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Protein

Mitochondrial ribosome-associated GTPase 1

Gene

MTG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity. Displays mitochondrial GTPase activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei205 – 2051GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi83 – 864GTPBy similarity
Nucleotide bindingi153 – 1586GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • regulation of mitochondrial translation Source: UniProtKB
  • regulation of respiratory system process Source: UniProtKB
  • ribosome biogenesis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial ribosome-associated GTPase 1
Alternative name(s):
GTP-binding protein 7
Mitochondrial GTPase 1
Gene namesi
Name:MTG1
Synonyms:GTPBP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:32159. MTG1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB
  • mitochondrial ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671306.

Polymorphism and mutation databases

BioMutaiMTG1.
DMDMi134034174.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 334Mitochondrial ribosome-associated GTPase 1PRO_0000280262
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiQ9BT17.
MaxQBiQ9BT17.
PaxDbiQ9BT17.
PRIDEiQ9BT17.

PTM databases

iPTMnetiQ9BT17.
PhosphoSiteiQ9BT17.

Expressioni

Gene expression databases

BgeeiQ9BT17.
CleanExiHS_MTG1.
ExpressionAtlasiQ9BT17. baseline and differential.
GenevisibleiQ9BT17. HS.

Organism-specific databases

HPAiHPA037826.
HPA037827.

Interactioni

Subunit structurei

Associates with the mitochondrial ribosome large subunit; the association occurs in a GTP-dependent manner (PubMed:23396448).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRNPP041561EBI-2602570,EBI-977302

Protein-protein interaction databases

BioGridi124916. 14 interactions.
IntActiQ9BT17. 2 interactions.
MINTiMINT-1431727.
STRINGi9606.ENSP00000323047.

Structurei

3D structure databases

ProteinModelPortaliQ9BT17.
SMRiQ9BT17. Positions 34-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 209174CP-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily.PROSITE-ProRule annotation
Contains 1 CP-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2485. Eukaryota.
COG1161. LUCA.
GeneTreeiENSGT00500000044923.
HOGENOMiHOG000003790.
HOVERGENiHBG059228.
InParanoidiQ9BT17.
KOiK19828.
OMAiDCIIEIH.
PhylomeDBiQ9BT17.

Family and domain databases

Gene3Di1.10.1580.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR030378. G_CP_dom.
IPR023179. GTP-bd_ortho_bundle.
IPR019991. GTP-bd_ribosome_bgen.
IPR006073. GTP_binding_domain.
IPR016478. GTPase_MTG1.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
PIRSFiPIRSF006230. MG442. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03596. GTPase_YlqF. 1 hit.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BT17-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRLTPRALCS AAQAAWRENF PLCGRDVARW FPGHMAKGLK KMQSSLKLVD
60 70 80 90 100
CIIEVHDARI PLSGRNPLFQ ETLGLKPHLL VLNKMDLADL TEQQKIMQHL
110 120 130 140 150
EGEGLKNVIF TNCVKDENVK QIIPMVTELI GRSHRYHRKE NLEYCIMVIG
160 170 180 190 200
VPNVGKSSLI NSLRRQHLRK GKATRVGGEP GITRAVMSKI QVSERPLMFL
210 220 230 240 250
LDTPGVLAPR IESVETGLKL ALCGTVLDHL VGEETMADYL LYTLNKHQRF
260 270 280 290 300
GYVQHYGLGS ACDNVERVLK SVAVKLGKTQ KVKVLTGTGN VNIIQPNYPA
310 320 330
AARDFLQTFR RGLLGSVMLD LDVLRGHPPA ETLP
Length:334
Mass (Da):37,237
Last modified:March 20, 2007 - v2
Checksum:iCEE3812DA5B588DA
GO
Isoform 2 (identifier: Q9BT17-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     193-267: SERPLMFLLD...LGSACDNVER → ESSGARPSTL...GRHAVFPISR
     268-334: Missing.

Note: No experimental confirmation available.
Show »
Length:267
Mass (Da):29,743
Checksum:i03DA2DED20220435
GO

Sequence cautioni

The sequence AAH04409.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH35721.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti293 – 2931I → V.1 Publication
Corresponds to variant rs2255246 [ dbSNP | Ensembl ].
VAR_062181

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei193 – 26775SERPL…DNVER → ESSGARPSTLSRALQASGTC RPLCGFRLLTTLPSPPLSVP AEHPRGRHCPCPYSTVVIVF APNLWGRHAVFPISR in isoform 2. 1 PublicationVSP_023581Add
BLAST
Alternative sequencei268 – 33467Missing in isoform 2. 1 PublicationVSP_023582Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074976 mRNA. Translation: BAC11327.1.
AL360181, AL161645 Genomic DNA. Translation: CAH70289.1.
AL161645, AL360181 Genomic DNA. Translation: CAH70046.1.
BC000920 mRNA. Translation: AAH00920.1.
BC004409 mRNA. Translation: AAH04409.1. Different initiation.
BC026039 mRNA. Translation: AAH26039.1.
BC035721 mRNA. Translation: AAH35721.1. Different initiation.
CCDSiCCDS31320.1. [Q9BT17-1]
RefSeqiNP_612393.2. NM_138384.2. [Q9BT17-1]
UniGeneiHs.501578.

Genome annotation databases

EnsembliENST00000317502; ENSP00000323047; ENSG00000148824. [Q9BT17-1]
GeneIDi92170.
KEGGihsa:92170.
UCSCiuc001lnd.4. human. [Q9BT17-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074976 mRNA. Translation: BAC11327.1.
AL360181, AL161645 Genomic DNA. Translation: CAH70289.1.
AL161645, AL360181 Genomic DNA. Translation: CAH70046.1.
BC000920 mRNA. Translation: AAH00920.1.
BC004409 mRNA. Translation: AAH04409.1. Different initiation.
BC026039 mRNA. Translation: AAH26039.1.
BC035721 mRNA. Translation: AAH35721.1. Different initiation.
CCDSiCCDS31320.1. [Q9BT17-1]
RefSeqiNP_612393.2. NM_138384.2. [Q9BT17-1]
UniGeneiHs.501578.

3D structure databases

ProteinModelPortaliQ9BT17.
SMRiQ9BT17. Positions 34-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124916. 14 interactions.
IntActiQ9BT17. 2 interactions.
MINTiMINT-1431727.
STRINGi9606.ENSP00000323047.

PTM databases

iPTMnetiQ9BT17.
PhosphoSiteiQ9BT17.

Polymorphism and mutation databases

BioMutaiMTG1.
DMDMi134034174.

Proteomic databases

EPDiQ9BT17.
MaxQBiQ9BT17.
PaxDbiQ9BT17.
PRIDEiQ9BT17.

Protocols and materials databases

DNASUi92170.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317502; ENSP00000323047; ENSG00000148824. [Q9BT17-1]
GeneIDi92170.
KEGGihsa:92170.
UCSCiuc001lnd.4. human. [Q9BT17-1]

Organism-specific databases

CTDi92170.
GeneCardsiMTG1.
H-InvDBHIX0079269.
HGNCiHGNC:32159. MTG1.
HPAiHPA037826.
HPA037827.
neXtProtiNX_Q9BT17.
PharmGKBiPA142671306.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2485. Eukaryota.
COG1161. LUCA.
GeneTreeiENSGT00500000044923.
HOGENOMiHOG000003790.
HOVERGENiHBG059228.
InParanoidiQ9BT17.
KOiK19828.
OMAiDCIIEIH.
PhylomeDBiQ9BT17.

Miscellaneous databases

GeneWikiiMTG1.
GenomeRNAii92170.
NextBioi77622.
PROiQ9BT17.

Gene expression databases

BgeeiQ9BT17.
CleanExiHS_MTG1.
ExpressionAtlasiQ9BT17. baseline and differential.
GenevisibleiQ9BT17. HS.

Family and domain databases

Gene3Di1.10.1580.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR030378. G_CP_dom.
IPR023179. GTP-bd_ortho_bundle.
IPR019991. GTP-bd_ribosome_bgen.
IPR006073. GTP_binding_domain.
IPR016478. GTPase_MTG1.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
PIRSFiPIRSF006230. MG442. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03596. GTPase_YlqF. 1 hit.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Teratocarcinoma.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [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] (ISOFORM 1), VARIANT VAL-293.
    Tissue: Ovary, Pancreas, Placenta and Skin.
  4. "MTG1 codes for a conserved protein required for mitochondrial translation."
    Barrientos A., Korr D., Barwell K.J., Sjulsen C., Gajewski C.D., Manfredi G., Ackerman S., Tzagoloff A.
    Mol. Biol. Cell 14:2292-2302(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION, SUBCELLULAR LOCATION.
  5. "Human G-proteins, ObgH1 and Mtg1, associate with the large mitochondrial ribosome subunit and are involved in translation and assembly of respiratory complexes."
    Kotani T., Akabane S., Takeyasu K., Ueda T., Takeuchi N.
    Nucleic Acids Res. 41:3713-3722(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH MITOCHONDRIAL RIBOSOME LARGE SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMTG1_HUMAN
AccessioniPrimary (citable) accession number: Q9BT17
Secondary accession number(s): Q5VWX8
, Q6PIY9, Q8IYJ4, Q8NC48, Q9BVU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: April 13, 2016
This is version 120 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 10
    Human chromosome 10: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.