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Protein

Eukaryotic translation initiation factor 3 subunit A

Gene

tif32

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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 involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit AUniRule annotation
Short name:
eIF3aUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 110 kDa subunit
Short name:
eIF3 p110UniRule annotation
Translation initiation factor eIF3, p110 subunit
Gene namesi
Name:tif32
Synonyms:eif3a
ORF Names:SPBC17D11.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC17D11.05.
PomBaseiSPBC17D11.05. tif32.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytoplasmic stress granule Source: PomBase
  • eukaryotic 43S preinitiation complex Source: PomBase
  • eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic translation initiation factor 3 complex, eIF3e Source: PomBase
  • eukaryotic translation initiation factor 3 complex, eIF3m Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 932932Eukaryotic translation initiation factor 3 subunit APRO_0000123543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei374 – 3741PhosphoserineUniRule annotation1 Publication
Modified residuei501 – 5011PhosphoserineUniRule annotation1 Publication
Modified residuei874 – 8741PhosphoserineUniRule annotation1 Publication
Modified residuei875 – 8751PhosphoserineUniRule annotation1 Publication
Modified residuei877 – 8771PhosphoserineUniRule annotation1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74760.

PTM databases

iPTMnetiO74760.

Interactioni

Subunit structurei

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex. The eIF-3 complex appears to include tif32/eif3a, SPAC25G10.08/eif3b, tif33/eif3c, SPBC4C3.07/eif3f, tif35/eif3g and sum1/eif3i. This set of common subunits may also associate exclusively with either moe1/eif3d and int6/eif3e, or with SPAC821.05/eif3h and SPAC1751.03/eif3m. The eIF-3 complex may also include SPAC3A12.13c/eif3j.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi276482. 9 interactions.
IntActiO74760. 1 interaction.
MINTiMINT-4680529.

Structurei

3D structure databases

ProteinModelPortaliO74760.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini361 – 488128PCIUniRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili537 – 862326UniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit A family.UniRule annotation
Contains 1 PCI domain.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000246822.
InParanoidiO74760.
KOiK03254.
OMAiIGKRIDH.
OrthoDBiEOG7N63WB.
PhylomeDBiO74760.

Family and domain databases

HAMAPiMF_03000. eIF3a.
InterProiIPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74760-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPQGKPEN VLRLADELIA LDQHSSALQS LHETIVLKRS RNAQGFSLEP
60 70 80 90 100
IMMRFIELCV HLRKGKIAKE GLYTYKNAVQ NTSVTAIENV VKHFIELANK
110 120 130 140 150
RVQEAQEKAD KISVEYVDDL EATETPESIM MSLVSGDLSK SRTDRALVTP
160 170 180 190 200
WLKFLWDAYR TVLDILRNNA RLEVMYQLIA NSAFQFCLKY QRKTEFRRLC
210 220 230 240 250
ELLRSHLGNA SKFSNAPHSI NLNDAETMQR HLDMRFSQLN VAVELELWQE
260 270 280 290 300
AFRSIEDIHS LLTFSKRAPA AVMLGNYYRK LIKIFLVCDN YLLHAAAWNR
310 320 330 340 350
YFTFTNVQKP ATANFVILSA LSIPIIDANK LSGPSIEAED AKSKNARLAL
360 370 380 390 400
LLNLSKTPTR ETLIKDAISR GVLSFCDQAI RDLYQILEVE FHPLSICKKL
410 420 430 440 450
QPIIKRLAES NDTAQYIRPL QQVILTRLFQ QLSQVYDSIS LKYVMDLATF
460 470 480 490 500
EEPYDFNPGQ IEKFIMNGNK KGAFSIRLNH IENSISFSSD LFSNPIKSSD
510 520 530 540 550
SVSLQSTPSE LITSQLTRIA KSLSSVLMRF DTDFCLLRKQ QAEAAYERAQ
560 570 580 590 600
AGVEQERKAV IAQRSLLELR RGQADTLATQ REAELAAQRA LKQKQESEAE
610 620 630 640 650
SLRVQEEINK RNAERIRREK EAIRINEAKK LAEELKAKGG LEVNAEDLEH
660 670 680 690 700
LDADKLRAMQ IEQVEKQNKS MNERLRVIGK RIDHLERAYR REAIPLWEED
710 720 730 740 750
AKQQAEHDRE IFYEREKQRK EVQERKHEQA IKDKKAFAQF ASYIHAYKQN
760 770 780 790 800
IDDERDKAYQ EAYAKAKNVI DAERERQRKE IFEQKLAEAI REAEEEAARA
810 820 830 840 850
AEEEANRELH EQEEAQKRAI EERTRAAREA KEREQREMAE KLERQRRIQQ
860 870 880 890 900
ERDEEISRKL AEKAAARRAN IGASSPSPGA WRRGGASAGG VSRDSPRYSR
910 920 930
GGYSRGSVPP RETLAPSKGA YVPPSRRNQQ QQ
Length:932
Mass (Da):107,071
Last modified:November 1, 1998 - v1
Checksum:i120EEDBC5C43DBC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti569 – 5691L → I in BAA13936 (PubMed:9501991).Curated
Sequence conflicti609 – 6102NK → DE in BAA13936 (PubMed:9501991).Curated
Sequence conflicti726 – 74621KHEQA…SYIHA → TSVLLPLMLRCLNDNYVKLL F in BAA13936 (PubMed:9501991).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21076.1.
D89275 mRNA. Translation: BAA13936.1.
PIRiT39716.
T43205.
RefSeqiNP_596379.1. NM_001022300.2.

Genome annotation databases

EnsemblFungiiSPBC17D11.05.1; SPBC17D11.05.1:pep; SPBC17D11.05.
GeneIDi2539938.
KEGGispo:SPBC17D11.05.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21076.1.
D89275 mRNA. Translation: BAA13936.1.
PIRiT39716.
T43205.
RefSeqiNP_596379.1. NM_001022300.2.

3D structure databases

ProteinModelPortaliO74760.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276482. 9 interactions.
IntActiO74760. 1 interaction.
MINTiMINT-4680529.

PTM databases

iPTMnetiO74760.

Proteomic databases

MaxQBiO74760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC17D11.05.1; SPBC17D11.05.1:pep; SPBC17D11.05.
GeneIDi2539938.
KEGGispo:SPBC17D11.05.

Organism-specific databases

EuPathDBiFungiDB:SPBC17D11.05.
PomBaseiSPBC17D11.05. tif32.

Phylogenomic databases

HOGENOMiHOG000246822.
InParanoidiO74760.
KOiK03254.
OMAiIGKRIDH.
OrthoDBiEOG7N63WB.
PhylomeDBiO74760.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20801081.
PROiO74760.

Family and domain databases

HAMAPiMF_03000. eIF3a.
InterProiIPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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.
  2. "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 447-746.
    Strain: PR745.
  3. "Fission yeast homolog of murine Int-6 protein, encoded by mouse mammary tumor virus integration site, is associated with the conserved core subunits of eukaryotic translation initiation factor 3."
    Akiyoshi Y., Clayton J., Phan L., Yamamoto M., Hinnebusch A.G., Watanabe Y., Asano K.
    J. Biol. Chem. 276:10056-10062(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes."
    Zhou C., Arslan F., Wee S., Krishnan S., Ivanov A.R., Oliva A., Leatherwood J., Wolf D.A.
    BMC Biol. 3:14-14(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-501; SER-874; SER-875 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiEIF3A_SCHPO
AccessioniPrimary (citable) accession number: O74760
Secondary accession number(s): P78924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: January 20, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.