Full text data of EIF2S2
EIF2S2
(EIF2B)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Eukaryotic translation initiation factor 2 subunit 2 (Eukaryotic translation initiation factor 2 subunit beta; eIF-2-beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation initiation factor 2 subunit 2 (Eukaryotic translation initiation factor 2 subunit beta; eIF-2-beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P20042
ID IF2B_HUMAN Reviewed; 333 AA.
AC P20042; Q9BVU0; Q9UJE4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 2.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 2;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE Short=eIF-2-beta;
GN Name=EIF2S2; Synonyms=EIF2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3044606; DOI=10.1016/S0092-8674(88)80007-2;
RA Pathak V.K., Nielsen P.J., Trachsel H., Hershey J.W.B.;
RT "Structure of the beta subunit of translational initiation factor eIF-
RT 2.";
RL Cell 54:633-639(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-177.
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND THR-111, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-293, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67 AND SER-158,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2; SER-67; SER-105 AND THR-111, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis
CC by forming a ternary complex with GTP and initiator tRNA. This
CC complex binds to a 40S ribosomal subunit, followed by mRNA binding
CC to form a 43S preinitiation complex. Junction of the 60S ribosomal
CC subunit to form the 80S initiation complex is preceded by
CC hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP
CC binary complex. In order for eIF-2 to recycle and catalyze another
CC round of initiation, the GDP bound to eIF-2 must exchange with GTP
CC by way of a reaction catalyzed by eIF-2B.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma
CC chain. Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By
CC similarity).
CC -!- INTERACTION:
CC P05198:EIF2S1; NbExp=6; IntAct=EBI-711977, EBI-1056162;
CC P41091:EIF2S3; NbExp=3; IntAct=EBI-711977, EBI-1054228;
CC P78344:EIF4G2; NbExp=4; IntAct=EBI-711977, EBI-296519;
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M29536; AAA52383.1; -; mRNA.
DR EMBL; AL031668; CAB43741.1; -; Genomic_DNA.
DR EMBL; BC000461; AAH00461.1; -; mRNA.
DR EMBL; BC000934; AAH00934.1; -; mRNA.
DR PIR; A31226; A31226.
DR RefSeq; NP_003899.2; NM_003908.3.
DR UniGene; Hs.429180; -.
DR ProteinModelPortal; P20042; -.
DR SMR; P20042; 174-305.
DR IntAct; P20042; 22.
DR MINT; MINT-5004121; -.
DR STRING; 9606.ENSP00000364119; -.
DR PhosphoSite; P20042; -.
DR DMDM; 12644154; -.
DR PRIDE; P20042; -.
DR DNASU; 8894; -.
DR Ensembl; ENST00000374980; ENSP00000364119; ENSG00000125977.
DR GeneID; 8894; -.
DR KEGG; hsa:8894; -.
DR UCSC; uc002xaf.3; human.
DR CTD; 8894; -.
DR GeneCards; GC20M032676; -.
DR HGNC; HGNC:3266; EIF2S2.
DR HPA; CAB034415; -.
DR MIM; 603908; gene.
DR neXtProt; NX_P20042; -.
DR PharmGKB; PA27696; -.
DR HOGENOM; HOG000107198; -.
DR HOVERGEN; HBG000927; -.
DR InParanoid; P20042; -.
DR KO; K03238; -.
DR OMA; PTEDKDM; -.
DR OrthoDB; EOG71ZP2X; -.
DR PhylomeDB; P20042; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF2S2; human.
DR GeneWiki; EIF2S2; -.
DR GenomeRNAi; 8894; -.
DR NextBio; 33403; -.
DR PRO; PR:P20042; -.
DR ArrayExpress; P20042; -.
DR Bgee; P20042; -.
DR CleanEx; HS_EIF2S2; -.
DR Genevestigator; P20042; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0002176; P:male germ cell proliferation; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR Gene3D; 3.30.30.50; -; 1.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Initiation factor; Metal-binding;
KW Phosphoprotein; Polymorphism; Protein biosynthesis;
KW Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 333 Eukaryotic translation initiation factor
FT 2 subunit 2.
FT /FTId=PRO_0000137406.
FT ZN_FING 281 305 C4-type (Potential).
FT COMPBIAS 14 21 Poly-Lys.
FT COMPBIAS 79 87 Poly-Lys.
FT COMPBIAS 124 129 Poly-Lys.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 13 13 Phosphoserine (By similarity).
FT MOD_RES 67 67 Phosphoserine.
FT MOD_RES 105 105 Phosphoserine.
FT MOD_RES 111 111 Phosphothreonine.
FT MOD_RES 158 158 Phosphoserine.
FT MOD_RES 218 218 Phosphoserine (By similarity).
FT MOD_RES 265 265 N6-acetyllysine.
FT MOD_RES 293 293 N6-acetyllysine.
FT VARIANT 177 177 E -> D (in dbSNP:rs17856024).
FT /FTId=VAR_048909.
FT CONFLICT 295 295 T -> I (in Ref. 1; AAA52383).
SQ SEQUENCE 333 AA; 38388 MW; 3E9FD4B48AA61A51 CRC64;
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE DKDLEADEED
TRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD LKIESDVQEP TEPEDDLDIM
LGNKKKKKKN VKFPDEDEIL EKDEALEDED NKKDDGISFS NQTGPAWAGS ERDYTYEELL
NRVFNIMREK NPDMVAGEKR KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL
LAELGTSGSI DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL
QCETCHSRCS VASIKTGFQA VTGKRAQLRA KAN
//
ID IF2B_HUMAN Reviewed; 333 AA.
AC P20042; Q9BVU0; Q9UJE4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 2.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 2;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE Short=eIF-2-beta;
GN Name=EIF2S2; Synonyms=EIF2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3044606; DOI=10.1016/S0092-8674(88)80007-2;
RA Pathak V.K., Nielsen P.J., Trachsel H., Hershey J.W.B.;
RT "Structure of the beta subunit of translational initiation factor eIF-
RT 2.";
RL Cell 54:633-639(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-177.
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND THR-111, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-293, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-67 AND SER-158,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2; SER-67; SER-105 AND THR-111, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis
CC by forming a ternary complex with GTP and initiator tRNA. This
CC complex binds to a 40S ribosomal subunit, followed by mRNA binding
CC to form a 43S preinitiation complex. Junction of the 60S ribosomal
CC subunit to form the 80S initiation complex is preceded by
CC hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP
CC binary complex. In order for eIF-2 to recycle and catalyze another
CC round of initiation, the GDP bound to eIF-2 must exchange with GTP
CC by way of a reaction catalyzed by eIF-2B.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma
CC chain. Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By
CC similarity).
CC -!- INTERACTION:
CC P05198:EIF2S1; NbExp=6; IntAct=EBI-711977, EBI-1056162;
CC P41091:EIF2S3; NbExp=3; IntAct=EBI-711977, EBI-1054228;
CC P78344:EIF4G2; NbExp=4; IntAct=EBI-711977, EBI-296519;
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M29536; AAA52383.1; -; mRNA.
DR EMBL; AL031668; CAB43741.1; -; Genomic_DNA.
DR EMBL; BC000461; AAH00461.1; -; mRNA.
DR EMBL; BC000934; AAH00934.1; -; mRNA.
DR PIR; A31226; A31226.
DR RefSeq; NP_003899.2; NM_003908.3.
DR UniGene; Hs.429180; -.
DR ProteinModelPortal; P20042; -.
DR SMR; P20042; 174-305.
DR IntAct; P20042; 22.
DR MINT; MINT-5004121; -.
DR STRING; 9606.ENSP00000364119; -.
DR PhosphoSite; P20042; -.
DR DMDM; 12644154; -.
DR PRIDE; P20042; -.
DR DNASU; 8894; -.
DR Ensembl; ENST00000374980; ENSP00000364119; ENSG00000125977.
DR GeneID; 8894; -.
DR KEGG; hsa:8894; -.
DR UCSC; uc002xaf.3; human.
DR CTD; 8894; -.
DR GeneCards; GC20M032676; -.
DR HGNC; HGNC:3266; EIF2S2.
DR HPA; CAB034415; -.
DR MIM; 603908; gene.
DR neXtProt; NX_P20042; -.
DR PharmGKB; PA27696; -.
DR HOGENOM; HOG000107198; -.
DR HOVERGEN; HBG000927; -.
DR InParanoid; P20042; -.
DR KO; K03238; -.
DR OMA; PTEDKDM; -.
DR OrthoDB; EOG71ZP2X; -.
DR PhylomeDB; P20042; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF2S2; human.
DR GeneWiki; EIF2S2; -.
DR GenomeRNAi; 8894; -.
DR NextBio; 33403; -.
DR PRO; PR:P20042; -.
DR ArrayExpress; P20042; -.
DR Bgee; P20042; -.
DR CleanEx; HS_EIF2S2; -.
DR Genevestigator; P20042; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0002176; P:male germ cell proliferation; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR Gene3D; 3.30.30.50; -; 1.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Initiation factor; Metal-binding;
KW Phosphoprotein; Polymorphism; Protein biosynthesis;
KW Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 333 Eukaryotic translation initiation factor
FT 2 subunit 2.
FT /FTId=PRO_0000137406.
FT ZN_FING 281 305 C4-type (Potential).
FT COMPBIAS 14 21 Poly-Lys.
FT COMPBIAS 79 87 Poly-Lys.
FT COMPBIAS 124 129 Poly-Lys.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 13 13 Phosphoserine (By similarity).
FT MOD_RES 67 67 Phosphoserine.
FT MOD_RES 105 105 Phosphoserine.
FT MOD_RES 111 111 Phosphothreonine.
FT MOD_RES 158 158 Phosphoserine.
FT MOD_RES 218 218 Phosphoserine (By similarity).
FT MOD_RES 265 265 N6-acetyllysine.
FT MOD_RES 293 293 N6-acetyllysine.
FT VARIANT 177 177 E -> D (in dbSNP:rs17856024).
FT /FTId=VAR_048909.
FT CONFLICT 295 295 T -> I (in Ref. 1; AAA52383).
SQ SEQUENCE 333 AA; 38388 MW; 3E9FD4B48AA61A51 CRC64;
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE DKDLEADEED
TRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEGVKD LKIESDVQEP TEPEDDLDIM
LGNKKKKKKN VKFPDEDEIL EKDEALEDED NKKDDGISFS NQTGPAWAGS ERDYTYEELL
NRVFNIMREK NPDMVAGEKR KFVMKPPQVV RVGTKKTSFV NFTDICKLLH RQPKHLLAFL
LAELGTSGSI DGNNQLVIKG RFQQKQIENV LRRYIKEYVT CHTCRSPDTI LQKDTRLYFL
QCETCHSRCS VASIKTGFQA VTGKRAQLRA KAN
//
MIM
603908
*RECORD*
*FIELD* NO
603908
*FIELD* TI
*603908 EUKARYOTIC TRANSLATION INITIATION FACTOR 2, SUBUNIT 2; EIF2S2
;;EUKARYOTIC TRANSLATION INITIATION FACTOR 2-BETA
read more*FIELD* TX
DESCRIPTION
The translation initiation factor eIF2 consists of 3 nonidentical
subunits, alpha (EIF2S1; 603907), beta, and gamma (EIF2S3; 300161), all
of which are required for the catalytic utilization of eIF2 during
protein synthesis initiation.
CLONING
By screening a mouse expression library with antibodies against eIF2,
Pathak et al. (1988) isolated partial mouse cDNAs encoding eIF2-beta.
They then used a mouse cDNA to screen a human liver library and
recovered human eIF2-beta cDNAs. The predicted 333-amino acid human
protein contains putative GTP-binding sites, a zinc finger motif, and a
highly charged N-terminal region composed of 3 basic polylysine blocks
separated by acidic domains. Overall, human eIF2-beta shares 42%
sequence identity with the yeast Sui3/eIF2-beta protein; the polylysine
and zinc finger domains are highly conserved. Pathak et al. (1988)
stated that the presence of these domains suggests that eIF2-beta
interacts with RNA. Northern blot analysis revealed that eIF2-beta is
expressed as a 1.6-kb mRNA in HeLa cells.
GENE STRUCTURE
Based on Southern blot analysis, Chiorini et al. (1999) reported that
there are 4 copies of the eIF2-beta gene in the human genome, but only 1
contains the entire cDNA sequence and introns. The functional eIF2-beta
gene contains 9 exons and spans 28 kb.
GENE FUNCTION
Chiorini et al. (1999) demonstrated that, as with eIF2-alpha, eIF2-beta
expression is regulated at the transcriptional level by the alpha-Pal
(NRF1; 600879) transcription factor. However, while the eIF2-alpha
promoter contains 2 alpha-Pal binding sites, the eIF2-beta promoter has
only 1.
Eukaryotic translation initiation factor-5 (EIF5; 601710) functions in
start site selection as a GTPase accelerating protein (GAP) for the
EIF2-GTP-tRNAi(Met) ternary complex within the ribosome-bound
preinitiation complex (summary by Jennings and Pavitt (2010)). Jennings
and Pavitt (2010) defined new regulatory functions of EIF5 in the
recycling of EIF2 from its inactive EIF2-GDP state between successive
rounds of translation initiation. First, the authors showed that EIF5
stabilizes the binding of GDP to EIF2 and is therefore a bifunctional
protein that acts as a GDP dissociation inhibitor (GDI). Jennings and
Pavitt (2010) found that this activity is independent of the GAP
function and identified conserved residues within EIF5 that are
necessary for this role. In addition, Jennings and Pavitt (2010) showed
that EIF5 is a critical component of the EIF2(alpha-P) regulatory
complex that inhibits the activity of the guanine-nucleotide exchange
factor (GEF) EIF2B. Jennings and Pavitt (2010) concluded that their
findings defined a new step in the translation initiation pathway, one
that is critical for normal translational controls.
ANIMAL MODEL
The agouti (ASIP; 600201)-yellow (Ay) deletion is the only genetic
modifier known to suppress testicular germ cell tumor (TGCT; 273300)
susceptibility in mice or human. The Ay mutation deletes Raly and Eif2s2
and induces the ectopic expression of agouti, all of which are potential
TGCT-modifying mutations. Heaney et al. (2009) reported that the reduced
TGCT incidence of heterozygous Ay male mice and the recessive embryonic
lethality of Ay are caused by the deletion of Eif2s2. The incidence of
affected males was reduced 2-fold in mice that were partially deficient
for Eif2s2 and that embryonic lethality occurred near the time of
implantation in mice that were fully deficient for Eif2s2. In contrast,
neither reduced expression of Raly in gene-trap mice nor ectopic
expression of agouti in transgenic or viable-yellow (Avy) mutants
affected TGCT incidence or embryonic viability. Partial deficiency of
Eif2s2 attenuated germ cell proliferation and differentiation, both of
which are important to TGCT formation. Heaney et al. (2009) concluded
that germ cell development and TGCT pathogenesis are sensitive to the
availability of the eIF2 translation initiation complex and to changes
in the rate of translation.
*FIELD* RF
1. Chiorini, J. A.; Miyamoto, S.; Harkin, S. J.; Safer, B.: Genomic
cloning and characterization of the human eukaryotic initiation factor-2-beta
promoter. J. Biol. Chem. 274: 4195-4201, 1999.
2. Heaney, J. D.; Michelson, M. V.; Youngren, K. K.; Lam, M.-Y. J.;
Nadeau, J. H.: Deletion of eIF2beta suppresses testicular cancer
incidence and causes recessive lethality in agouti-yellow mice. Hum.
Molec. Genet. 18: 1395-1404, 2009.
3. Jennings, M. D.; Pavitt, G. D.: eIF5 has GDI activity necessary
for translational control by eIF2 phosphorylation. Nature 465: 378-381,
2010. Note: Erratum: Nature 468: 122 only, 2010.
4. Pathak, V. K.; Nielsen, P. J.; Trachsel, H.; Hershey, J. W. B.
: Structure of the beta subunit of translational initiation factor
eIF-2. Cell 54: 633-639, 1988.
*FIELD* CN
Ada Hamosh - updated: 6/2/2010
George E. Tiller - updated: 11/25/2009
*FIELD* CD
Rebekah S. Rasooly: 6/15/1999
*FIELD* ED
alopez: 03/08/2012
alopez: 1/5/2011
alopez: 6/7/2010
terry: 6/2/2010
wwang: 1/6/2010
terry: 11/25/2009
alopez: 7/20/1999
alopez: 6/16/1999
*RECORD*
*FIELD* NO
603908
*FIELD* TI
*603908 EUKARYOTIC TRANSLATION INITIATION FACTOR 2, SUBUNIT 2; EIF2S2
;;EUKARYOTIC TRANSLATION INITIATION FACTOR 2-BETA
read more*FIELD* TX
DESCRIPTION
The translation initiation factor eIF2 consists of 3 nonidentical
subunits, alpha (EIF2S1; 603907), beta, and gamma (EIF2S3; 300161), all
of which are required for the catalytic utilization of eIF2 during
protein synthesis initiation.
CLONING
By screening a mouse expression library with antibodies against eIF2,
Pathak et al. (1988) isolated partial mouse cDNAs encoding eIF2-beta.
They then used a mouse cDNA to screen a human liver library and
recovered human eIF2-beta cDNAs. The predicted 333-amino acid human
protein contains putative GTP-binding sites, a zinc finger motif, and a
highly charged N-terminal region composed of 3 basic polylysine blocks
separated by acidic domains. Overall, human eIF2-beta shares 42%
sequence identity with the yeast Sui3/eIF2-beta protein; the polylysine
and zinc finger domains are highly conserved. Pathak et al. (1988)
stated that the presence of these domains suggests that eIF2-beta
interacts with RNA. Northern blot analysis revealed that eIF2-beta is
expressed as a 1.6-kb mRNA in HeLa cells.
GENE STRUCTURE
Based on Southern blot analysis, Chiorini et al. (1999) reported that
there are 4 copies of the eIF2-beta gene in the human genome, but only 1
contains the entire cDNA sequence and introns. The functional eIF2-beta
gene contains 9 exons and spans 28 kb.
GENE FUNCTION
Chiorini et al. (1999) demonstrated that, as with eIF2-alpha, eIF2-beta
expression is regulated at the transcriptional level by the alpha-Pal
(NRF1; 600879) transcription factor. However, while the eIF2-alpha
promoter contains 2 alpha-Pal binding sites, the eIF2-beta promoter has
only 1.
Eukaryotic translation initiation factor-5 (EIF5; 601710) functions in
start site selection as a GTPase accelerating protein (GAP) for the
EIF2-GTP-tRNAi(Met) ternary complex within the ribosome-bound
preinitiation complex (summary by Jennings and Pavitt (2010)). Jennings
and Pavitt (2010) defined new regulatory functions of EIF5 in the
recycling of EIF2 from its inactive EIF2-GDP state between successive
rounds of translation initiation. First, the authors showed that EIF5
stabilizes the binding of GDP to EIF2 and is therefore a bifunctional
protein that acts as a GDP dissociation inhibitor (GDI). Jennings and
Pavitt (2010) found that this activity is independent of the GAP
function and identified conserved residues within EIF5 that are
necessary for this role. In addition, Jennings and Pavitt (2010) showed
that EIF5 is a critical component of the EIF2(alpha-P) regulatory
complex that inhibits the activity of the guanine-nucleotide exchange
factor (GEF) EIF2B. Jennings and Pavitt (2010) concluded that their
findings defined a new step in the translation initiation pathway, one
that is critical for normal translational controls.
ANIMAL MODEL
The agouti (ASIP; 600201)-yellow (Ay) deletion is the only genetic
modifier known to suppress testicular germ cell tumor (TGCT; 273300)
susceptibility in mice or human. The Ay mutation deletes Raly and Eif2s2
and induces the ectopic expression of agouti, all of which are potential
TGCT-modifying mutations. Heaney et al. (2009) reported that the reduced
TGCT incidence of heterozygous Ay male mice and the recessive embryonic
lethality of Ay are caused by the deletion of Eif2s2. The incidence of
affected males was reduced 2-fold in mice that were partially deficient
for Eif2s2 and that embryonic lethality occurred near the time of
implantation in mice that were fully deficient for Eif2s2. In contrast,
neither reduced expression of Raly in gene-trap mice nor ectopic
expression of agouti in transgenic or viable-yellow (Avy) mutants
affected TGCT incidence or embryonic viability. Partial deficiency of
Eif2s2 attenuated germ cell proliferation and differentiation, both of
which are important to TGCT formation. Heaney et al. (2009) concluded
that germ cell development and TGCT pathogenesis are sensitive to the
availability of the eIF2 translation initiation complex and to changes
in the rate of translation.
*FIELD* RF
1. Chiorini, J. A.; Miyamoto, S.; Harkin, S. J.; Safer, B.: Genomic
cloning and characterization of the human eukaryotic initiation factor-2-beta
promoter. J. Biol. Chem. 274: 4195-4201, 1999.
2. Heaney, J. D.; Michelson, M. V.; Youngren, K. K.; Lam, M.-Y. J.;
Nadeau, J. H.: Deletion of eIF2beta suppresses testicular cancer
incidence and causes recessive lethality in agouti-yellow mice. Hum.
Molec. Genet. 18: 1395-1404, 2009.
3. Jennings, M. D.; Pavitt, G. D.: eIF5 has GDI activity necessary
for translational control by eIF2 phosphorylation. Nature 465: 378-381,
2010. Note: Erratum: Nature 468: 122 only, 2010.
4. Pathak, V. K.; Nielsen, P. J.; Trachsel, H.; Hershey, J. W. B.
: Structure of the beta subunit of translational initiation factor
eIF-2. Cell 54: 633-639, 1988.
*FIELD* CN
Ada Hamosh - updated: 6/2/2010
George E. Tiller - updated: 11/25/2009
*FIELD* CD
Rebekah S. Rasooly: 6/15/1999
*FIELD* ED
alopez: 03/08/2012
alopez: 1/5/2011
alopez: 6/7/2010
terry: 6/2/2010
wwang: 1/6/2010
terry: 11/25/2009
alopez: 7/20/1999
alopez: 6/16/1999