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P20042

- IF2B_HUMAN

UniProt

P20042 - IF2B_HUMAN

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Protein

Eukaryotic translation initiation factor 2 subunit 2

Gene

EIF2S2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri281 – 30525C4-typeSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: ProtInc
  4. translation factor activity, nucleic acid binding Source: ProtInc
  5. translation initiation factor activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. in utero embryonic development Source: Ensembl
  4. male germ cell proliferation Source: Ensembl
  5. male gonad development Source: Ensembl
  6. translation Source: Reactome
  7. translational initiation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1815. Recycling of eIF2:GDP.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:3266. EIF2S2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic translation initiation factor 2 complex Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27696.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 333332Eukaryotic translation initiation factor 2 subunit 2PRO_0000137406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei2 – 21Phosphoserine3 Publications
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei67 – 671Phosphoserine2 Publications
Modified residuei105 – 1051Phosphoserine2 Publications
Modified residuei111 – 1111Phosphothreonine2 Publications
Modified residuei158 – 1581Phosphoserine1 Publication
Modified residuei218 – 2181PhosphoserineBy similarity
Modified residuei265 – 2651N6-acetyllysine1 Publication
Modified residuei293 – 2931N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP20042.
PRIDEiP20042.

PTM databases

PhosphoSiteiP20042.

Expressioni

Gene expression databases

BgeeiP20042.
CleanExiHS_EIF2S2.
ExpressionAtlasiP20042. baseline and differential.
GenevestigatoriP20042.

Organism-specific databases

HPAiCAB034415.
HPA041262.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF2S1P051985EBI-711977,EBI-1056162
EIF2S3P410914EBI-711977,EBI-1054228
EIF4G2P783444EBI-711977,EBI-296519

Protein-protein interaction databases

BioGridi114411. 46 interactions.
IntActiP20042. 22 interactions.
MINTiMINT-5004121.
STRINGi9606.ENSP00000364119.

Structurei

3D structure databases

ProteinModelPortaliP20042.
SMRiP20042. Positions 174-305.
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

HOGENOMiHOG000107198.
HOVERGENiHBG000927.
InParanoidiP20042.
KOiK03238.
OMAiPTEDKDM.
OrthoDBiEOG71ZP2X.
PhylomeDBiP20042.
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.

P20042-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE
60 70 80 90 100
DKDLEADEED TRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD
110 120 130 140 150
LKIESDVQEP TEPEDDLDIM LGNKKKKKKN VKFPDEDEIL EKDEALEDED
160 170 180 190 200
NKKDDGISFS 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):38,388
Last modified:December 1, 2000 - v2
Checksum:i3E9FD4B48AA61A51
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti295 – 2951T → I in AAA52383. (PubMed:3044606)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771E → D.1 Publication
Corresponds to variant rs17856024 [ dbSNP | Ensembl ].
VAR_048909

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29536 mRNA. Translation: AAA52383.1.
AL031668 Genomic DNA. Translation: CAB43741.1.
BC000461 mRNA. Translation: AAH00461.1.
BC000934 mRNA. Translation: AAH00934.1.
CCDSiCCDS13231.1.
PIRiA31226.
RefSeqiNP_003899.2. NM_003908.3.
UniGeneiHs.429180.

Genome annotation databases

EnsembliENST00000374980; ENSP00000364119; ENSG00000125977.
GeneIDi8894.
KEGGihsa:8894.
UCSCiuc002xaf.3. human.

Polymorphism databases

DMDMi12644154.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29536 mRNA. Translation: AAA52383.1 .
AL031668 Genomic DNA. Translation: CAB43741.1 .
BC000461 mRNA. Translation: AAH00461.1 .
BC000934 mRNA. Translation: AAH00934.1 .
CCDSi CCDS13231.1.
PIRi A31226.
RefSeqi NP_003899.2. NM_003908.3.
UniGenei Hs.429180.

3D structure databases

ProteinModelPortali P20042.
SMRi P20042. Positions 174-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114411. 46 interactions.
IntActi P20042. 22 interactions.
MINTi MINT-5004121.
STRINGi 9606.ENSP00000364119.

PTM databases

PhosphoSitei P20042.

Polymorphism databases

DMDMi 12644154.

Proteomic databases

MaxQBi P20042.
PRIDEi P20042.

Protocols and materials databases

DNASUi 8894.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374980 ; ENSP00000364119 ; ENSG00000125977 .
GeneIDi 8894.
KEGGi hsa:8894.
UCSCi uc002xaf.3. human.

Organism-specific databases

CTDi 8894.
GeneCardsi GC20M032676.
HGNCi HGNC:3266. EIF2S2.
HPAi CAB034415.
HPA041262.
MIMi 603908. gene.
neXtProti NX_P20042.
PharmGKBi PA27696.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000107198.
HOVERGENi HBG000927.
InParanoidi P20042.
KOi K03238.
OMAi PTEDKDM.
OrthoDBi EOG71ZP2X.
PhylomeDBi P20042.
TreeFami TF101503.

Enzyme and pathway databases

Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1815. Recycling of eIF2:GDP.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSi EIF2S2. human.
GeneWikii EIF2S2.
GenomeRNAii 8894.
NextBioi 33403.
PROi P20042.
SOURCEi Search...

Gene expression databases

Bgeei P20042.
CleanExi HS_EIF2S2.
ExpressionAtlasi P20042. baseline and differential.
Genevestigatori P20042.

Family and domain databases

Gene3Di 3.30.30.50. 1 hit.
InterProi IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view ]
Pfami PF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view ]
SMARTi SM00653. eIF2B_5. 1 hit.
[Graphical view ]
SUPFAMi SSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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].

Entry informationi

Entry nameiIF2B_HUMAN
AccessioniPrimary (citable) accession number: P20042
Secondary accession number(s): Q9BVU0, Q9UJE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: December 1, 2000
Last modified: November 26, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3