Full text data of EIF2S3
EIF2S3
(EIF2G)
[Confidence: low (only semi-automatic identification from reviews)]
Eukaryotic translation initiation factor 2 subunit 3 (Eukaryotic translation initiation factor 2 subunit gamma X; eIF-2-gamma X; eIF-2gX)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation initiation factor 2 subunit 3 (Eukaryotic translation initiation factor 2 subunit gamma X; eIF-2-gamma X; eIF-2gX)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P41091
ID IF2G_HUMAN Reviewed; 472 AA.
AC P41091; B5BTZ4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 3;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma X;
DE Short=eIF-2-gamma X;
DE Short=eIF-2gX;
GN Name=EIF2S3; Synonyms=EIF2G;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Leukemia;
RX PubMed=8106381;
RA Gaspar N.J., Kinzy T.G., Scherer B.J., Huembelin M., Hershey J.W.B.,
RA Merrick W.C.;
RT "Translation initiation factor eIF-2. Cloning and expression of the
RT human cDNA encoding the gamma-subunit.";
RL J. Biol. Chem. 269:3415-3422(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [5]
RP PROTEIN SEQUENCE OF 2-17.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PROTEIN SEQUENCE OF 2-54; 60-75; 182-191; 242-255; 276-285; 290-303;
RP 318-342; 401-416; 453-460 AND 462-472, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, Hepatoma, Lung carcinoma, and
RC Ovarian carcinoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A., Kolch W., Heiserich L.,
RA Gottlieb E., Vousden K.H., Lukashchuk N., Lilla S., Lempens A.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
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).
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.
CC -!- INTERACTION:
CC P05198:EIF2S1; NbExp=4; IntAct=EBI-1054228, EBI-1056162;
CC P20042:EIF2S2; NbExp=3; IntAct=EBI-1054228, EBI-711977;
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EIF2G subfamily.
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; L19161; AAA19696.1; -; mRNA.
DR EMBL; AB451230; BAG70044.1; -; mRNA.
DR EMBL; AB451353; BAG70167.1; -; mRNA.
DR EMBL; CH471074; EAW99010.1; -; Genomic_DNA.
DR EMBL; BC019906; AAH19906.1; -; mRNA.
DR PIR; A53048; A53048.
DR RefSeq; NP_001406.1; NM_001415.3.
DR UniGene; Hs.539684; -.
DR ProteinModelPortal; P41091; -.
DR SMR; P41091; 39-459.
DR IntAct; P41091; 12.
DR MINT; MINT-3015066; -.
DR STRING; 9606.ENSP00000253039; -.
DR PhosphoSite; P41091; -.
DR DMDM; 729816; -.
DR PaxDb; P41091; -.
DR PeptideAtlas; P41091; -.
DR PRIDE; P41091; -.
DR DNASU; 1968; -.
DR Ensembl; ENST00000253039; ENSP00000253039; ENSG00000130741.
DR GeneID; 1968; -.
DR KEGG; hsa:1968; -.
DR UCSC; uc004dbc.3; human.
DR CTD; 1968; -.
DR GeneCards; GC0XP024072; -.
DR HGNC; HGNC:3267; EIF2S3.
DR HPA; CAB012471; -.
DR MIM; 300161; gene.
DR neXtProt; NX_P41091; -.
DR PharmGKB; PA27697; -.
DR eggNOG; COG5257; -.
DR HOVERGEN; HBG006123; -.
DR InParanoid; P41091; -.
DR KO; K03242; -.
DR OMA; CPQPQTK; -.
DR OrthoDB; EOG7H1JK8; -.
DR PhylomeDB; P41091; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF2S3; human.
DR GeneWiki; EIF2S3; -.
DR GenomeRNAi; 1968; -.
DR NextBio; 7979; -.
DR PRO; PR:P41091; -.
DR Bgee; P41091; -.
DR CleanEx; HS_EIF2S3; -.
DR Genevestigator; P41091; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015256; TIF2_gsu_C.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 472 Eukaryotic translation initiation factor
FT 2 subunit 3.
FT /FTId=PRO_0000137438.
FT NP_BIND 48 55 GTP (By similarity).
FT NP_BIND 134 138 GTP (By similarity).
FT NP_BIND 190 193 GTP (By similarity).
FT MOD_RES 2 2 N-acetylalanine; partial.
FT MOD_RES 16 16 Phosphoserine (By similarity).
FT VARIANT 125 125 K -> R (in dbSNP:rs16997659).
FT /FTId=VAR_002352.
SQ SEQUENCE 472 AA; 51109 MW; 7A292A6AAF6DF983 CRC64;
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA
ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE CYRSCGSSTP DEFPTDIPGT
KGNFKLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM
KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV
KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV
KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD
//
ID IF2G_HUMAN Reviewed; 472 AA.
AC P41091; B5BTZ4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 3;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma X;
DE Short=eIF-2-gamma X;
DE Short=eIF-2gX;
GN Name=EIF2S3; Synonyms=EIF2G;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Leukemia;
RX PubMed=8106381;
RA Gaspar N.J., Kinzy T.G., Scherer B.J., Huembelin M., Hershey J.W.B.,
RA Merrick W.C.;
RT "Translation initiation factor eIF-2. Cloning and expression of the
RT human cDNA encoding the gamma-subunit.";
RL J. Biol. Chem. 269:3415-3422(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [5]
RP PROTEIN SEQUENCE OF 2-17.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PROTEIN SEQUENCE OF 2-54; 60-75; 182-191; 242-255; 276-285; 290-303;
RP 318-342; 401-416; 453-460 AND 462-472, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, Hepatoma, Lung carcinoma, and
RC Ovarian carcinoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A., Kolch W., Heiserich L.,
RA Gottlieb E., Vousden K.H., Lukashchuk N., Lilla S., Lempens A.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
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).
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.
CC -!- INTERACTION:
CC P05198:EIF2S1; NbExp=4; IntAct=EBI-1054228, EBI-1056162;
CC P20042:EIF2S2; NbExp=3; IntAct=EBI-1054228, EBI-711977;
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EIF2G subfamily.
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; L19161; AAA19696.1; -; mRNA.
DR EMBL; AB451230; BAG70044.1; -; mRNA.
DR EMBL; AB451353; BAG70167.1; -; mRNA.
DR EMBL; CH471074; EAW99010.1; -; Genomic_DNA.
DR EMBL; BC019906; AAH19906.1; -; mRNA.
DR PIR; A53048; A53048.
DR RefSeq; NP_001406.1; NM_001415.3.
DR UniGene; Hs.539684; -.
DR ProteinModelPortal; P41091; -.
DR SMR; P41091; 39-459.
DR IntAct; P41091; 12.
DR MINT; MINT-3015066; -.
DR STRING; 9606.ENSP00000253039; -.
DR PhosphoSite; P41091; -.
DR DMDM; 729816; -.
DR PaxDb; P41091; -.
DR PeptideAtlas; P41091; -.
DR PRIDE; P41091; -.
DR DNASU; 1968; -.
DR Ensembl; ENST00000253039; ENSP00000253039; ENSG00000130741.
DR GeneID; 1968; -.
DR KEGG; hsa:1968; -.
DR UCSC; uc004dbc.3; human.
DR CTD; 1968; -.
DR GeneCards; GC0XP024072; -.
DR HGNC; HGNC:3267; EIF2S3.
DR HPA; CAB012471; -.
DR MIM; 300161; gene.
DR neXtProt; NX_P41091; -.
DR PharmGKB; PA27697; -.
DR eggNOG; COG5257; -.
DR HOVERGEN; HBG006123; -.
DR InParanoid; P41091; -.
DR KO; K03242; -.
DR OMA; CPQPQTK; -.
DR OrthoDB; EOG7H1JK8; -.
DR PhylomeDB; P41091; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF2S3; human.
DR GeneWiki; EIF2S3; -.
DR GenomeRNAi; 1968; -.
DR NextBio; 7979; -.
DR PRO; PR:P41091; -.
DR Bgee; P41091; -.
DR CleanEx; HS_EIF2S3; -.
DR Genevestigator; P41091; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015256; TIF2_gsu_C.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 472 Eukaryotic translation initiation factor
FT 2 subunit 3.
FT /FTId=PRO_0000137438.
FT NP_BIND 48 55 GTP (By similarity).
FT NP_BIND 134 138 GTP (By similarity).
FT NP_BIND 190 193 GTP (By similarity).
FT MOD_RES 2 2 N-acetylalanine; partial.
FT MOD_RES 16 16 Phosphoserine (By similarity).
FT VARIANT 125 125 K -> R (in dbSNP:rs16997659).
FT /FTId=VAR_002352.
SQ SEQUENCE 472 AA; 51109 MW; 7A292A6AAF6DF983 CRC64;
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA
ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE CYRSCGSSTP DEFPTDIPGT
KGNFKLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM
KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV
KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV
KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD
//
MIM
300161
*RECORD*
*FIELD* NO
300161
*FIELD* TI
*300161 EUKARYOTIC TRANSLATION INITIATION FACTOR 2, SUBUNIT 3; EIF2S3
;;EUKARYOTIC TRANSLATION INITIATION FACTOR 2, GAMMA; EIF2G
read more*FIELD* TX
Translation initiation factor eIF-2 is a heterotrimeric GTP-binding
protein involved in the recruitment of methionyl-tRNA(i) to the 40 S
ribosomal subunit. Gaspar et al. (1994) cloned a human cDNA encoding the
largest subunit of eIF-2, EIF2G. The EIF2G cDNA encodes a 472-amino acid
protein with a molecular mass of 51.8 kD and contains 3 consensus
GTP-binding elements. Human EIF2G is highly related to the yeast
homolog, GCD11, exhibiting 71% sequence identity and an additional 13%
similarity.
Genes controlling the functions of spermatogenesis, Spy, and expression
of the male-specific minor transplantation antigen H-Y, Hya (426000),
map to a region of the short arm of the mouse Y chromosome,
delta-Sxr(b), that lies between the zinc finger genes Zfy1 and Zfy2
(490000) and is deleted in Sxr(b) mutant mice. These Sxr(b) mice arose
from an original sex-reversed mutation, Sxr(a), that carries a
duplication of most of the Y chromosome short arm translocated to the
telomeric end of the pseudoautosomal region of the Y chromosome. Several
genes were mapped to that interval of the mouse Y chromosome and each
was found to have a homolog on the X chromosome. Four of them, Zfy1 and
Zfy2 (490000), Ube1y (489000), and Dffry (400005), are expressed
specifically in the testis and their X homologs (Zfx, 314980; Ube1x,
314370; Dffrx, 300072) are not transcribed from the inactive X
chromosome. A further 2, Smyc (426000) and Uty (400009), are
ubiquitously expressed and their X homologs (Jarid1c/Smcx, 314690; Utx,
300128) escape X inactivation. Ehrmann et al. (1998) identified another
gene from this region of the mouse Y chromosome. It was found to encode
the highly conserved eukaryotic translation initiation factor
eIF-2-gamma. In the mouse this gene was found to be ubiquitously
expressed, to have an X chromosome homolog that maps close to Dmd
(300377), and to escape X inactivation. The coding regions of the X and
Y genes show 86% nucleotide identity and encode the putative products
with 98% amino acid identity. Ehrmann et al. (1998) found that the human
homolog is located on Xp21 and also escapes X inactivation. No evidence
of a Y copy of this gene was found in humans, however. In both humans
and mice, Ehrmann et al. (1998) identified autosomal retroposons of
EIF2G in both humans and mice and an additional retroposon on the X
chromosome in some mouse strains. Ark blot analysis of eutherian and
metatherian genomic DNA indicated that X-Y homologs are present in all
species tested except in simian primates and kangaroo and that
retroposons are common to a wide range of mammals. ('Zoo blots' are
Southern blots of genomic DNA from multiple species without regard to
gender; 'ark blots' are Southern blots used to compare male and female
from multiple species.)
Ehrmann et al. (1998) mapped the human EIF2S3 gene to Xp21 by isotopic
in situ hybridization. The largest number of grains were located on the
region Xp22.2-p22.1. A secondary hybridization repeat was detected on
12p13.2-p12.3. No significant accumulation of grains was detected on the
human Y chromosome.
*FIELD* RF
1. Ehrmann, I. E.; Ellis, P. S.; Mazeyrat, S.; Duthie, S.; Brockdorff,
N.; Mattei, M. G.; Gavin, M. A.; Affara, N. A.; Brown, G. M.; Simpson,
E.; Mitchell, M. J.; Scott, D. M.: Characterization of genes encoding
translation initiation factor eIF-2-gamma in mouse and human: sex
chromosome localization, escape from X-inactivation and evolution. Hum.
Molec. Genet. 7: 1725-1737, 1998.
2. Gaspar, N. J.; Kinzy, T. G.; Scherer, B. J.; Humbelin, M.; Hershey,
J. W. B.; Merrick, W. C.: Translation initiation factor eIF-2: cloning
and expression of the human cDNA encoding the gamma-subunit. J. Biol.
Chem. 269: 3415-3422, 1994.
*FIELD* CD
Victor A. McKusick: 11/30/1998
*FIELD* ED
wwang: 03/13/2008
carol: 8/26/2005
cwells: 3/13/2002
carol: 8/25/2000
carol: 12/2/1998
*RECORD*
*FIELD* NO
300161
*FIELD* TI
*300161 EUKARYOTIC TRANSLATION INITIATION FACTOR 2, SUBUNIT 3; EIF2S3
;;EUKARYOTIC TRANSLATION INITIATION FACTOR 2, GAMMA; EIF2G
read more*FIELD* TX
Translation initiation factor eIF-2 is a heterotrimeric GTP-binding
protein involved in the recruitment of methionyl-tRNA(i) to the 40 S
ribosomal subunit. Gaspar et al. (1994) cloned a human cDNA encoding the
largest subunit of eIF-2, EIF2G. The EIF2G cDNA encodes a 472-amino acid
protein with a molecular mass of 51.8 kD and contains 3 consensus
GTP-binding elements. Human EIF2G is highly related to the yeast
homolog, GCD11, exhibiting 71% sequence identity and an additional 13%
similarity.
Genes controlling the functions of spermatogenesis, Spy, and expression
of the male-specific minor transplantation antigen H-Y, Hya (426000),
map to a region of the short arm of the mouse Y chromosome,
delta-Sxr(b), that lies between the zinc finger genes Zfy1 and Zfy2
(490000) and is deleted in Sxr(b) mutant mice. These Sxr(b) mice arose
from an original sex-reversed mutation, Sxr(a), that carries a
duplication of most of the Y chromosome short arm translocated to the
telomeric end of the pseudoautosomal region of the Y chromosome. Several
genes were mapped to that interval of the mouse Y chromosome and each
was found to have a homolog on the X chromosome. Four of them, Zfy1 and
Zfy2 (490000), Ube1y (489000), and Dffry (400005), are expressed
specifically in the testis and their X homologs (Zfx, 314980; Ube1x,
314370; Dffrx, 300072) are not transcribed from the inactive X
chromosome. A further 2, Smyc (426000) and Uty (400009), are
ubiquitously expressed and their X homologs (Jarid1c/Smcx, 314690; Utx,
300128) escape X inactivation. Ehrmann et al. (1998) identified another
gene from this region of the mouse Y chromosome. It was found to encode
the highly conserved eukaryotic translation initiation factor
eIF-2-gamma. In the mouse this gene was found to be ubiquitously
expressed, to have an X chromosome homolog that maps close to Dmd
(300377), and to escape X inactivation. The coding regions of the X and
Y genes show 86% nucleotide identity and encode the putative products
with 98% amino acid identity. Ehrmann et al. (1998) found that the human
homolog is located on Xp21 and also escapes X inactivation. No evidence
of a Y copy of this gene was found in humans, however. In both humans
and mice, Ehrmann et al. (1998) identified autosomal retroposons of
EIF2G in both humans and mice and an additional retroposon on the X
chromosome in some mouse strains. Ark blot analysis of eutherian and
metatherian genomic DNA indicated that X-Y homologs are present in all
species tested except in simian primates and kangaroo and that
retroposons are common to a wide range of mammals. ('Zoo blots' are
Southern blots of genomic DNA from multiple species without regard to
gender; 'ark blots' are Southern blots used to compare male and female
from multiple species.)
Ehrmann et al. (1998) mapped the human EIF2S3 gene to Xp21 by isotopic
in situ hybridization. The largest number of grains were located on the
region Xp22.2-p22.1. A secondary hybridization repeat was detected on
12p13.2-p12.3. No significant accumulation of grains was detected on the
human Y chromosome.
*FIELD* RF
1. Ehrmann, I. E.; Ellis, P. S.; Mazeyrat, S.; Duthie, S.; Brockdorff,
N.; Mattei, M. G.; Gavin, M. A.; Affara, N. A.; Brown, G. M.; Simpson,
E.; Mitchell, M. J.; Scott, D. M.: Characterization of genes encoding
translation initiation factor eIF-2-gamma in mouse and human: sex
chromosome localization, escape from X-inactivation and evolution. Hum.
Molec. Genet. 7: 1725-1737, 1998.
2. Gaspar, N. J.; Kinzy, T. G.; Scherer, B. J.; Humbelin, M.; Hershey,
J. W. B.; Merrick, W. C.: Translation initiation factor eIF-2: cloning
and expression of the human cDNA encoding the gamma-subunit. J. Biol.
Chem. 269: 3415-3422, 1994.
*FIELD* CD
Victor A. McKusick: 11/30/1998
*FIELD* ED
wwang: 03/13/2008
carol: 8/26/2005
cwells: 3/13/2002
carol: 8/25/2000
carol: 12/2/1998