Q9NTK5 (OLA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Obg-like ATPase 1
EC=3.6.3.-

Alternative name(s):
GTP-binding protein 9

Gene names

Name:	OLA1
Synonyms:	GTPBP9
ORF Names:	PTD004, PRO2455

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Monomer. Ref.9
Sequence similarities	Belongs to the GTP1/OBG family. Contains 1 G (guanine nucleotide-binding) domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP catabolic process Inferred from direct assay Ref.9. Source: HGNC
Cellular component	cytoplasm Inferred from direct assay. Source: LIFEdb
Molecular function	ATP binding Inferred from direct assay Ref.9. Source: HGNC GTP binding Inferred from electronic annotation. Source: InterPro hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NTK5-1)

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.

Isoform 2 (identifier: Q9NTK5-2)

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

Isoform 3 (identifier: Q9NTK5-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

Obg-like ATPase 1

PRO_0000122456

Regions

Domain

34 – 158

125

G

Nucleotide binding

32 – 37

6

ATP

Sites

Binding site

231

1

ATP; via carbonyl oxygen

Amino acid modifications

Modified residue

216

1

N6-acetyllysine Ref.7

Modified residue

242

1

N6-acetyllysine Ref.7

Modified residue

294

1

N6-acetyllysine Ref.7

Natural variations

Alternative sequence

1 – 158

158

Missing in isoform 2.

VSP_002049

Alternative sequence

245 – 278

34

IKIKE…LSAEE → LESTDNKAEIILLKMEILSS SNLTHLNNRRRNKI in isoform 3.

VSP_002050

Alternative sequence

279 – 396

118

Missing in isoform 3.

VSP_002051

Natural variant

168

1

E → Q in a breast cancer sample; somatic mutation. Ref.10

VAR_036613

Experimental info

Mutagenesis

127

1

F → A: Loss of ATP-binding. Ref.9

Mutagenesis

230

1

N → A: Loss of ATP-binding. Ref.9

Mutagenesis

231 – 233

3

LSE → KSD: Retention of ATP-binding specificity. Ref.9

Sequence conflict

33

1

V → A in BAB55174. Ref.5

Sequence conflict

97

1

V → A in AAD44500. Ref.3

Sequence conflict

254

1

Y → C in CAB66481. Ref.2

Sequence conflict

391

1

Q → R in AAF71123. Ref.4

Secondary structure

1

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396

Helix Strand Turn

Details...

Beta strand

19 – 21

3

Beta strand

25 – 28

4

Beta strand

31 – 34

4

Helix

35 – 43

9

Beta strand

60 – 65

6

Helix

69 – 78

10

Beta strand

81 – 84

4

Beta strand

87 – 92

6

Helix

109 – 115

7

Beta strand

117 – 125

9

Helix

142 – 165

24

Helix

182 – 192

11

Helix

200 – 202

3

Helix

208 – 217

10

Helix

220 – 222

3

Beta strand

225 – 230

6

Helix

233 – 238

6

Helix

242 – 254

13

Beta strand

259 – 263

5

Helix

265 – 273

9

Helix

276 – 285

10

Helix

292 – 302

11

Beta strand

305 – 322

18

Helix

327 – 332

6

Helix

337 – 341

5

Beta strand

342 – 348

7

Helix

350 – 356

7

Helix

359 – 364

6

Beta strand

369 – 371

3

Beta strand

382 – 387

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2002. Version 2. Checksum: 4C7629BFC27CBEB2	FASTA	396	44,744
	10 20 30 40 50 60 MPPKKGGDGI KPPPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTNSQASAE NFPFCTIDPN 70 80 90 100 110 120 ESRVPVPDER FDFLCQYHKP ASKIPAFLNV VDIAGLVKGA HNGQGLGNAF LSHISACDGI 130 140 150 160 170 180 FHLTRAFEDD DITHVEGSVD PIRDIEIIHE ELQLKDEEMI GPIIDKLEKV AVRGGDKKLK 190 200 210 220 230 240 PEYDIMCKVK SWVIDQKKPV RFYHDWNDKE IEVLNKHLFL TSKPMVYLVN LSEKDYIRKK 250 260 270 280 290 300 NKWLIKIKEW VDKYDPGALV IPFSGALELK LQELSAEERQ KYLEANMTQS ALPKIIKAGF 310 320 330 340 350 360 AALQLEYFFT AGPDEVRAWT IRKGTKAPQA AGKIHTDFEK GFIMAEVMKY EDFKEEGSEN 370 380 390 AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQPKKK
	Isoform 2 [UniParc]. Checksum: 33A74AFEC0331464	FASTA	238	27,584
	10 20 30 40 50 60 MIGPIIDKLE KVAVRGGDKK LKPEYDIMCK VKSWVIDQKK PVRFYHDWND KEIEVLNKHL 70 80 90 100 110 120 FLTSKPMVYL VNLSEKDYIR KKNKWLIKIK EWVDKYDPGA LVIPFSGALE LKLQELSAEE 130 140 150 160 170 180 RQKYLEANMT QSALPKIIKA GFAALQLEYF FTAGPDEVRA WTIRKGTKAP QAAGKIHTDF 190 200 210 220 230 EKGFIMAEVM KYEDFKEEGS ENAVKAAGKY RQQGRNYIVE DGDIIFFKFN TPQQPKKK
	Isoform 3 [UniParc]. Checksum: DDB37373907EB18D	FASTA	278	31,440
	10 20 30 40 50 60 MPPKKGGDGI KPPPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTNSQASAE NFPFCTIDPN 70 80 90 100 110 120 ESRVPVPDER FDFLCQYHKP ASKIPAFLNV VDIAGLVKGA HNGQGLGNAF LSHISACDGI 130 140 150 160 170 180 FHLTRAFEDD DITHVEGSVD PIRDIEIIHE ELQLKDEEMI GPIIDKLEKV AVRGGDKKLK 190 200 210 220 230 240 PEYDIMCKVK SWVIDQKKPV RFYHDWNDKE IEVLNKHLFL TSKPMVYLVN LSEKDYIRKK 250 260 270 NKWLLESTDN KAEIILLKME ILSSSNLTHL NNRRRNKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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).
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Amygdala.
[3]	"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.
[4]	"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.
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Teratocarcinoma.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Brain, Ovary, Testis and Urinary bladder.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216; LYS-242 AND LYS-294, MASS SPECTROMETRY.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"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: 17430889] [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.
[10]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-168.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
BC012842 mRNA. Translation: AAH12842.1.
BC013925 mRNA. Translation: AAH13925.1.
BC029376 mRNA. Translation: AAH29376.1.
BC091522 mRNA. Translation: AAH91522.1.

IPI

IPI00216105.
IPI00216106.
IPI00290416.

PIR

T46901.

RefSeq

NP_001011708.1. NM_001011708.1.
NP_037473.3. NM_013341.3.

UniGene

Hs.157351.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OHF	X-ray	2.70	A	1-396	[»]

ProteinModelPortal

Q9NTK5.

SMR

Q9NTK5. Positions 16-388.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NTK5. 4 interactions.

MINT

MINT-1407274.

STRING

Q9NTK5.

PTM databases

PhosphoSite

Q9NTK5.

Polymorphism databases

DMDM

25453240.

2D gel databases

OGP

Q9NTK5.

UCD-2DPAGE

Q9NTK5.

Proteomic databases

PRIDE

Q9NTK5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000284719; ENSP00000284719; ENSG00000138430.
ENST00000409546; ENSP00000386350; ENSG00000138430.

GeneID

29789.

KEGG

hsa:29789.

UCSC

uc002uih.1. human.
uc010fqr.1. human.

Organism-specific databases

CTD

29789.

GeneCards

GC02M174937.

H-InvDB

HIX0020292.

HGNC

HGNC:28833. OLA1.

HPA

HPA035790.

MIM

611175. gene.

neXtProt

NX_Q9NTK5.

PharmGKB

PA162398388.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000000673.

HOVERGEN

HBG031861.

InParanoid

Q9NTK5.

OrthoDB

EOG4C2H9M.

PhylomeDB

Q9NTK5.

Gene expression databases

ArrayExpress

Q9NTK5.

Bgee

Q9NTK5.

CleanEx

HS_OLA1.

Genevestigator

Q9NTK5.

GermOnline

ENSG00000138430. Homo sapiens.

Family and domain databases

InterPro

IPR012675. Beta-grasp_ferredoxin-type.
IPR004396. CHP00092.
IPR013029. DUF933.
IPR006073. GTP_binding_domain.
IPR012676. TGS-like.
IPR023192. TGS-like_dom.
[Graphical view]

Gene3D

G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
G3DSA:1.10.150.300. G3DSA:1.10.150.300. 1 hit.

KO

K06942.

Pfam

PF01926. MMR_HSR1. 1 hit.
PF06071. YchF-GTPase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF006641. CHP00092. 1 hit.

PRINTS

PR00326. GTP1OBG.

SUPFAM

SSF81271. TGS-like. 1 hit.

TIGRFAMs

TIGR00092. TIGR00092. 1 hit.

ProtoNet

Search...

Other

NextBio

52323.

SOURCE

Search...

Entry information

Entry name

OLA1_HUMAN

Accession

Primary (citable) accession number: Q9NTK5
Secondary accession number(s): Q5BJD7 , Q8NCI8, Q96CU1, Q96SV2, Q9P1D3, Q9UNY9, Q9Y6G4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	November 25, 2002
Last modified:	January 25, 2012
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.