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Protein

Eukaryotic translation initiation factor 5B

Gene

Eif5b

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

Functioni

Plays a role in translation initiation. Translational GTPase that catalyzes the joining of the 40S and 60S subunits to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. GTP binding and hydrolysis induces conformational changes in the enzyme that renders it active for productive interactions with the ribosome. The release of the enzyme after formation of the initiation complex is a prerequisite to form elongation-competent ribosomes.By similarity

Catalytic activityi

GTP + H2O = GDP + phosphate.By similarity

Cofactori

a monovalent cationBy similarityNote: Binds 1 monovalent cation per monomer in the active site. Structural cofactor that stabilizes the GTP-bound "on" state. May also act as a transition state stabilizer of the hydrolysis reaction.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi634 – 6418GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 5B (EC:3.6.5.3)
Short name:
eIF-5B
Alternative name(s):
Annexin V-binding protein ABP-7
Translation initiation factor IF-2
Gene namesi
Name:Eif5b
Synonyms:If2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi735017. Eif5b.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12161216Eukaryotic translation initiation factor 5BPRO_0000354073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661PhosphoserineBy similarity
Modified residuei107 – 1071PhosphothreonineBy similarity
Modified residuei108 – 1081PhosphoserineBy similarity
Modified residuei114 – 1141PhosphoserineBy similarity
Modified residuei137 – 1371PhosphoserineBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei184 – 1841PhosphoserineBy similarity
Modified residuei187 – 1871PhosphoserineBy similarity
Modified residuei191 – 1911PhosphoserineBy similarity
Modified residuei209 – 2091PhosphoserineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei223 – 2231PhosphoserineBy similarity
Modified residuei437 – 4371PhosphoserineBy similarity
Modified residuei497 – 4971PhosphothreonineBy similarity
Modified residuei544 – 5441PhosphoserineCombined sources
Modified residuei553 – 5531PhosphoserineCombined sources
Modified residuei556 – 5561PhosphoserineCombined sources
Modified residuei584 – 5841PhosphoserineBy similarity
Modified residuei585 – 5851PhosphoserineBy similarity
Modified residuei587 – 5871PhosphoserineBy similarity
Modified residuei591 – 5911PhosphoserineBy similarity
Modified residuei1164 – 11641PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiB2GUV7.
PeptideAtlasiB2GUV7.
PRIDEiB2GUV7.

PTM databases

iPTMnetiB2GUV7.
PhosphoSiteiB2GUV7.

Expressioni

Gene expression databases

GenevisibleiB2GUV7. RN.

Interactioni

Subunit structurei

Interacts with ANXA5 in a calcium and phospholipid-dependent manner.1 Publication

Protein-protein interaction databases

IntActiB2GUV7. 1 interaction.
STRINGi10116.ENSRNOP00000036844.

Structurei

3D structure databases

ProteinModelPortaliB2GUV7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini625 – 842218tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni634 – 6418G1PROSITE-ProRule annotation
Regioni659 – 6635G2PROSITE-ProRule annotation
Regioni698 – 7014G3PROSITE-ProRule annotation
Regioni752 – 7554G4PROSITE-ProRule annotation
Regioni820 – 8223G5PROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 452414Lys-richAdd
BLAST
Compositional biasi235 – 561327Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1144. Eukaryota.
COG0532. LUCA.
HOGENOMiHOG000105770.
HOVERGENiHBG019036.
InParanoidiB2GUV7.
KOiK03243.
OMAiTEVQENQ.
OrthoDBiEOG7034GC.
PhylomeDBiB2GUV7.
TreeFamiTF101535.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2GUV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKQKNKSE DSTKDDTDLG ALAAEIEGAG AAKEQEPQKG KGKKKKEKKK
60 70 80 90 100
QDFDENDILR ELEELSLEAQ GIGADRDAAT VKPTENNEEE SASKQDKKKK
110 120 130 140 150
GQKGKKTSFD ENDSEELEDK DSKSKKPARP NSEVLLSGSE DADDPNKLSK
160 170 180 190 200
KGKKAQKSTK KRDGSEEDED NSKRSKERSR VNSSGESGGE SDEFLQSRKG
210 220 230 240 250
QKKNQKNKSV PTIDSGNEDD DSSFKIKTVA QKKAEKKERE RKKREEEKAK
260 270 280 290 300
LRKVKEKEEL EKGRKEQSKQ REPQKRPDEE VLVLRGTPDA GAASEEKGDI
310 320 330 340 350
AATLEDDNEG DKKKKDKKKK KTEKDDKEKE KKKGPSKSTV KAIQEALAKL
360 370 380 390 400
REEEERQKRE EEERIKRLEE LEAKRKEEER LEQEKRERKK QKEKERKERL
410 420 430 440 450
KKEGKLLTKS QREARARAEV TLRHLQAQGV EVPSKDSLPK KRPVYEDKKK
460 470 480 490 500
KKTPQQLESK EALETVEVSA PVEVVDQGVP EKEETPPSVD AEEDEETEDA
510 520 530 540 550
GLDDWEAMAS DEEREKEGNM IHIEVEENPE EEEEEEEDED EEDSEDEEDE
560 570 580 590 600
GDSEGSDGDE EDYKLSDEKD LGKAGDTKPN KDASSDSEYD SDDDRTKEER
610 620 630 640 650
AYDKAKRRIE KRRLEHGKNV NTEKLRAPII CVLGHVDTGK TKILDKLRHT
660 670 680 690 700
HVQDGEAGGI TQQIGATNVP LEAINEQTKM IKNFDRENVR IPGMLIIDTP
710 720 730 740 750
GHESFSNLRN RGSSLCDIAI LVVDIMHGLE PQTIESINIL KSKKCPFIVA
760 770 780 790 800
LNKIDRLYDW KKSPDSDVAV TLKKQKKNTK DEFEERAKAI IVEFAQQGLN
810 820 830 840 850
AALFYENKDP RTFVSLVPTS AHTGDGMGSL IYLLVELTQT MLSKRLAHCE
860 870 880 890 900
ELRAQVMEVK ALPGMGTTID VILINGRLKE GDTIIVPGVE GPIVTQIRGL
910 920 930 940 950
LLPPPMKELR VKNQYEKHKE VEAAQGVKIL GKDLEKTLAG LPLLVAYKDD
960 970 980 990 1000
EIPVLKDELI HELKQTLNAI KLEEKGVYVQ ASTLGSLEAL LEFLKTSEVP
1010 1020 1030 1040 1050
YAGINIGPVH KKDVMKASVM LEHDPQYAVI LAFDVRIERD AQEMADSLGV
1060 1070 1080 1090 1100
RIFSAEIIYH LFDAFTKYRQ DYKKQKQEEF KHIAVFPCKM KILPQYIFNS
1110 1120 1130 1140 1150
RDPIVIGVTV EAGQVKQGTP MCVPSKNFVD IGIVTSIEIN HKQVDVAKKG
1160 1170 1180 1190 1200
QEVCVKIEPI PGESPKMFGR HFEATDILVS KISRQSIDAL KDWFRDEMQK
1210
SDWQLIVELK KVFEII
Length:1,216
Mass (Da):137,686
Last modified:June 10, 2008 - v1
Checksum:i515ACABDF33C3D00
GO

Sequence cautioni

The sequence AAI26103.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI67065.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti393 – 3931E → K in AAI26103 (PubMed:15489334).Curated
Sequence conflicti393 – 3931E → K in AAI67065 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC126102 mRNA. Translation: AAI26103.1. Sequence problems.
BC166424 mRNA. Translation: AAI66424.1.
BC167065 mRNA. Translation: AAI67065.1. Sequence problems.
D64061 mRNA. Translation: BAA10937.1.
RefSeqiNP_001103611.1. NM_001110141.1.
UniGeneiRn.107482.

Genome annotation databases

GeneIDi308306.
KEGGirno:308306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC126102 mRNA. Translation: AAI26103.1. Sequence problems.
BC166424 mRNA. Translation: AAI66424.1.
BC167065 mRNA. Translation: AAI67065.1. Sequence problems.
D64061 mRNA. Translation: BAA10937.1.
RefSeqiNP_001103611.1. NM_001110141.1.
UniGeneiRn.107482.

3D structure databases

ProteinModelPortaliB2GUV7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiB2GUV7. 1 interaction.
STRINGi10116.ENSRNOP00000036844.

PTM databases

iPTMnetiB2GUV7.
PhosphoSiteiB2GUV7.

Proteomic databases

PaxDbiB2GUV7.
PeptideAtlasiB2GUV7.
PRIDEiB2GUV7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi308306.
KEGGirno:308306.

Organism-specific databases

CTDi9669.
RGDi735017. Eif5b.

Phylogenomic databases

eggNOGiKOG1144. Eukaryota.
COG0532. LUCA.
HOGENOMiHOG000105770.
HOVERGENiHBG019036.
InParanoidiB2GUV7.
KOiK03243.
OMAiTEVQENQ.
OrthoDBiEOG7034GC.
PhylomeDBiB2GUV7.
TreeFamiTF101535.

Miscellaneous databases

PROiB2GUV7.

Gene expression databases

GenevisibleiB2GUV7. RN.

Family and domain databases

Gene3Di3.40.50.10050. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR023115. TIF_IF2_dom3.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF11987. IF-2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52156. SSF52156. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Embryo, Liver and Lung.
  2. "Molecular cloning and characterization of annexin V-binding proteins with highly hydrophilic peptide structure."
    Ohsawa K., Imai Y., Ito D., Kohsaka S.
    J. Neurochem. 67:89-97(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-334, INTERACTION WITH ANXA5.
    Strain: Wistar.
    Tissue: Brain.
  3. "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-544; SER-553 AND SER-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIF2P_RAT
AccessioniPrimary (citable) accession number: B2GUV7
Secondary accession number(s): A0JN31, P70488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: June 10, 2008
Last modified: July 6, 2016
This is version 71 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, Reference proteome

Documents

  1. 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.