MTG2_HUMAN
ID MTG2_HUMAN Reviewed; 406 AA.
AC Q9H4K7; A6NDR3; B4DR85; Q96I17; Q9NVG9; Q9UFR4;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Mitochondrial ribosome-associated GTPase 2;
DE AltName: Full=GTP-binding protein 5;
DE AltName: Full=Protein obg homolog 1;
DE Short=ObgH1;
GN Name=MTG2; Synonyms=GTPBP5, OBGH1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., 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., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., 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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-406 (ISOFORM 1/2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=17054726; DOI=10.1111/j.1365-2443.2006.01017.x;
RA Hirano Y., Ohniwa R.L., Wada C., Yoshimura S.H., Takeyasu K.;
RT "Human small G proteins, ObgH1, and ObgH2, participate in the maintenance
RT of mitochondria and nucleolar architectures.";
RL Genes Cells 11:1295-1304(2006).
RN [7]
RP FUNCTION, ASSOCIATION WITH MITOCHONDRIAL RIBOSOME LARGE SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23396448; DOI=10.1093/nar/gkt079;
RA Kotani T., Akabane S., Takeyasu K., Ueda T., Takeuchi N.;
RT "Human G-proteins, ObgH1 and Mtg1, associate with the large mitochondrial
RT ribosome subunit and are involved in translation and assembly of
RT respiratory complexes.";
RL Nucleic Acids Res. 41:3713-3722(2013).
CC -!- FUNCTION: Plays a role in the regulation of the mitochondrial ribosome
CC assembly and of translational activity. Displays GTPase activity.
CC Involved in the ribosome maturation process.
CC {ECO:0000269|PubMed:17054726, ECO:0000269|PubMed:23396448}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Associates with the mitochondrial ribosome large subunit; the
CC association occurs in a GTP-dependent manner.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane;
CC Peripheral membrane protein; Matrix side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4K7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4K7-2; Sequence=VSP_056672;
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91783.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK001603; BAA91783.1; ALT_TERM; mRNA.
DR EMBL; AK299147; BAG61197.1; -; mRNA.
DR EMBL; AK316027; BAH14398.1; -; mRNA.
DR EMBL; AK316325; BAH14696.1; -; mRNA.
DR EMBL; AL078633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75386.1; -; Genomic_DNA.
DR EMBL; BC007885; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC036716; AAH36716.1; -; mRNA.
DR EMBL; AL117498; CAB55963.1; -; mRNA.
DR CCDS; CCDS13492.1; -. [Q9H4K7-1]
DR PIR; T17273; T17273.
DR RefSeq; NP_056481.1; NM_015666.3. [Q9H4K7-1]
DR RefSeq; XP_005260450.1; XM_005260393.1.
DR RefSeq; XP_011527078.1; XM_011528776.1. [Q9H4K7-1]
DR RefSeq; XP_016883295.1; XM_017027806.1. [Q9H4K7-1]
DR PDB; 7O9K; EM; 3.10 A; G=1-406.
DR PDB; 7ODT; EM; 3.10 A; t=1-406.
DR PDB; 7OF5; EM; 2.90 A; x=1-406.
DR PDB; 7OF7; EM; 2.50 A; x=1-406.
DR PDBsum; 7O9K; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF7; -.
DR AlphaFoldDB; Q9H4K7; -.
DR SMR; Q9H4K7; -.
DR BioGRID; 117590; 279.
DR IntAct; Q9H4K7; 22.
DR MINT; Q9H4K7; -.
DR STRING; 9606.ENSP00000359859; -.
DR iPTMnet; Q9H4K7; -.
DR PhosphoSitePlus; Q9H4K7; -.
DR BioMuta; MTG2; -.
DR DMDM; 32469779; -.
DR EPD; Q9H4K7; -.
DR jPOST; Q9H4K7; -.
DR MassIVE; Q9H4K7; -.
DR MaxQB; Q9H4K7; -.
DR PaxDb; Q9H4K7; -.
DR PeptideAtlas; Q9H4K7; -.
DR PRIDE; Q9H4K7; -.
DR ProteomicsDB; 4933; -.
DR ProteomicsDB; 80850; -. [Q9H4K7-1]
DR Antibodypedia; 29445; 139 antibodies from 26 providers.
DR DNASU; 26164; -.
DR Ensembl; ENST00000370823.8; ENSP00000359859.3; ENSG00000101181.18. [Q9H4K7-1]
DR GeneID; 26164; -.
DR KEGG; hsa:26164; -.
DR MANE-Select; ENST00000370823.8; ENSP00000359859.3; NM_015666.4; NP_056481.1.
DR UCSC; uc002yce.5; human. [Q9H4K7-1]
DR CTD; 26164; -.
DR DisGeNET; 26164; -.
DR GeneCards; MTG2; -.
DR HGNC; HGNC:16239; MTG2.
DR HPA; ENSG00000101181; Low tissue specificity.
DR MIM; 610919; gene.
DR neXtProt; NX_Q9H4K7; -.
DR OpenTargets; ENSG00000101181; -.
DR PharmGKB; PA29059; -.
DR VEuPathDB; HostDB:ENSG00000101181; -.
DR eggNOG; KOG1489; Eukaryota.
DR GeneTree; ENSGT00940000157379; -.
DR HOGENOM; CLU_011747_2_3_1; -.
DR InParanoid; Q9H4K7; -.
DR OMA; VVFDWEP; -.
DR OrthoDB; 1150635at2759; -.
DR PhylomeDB; Q9H4K7; -.
DR TreeFam; TF314774; -.
DR PathwayCommons; Q9H4K7; -.
DR SignaLink; Q9H4K7; -.
DR BioGRID-ORCS; 26164; 327 hits in 1046 CRISPR screens.
DR ChiTaRS; MTG2; human.
DR GenomeRNAi; 26164; -.
DR Pharos; Q9H4K7; Tbio.
DR PRO; PR:Q9H4K7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H4K7; protein.
DR Bgee; ENSG00000101181; Expressed in cerebellar hemisphere and 155 other tissues.
DR ExpressionAtlas; Q9H4K7; baseline and differential.
DR Genevisible; Q9H4K7; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005761; C:mitochondrial ribosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0070129; P:regulation of mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0044065; P:regulation of respiratory system process; IMP:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd01898; Obg; 1.
DR Gene3D; 2.70.210.12; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01454; GTPase_Obg; 1.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR InterPro; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF01018; GTP1_OBG; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTP-binding; Magnesium; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Ribosome biogenesis;
KW Translation regulation.
FT CHAIN 1..406
FT /note="Mitochondrial ribosome-associated GTPase 2"
FT /id="PRO_0000205429"
FT DOMAIN 70..224
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 225..390
FT /note="OBG-type G"
FT REGION 15..406
FT /note="Localized in the mitochondria"
FT REGION 30..406
FT /note="Not localized in the mitochondria"
FT BINDING 231..238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 256..260
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 278..281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 345..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 371..373
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..228
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056672"
FT VARIANT 47
FT /note="G -> S (in dbSNP:rs6062133)"
FT /id="VAR_033983"
FT VARIANT 93
FT /note="H -> R (in dbSNP:rs11700220)"
FT /id="VAR_049299"
FT VARIANT 337
FT /note="A -> V (in dbSNP:rs35693261)"
FT /id="VAR_049300"
SQ SEQUENCE 406 AA; 43955 MW; 08756F661F79DDBB CRC64;
MAPARCFSAR LRTVFQGVGH WALSTWAGLK PSRLLPQRAS PRLLSVGRAD LAKHQELPGK
KLLSEKKLKR YFVDYRRVLV CGGNGGAGAS CFHSEPRKEF GGPDGGDGGN GGHVILRVDQ
QVKSLSSVLS RYQGFSGEDG GSKNCFGRSG AVLYIRVPVG TLVKEGGRVV ADLSCVGDEY
IAALGGAGGK GNRFFLANNN RAPVTCTPGQ PGQQRVLHLE LKTVAHAGMV GFPNAGKSSL
LRAISNARPA VASYPFTTLK PHVGIVHYEG HLQIAVADIP GIIRGAHQNR GLGSAFLRHI
ERCRFLLFVV DLSQPEPWTQ VDDLKYELEM YEKGLSARPH AIVANKIDLP EAQANLSQLR
DHLGQEVIVL SALTGENLEQ LLLHLKVLYD AYAEAELGQG RQPLRW
