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P20042 (IF2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 2 subunit 2
Alternative name(s):
Eukaryotic translation initiation factor 2 subunit beta
Short name=eIF-2-beta
Gene names
Name:EIF2S2
Synonyms:EIF2B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

male germ cell proliferation

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

translation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 2 complex

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16288713PubMed 16932749. Source: IntAct

translation factor activity, nucleic acid binding

Traceable author statement PubMed 10805737Ref.1. Source: ProtInc

translation initiation factor activity

Inferred from direct assay PubMed 16289705. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 333332Eukaryotic translation initiation factor 2 subunit 2
PRO_0000137406

Regions

Zinc finger281 – 30525C4-type Potential
Compositional bias14 – 218Poly-Lys
Compositional bias79 – 879Poly-Lys
Compositional bias124 – 1296Poly-Lys

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.11 Ref.12
Modified residue21Phosphoserine Ref.4 Ref.9 Ref.11
Modified residue131Phosphoserine By similarity
Modified residue671Phosphoserine Ref.9 Ref.11
Modified residue1051Phosphoserine Ref.7 Ref.11
Modified residue1111Phosphothreonine Ref.7 Ref.11
Modified residue1581Phosphoserine Ref.9
Modified residue2181Phosphoserine By similarity
Modified residue2651N6-acetyllysine Ref.8
Modified residue2931N6-acetyllysine Ref.8

Natural variations

Natural variant1771E → D. Ref.3
Corresponds to variant rs17856024 [ dbSNP | Ensembl ].
VAR_048909

Experimental info

Sequence conflict2951T → I in AAA52383. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P20042 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 3E9FD4B48AA61A51

FASTA33338,388
        10         20         30         40         50         60 
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE DKDLEADEED 

        70         80         90        100        110        120 
TRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD LKIESDVQEP TEPEDDLDIM 

       130        140        150        160        170        180 
LGNKKKKKKN VKFPDEDEIL EKDEALEDED NKKDDGISFS NQTGPAWAGS ERDYTYEELL 

       190        200        210        220        230        240 
NRVFNIMREK NPDMVAGEKR KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL 

       250        260        270        280        290        300 
LAELGTSGSI DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL 

       310        320        330 
QCETCHSRCS VASIKTGFQA VTGKRAQLRA KAN 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the beta subunit of translational initiation factor eIF-2."
Pathak V.K., Nielsen P.J., Trachsel H., Hershey J.W.B.
Cell 54:633-639(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANT ASP-177.
Tissue: Lung and Placenta.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND THR-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67 AND SER-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67; SER-105 AND THR-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29536 mRNA. Translation: AAA52383.1.
AL031668 Genomic DNA. Translation: CAB43741.1.
BC000461 mRNA. Translation: AAH00461.1.
BC000934 mRNA. Translation: AAH00934.1.
CCDSCCDS13231.1.
PIRA31226.
RefSeqNP_003899.2. NM_003908.3.
UniGeneHs.429180.

3D structure databases

ProteinModelPortalP20042.
SMRP20042. Positions 174-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114411. 34 interactions.
IntActP20042. 22 interactions.
MINTMINT-5004121.
STRING9606.ENSP00000364119.

PTM databases

PhosphoSiteP20042.

Polymorphism databases

DMDM12644154.

Proteomic databases

MaxQBP20042.
PRIDEP20042.

Protocols and materials databases

DNASU8894.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374980; ENSP00000364119; ENSG00000125977.
GeneID8894.
KEGGhsa:8894.
UCSCuc002xaf.3. human.

Organism-specific databases

CTD8894.
GeneCardsGC20M032676.
HGNCHGNC:3266. EIF2S2.
HPACAB034415.
HPA041262.
MIM603908. gene.
neXtProtNX_P20042.
PharmGKBPA27696.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000107198.
HOVERGENHBG000927.
InParanoidP20042.
KOK03238.
OMAPTEDKDM.
OrthoDBEOG71ZP2X.
PhylomeDBP20042.
TreeFamTF101503.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP20042.
BgeeP20042.
CleanExHS_EIF2S2.
GenevestigatorP20042.

Family and domain databases

Gene3D3.30.30.50. 1 hit.
InterProIPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SMARTSM00653. eIF2B_5. 1 hit.
[Graphical view]
SUPFAMSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.
ProtoNetSearch...

Other

ChiTaRSEIF2S2. human.
GeneWikiEIF2S2.
GenomeRNAi8894.
NextBio33403.
PROP20042.
SOURCESearch...

Entry information

Entry nameIF2B_HUMAN
AccessionPrimary (citable) accession number: P20042
Secondary accession number(s): Q9BVU0, Q9UJE4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM