00000264211.

Structurei

Secondary structure

1
1585
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi746 – 76217Combined sources
Helixi770 – 7778Combined sources
Helixi785 – 80117Combined sources
Helixi803 – 8053Combined sources
Helixi806 – 81611Combined sources
Helixi833 – 84816Combined sources
Helixi885 – 90016Combined sources
Turni901 – 9033Combined sources
Helixi907 – 91913Combined sources
Helixi923 – 94018Combined sources
Turni943 – 9453Combined sources
Helixi946 – 96116Combined sources
Helixi967 – 98115Combined sources
Turni982 – 9843Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO43432.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati745 – 78339HEAT 1Add
BLAST
Domaini755 – 983229MIF4GPROSITE-ProRule annotationAdd
BLAST
Repeati784 – 83148HEAT 2Add
BLAST
Repeati832 – 90574HEAT 3Add
BLAST
Repeati906 – 94439HEAT 4Add
BLAST
Repeati945 – 98440HEAT 5Add
BLAST
Domaini1221 – 1343123MIPROSITE-ProRule annotationAdd
BLAST
Domaini1416 – 1585170W2PROSITE-ProRule annotationAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili447 – 47529Sequence AnalysisAdd
BLAST
Coiled coili994 – 102330Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 5 HEAT repeats.Curated
Contains 1 MI domain.PROSITE-ProRule annotation
Contains 1 MIF4G domain.Curated
Contains 1 W2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG301289.
GeneTreeiENSGT00530000063038.
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

        10         20         30         40         50
MNSQPQTRSP FFQRPQIQPP RATIPNSSPS IRPGAQTPTA VYQANQHIMM
60 70 80 90 100
VNHLPMPYPV PQGPQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG
110 120 130 140 150
PGDFPNAYGT PFYPSQPVYQ SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG
160 170 180 190 200
GKDITEEIMS GGGSRNPTPP IGRPTSTPTP PQQLPSQVPE HSPVVYGTVE
210 220 230 240 250
SAHLAASTPV TAASDQKQEE KPKPDPVLKS PSPVLRLVLS GEKKEQEGQT
260 270 280 290 300
SETTAIVSIA ELPLPPSPTT VSSVARSTIA APTSSALSSQ PIFTTAIDDR
310 320 330 340 350
CELSSPREDT IPIPSLTSCT ETSDPLPTNE NDDDICKKPC SVAPNDIPLV
360 370 380 390 400
SSTNLINEIN GVSEKLSATE SIVEIVKQEV LPLTLELEIL ENPPEEMKLE
410 420 430 440 450
CIPAPITPST VPSFPPTPPT PPASPPHTPV IVPAAATTVS SPSAAITVQR
460 470 480 490 500
VLEEDESIRT CLSEDAKEIQ NKIEVEADGQ TEEILDSQNL NSRRSPVPAQ
510 520 530 540 550
IAITVPKTWK KPKDRTRTTE EMLEAELELK AEEELSIDKV LESEQDKMSQ
560 570 580 590 600
GFHPERDPSD LKKVKAVEEN GEEAEPVRNG AESVSEGEGI DANSGSTDSS
610 620 630 640 650
GDGVTFPFKP ESWKPTDTEG KKQYDREFLL DFQFMPACIQ KPEGLPPISD
660 670 680 690 700
VVLDKINQPK LPMRTLDPRI LPRGPDFTPA FADFGRQTPG GRGVPLLNVG
710 720 730 740 750
SRRSQPGQRR EPRKIITVSV KEDVHLKKAE NAWKPSQKRD SQADDPENIK
760 770 780 790 800
TQELFRKVRS ILNKLTPQMF NQLMKQVSGL TVDTEERLKG VIDLVFEKAI
810 820 830 840 850
DEPSFSVAYA NMCRCLVTLK VPMADKPGNT VNFRKLLLNR CQKEFEKDKA
860 870 880 890 900
DDDVFEKKQK ELEAASAPEE RTRLHDELEE AKDKARRRSI GNIKFIGELF
910 920 930 940 950
KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFEKAKPRMD
960 970 980 990 1000
QYFNQMEKIV KERKTSSRIR FMLQDVIDLR LCNWVSRRAD QGPKTIEQIH
1010 1020 1030 1040 1050
KEAKIEEQEE QRKVQQLMTK EKRRPGVQRV DEGGWNTVQG AKNSRVLDPS
1060 1070 1080 1090 1100
KFLKITKPTI DEKIQLVPKA QLGSWGKGSS GGAKASETDA LRSSASSLNR
1110 1120 1130 1140 1150
FSALQPPAPS GSTPSTPVEF DSRRTLTSRG SMGREKNDKP LPSATARPNT
1160 1170 1180 1190 1200
FMRGGSSKDL LDNQSQEEQR REMLETVKQL TGGVDVERNS TEAERNKTRE
1210 1220 1230 1240 1250
SAKPEISAMS AHDKAALSEE ELERKSKSII DEFLHINDFK EAMQCVEELN
1260 1270 1280 1290 1300
AQGLLHVFVR VGVESTLERS QITRDHMGQL LYQLVQSEKL SKQDFFKGFS
1310 1320 1330 1340 1350
ETLELADDMA IDIPHIWLYL AELVTPMLKE GGISMRELTI EFSKPLLPVG
1360 1370 1380 1390 1400
RAGVLLSEIL HLLCKQMSHK KVGALWREAD LSWKDFLPEG EDVHNFLLEQ
1410 1420 1430 1440 1450
KLDFIESDSP CSSEALSKKE LSAEELYKRL EKLIIEDKAN DEQIFDWVEA
1460 1470 1480 1490 1500
NLDEIQMSSP TFLRALMTAV CKAAIIADSS TFRVDTAVIK QRVPILLKYL
1510 1520 1530 1540 1550
DSDTEKELQA LYALQASIVK LDQPANLLRM FFDCLYDEEV ISEDAFYKWE
1560 1570 1580
SSKDPAEQNG KGVALKSVTA FFTWLREAEE ESEDN
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591M → I in AAH30578. (PubMed:15489334)Curated
Sequence conflicti333 – 3331D → G in AAH30578. (PubMed:15489334)Curated

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. 1 PublicationVSP_043447
Alternative sequencei11 – 111F → FAAGPRPPHHQF in isoform 2. 1 PublicationVSP_010487
Alternative sequencei182 – 1821Missing in isoform 3. 1 PublicationVSP_043448
Alternative sequencei219 – 498280Missing in isoform 4. 1 PublicationVSP_054502Add
BLAST
Alternative sequencei499 – 5046AQIAIT → ETSNEC in isoform 2. 1 PublicationVSP_010488
Alternative sequencei505 – 15851081Missing in isoform 2. 1 PublicationVSP_010489Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [O43432-4]
ENST00000602326; ENSP00000473510; ENSG00000075151. [O43432-3]
GeneIDi8672.
KEGGihsa:8672.
UCSCiuc001bec.3. human. [O43432-1]
uc001bee.3. human. [O43432-3]
uc001beh.3. human. [O43432-2]
uc009vpz.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 25 interactions.
DIPi DIP-33245N.
IntActi O43432. 13 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 . [O43432-4 ]
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 ]
uc009vpz.3. human.

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.
GeneTreei ENSGT00530000063038.
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

Bgeei O43432.
CleanExi HS_EIF4G3.
ExpressionAtlasi O43432. baseline and differential.
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: November 26, 2014
This is version 138 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