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Q9H4K7 (GTPB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP-binding protein 5
Alternative name(s):
Protein obg homolog 1
Short name=ObgH1
Gene names
Name:GTPBP5
Synonyms:OBGH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the ribosome maturation process. Plays a role of GTPase in vitro. When missing, mitochondria elongation and abnormal nuclear morphology are observed. Ref.5

Subcellular location

Mitochondrion Ref.5.

Sequence similarities

Belongs to the GTP1/OBG family.

Contains 1 G (guanine nucleotide-binding) domain.

Sequence caution

The sequence BAA91783.1 differs from that shown. Reason: Erroneous termination at position 402. Translated as Gln.

Ontologies

Keywords
   Biological processRibosome biogenesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from electronic annotation. Source: GOC

ribosome biogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406GTP-binding protein 5
PRO_0000205429

Regions

Domain236 – 346111G
Nucleotide binding231 – 2388GTP Potential
Nucleotide binding278 – 2825GTP Potential
Nucleotide binding345 – 3484GTP Potential
Region15 – 406392Localized in the mitochondria
Region30 – 406377Not localized in the mitochondria

Natural variations

Natural variant471G → S.
Corresponds to variant rs6062133 [ dbSNP | Ensembl ].
VAR_033983
Natural variant931H → R.
Corresponds to variant rs11700220 [ dbSNP | Ensembl ].
VAR_049299
Natural variant3371A → V.
Corresponds to variant rs35693261 [ dbSNP | Ensembl ].
VAR_049300

Sequences

Sequence LengthMass (Da)Tools
Q9H4K7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 08756F661F79DDBB

FASTA40643,955
        10         20         30         40         50         60 
MAPARCFSAR LRTVFQGVGH WALSTWAGLK PSRLLPQRAS PRLLSVGRAD LAKHQELPGK 

        70         80         90        100        110        120 
KLLSEKKLKR YFVDYRRVLV CGGNGGAGAS CFHSEPRKEF GGPDGGDGGN GGHVILRVDQ 

       130        140        150        160        170        180 
QVKSLSSVLS RYQGFSGEDG GSKNCFGRSG AVLYIRVPVG TLVKEGGRVV ADLSCVGDEY 

       190        200        210        220        230        240 
IAALGGAGGK GNRFFLANNN RAPVTCTPGQ PGQQRVLHLE LKTVAHAGMV GFPNAGKSSL 

       250        260        270        280        290        300 
LRAISNARPA VASYPFTTLK PHVGIVHYEG HLQIAVADIP GIIRGAHQNR GLGSAFLRHI 

       310        320        330        340        350        360 
ERCRFLLFVV DLSQPEPWTQ VDDLKYELEM YEKGLSARPH AIVANKIDLP EAQANLSQLR 

       370        380        390        400 
DHLGQEVIVL SALTGENLEQ LLLHLKVLYD AYAEAELGQG RQPLRW 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [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].
Tissue: Muscle.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-406.
Tissue: Testis.
[5]"Human small G proteins, ObgH1, and ObgH2, participate in the maintenance of mitochondria and nucleolar architectures."
Hirano Y., Ohniwa R.L., Wada C., Yoshimura S.H., Takeyasu K.
Genes Cells 11:1295-1304(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, REGION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001603 mRNA. Translation: BAA91783.1. Different termination.
AL078633 Genomic DNA. Translation: CAC04015.1.
BC007885 mRNA. No translation available.
BC036716 mRNA. Translation: AAH36716.1.
AL117498 mRNA. Translation: CAB55963.1.
IPIIPI00878209.
PIRT17273.
RefSeqNP_056481.1. NM_015666.3.
UniGeneHs.340636.

3D structure databases

ProteinModelPortalQ9H4K7.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000359859.

PTM databases

PhosphoSiteQ9H4K7.

Polymorphism databases

DMDM32469779.

Proteomic databases

PaxDbQ9H4K7.
PRIDEQ9H4K7.

Protocols and materials databases

DNASU26164.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370823; ENSP00000359859; ENSG00000101181.
GeneID26164.
KEGGhsa:26164.
UCSCuc002yce.4. human.

Organism-specific databases

CTD26164.
GeneCardsGC20P060758.
HGNCHGNC:16239. GTPBP5.
HPAHPA047379.
MIM610919. gene.
neXtProtNX_Q9H4K7.
PharmGKBPA29059.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0536.
HOGENOMHOG000019084.
HOVERGENHBG051857.
InParanoidQ9H4K7.
KOK03979.
OMASCVGDEY.
OrthoDBEOG4BZN33.
PhylomeDBQ9H4K7.

Gene expression databases

ArrayExpressQ9H4K7.
BgeeQ9H4K7.
CleanExHS_GTPBP5.
GenevestigatorQ9H4K7.
GermOnlineENSG00000101181. Homo sapiens.

Family and domain databases

Gene3D2.70.210.12. 1 hit.
InterProIPR014100. GTP-bd_Obg/CgtA.
IPR006169. GTP1_OBG_dom.
IPR006073. GTP_binding_domain.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PANTHERPTHR11702:SF3. PTHR11702:SF3. 1 hit.
PfamPF01018. GTP1_OBG. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
PIRSFPIRSF002401. GTP_bd_Obg/CgtA. 1 hit.
PRINTSPR00326. GTP1OBG.
SUPFAMSSF82051. GTP1_OBG_sub. 1 hit.
TIGRFAMsTIGR02729. Obg_CgtA. 1 hit.
TIGR00231. small_GTP. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi26164.
NextBio48263.
SOURCESearch...

Entry information

Entry nameGTPB5_HUMAN
AccessionPrimary (citable) accession number: Q9H4K7
Secondary accession number(s): A6NDR3 expand/collapse secondary AC list , Q96I17, Q9NVG9, Q9UFR4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: March 1, 2001
Last modified: May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families