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Protein

Obg-like ATPase 1

Gene

OLA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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+PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361MagnesiumPROSITE-ProRule annotation
Metal bindingi56 – 561MagnesiumPROSITE-ProRule annotation
Binding sitei231 – 2311ATP; via carbonyl oxygen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 376ATP1 Publication

GO - Molecular functioni

  • ATPase activity Source: BHF-UCL
  • ATP binding Source: HGNC
  • GTP binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • ribosomal large subunit binding Source: UniProtKB-HAMAP
  • ribosome binding Source: UniProtKB-HAMAP

GO - Biological processi

  • ATP metabolic process Source: BHF-UCL
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):
DNA damage-regulated overexpressed in cancer 45
Short name:
DOC45
GTP-binding protein 9
Gene namesi
Name:OLA1UniRule annotation
Synonyms:GTPBP9
ORF Names:PRO2455, PTD004
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:28833. OLA1.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication
  • Nucleus UniRule annotation1 Publication
  • Nucleusnucleolus UniRule annotation1 Publication

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

GO - Cellular componenti

  • centrosome Source: HPA
  • cytoplasm Source: LIFEdb
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271F → A: Loss of ATP-binding. 1 Publication
Mutagenesisi230 – 2301N → A: Loss of ATP-binding. 1 Publication
Mutagenesisi231 – 2333LSE → KSD: Retention of ATP-binding specificity. 1 Publication

Organism-specific databases

PharmGKBiPA162398388.

Polymorphism and mutation databases

BioMutaiOLA1.
DMDMi25453240.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Obg-like ATPase 1PRO_0000122456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei294 – 2941N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9NTK5.
MaxQBiQ9NTK5.
PaxDbiQ9NTK5.
PeptideAtlasiQ9NTK5.
PRIDEiQ9NTK5.

2D gel databases

OGPiQ9NTK5.
UCD-2DPAGEQ9NTK5.

PTM databases

iPTMnetiQ9NTK5.
PhosphoSiteiQ9NTK5.
SwissPalmiQ9NTK5.

Expressioni

Tissue specificityi

Expressed in all tissues tested but its expression is more abundant in testis, liver, lung, and brain. Overexpressed in several malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.

Inductioni

Strongly down-regulated by DNA damage-inducing agents.1 Publication

Gene expression databases

BgeeiQ9NTK5.
CleanExiHS_OLA1.
ExpressionAtlasiQ9NTK5. baseline and differential.
GenevisibleiQ9NTK5. HS.

Organism-specific databases

HPAiHPA035790.
HPA041443.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
gagP045914EBI-766468,EBI-6179719From a different organism.

Protein-protein interaction databases

BioGridi118917. 42 interactions.
IntActiQ9NTK5. 10 interactions.
MINTiMINT-1407274.
STRINGi9606.ENSP00000284719.

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 213Combined sources
Beta strandi25 – 284Combined sources
Beta strandi31 – 344Combined sources
Helixi35 – 439Combined sources
Beta strandi60 – 656Combined sources
Helixi69 – 7810Combined sources
Beta strandi81 – 844Combined sources
Beta strandi87 – 926Combined sources
Helixi109 – 1157Combined sources
Beta strandi117 – 1259Combined sources
Helixi142 – 16524Combined sources
Helixi182 – 19211Combined sources
Helixi200 – 2023Combined sources
Helixi208 – 21710Combined sources
Helixi220 – 2223Combined sources
Beta strandi225 – 2306Combined sources
Helixi233 – 2386Combined sources
Helixi242 – 25413Combined sources
Beta strandi259 – 2635Combined sources
Helixi265 – 2739Combined sources
Helixi276 – 28510Combined sources
Helixi292 – 30211Combined sources
Beta strandi305 – 32218Combined sources
Helixi327 – 3326Combined sources
Helixi337 – 3415Combined sources
Beta strandi342 – 3487Combined sources
Helixi350 – 3567Combined sources
Helixi359 – 3646Combined sources
Beta strandi369 – 3713Combined sources
Beta strandi382 – 3876Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OHFX-ray2.70A1-396[»]
ProteinModelPortaliQ9NTK5.
SMRiQ9NTK5. Positions 16-388.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NTK5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 283261OBG-type GPROSITE-ProRule annotationAdd
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
Contains 1 OBG-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1491. Eukaryota.
COG0012. LUCA.
GeneTreeiENSGT00390000000673.
HOVERGENiHBG031861.
InParanoidiQ9NTK5.
KOiK19788.
OrthoDBiEOG7X3QQF.
PhylomeDBiQ9NTK5.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NTK5-1) [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 GPIIDKLEKV 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
EDFKEEGSEN AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQPKKK
Length:396
Mass (Da):44,744
Last modified:November 25, 2002 - v2
Checksum:i4C7629BFC27CBEB2
GO
Isoform 2 (identifier: Q9NTK5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: Missing.

Show »
Length:238
Mass (Da):27,584
Checksum:i33A74AFEC0331464
GO
Isoform 3 (identifier: Q9NTK5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     245-278: IKIKEWVDKYDPGALVIPFSGALELKLQELSAEE → LESTDNKAEIILLKMEILSSSNLTHLNNRRRNKI
     279-396: Missing.

Note: No experimental confirmation available.
Show »
Length:278
Mass (Da):31,440
Checksum:iDDB37373907EB18D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331V → A in BAB55174 (PubMed:14702039).Curated
Sequence conflicti97 – 971V → A in AAD44500 (Ref. 4) Curated
Sequence conflicti254 – 2541Y → C in CAB66481 (PubMed:11230166).Curated
Sequence conflicti391 – 3911Q → R in AAF71123 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036613

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 158158Missing in isoform 2. 2 PublicationsVSP_002049Add
BLAST
Alternative sequencei245 – 27834IKIKE…LSAEE → LESTDNKAEIILLKMEILSS SNLTHLNNRRRNKI in isoform 3. 1 PublicationVSP_002050Add
BLAST
Alternative sequencei279 – 396118Missing in isoform 3. 1 PublicationVSP_002051Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ250006 mRNA. Translation: ABB72766.1.
AF134478 mRNA. Translation: AAP97255.1.
AL136546 mRNA. Translation: CAB66481.1.
AF078859 mRNA. Translation: AAD44491.1.
AF078868 mRNA. Translation: AAD44500.1.
AF116703 mRNA. Translation: AAF71123.1.
AK027523 mRNA. Translation: BAB55174.1.
AK074710 mRNA. Translation: BAC11153.1.
CH471058 Genomic DNA. Translation: EAX11151.1.
BC012842 mRNA. Translation: AAH12842.1.
BC013925 mRNA. Translation: AAH13925.1.
BC029376 mRNA. Translation: AAH29376.1.
BC091522 mRNA. Translation: AAH91522.1.
CCDSiCCDS2255.1. [Q9NTK5-1]
CCDS42779.1. [Q9NTK5-2]
PIRiT46901.
RefSeqiNP_001011708.1. NM_001011708.1. [Q9NTK5-2]
NP_037473.3. NM_013341.3. [Q9NTK5-1]
UniGeneiHs.157351.

Genome annotation databases

EnsembliENST00000284719; ENSP00000284719; ENSG00000138430. [Q9NTK5-1]
ENST00000344357; ENSP00000340167; ENSG00000138430. [Q9NTK5-2]
ENST00000428402; ENSP00000410385; ENSG00000138430. [Q9NTK5-3]
GeneIDi29789.
KEGGihsa:29789.
UCSCiuc002uih.4. human. [Q9NTK5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ250006 mRNA. Translation: ABB72766.1.
AF134478 mRNA. Translation: AAP97255.1.
AL136546 mRNA. Translation: CAB66481.1.
AF078859 mRNA. Translation: AAD44491.1.
AF078868 mRNA. Translation: AAD44500.1.
AF116703 mRNA. Translation: AAF71123.1.
AK027523 mRNA. Translation: BAB55174.1.
AK074710 mRNA. Translation: BAC11153.1.
CH471058 Genomic DNA. Translation: EAX11151.1.
BC012842 mRNA. Translation: AAH12842.1.
BC013925 mRNA. Translation: AAH13925.1.
BC029376 mRNA. Translation: AAH29376.1.
BC091522 mRNA. Translation: AAH91522.1.
CCDSiCCDS2255.1. [Q9NTK5-1]
CCDS42779.1. [Q9NTK5-2]
PIRiT46901.
RefSeqiNP_001011708.1. NM_001011708.1. [Q9NTK5-2]
NP_037473.3. NM_013341.3. [Q9NTK5-1]
UniGeneiHs.157351.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OHFX-ray2.70A1-396[»]
ProteinModelPortaliQ9NTK5.
SMRiQ9NTK5. Positions 16-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118917. 42 interactions.
IntActiQ9NTK5. 10 interactions.
MINTiMINT-1407274.
STRINGi9606.ENSP00000284719.

PTM databases

iPTMnetiQ9NTK5.
PhosphoSiteiQ9NTK5.
SwissPalmiQ9NTK5.

Polymorphism and mutation databases

BioMutaiOLA1.
DMDMi25453240.

2D gel databases

OGPiQ9NTK5.
UCD-2DPAGEQ9NTK5.

Proteomic databases

EPDiQ9NTK5.
MaxQBiQ9NTK5.
PaxDbiQ9NTK5.
PeptideAtlasiQ9NTK5.
PRIDEiQ9NTK5.

Protocols and materials databases

DNASUi29789.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284719; ENSP00000284719; ENSG00000138430. [Q9NTK5-1]
ENST00000344357; ENSP00000340167; ENSG00000138430. [Q9NTK5-2]
ENST00000428402; ENSP00000410385; ENSG00000138430. [Q9NTK5-3]
GeneIDi29789.
KEGGihsa:29789.
UCSCiuc002uih.4. human. [Q9NTK5-1]

Organism-specific databases

CTDi29789.
GeneCardsiOLA1.
HGNCiHGNC:28833. OLA1.
HPAiHPA035790.
HPA041443.
MIMi611175. gene.
neXtProtiNX_Q9NTK5.
PharmGKBiPA162398388.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1491. Eukaryota.
COG0012. LUCA.
GeneTreeiENSGT00390000000673.
HOVERGENiHBG031861.
InParanoidiQ9NTK5.
KOiK19788.
OrthoDBiEOG7X3QQF.
PhylomeDBiQ9NTK5.
TreeFamiTF300774.

Miscellaneous databases

ChiTaRSiOLA1. human.
EvolutionaryTraceiQ9NTK5.
GeneWikiiOLA1.
GenomeRNAii29789.
PROiQ9NTK5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NTK5.
CleanExiHS_OLA1.
ExpressionAtlasiQ9NTK5. baseline and differential.
GenevisibleiQ9NTK5. HS.

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. "DOC45, a novel DNA damage-regulated nucleocytoplasmic ATPase that is overexpressed in multiple human malignancies."
    Sun H., Luo X., Montalbano J., Jin W., Shi J., Sheikh M.S., Huang Y.
    Mol. Cancer Res. 8:57-66(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION.
  2. "Cloning of a new human cDNA homologous to Caenorhabditis elegans putative GTP-binding protein."
    Yue P., Yu L., Zhao S.Y.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala.
  4. "Human homologous yeast-44.2 protein, complete cds."
    Zhang Q., Huang Q., Song H., Peng J., Fu G., Mao M., Dai M., Mao Y., Zhou J., Chen Z., Chen J., Luo M., Hu R.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Pituitary tumor.
  5. "Functional prediction of the coding sequences of 121 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., Liu M., He F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal liver.
  6. "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] (ISOFORMS 1 AND 2).
    Tissue: Teratocarcinoma.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORMS 1 AND 3).
    Tissue: Brain, Ovary, Testis and Urinary bladder.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Human OLA1 defines an ATPase subfamily in the Obg family of GTP-binding proteins."
    Koller-Eichhorn R., Marquardt T., Gail R., Wittinghofer A., Kostrewa D., Kutay U., Kambach C.
    J. Biol. Chem. 282:19928-19937(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, SUBUNIT, MUTAGENESIS OF PHE-127; ASN-230 AND 231-LEU--GLU-233.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-168.

Entry informationi

Entry nameiOLA1_HUMAN
AccessioniPrimary (citable) accession number: Q9NTK5
Secondary accession number(s): D7EHM2
, Q5BJD7, Q8NCI8, Q96CU1, Q96SV2, Q9P1D3, Q9UNY9, Q9Y6G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: November 25, 2002
Last modified: July 6, 2016
This is version 155 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.