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Q10475 (IF4G_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 4 gamma

Short name=eIF-4-gamma
Short name=eIF-4G
Gene names
Name:tif471
ORF Names:SPAC17C9.03
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1403 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subcellular location

Cytoplasmperinuclear region. Note: Localized to the perinuclear region, the growing tips and septum. Ref.1

Sequence similarities

Belongs to the eukaryotic initiation factor 4G family.

Contains 1 MIF4G domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14031403Eukaryotic translation initiation factor 4 gamma
PRO_0000213333

Regions

Domain1009 – 1245237MIF4G

Amino acid modifications

Modified residue831Phosphoserine Ref.4
Modified residue4521Phosphoserine Ref.4
Modified residue4551Phosphoserine Ref.4
Modified residue4561Phosphoserine Ref.4
Modified residue4591Phosphoserine Ref.4
Modified residue8661Phosphoserine Ref.4
Modified residue8821Phosphoserine Ref.4
Modified residue8841Phosphothreonine Ref.4
Modified residue8861Phosphoserine Ref.4
Modified residue9111Phosphoserine Ref.4
Modified residue9191Phosphoserine Ref.4
Modified residue9211Phosphoserine Ref.4
Modified residue9231Phosphotyrosine Ref.4
Modified residue13331Phosphoserine Ref.4

Experimental info

Sequence conflict10171N → T in BAA13842. Ref.3
Sequence conflict12491K → L in BAA13842. Ref.3
Sequence conflict12531E → G in BAA13842. Ref.3
Sequence conflict12571K → G in BAA13842. Ref.3
Sequence conflict13011N → T in BAA13842. Ref.3
Sequence conflict13041F → P in BAA13842. Ref.3
Sequence conflict13531S → Y in BAA13842. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q10475 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0317EE65BE2A1E63

FASTA1,403154,035
        10         20         30         40         50         60 
MSSKPPSNTP KFSYARALAS SQSNKSNSTK ASENNTATAE KQAVKPSGVE PTNTSRANAQ 

        70         80         90        100        110        120 
KKTESTGKIT SEADTEKYNS SKSPVNKEGS VEKKSSEKSS TNNKPWRGDN TSKPSANSSA 

       130        140        150        160        170        180 
ERTSSQHQKP ETSSQIGKDN AAPVENVNEK STSQETAPPV STVPIQFGSI TRNAAIPSKP 

       190        200        210        220        230        240 
KVSGNMQNKS GVSSYSSKSQ SVNSSVTSNP PHTEEPVAAK PEASSTATKG PRPTTSASNT 

       250        260        270        280        290        300 
NTSPANGAPT NKPSTDINTT DPATQTTQVS ASNSPALSGS STPSNTSSRS NRQNHGNFSE 

       310        320        330        340        350        360 
KRHYDRYGNS HPSYNKYSHY QHGFNYNNSG NNRNESGHPR FRNSRRNYNN QGAYPTYMSN 

       370        380        390        400        410        420 
GRSANQSPRN NPQNVNNGST PIQIPVSLQT PYGQVYGQPQ YIVDPNMVQY GPILQPGYVP 

       430        440        450        460        470        480 
QYYPVYHQTP YTQNFPNMSR SGSQVSDQVV ESPNSSTLSP RNGFAPIVKQ QKKSSALKIV 

       490        500        510        520        530        540 
NPVTHTEVVV PQKNASSPNP SETNSRAETP TAAPPQISEE EASQRKDAIK LAIQQRIQEK 

       550        560        570        580        590        600 
AEAEAKRKAE EKARLEAEEN AKREAEEQAK REAEEKAKRE AEEKAKREAE EKAKREAEEN 

       610        620        630        640        650        660 
AKREAEEKAK REAEEKAKRE AEEKAKREAE EKAKREAEEK AKREAEEKAK REAEEKAKRE 

       670        680        690        700        710        720 
AEENAKREAE EKAKREAEEN AKREAEEKVK RETEENAKRK AEEEGKREAD KNPEIKSSAP 

       730        740        750        760        770        780 
LASSEANVDT SKQTNATEPE VVDKTKVEKL KASEGKSTSS LSSPSHSTSS KRDLLSGLES 

       790        800        810        820        830        840 
LSLKTNPKSE QCLESLLNSQ FITDFSALVY PSTIKPPSTE EALKAGKYEY DVPFLLQFQS 

       850        860        870        880        890        900 
VYTDKPMKGW DERMKETVAS AFSDKSSRGM YSSSRQSSRS GSNTHSHAGP GFGGPSERKG 

       910        920        930        940        950        960 
ISRLGIDRGF SSSGAGFGSG SNYKSAPSRG VSHHGHGGMS GSHRGSQRGS RRGGGERDKP 

       970        980        990       1000       1010       1020 
DPSSLTIPVD QVAPLQLSAN RWQPKKLTEK PAETKGEDEE ALLPPEVVQR KVKGSLNKMT 

      1030       1040       1050       1060       1070       1080 
LEKFDKISDQ ILEIAMQSRK ENDGRTLKQV IQLTFEKATD EPNFSNMYAR FARKMMDSID 

      1090       1100       1110       1120       1130       1140 
DSIRDEGVLD KNNQPVRGGL LFRKYLLSRC QEDFERGWKA NLPSGKAGEA EIMSDEYYVA 

      1150       1160       1170       1180       1190       1200 
AAIKRRGLGL VRFIGELFKL SMLSEKIMHE CIKRLLGNVT DPEEEEIESL CRLLMTVGVN 

      1210       1220       1230       1240       1250       1260 
IDATEKGHAA MDVYVLRMET ITKIPNLPSR IKFMLMDVMD SRKNGWAVKN EVEKGPKTIA 

      1270       1280       1290       1300       1310       1320 
EIHEEAERKK ALAESQRPSS GRMHGRDMNR GDSRMGGRGS NPPFSSSDWS NNKDGYARLG 

      1330       1340       1350       1360       1370       1380 
QGIRGLKSGT QGSHGPTSLS SMLKGGSVSR TPSRQNSALR REQSVRAPPS NVAVTSANSF 

      1390       1400 
ELLEEHDHDN DGGQKDSNSK TSS 

« Hide

References

« Hide 'large scale' references
[1]"Overproduction of a conserved domain of fission yeast and mammalian translation initiation factor eIF4G causes aberrant cell morphology and results in disruption of the localization of F-actin and the organization of microtubules."
Hashemzadeh-Bonehi L., Curtis P.S., Morley S.J., Thorpe J.R., Pain V.M.
Genes Cells 8:163-178(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 865-1403.
Strain: PR745.
[4]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-452; SER-455; SER-456; SER-459; SER-866; SER-882; THR-884; SER-886; SER-911; SER-919; SER-921; TYR-923 AND SER-1333, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAA97349.1.
D89180 mRNA. Translation: BAA13842.1.
PIRT11583.
T42624.
RefSeqNP_594602.1. NM_001020030.2.

3D structure databases

ProteinModelPortalQ10475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278758. 9 interactions.
IntActQ10475. 2 interactions.
MINTMINT-4699578.
STRING4896.SPAC17C9.03-1.

Proteomic databases

PaxDbQ10475.
PRIDEQ10475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC17C9.03.1; SPAC17C9.03.1:pep; SPAC17C9.03.
GeneID2542290.
KEGGspo:SPAC17C9.03.

Organism-specific databases

PomBaseSPAC17C9.03.

Phylogenomic databases

eggNOGNOG301289.
KOK03260.
OMANPVSAQN.
OrthoDBEOG7VTDWG.

Family and domain databases

Gene3D1.25.40.180. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR022745. eIF4G1_eIF4E-bd.
IPR012969. Fibrinogen_BP.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamPF12152. eIF_4G1. 1 hit.
PF08017. Fibrinogen_BP. 1 hit.
PF02854. MIF4G. 1 hit.
[Graphical view]
SMARTSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMSSF101489. SSF101489. 1 hit.
SSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

NextBio20803353.
PROQ10475.

Entry information

Entry nameIF4G_SCHPO
AccessionPrimary (citable) accession number: Q10475
Secondary accession number(s): P78832
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Translation initiation factors

List of translation initiation factor entries