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P78344

- IF4G2_HUMAN

UniProt

P78344 - IF4G2_HUMAN

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Protein

Eukaryotic translation initiation factor 4 gamma 2

Gene

EIF4G2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases.4 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. cell cycle arrest Source: ProtInc
  2. cell death Source: ProtInc
  3. cytokine-mediated signaling pathway Source: Reactome
  4. regulation of translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor, Repressor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4 gamma 2
Short name:
eIF-4-gamma 2
Short name:
eIF-4G 2
Short name:
eIF4G 2
Alternative name(s):
Death-associated protein 5
Short name:
DAP-5
p97
Gene namesi
Name:EIF4G2Imported
Synonyms:DAP51 Publication
ORF Names:OK/SW-cl.75
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3297. EIF4G2.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27723.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 907907Eukaryotic translation initiation factor 4 gamma 2PRO_0000213325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei395 – 3951Phosphoserine1 Publication
Modified residuei508 – 5081Phosphothreonine2 Publications
Modified residuei514 – 5141Phosphothreonine1 Publication
Modified residuei902 – 9021Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation; hyperphosphorylated during mitosis.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP78344.
PaxDbiP78344.
PRIDEiP78344.

PTM databases

PhosphoSiteiP78344.

Miscellaneous databases

PMAP-CutDBP78344.

Expressioni

Tissue specificityi

Ubiquitously expressed in all adult tissues examined, with high levels in skeletal muscle and heart. Also expressed in fetal brain, lung, liver and kidney.3 Publications

Gene expression databases

BgeeiP78344.
CleanExiHS_EIF4G2.
ExpressionAtlasiP78344. baseline and differential.
GenevestigatoriP78344.

Organism-specific databases

HPAiCAB005163.
HPA006773.
HPA016965.

Interactioni

Subunit structurei

Interacts with the serine/threonine protein kinases MKNK1 and MKNK2. Binds EIF4A and EIF3. Interacts with MIF4GD.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P299914EBI-296519,EBI-8826747From a different organism.
EIF2S2P200424EBI-296519,EBI-711977
EIF4A1P608423EBI-296519,EBI-73449

Protein-protein interaction databases

BioGridi108297. 25 interactions.
DIPiDIP-31366N.
IntActiP78344. 17 interactions.
MINTiMINT-1182471.
STRINGi9606.ENSP00000340281.

Structurei

Secondary structure

1
907
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi68 – 8619
Turni90 – 923
Helixi93 – 10311
Helixi108 – 12417
Helixi126 – 1283
Helixi129 – 14214
Helixi162 – 18221
Helixi196 – 21823
Turni219 – 2213
Helixi225 – 23612
Beta strandi240 – 2423
Helixi244 – 2463
Helixi248 – 26518
Helixi268 – 2703
Helixi271 – 28212
Turni283 – 2864
Helixi292 – 30615
Turni307 – 3093
Helixi541 – 55818
Helixi561 – 57111
Helixi575 – 5773
Helixi578 – 59013
Helixi594 – 60916
Helixi615 – 62713
Helixi629 – 6357
Helixi639 – 65214
Helixi658 – 6658
Helixi666 – 6683
Turni669 – 6724
Helixi673 – 68412
Helixi687 – 69711
Helixi702 – 7043
Helixi707 – 7093
Helixi712 – 72211
Helixi725 – 7273
Helixi731 – 74313
Helixi747 – 75711
Helixi760 – 7645
Helixi766 – 78419
Helixi799 – 82022
Helixi824 – 84017
Helixi847 – 85711
Helixi863 – 8719
Helixi880 – 89516

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D3MX-ray1.90A/B730-897[»]
3L6AX-ray2.00A540-897[»]
4IULX-ray2.30A/B61-323[»]
ProteinModelPortaliP78344.
SMRiP78344. Positions 78-311, 540-897.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78344.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 308231MIF4GPROSITE-ProRule annotationAdd
BLAST
Domaini543 – 666124MIPROSITE-ProRule annotationAdd
BLAST
Domaini720 – 904185W2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG301289.
HOVERGENiHBG052084.
InParanoidiP78344.
KOiK03260.
OrthoDBiEOG73FQMQ.
PhylomeDBiP78344.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78344-1) [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
MESAIAEGGA SRFSASSGGG GSRGAPQHYP KTAGNSEFLG KTPGQNAQKW
60 70 80 90 100
IPARSTRRDD NSAANNSANE KERHDAIFRK VRGILNKLTP EKFDKLCLEL
110 120 130 140 150
LNVGVESKLI LKGVILLIVD KALEEPKYSS LYAQLCLRLA EDAPNFDGPA
160 170 180 190 200
AEGQPGQKQS TTFRRLLISK LQDEFENRTR NVDVYDKREN PLLPEEEEQR
210 220 230 240 250
AIAKIKMLGN IKFIGELGKL DLIHESILHK CIKTLLEKKK RVQLKDMGED
260 270 280 290 300
LECLCQIMRT VGPRLDHERA KSLMDQYFAR MCSLMLSKEL PARIRFLLQD
310 320 330 340 350
TVELREHHWV PRKAFLDNGP KTINQIRQDA VKDLGVFIPA PMAQGMRSDF
360 370 380 390 400
FLEGPFMPPR MKMDRDPLGG LADMFGQMPG SGIGTGPGVI QDRFSPTMGR
410 420 430 440 450
HRSNQLFNGH GGHIMPPTQS QFGEMGGKFM KSQGLSQLYH NQSQGLLSQL
460 470 480 490 500
QGQSKDMPPR FSKKGQLNAD EISLRPAQSF LMNKNQVPKL QPQITMIPPS
510 520 530 540 550
AQPPRTQTPP LGQTPQLGLK TNPPLIQEKP AKTSKKPPPS KEELLKLTET
560 570 580 590 600
VVTEYLNSGN ANEAVNGVRE MRAPKHFLPE MLSKVIILSL DRSDEDKEKA
610 620 630 640 650
SSLISLLKQE GIATSDNFMQ AFLNVLDQCP KLEVDIPLVK SYLAQFAARA
660 670 680 690 700
IISELVSISE LAQPLESGTH FPLFLLCLQQ LAKLQDREWL TELFQQSKVN
710 720 730 740 750
MQKMLPEIDQ NKDRMLEILE GKGLSFLFPL LKLEKELLKQ IKLDPSPQTI
760 770 780 790 800
YKWIKDNISP KLHVDKGFVN ILMTSFLQYI SSEVNPPSDE TDSSSAPSKE
810 820 830 840 850
QLEQEKQLLL SFKPVMQKFL HDHVDLQVSA LYALQVHCYN SNFPKGMLLR
860 870 880 890 900
FFVHFYDMEI IEEEAFLAWK EDITQEFPGK GKALFQVNQW LTWLETAEEE

ESEEEAD
Length:907
Mass (Da):102,362
Last modified:May 1, 1997 - v1
Checksum:i4EF050B5EEA4DF91
GO
Isoform 2 (identifier: P78344-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     434-471: Missing.

Note: No experimental confirmation available.

Show »
Length:869
Mass (Da):98,150
Checksum:iF400E1E28654A2E4
GO

Sequence cautioni

The sequence BAD97268.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.
The sequence CAA61857.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.
The sequence BAB93515.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691S → P in AAC51166. (PubMed:9030685)Curated
Sequence conflicti233 – 2331K → Q in AAC51166. (PubMed:9030685)Curated
Sequence conflicti245 – 2451K → Q in AAC51166. (PubMed:9030685)Curated
Sequence conflicti351 – 3511F → L in AAC51166. (PubMed:9030685)Curated
Sequence conflicti441 – 4411N → S in AAH18746. (PubMed:15489334)Curated
Sequence conflicti531 – 5311A → G in AAC51166. (PubMed:9030685)Curated
Sequence conflicti534 – 5341S → N in AAH43149. (PubMed:15489334)Curated
Sequence conflicti613 – 6131A → G in AAC51166. (PubMed:9030685)Curated
Sequence conflicti861 – 8611I → S in AAC51166. (PubMed:9030685)Curated
Sequence conflicti899 – 8991E → G in AAC51166. (PubMed:9030685)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti236 – 2361L → M.
Corresponds to variant rs34885591 [ dbSNP | Ensembl ].
VAR_048923

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei434 – 47138Missing in isoform 2. 1 PublicationVSP_038726Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73824 mRNA. Translation: AAB49973.1.
U76111 mRNA. Translation: AAC51166.1.
X89713 mRNA. Translation: CAA61857.1. Sequence problems.
AK223548 mRNA. Translation: BAD97268.1. Sequence problems.
AC116535 Genomic DNA. No translation available.
BC014930 mRNA. Translation: AAH14930.2.
BC018746 mRNA. Translation: AAH18746.1.
BC018975 mRNA. Translation: AAH18975.1.
BC039851 mRNA. Translation: AAH39851.1.
BC043149 mRNA. Translation: AAH43149.2.
BC111415 mRNA. Translation: AAI11416.1.
BC111548 mRNA. Translation: AAI11549.2.
AB063323 mRNA. Translation: BAB93515.1. Different initiation.
CCDSiCCDS31428.1. [P78344-1]
CCDS41618.1. [P78344-2]
RefSeqiNP_001036024.3. NM_001042559.2. [P78344-2]
NP_001166176.1. NM_001172705.1. [P78344-1]
NP_001409.3. NM_001418.3. [P78344-1]
UniGeneiHs.183684.

Genome annotation databases

EnsembliENST00000339995; ENSP00000340281; ENSG00000110321.
GeneIDi1982.
KEGGihsa:1982.
UCSCiuc001mjb.3. human. [P78344-1]
uc001mjd.3. human. [P78344-2]

Polymorphism databases

DMDMi30315906.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73824 mRNA. Translation: AAB49973.1 .
U76111 mRNA. Translation: AAC51166.1 .
X89713 mRNA. Translation: CAA61857.1 . Sequence problems.
AK223548 mRNA. Translation: BAD97268.1 . Sequence problems.
AC116535 Genomic DNA. No translation available.
BC014930 mRNA. Translation: AAH14930.2 .
BC018746 mRNA. Translation: AAH18746.1 .
BC018975 mRNA. Translation: AAH18975.1 .
BC039851 mRNA. Translation: AAH39851.1 .
BC043149 mRNA. Translation: AAH43149.2 .
BC111415 mRNA. Translation: AAI11416.1 .
BC111548 mRNA. Translation: AAI11549.2 .
AB063323 mRNA. Translation: BAB93515.1 . Different initiation.
CCDSi CCDS31428.1. [P78344-1 ]
CCDS41618.1. [P78344-2 ]
RefSeqi NP_001036024.3. NM_001042559.2. [P78344-2 ]
NP_001166176.1. NM_001172705.1. [P78344-1 ]
NP_001409.3. NM_001418.3. [P78344-1 ]
UniGenei Hs.183684.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3D3M X-ray 1.90 A/B 730-897 [» ]
3L6A X-ray 2.00 A 540-897 [» ]
4IUL X-ray 2.30 A/B 61-323 [» ]
ProteinModelPortali P78344.
SMRi P78344. Positions 78-311, 540-897.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108297. 25 interactions.
DIPi DIP-31366N.
IntActi P78344. 17 interactions.
MINTi MINT-1182471.
STRINGi 9606.ENSP00000340281.

PTM databases

PhosphoSitei P78344.

Polymorphism databases

DMDMi 30315906.

Proteomic databases

MaxQBi P78344.
PaxDbi P78344.
PRIDEi P78344.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339995 ; ENSP00000340281 ; ENSG00000110321 .
GeneIDi 1982.
KEGGi hsa:1982.
UCSCi uc001mjb.3. human. [P78344-1 ]
uc001mjd.3. human. [P78344-2 ]

Organism-specific databases

CTDi 1982.
GeneCardsi GC11M010775.
HGNCi HGNC:3297. EIF4G2.
HPAi CAB005163.
HPA006773.
HPA016965.
MIMi 602325. gene.
neXtProti NX_P78344.
PharmGKBi PA27723.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301289.
HOVERGENi HBG052084.
InParanoidi P78344.
KOi K03260.
OrthoDBi EOG73FQMQ.
PhylomeDBi P78344.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.

Miscellaneous databases

ChiTaRSi EIF4G2. human.
EvolutionaryTracei P78344.
GeneWikii EIF4G2.
GenomeRNAii 1982.
NextBioi 8025.
PMAP-CutDB P78344.
PROi P78344.
SOURCEi Search...

Gene expression databases

Bgeei P78344.
CleanExi HS_EIF4G2.
ExpressionAtlasi P78344. baseline and differential.
Genevestigatori P78344.

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 new translational regulator with homology to eukaryotic translation initiation factor 4G."
    Imataka H., Olsen H.S., Sonenberg N.
    EMBO J. 16:817-825(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION OF A NON-AUG INITIATOR START CODON, INTERACTION WITH EIF4A AND EIF3.
    Tissue: Placenta1 Publication.
  2. "A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme."
    Yamanaka S., Poksay K.S., Arnold K.S., Innerarity T.L.
    Genes Dev. 11:321-333(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH EIF4A.
    Tissue: Liver1 Publication.
  3. "DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death."
    Levy-Strumpf N., Deiss L.P., Berissi H., Kimchi A.
    Mol. Cell. Biol. 17:1615-1625(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Kidney1 Publication.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 1 AND 2).
    Tissue: Retinal pigment epithelium, Skin1 Publication and Testis1 Publication.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12, ACETYLATION AT MET-1.
    Tissue: Platelet1 Publication.
  8. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 679-907.
    Tissue: Colon adenocarcinoma1 Publication.
  9. "Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E."
    Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N.
    EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MKNK1.
  10. "Suppression of cap-dependent translation in mitosis."
    Pyronnet S., Dostie J., Sonenberg N.
    Genes Dev. 15:2083-2093(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  11. "The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins."
    Henis-Korenblit S., Shani G., Sines T., Marash L., Shohat G., Kimchi A.
    Proc. Natl. Acad. Sci. U.S.A. 99:5400-5405(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  14. "SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein."
    Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.
    Mol. Cell. Biol. 28:1182-1194(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIF4GD.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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 THR-508, 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-395 AND SER-902, 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-902, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF4G2_HUMAN
AccessioniPrimary (citable) accession number: P78344
Secondary accession number(s): O60877
, P78404, Q0VH00, Q0VH01, Q2NKW9, Q49A79, Q53EU1, Q58EZ2, Q8NI71, Q96C16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 139 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

Miscellaneous

This gene has been shown to be extensively edited in the liver of APOBEC1 transgenic animal model. Its aberrant editing could contribute to the potent oncogenesis induced by overexpression of APOBEC1. The aberrant edited sequence, called NAT1, is likely to be a fundamental translational repressor.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. 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