IF2M_HUMAN
ID IF2M_HUMAN Reviewed; 727 AA.
AC P46199; D6W5D0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial;
DE Short=IF-2(Mt);
DE Short=IF-2Mt;
DE Short=IF2(mt);
DE Flags: Precursor;
GN Name=MTIF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-59 AND ILE-556.
RC TISSUE=Liver;
RX PubMed=7829522; DOI=10.1074/jbc.270.4.1859;
RA Ma L., Spremulli L.L.;
RT "Cloning and sequence analysis of the human mitochondrial translational
RT initiation factor 2 cDNA.";
RL J. Biol. Chem. 270:1859-1865(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS ASN-59 AND ILE-556.
RC TISSUE=Heart;
RX PubMed=12932832; DOI=10.1016/s0167-4781(03)00144-1;
RA Overman R.G. Jr., Enderle P.J., Farrow J.M. III, Wiley J.E., Farwell M.A.;
RT "The human mitochondrial translation initiation factor 2 gene (MTIF2):
RT transcriptional analysis and identification of a pseudogene.";
RL Biochim. Biophys. Acta 1628:195-205(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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., Buerckstuemmer T.,
RA 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest level in
CC skeletal muscle.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; L34600; AAA67038.1; -; mRNA.
DR EMBL; AF494407; AAM14617.1; -; mRNA.
DR EMBL; AF495546; AAM70196.1; -; Genomic_DNA.
DR EMBL; AF495543; AAM70196.1; JOINED; Genomic_DNA.
DR EMBL; AF495544; AAM70196.1; JOINED; Genomic_DNA.
DR EMBL; AF495545; AAM70196.1; JOINED; Genomic_DNA.
DR EMBL; AC012358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00104.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00105.1; -; Genomic_DNA.
DR CCDS; CCDS1853.1; -.
DR PIR; A55628; A55628.
DR RefSeq; NP_001005369.1; NM_001005369.1.
DR RefSeq; NP_001307930.1; NM_001321001.1.
DR RefSeq; NP_001307931.1; NM_001321002.1.
DR RefSeq; NP_001307932.1; NM_001321003.1.
DR RefSeq; NP_001307933.1; NM_001321004.1.
DR RefSeq; NP_001307934.1; NM_001321005.1.
DR RefSeq; NP_002444.2; NM_002453.2.
DR RefSeq; XP_005264392.1; XM_005264335.3.
DR RefSeq; XP_011531173.1; XM_011532871.2.
DR RefSeq; XP_016859651.1; XM_017004162.1.
DR RefSeq; XP_016859652.1; XM_017004163.1.
DR PDB; 6GAW; EM; 3.20 A; BC=78-727.
DR PDB; 6GAZ; EM; 3.10 A; BC=78-727.
DR PDB; 6GB2; EM; 3.20 A; BC=78-727.
DR PDB; 6RW5; EM; 3.14 A; 7=37-727.
DR PDBsum; 6GAW; -.
DR PDBsum; 6GAZ; -.
DR PDBsum; 6GB2; -.
DR PDBsum; 6RW5; -.
DR AlphaFoldDB; P46199; -.
DR SMR; P46199; -.
DR BioGRID; 110625; 329.
DR CORUM; P46199; -.
DR DIP; DIP-27596N; -.
DR IntAct; P46199; 42.
DR MINT; P46199; -.
DR STRING; 9606.ENSP00000263629; -.
DR GlyGen; P46199; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46199; -.
DR PhosphoSitePlus; P46199; -.
DR BioMuta; MTIF2; -.
DR DMDM; 223590069; -.
DR EPD; P46199; -.
DR jPOST; P46199; -.
DR MassIVE; P46199; -.
DR MaxQB; P46199; -.
DR PaxDb; P46199; -.
DR PeptideAtlas; P46199; -.
DR PRIDE; P46199; -.
DR ProteomicsDB; 55735; -.
DR Antibodypedia; 1037; 82 antibodies from 19 providers.
DR DNASU; 4528; -.
DR Ensembl; ENST00000263629.9; ENSP00000263629.4; ENSG00000085760.15.
DR Ensembl; ENST00000394600.7; ENSP00000378099.3; ENSG00000085760.15.
DR Ensembl; ENST00000403721.5; ENSP00000384481.1; ENSG00000085760.15.
DR GeneID; 4528; -.
DR KEGG; hsa:4528; -.
DR MANE-Select; ENST00000263629.9; ENSP00000263629.4; NM_002453.3; NP_002444.2.
DR UCSC; uc002ryo.3; human.
DR CTD; 4528; -.
DR DisGeNET; 4528; -.
DR GeneCards; MTIF2; -.
DR HGNC; HGNC:7441; MTIF2.
DR HPA; ENSG00000085760; Low tissue specificity.
DR MIM; 603766; gene.
DR neXtProt; NX_P46199; -.
DR OpenTargets; ENSG00000085760; -.
DR PharmGKB; PA31243; -.
DR VEuPathDB; HostDB:ENSG00000085760; -.
DR eggNOG; KOG1145; Eukaryota.
DR GeneTree; ENSGT00900000141103; -.
DR HOGENOM; CLU_006301_5_2_1; -.
DR InParanoid; P46199; -.
DR OMA; LYAWPWP; -.
DR OrthoDB; 1124591at2759; -.
DR PhylomeDB; P46199; -.
DR TreeFam; TF105682; -.
DR PathwayCommons; P46199; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR SignaLink; P46199; -.
DR BioGRID-ORCS; 4528; 168 hits in 1078 CRISPR screens.
DR ChiTaRS; MTIF2; human.
DR GeneWiki; MTIF2; -.
DR GenomeRNAi; 4528; -.
DR Pharos; P46199; Tbio.
DR PRO; PR:P46199; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P46199; protein.
DR Bgee; ENSG00000085760; Expressed in esophagus squamous epithelium and 213 other tissues.
DR ExpressionAtlas; P46199; baseline and differential.
DR Genevisible; P46199; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:HGNC-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; ISS:HGNC-UCL.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0070124; P:mitochondrial translational initiation; ISS:BHF-UCL.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR GO; GO:0032790; P:ribosome disassembly; ISS:BHF-UCL.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Initiation factor; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..727
FT /note="Translation initiation factor IF-2, mitochondrial"
FT /id="PRO_0000014480"
FT DOMAIN 178..348
FT /note="tr-type G"
FT REGION 187..194
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 212..216
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 234..237
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 288..291
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 324..326
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 187..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 234..237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 288..291
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 688
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91YJ5"
FT VARIANT 59
FT /note="T -> N (in dbSNP:rs1056445)"
FT /evidence="ECO:0000269|PubMed:12932832,
FT ECO:0000269|PubMed:7829522"
FT /id="VAR_054428"
FT VARIANT 556
FT /note="V -> I (in dbSNP:rs11357)"
FT /evidence="ECO:0000269|PubMed:12932832,
FT ECO:0000269|PubMed:7829522"
FT /id="VAR_014883"
SQ SEQUENCE 727 AA; 81317 MW; AD2951AF3A5EB9E6 CRC64;
MNQKLLKLEN LLRFHTIYRQ LHSLCQRRAL RQWRHGFSSA YPVWTAQLCA WPWPTDVLTG
AALSQYRLLV TKKEEGPWKS QLSSTKSKKV VEVWIGMTIE ELARAMEKNT DYVYEALLNT
DIDIDSLEAD SHLDEVWIKE VITKAGMKLK WSKLKQDKVR KNKDAVRRPQ ADPALLTPRS
PVVTIMGHVD HGKTTLLDKF RKTQVAAVET GGITQHIGAF LVSLPSGEKI TFLDTPGHAA
FSAMRARGAQ VTDIVVLVVA ADDGVMKQTV ESIQHAKDAQ VPIILAVNKC DKAEADPEKV
KKELLAYDVV CEDYGGDVQA VPVSALTGDN LMALAEATVA LAEMLELKAD PNGPVEGTVI
ESFTDKGRGL VTTAIIQRGT LRKGSVLVAG KCWAKVRLMF DENGKTIDEA YPSMPVGITG
WRDLPSAGEE ILEVESEPRA REVVDWRKYE QEQEKGQEDL KIIEEKRKEH KEAHQKAREK
YGHLLWKKRS ILRFLERKEQ IPLKPKEKRE RDSNVLSVII KGDVDGSVEA ILNIIDTYDA
SHECELELVH FGVGDVSAND VNLAETFDGV IYGFNVNAGN VIQQSAAKKG VKIKLHKIIY
RLVEDLQEEL SSRLPCAVEE HPVGEASILA TFSVTEGKKK VPVAGCRVQK GQLEKQKKFK
LTRNGHVIWK GSLTSLKHHK DDISIVKTGM DCGLSLDEDN MEFQVGDRIV CYEEKQIQAK
TSWDPGF
