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Protein

Eukaryotic translation initiation factor 2 subunit 2

Gene

EIF2S2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri281 – 30525C4-typeSequence analysisAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 2 subunit 2
Alternative name(s):
Eukaryotic translation initiation factor 2 subunit beta
Short name:
eIF-2-beta
Gene namesi
Name:EIF2S2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 333332Eukaryotic translation initiation factor 2 subunit 2PRO_0000247193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei105 – 1051PhosphoserineBy similarity
Modified residuei158 – 1581PhosphoserineBy similarity
Modified residuei218 – 2181PhosphoserineBy similarity
Modified residuei265 – 2651N6-acetyllysineBy similarity
Modified residuei293 – 2931N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5E9D0.
PRIDEiQ5E9D0.

Interactioni

Subunit structurei

Heterotrimer composed of an alpha, a beta and a gamma chain. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007832.

Structurei

3D structure databases

ProteinModelPortaliQ5E9D0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 218Poly-Lys
Compositional biasi79 – 879Poly-Lys
Compositional biasi124 – 1296Poly-Lys

Sequence similaritiesi

Belongs to the eIF-2-beta/eIF-5 family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri281 – 30525C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2768. Eukaryota.
COG1601. LUCA.
HOGENOMiHOG000107198.
HOVERGENiHBG000927.
InParanoidiQ5E9D0.
KOiK03238.
OrthoDBiEOG71ZP2X.
TreeFamiTF101503.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
InterProiIPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5E9D0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD AQTEETQPSE TKEVEPEPTE
60 70 80 90 100
DKDVEADEED SRKKDASDDL DDLNFFNQKK KKKKSKKIFD IDEAEEGIKD
110 120 130 140 150
LKIESDVQEP AEPEEDLDIM LGNKKKKKKV VKFPDEDEVL EKDEALEDED
160 170 180 190 200
SKKDDGISFS NQTGPAWAGS ERDYTYEELL NRVFNIMREK NPDMVAGEKR
210 220 230 240 250
KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL LAELGTSGSI
260 270 280 290 300
DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL
310 320 330
QCETCHSRCS VASIKTGFQA VTGRRAQLRA KAN
Length:333
Mass (Da):38,286
Last modified:March 15, 2005 - v1
Checksum:i96DD5CD2D50FC0B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti324 – 3241R → K in AAI22610 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020990 mRNA. Translation: AAX09007.1.
BC122609 mRNA. Translation: AAI22610.1.
RefSeqiNP_001015621.1. NM_001015621.1.
UniGeneiBt.3458.

Genome annotation databases

GeneIDi520094.
KEGGibta:520094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020990 mRNA. Translation: AAX09007.1.
BC122609 mRNA. Translation: AAI22610.1.
RefSeqiNP_001015621.1. NM_001015621.1.
UniGeneiBt.3458.

3D structure databases

ProteinModelPortaliQ5E9D0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007832.

Proteomic databases

PaxDbiQ5E9D0.
PRIDEiQ5E9D0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi520094.
KEGGibta:520094.

Organism-specific databases

CTDi8894.

Phylogenomic databases

eggNOGiKOG2768. Eukaryota.
COG1601. LUCA.
HOGENOMiHOG000107198.
HOVERGENiHBG000927.
InParanoidiQ5E9D0.
KOiK03238.
OrthoDBiEOG71ZP2X.
TreeFamiTF101503.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
InterProiIPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SMARTiSM00653. eIF2B_5. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Basal ganglia.

Entry informationi

Entry nameiIF2B_BOVIN
AccessioniPrimary (citable) accession number: Q5E9D0
Secondary accession number(s): Q0IIJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 66 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. 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.