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Protein

Obg-like ATPase 1

Gene

Ola1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.UniRule annotation

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361MagnesiumBy similarity
Metal bindingi56 – 561MagnesiumBy similarity
Binding sitei231 – 2311ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 376ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Obg-like ATPase 1UniRule annotation
Alternative name(s):
GTP-binding protein 9
Gene namesi
Name:Ola1
Synonyms:Gtpbp9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914309. Ola1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation
  • Nucleusnucleolus UniRule annotation

  • Note: Predominantly cytoplasmic, shuttles between the nucleus and the cytoplasm.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Obg-like ATPase 1PRO_0000122457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei294 – 2941N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9CZ30.
MaxQBiQ9CZ30.
PaxDbiQ9CZ30.
PRIDEiQ9CZ30.

2D gel databases

REPRODUCTION-2DPAGEIPI00227836.

PTM databases

iPTMnetiQ9CZ30.
PhosphoSiteiQ9CZ30.
SwissPalmiQ9CZ30.

Expressioni

Gene expression databases

BgeeiQ9CZ30.
CleanExiMM_OLA1.
ExpressionAtlasiQ9CZ30. baseline and differential.
GenevisibleiQ9CZ30. MM.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi211910. 2 interactions.
IntActiQ9CZ30. 3 interactions.
MINTiMINT-1866446.
STRINGi10090.ENSMUSP00000028517.

Structurei

3D structure databases

ProteinModelPortaliQ9CZ30.
SMRiQ9CZ30. Positions 16-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 283261OBG-type GAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi267 – 2748Nuclear export signalUniRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG1491. Eukaryota.
COG0012. LUCA.
GeneTreeiENSGT00390000000673.
HOVERGENiHBG031861.
InParanoidiQ9CZ30.
KOiK19788.
OMAiLRFEDWN.
OrthoDBiEOG7X3QQF.
PhylomeDBiQ9CZ30.
TreeFamiTF300774.

Family and domain databases

Gene3Di1.10.150.300. 1 hit.
3.10.20.30. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00944. YchF_OLA1_ATPase.
InterProiIPR004396. ATPase_YchF/OLA1.
IPR012675. Beta-grasp_dom.
IPR013029. DUF933.
IPR031167. G_OBG.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR012676. TGS-like.
IPR023192. TGS-like_dom.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
PF06071. YchF-GTPase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006641. CHP00092. 1 hit.
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00092. TIGR00092. 1 hit.
PROSITEiPS51710. G_OBG. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9CZ30-1) [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
MPPKKGGDGI KPPPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTNSQASAE
60 70 80 90 100
NFPFCTIDPN ESRVPVPDER FDFLCQYHKP ASKIPAFLNV VDIAGLVKGA
110 120 130 140 150
HNGQGLGNAF LSHISACDGI FHLTRAFEDD DITHVEGSVD PIRDIEIIHE
160 170 180 190 200
ELQLKDEEMI GPILDKLEKV AVRGGDKKLK PEYDIMCKVK SWVIDQKKPV
210 220 230 240 250
RFYHDWNDKE IEVLNKHLFL TSKPMVYLVN LSEKDYIRKK NKWLIKIKEW
260 270 280 290 300
VDKYDPGALV IPFSGALELK LQELSAEERQ KYLEANMTQS ALPKIIKAGF
310 320 330 340 350
AALQLEYFFT AGPDEVRAWT IRKGTKAPQA AGKIHTDFEK GFIMAEVMKY
360 370 380 390
EDFKDEGSEN AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQPKKK
Length:396
Mass (Da):44,730
Last modified:June 1, 2001 - v1
Checksum:iCBBC54481E9B20CB
GO
Isoform 2 (identifier: Q9CZ30-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     243-270: WLIKIKEWVDKYDPGALVIPFSGALELK → CNFKFLSSGDGILVHIMRTMIIEVYLSL
     271-396: Missing.

Note: No experimental confirmation available.
Show »
Length:270
Mass (Da):30,376
Checksum:i266F143D1FAFC8FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221H → Y in BAB31566 (PubMed:16141072).Curated
Sequence conflicti358 – 3581S → Y in BAB27201 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei243 – 27028WLIKI…ALELK → CNFKFLSSGDGILVHIMRTM IIEVYLSL in isoform 2. 1 PublicationVSP_002054Add
BLAST
Alternative sequencei271 – 396126Missing in isoform 2. 1 PublicationVSP_002055Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010817 mRNA. Translation: BAB27201.1.
AK013055 mRNA. Translation: BAB28624.1.
AK017803 mRNA. No translation available.
AK019142 mRNA. Translation: BAB31566.1.
BX284615, AL928608 Genomic DNA. Translation: CAM17550.1.
BX284615, AL928608 Genomic DNA. Translation: CAM17551.1.
AL928608, BX284615 Genomic DNA. Translation: CAM19352.1.
AL928608, BX284615 Genomic DNA. Translation: CAM19354.1.
BC011318 mRNA. Translation: AAH11318.1.
BC029207 mRNA. Translation: AAH29207.1.
CCDSiCCDS16124.1. [Q9CZ30-1]
CCDS16125.1. [Q9CZ30-2]
RefSeqiNP_080218.1. NM_025942.2. [Q9CZ30-1]
NP_084367.1. NM_030091.1. [Q9CZ30-2]
UniGeneiMm.22661.

Genome annotation databases

EnsembliENSMUST00000028517; ENSMUSP00000028517; ENSMUSG00000027108. [Q9CZ30-1]
ENSMUST00000100015; ENSMUSP00000097592; ENSMUSG00000027108. [Q9CZ30-2]
GeneIDi67059.
KEGGimmu:67059.
UCSCiuc008kcg.1. mouse. [Q9CZ30-1]
uc008kch.1. mouse. [Q9CZ30-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010817 mRNA. Translation: BAB27201.1.
AK013055 mRNA. Translation: BAB28624.1.
AK017803 mRNA. No translation available.
AK019142 mRNA. Translation: BAB31566.1.
BX284615, AL928608 Genomic DNA. Translation: CAM17550.1.
BX284615, AL928608 Genomic DNA. Translation: CAM17551.1.
AL928608, BX284615 Genomic DNA. Translation: CAM19352.1.
AL928608, BX284615 Genomic DNA. Translation: CAM19354.1.
BC011318 mRNA. Translation: AAH11318.1.
BC029207 mRNA. Translation: AAH29207.1.
CCDSiCCDS16124.1. [Q9CZ30-1]
CCDS16125.1. [Q9CZ30-2]
RefSeqiNP_080218.1. NM_025942.2. [Q9CZ30-1]
NP_084367.1. NM_030091.1. [Q9CZ30-2]
UniGeneiMm.22661.

3D structure databases

ProteinModelPortaliQ9CZ30.
SMRiQ9CZ30. Positions 16-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211910. 2 interactions.
IntActiQ9CZ30. 3 interactions.
MINTiMINT-1866446.
STRINGi10090.ENSMUSP00000028517.

PTM databases

iPTMnetiQ9CZ30.
PhosphoSiteiQ9CZ30.
SwissPalmiQ9CZ30.

2D gel databases

REPRODUCTION-2DPAGEIPI00227836.

Proteomic databases

EPDiQ9CZ30.
MaxQBiQ9CZ30.
PaxDbiQ9CZ30.
PRIDEiQ9CZ30.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028517; ENSMUSP00000028517; ENSMUSG00000027108. [Q9CZ30-1]
ENSMUST00000100015; ENSMUSP00000097592; ENSMUSG00000027108. [Q9CZ30-2]
GeneIDi67059.
KEGGimmu:67059.
UCSCiuc008kcg.1. mouse. [Q9CZ30-1]
uc008kch.1. mouse. [Q9CZ30-2]

Organism-specific databases

CTDi29789.
MGIiMGI:1914309. Ola1.

Phylogenomic databases

eggNOGiKOG1491. Eukaryota.
COG0012. LUCA.
GeneTreeiENSGT00390000000673.
HOVERGENiHBG031861.
InParanoidiQ9CZ30.
KOiK19788.
OMAiLRFEDWN.
OrthoDBiEOG7X3QQF.
PhylomeDBiQ9CZ30.
TreeFamiTF300774.

Miscellaneous databases

PROiQ9CZ30.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CZ30.
CleanExiMM_OLA1.
ExpressionAtlasiQ9CZ30. baseline and differential.
GenevisibleiQ9CZ30. MM.

Family and domain databases

Gene3Di1.10.150.300. 1 hit.
3.10.20.30. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00944. YchF_OLA1_ATPase.
InterProiIPR004396. ATPase_YchF/OLA1.
IPR012675. Beta-grasp_dom.
IPR013029. DUF933.
IPR031167. G_OBG.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR012676. TGS-like.
IPR023192. TGS-like_dom.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
PF06071. YchF-GTPase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006641. CHP00092. 1 hit.
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00092. TIGR00092. 1 hit.
PROSITEiPS51710. G_OBG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Embryo, Embryonic liver and Embryonic stem cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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).
    Strain: Czech II.
    Tissue: Mammary gland.
  4. Lubec G., Kang S.U., Oh J.-E., Yang J.-W., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 71-98; 99-125; 247-253 AND 350-363.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiOLA1_MOUSE
AccessioniPrimary (citable) accession number: Q9CZ30
Secondary accession number(s): B1AYJ8
, B1AYK0, Q9CWE2, Q9CX91, Q9CYC9, Q9CZ56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.