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Protein

Eukaryotic translation initiation factor 2 subunit 2

Gene

EIF2S2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri281 – 305C4-typeSequence analysisAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionInitiation factor
Biological processProtein biosynthesis
LigandMetal-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
Synonyms:EIF2B
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 4

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001374082 – 333Eukaryotic translation initiation factor 2 subunit 2Add BLAST332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei13Phosphoserine; by PKC; in vitro1 Publication1
Modified residuei36PhosphothreonineBy similarity1
Modified residuei67Phosphoserine; by CK21 Publication1
Cross-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei158PhosphoserineBy similarity1
Modified residuei218Phosphoserine; by PKA; in vitro1 Publication1
Modified residuei265N6-acetyllysineBy similarity1
Modified residuei293N6-acetyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP41035.

PTM databases

iPTMnetiP41035.

Expressioni

Gene expression databases

BgeeiENSOCUG00000000481.

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

STRINGi9986.ENSOCUP00000000420.

Structurei

3D structure databases

ProteinModelPortaliP41035.
SMRiP41035.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi14 – 21Poly-Lys8
Compositional biasi79 – 87Poly-Lys9
Compositional biasi124 – 129Poly-Lys6

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri281 – 305C4-typeSequence analysisAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2768. Eukaryota.
COG1601. LUCA.
GeneTreeiENSGT00390000001804.
HOGENOMiHOG000107198.
HOVERGENiHBG000927.
InParanoidiP41035.
KOiK03238.
OMAiFITCNSC.
OrthoDBiEOG091G0H6A.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
InterProiView protein in InterPro
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
PfamiView protein in Pfam
PF01873. eIF-5_eIF-2B. 1 hit.
SMARTiView protein in SMART
SM00653. eIF2B_5. 1 hit.
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P41035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD AQTEETQPLE TKEVEPEPTE
60 70 80 90 100
DKDVEADEED SRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD
110 120 130 140 150
LKIENDVQEP AEPEDDLDIM LGNKKKKKKN VKFPDEDEIL 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 VTGKRAQLRA KAN
Length:333
Mass (Da):38,326
Last modified:February 1, 1995 - v1
Checksum:i3FFDBAB92DFC1465
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73836 mRNA. Translation: CAA52058.1.
PIRiJC2329.
S13147.
S17871.
RefSeqiNP_001075867.1. NM_001082398.2.
UniGeneiOcu.6223.

Genome annotation databases

EnsembliENSOCUT00000000482; ENSOCUP00000000420; ENSOCUG00000000481.
GeneIDi100009285.
KEGGiocu:100009285.

Similar proteinsi

Entry informationi

Entry nameiIF2B_RABIT
AccessioniPrimary (citable) accession number: P41035
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: August 30, 2017
This is version 110 of the entry and version 1 of the sequence. See 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