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Protein

Eukaryotic translation initiation factor 5

Gene

Eif5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 348GTPSequence analysis

GO - Molecular functioni

  • eukaryotic initiation factor eIF2 binding Source: RGD
  • GTP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: Ensembl
  • translation initiation factor activity Source: RGD

GO - Biological processi

  • activation of GTPase activity Source: RGD
  • formation of translation preinitiation complex Source: RGD
  • regulation of translational initiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-72702. Ribosomal scanning and start codon recognition.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 5
Short name:
eIF-5
Gene namesi
Name:Eif5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi619861. Eif5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Eukaryotic translation initiation factor 5PRO_0000212518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei225 – 2251PhosphothreonineBy similarity
Modified residuei227 – 2271PhosphoserineCombined sources
Modified residuei387 – 3871PhosphoserineCombined sources1 Publication
Modified residuei388 – 3881PhosphoserineCombined sources1 Publication
Modified residuei408 – 4081PhosphoserineBy similarity
Modified residuei417 – 4171PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ07205.
PRIDEiQ07205.

PTM databases

iPTMnetiQ07205.
PhosphoSiteiQ07205.
SwissPalmiQ07205.

Expressioni

Gene expression databases

GenevisibleiQ07205. RN.

Interactioni

Subunit structurei

Interacts with FMR1; this interaction occurs in a RNA-dependent manner.By similarity

GO - Molecular functioni

  • eukaryotic initiation factor eIF2 binding Source: RGD

Protein-protein interaction databases

BioGridi248584. 1 interaction.
STRINGi10116.ENSRNOP00000013695.

Structurei

3D structure databases

ProteinModelPortaliQ07205.
SMRiQ07205. Positions 3-150, 230-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini231 – 390160W2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi194 – 2007Asp/Glu-rich (highly acidic)
Compositional biasi382 – 40019Asp/Glu-rich (highly acidic)Add
BLAST
Compositional biasi421 – 4277Asp-rich (acidic)

Sequence similaritiesi

Belongs to the eIF-2-beta/eIF-5 family.Curated
Contains 1 W2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2767. Eukaryota.
COG1601. LUCA.
GeneTreeiENSGT00390000016478.
HOGENOMiHOG000214327.
HOVERGENiHBG006132.
InParanoidiQ07205.
KOiK03262.
OMAiPPHTMEE.
OrthoDBiEOG7FV3QF.
PhylomeDBiQ07205.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
3.30.30.50. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR016021. MIF4-like.
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
IPR003307. W2_domain.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
SM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF75689. SSF75689. 1 hit.
PROSITEiPS51363. W2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP
60 70 80 90 100
TYPTKYFGCE LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP
110 120 130 140 150
ECENPETDLH VNPKKQTIGN SCKACGYRGM LDTHHKLCTF ILKNPPENSD
160 170 180 190 200
IGTGKKEKEK KNRKGKDKEN GSVSTSETPP PPPPNEISPP HAVEEEEDDD
210 220 230 240 250
WGEDTTEEAQ RRRMDEISDH AKGLTLSDDL ERTVEERVNI LFDFVKKKKE
260 270 280 290 300
EGIIDSSDKD IVAEAERLDV KAMGPLVLTE VLFDEKIREQ IKKYRRHFLR
310 320 330 340 350
FCHNNKKAQR YLLHGLECVV AMHQAQLISK IPHILKEMYD ADLLEEEVII
360 370 380 390 400
SWSEKASKKY VSKELAKEIR VKAEPFIKWL KEAEEESSGG EEEDEDENIE
410 420
VVYSKTASVP KVETVKSDNK DDDIDIDAI
Length:429
Mass (Da):48,954
Last modified:October 1, 1994 - v1
Checksum:iB1A62E30936908EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11651 mRNA. Translation: AAA41112.1.
BC062398 mRNA. Translation: AAH62398.1.
PIRiA47305.
RefSeqiNP_064460.1. NM_020075.1.
XP_006240670.1. XM_006240608.1.
XP_006240671.1. XM_006240609.2.
UniGeneiRn.40123.

Genome annotation databases

EnsembliENSRNOT00000013695; ENSRNOP00000013695; ENSRNOG00000010218.
GeneIDi56783.
KEGGirno:56783.
UCSCiRGD:619861. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11651 mRNA. Translation: AAA41112.1.
BC062398 mRNA. Translation: AAH62398.1.
PIRiA47305.
RefSeqiNP_064460.1. NM_020075.1.
XP_006240670.1. XM_006240608.1.
XP_006240671.1. XM_006240609.2.
UniGeneiRn.40123.

3D structure databases

ProteinModelPortaliQ07205.
SMRiQ07205. Positions 3-150, 230-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248584. 1 interaction.
STRINGi10116.ENSRNOP00000013695.

PTM databases

iPTMnetiQ07205.
PhosphoSiteiQ07205.
SwissPalmiQ07205.

Proteomic databases

PaxDbiQ07205.
PRIDEiQ07205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000013695; ENSRNOP00000013695; ENSRNOG00000010218.
GeneIDi56783.
KEGGirno:56783.
UCSCiRGD:619861. rat.

Organism-specific databases

CTDi1983.
RGDi619861. Eif5.

Phylogenomic databases

eggNOGiKOG2767. Eukaryota.
COG1601. LUCA.
GeneTreeiENSGT00390000016478.
HOGENOMiHOG000214327.
HOVERGENiHBG006132.
InParanoidiQ07205.
KOiK03262.
OMAiPPHTMEE.
OrthoDBiEOG7FV3QF.
PhylomeDBiQ07205.

Enzyme and pathway databases

ReactomeiR-RNO-72702. Ribosomal scanning and start codon recognition.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

PROiQ07205.

Gene expression databases

GenevisibleiQ07205. RN.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
3.30.30.50. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR016021. MIF4-like.
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
IPR003307. W2_domain.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
SM00515. eIF5C. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF75689. SSF75689. 1 hit.
PROSITEiPS51363. W2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of cDNA for mammalian translation initiation factor 5."
    Das K., Chevesich J., Maitra U.
    Proc. Natl. Acad. Sci. U.S.A. 90:3058-3062(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 131-150; 215-242 AND 339-353.
    Tissue: Liver.
  2. "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].
    Tissue: Prostate.
  3. "Phosphorylation of mammalian translation initiation factor 5 (eIF5) in vitro and in vivo."
    Majumdar R., Bandyopadhyay A., Deng H., Maitra U.
    Nucleic Acids Res. 30:1154-1162(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-387 AND SER-388.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-227; SER-387 AND SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF5_RAT
AccessioniPrimary (citable) accession number: Q07205
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. 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.