Full text data of OLA1
OLA1
(GTPBP9)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Obg-like ATPase 1 (DNA damage-regulated overexpressed in cancer 45; DOC45; GTP-binding protein 9)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Obg-like ATPase 1 (DNA damage-regulated overexpressed in cancer 45; DOC45; GTP-binding protein 9)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NTK5
ID OLA1_HUMAN Reviewed; 396 AA.
AC Q9NTK5; D7EHM2; Q5BJD7; Q8NCI8; Q96CU1; Q96SV2; Q9P1D3; Q9UNY9;
read moreAC Q9Y6G4;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Obg-like ATPase 1;
DE AltName: Full=DNA damage-regulated overexpressed in cancer 45;
DE Short=DOC45;
DE AltName: Full=GTP-binding protein 9;
GN Name=OLA1; Synonyms=GTPBP9; ORFNames=PRO2455, PTD004;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=20053727; DOI=10.1158/1541-7786.MCR-09-0278;
RA Sun H., Luo X., Montalbano J., Jin W., Shi J., Sheikh M.S., Huang Y.;
RT "DOC45, a novel DNA damage-regulated nucleocytoplasmic ATPase that is
RT overexpressed in multiple human malignancies.";
RL Mol. Cancer Res. 8:57-66(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yue P., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Caenorhabditis elegans
RT putative GTP-binding protein.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pituitary tumor;
RA Zhang Q., Huang Q., Song H., Peng J., Fu G., Mao M., Dai M., Mao Y.,
RA Zhou J., Chen Z., Chen J., Luo M., Hu R.;
RT "Human homologous yeast-44.2 protein, complete cds.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Ovary, Testis, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ATP ANALOG,
RP SUBUNIT, AND MUTAGENESIS OF PHE-127; ASN-230 AND 231-LEU--GLU-233.
RX PubMed=17430889; DOI=10.1074/jbc.M700541200;
RA Koller-Eichhorn R., Marquardt T., Gail R., Wittinghofer A.,
RA Kostrewa D., Kutay U., Kambach C.;
RT "Human OLA1 defines an ATPase subfamily in the Obg family of GTP-
RT binding proteins.";
RL J. Biol. Chem. 282:19928-19937(2007).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-168.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC efficiency. Has lower affinity for GTP.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P04591:gag (xeno); NbExp=4; IntAct=EBI-766468, EBI-6179719;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
CC Note=Predominantly cytoplasmic, shuttles between the nucleus and
CC the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NTK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTK5-2; Sequence=VSP_002049;
CC Name=3;
CC IsoId=Q9NTK5-3; Sequence=VSP_002050, VSP_002051;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested but its
CC expression is more abundant in testis, liver, lung, and brain.
CC Overexpressed in several malignancies, including cancers of the
CC colon, rectum, ovary, lung, stomach, and uterus.
CC -!- INDUCTION: Strongly down-regulated by DNA damage-inducing agents.
CC -!- SIMILARITY: Belongs to the GTP1/OBG family. YchF/OLA1 subfamily.
CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
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DR EMBL; DQ250006; ABB72766.1; -; mRNA.
DR EMBL; AF134478; AAP97255.1; -; mRNA.
DR EMBL; AL136546; CAB66481.1; -; mRNA.
DR EMBL; AF078859; AAD44491.1; -; mRNA.
DR EMBL; AF078868; AAD44500.1; -; mRNA.
DR EMBL; AF116703; AAF71123.1; -; mRNA.
DR EMBL; AK027523; BAB55174.1; -; mRNA.
DR EMBL; AK074710; BAC11153.1; -; mRNA.
DR EMBL; CH471058; EAX11151.1; -; Genomic_DNA.
DR EMBL; BC012842; AAH12842.1; -; mRNA.
DR EMBL; BC013925; AAH13925.1; -; mRNA.
DR EMBL; BC029376; AAH29376.1; -; mRNA.
DR EMBL; BC091522; AAH91522.1; -; mRNA.
DR PIR; T46901; T46901.
DR RefSeq; NP_001011708.1; NM_001011708.1.
DR RefSeq; NP_037473.3; NM_013341.3.
DR RefSeq; XP_005246538.1; XM_005246481.1.
DR UniGene; Hs.157351; -.
DR PDB; 2OHF; X-ray; 2.70 A; A=1-396.
DR PDBsum; 2OHF; -.
DR ProteinModelPortal; Q9NTK5; -.
DR SMR; Q9NTK5; 16-388.
DR IntAct; Q9NTK5; 8.
DR MINT; MINT-1407274; -.
DR STRING; 9606.ENSP00000284719; -.
DR PhosphoSite; Q9NTK5; -.
DR DMDM; 25453240; -.
DR OGP; Q9NTK5; -.
DR UCD-2DPAGE; Q9NTK5; -.
DR PaxDb; Q9NTK5; -.
DR PRIDE; Q9NTK5; -.
DR DNASU; 29789; -.
DR Ensembl; ENST00000284719; ENSP00000284719; ENSG00000138430.
DR Ensembl; ENST00000344357; ENSP00000340167; ENSG00000138430.
DR Ensembl; ENST00000428402; ENSP00000410385; ENSG00000138430.
DR GeneID; 29789; -.
DR KEGG; hsa:29789; -.
DR UCSC; uc002uih.3; human.
DR CTD; 29789; -.
DR GeneCards; GC02M174937; -.
DR HGNC; HGNC:28833; OLA1.
DR HPA; HPA035790; -.
DR MIM; 611175; gene.
DR neXtProt; NX_Q9NTK5; -.
DR PharmGKB; PA162398388; -.
DR eggNOG; COG0012; -.
DR HOVERGEN; HBG031861; -.
DR InParanoid; Q9NTK5; -.
DR KO; K06942; -.
DR OrthoDB; EOG7X3QQF; -.
DR PhylomeDB; Q9NTK5; -.
DR ChiTaRS; OLA1; human.
DR EvolutionaryTrace; Q9NTK5; -.
DR GeneWiki; OLA1; -.
DR GenomeRNAi; 29789; -.
DR NextBio; 52323; -.
DR PRO; PR:Q9NTK5; -.
DR ArrayExpress; Q9NTK5; -.
DR Bgee; Q9NTK5; -.
DR CleanEx; HS_OLA1; -.
DR Genevestigator; Q9NTK5; -.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:HGNC.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006200; P:ATP catabolic process; IDA:HGNC.
DR Gene3D; 1.10.150.300; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1; -.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom.
DR InterPro; IPR013029; DUF933.
DR InterPro; IPR006073; GTP_binding_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00092; TIGR00092; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus;
KW Polymorphism; Reference proteome.
FT CHAIN 1 396 Obg-like ATPase 1.
FT /FTId=PRO_0000122456.
FT DOMAIN 24 131 G.
FT NP_BIND 32 37 ATP.
FT MOTIF 267 274 Nuclear export signal (Potential).
FT BINDING 231 231 ATP; via carbonyl oxygen.
FT MOD_RES 294 294 N6-acetyllysine.
FT VAR_SEQ 1 158 Missing (in isoform 2).
FT /FTId=VSP_002049.
FT VAR_SEQ 245 278 IKIKEWVDKYDPGALVIPFSGALELKLQELSAEE -> LES
FT TDNKAEIILLKMEILSSSNLTHLNNRRRNKI (in
FT isoform 3).
FT /FTId=VSP_002050.
FT VAR_SEQ 279 396 Missing (in isoform 3).
FT /FTId=VSP_002051.
FT VARIANT 168 168 E -> Q (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036613.
FT MUTAGEN 127 127 F->A: Loss of ATP-binding.
FT MUTAGEN 230 230 N->A: Loss of ATP-binding.
FT MUTAGEN 231 233 LSE->KSD: Retention of ATP-binding
FT specificity.
FT CONFLICT 33 33 V -> A (in Ref. 6; BAB55174).
FT CONFLICT 97 97 V -> A (in Ref. 4; AAD44500).
FT CONFLICT 254 254 Y -> C (in Ref. 3; CAB66481).
FT CONFLICT 391 391 Q -> R (in Ref. 5; AAF71123).
FT STRAND 19 21
FT STRAND 25 28
FT STRAND 31 34
FT HELIX 35 43
FT STRAND 60 65
FT HELIX 69 78
FT STRAND 81 84
FT STRAND 87 92
FT HELIX 109 115
FT STRAND 117 125
FT HELIX 142 165
FT HELIX 182 192
FT HELIX 200 202
FT HELIX 208 217
FT HELIX 220 222
FT STRAND 225 230
FT HELIX 233 238
FT HELIX 242 254
FT STRAND 259 263
FT HELIX 265 273
FT HELIX 276 285
FT HELIX 292 302
FT STRAND 305 322
FT HELIX 327 332
FT HELIX 337 341
FT STRAND 342 348
FT HELIX 350 356
FT HELIX 359 364
FT STRAND 369 371
FT STRAND 382 387
SQ SEQUENCE 396 AA; 44744 MW; 4C7629BFC27CBEB2 CRC64;
MPPKKGGDGI KPPPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTNSQASAE NFPFCTIDPN
ESRVPVPDER FDFLCQYHKP ASKIPAFLNV VDIAGLVKGA HNGQGLGNAF LSHISACDGI
FHLTRAFEDD DITHVEGSVD PIRDIEIIHE ELQLKDEEMI GPIIDKLEKV AVRGGDKKLK
PEYDIMCKVK SWVIDQKKPV RFYHDWNDKE IEVLNKHLFL TSKPMVYLVN LSEKDYIRKK
NKWLIKIKEW VDKYDPGALV IPFSGALELK LQELSAEERQ KYLEANMTQS ALPKIIKAGF
AALQLEYFFT AGPDEVRAWT IRKGTKAPQA AGKIHTDFEK GFIMAEVMKY EDFKEEGSEN
AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQPKKK
//
ID OLA1_HUMAN Reviewed; 396 AA.
AC Q9NTK5; D7EHM2; Q5BJD7; Q8NCI8; Q96CU1; Q96SV2; Q9P1D3; Q9UNY9;
read moreAC Q9Y6G4;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Obg-like ATPase 1;
DE AltName: Full=DNA damage-regulated overexpressed in cancer 45;
DE Short=DOC45;
DE AltName: Full=GTP-binding protein 9;
GN Name=OLA1; Synonyms=GTPBP9; ORFNames=PRO2455, PTD004;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=20053727; DOI=10.1158/1541-7786.MCR-09-0278;
RA Sun H., Luo X., Montalbano J., Jin W., Shi J., Sheikh M.S., Huang Y.;
RT "DOC45, a novel DNA damage-regulated nucleocytoplasmic ATPase that is
RT overexpressed in multiple human malignancies.";
RL Mol. Cancer Res. 8:57-66(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yue P., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Caenorhabditis elegans
RT putative GTP-binding protein.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pituitary tumor;
RA Zhang Q., Huang Q., Song H., Peng J., Fu G., Mao M., Dai M., Mao Y.,
RA Zhou J., Chen Z., Chen J., Luo M., Hu R.;
RT "Human homologous yeast-44.2 protein, complete cds.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Ovary, Testis, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ATP ANALOG,
RP SUBUNIT, AND MUTAGENESIS OF PHE-127; ASN-230 AND 231-LEU--GLU-233.
RX PubMed=17430889; DOI=10.1074/jbc.M700541200;
RA Koller-Eichhorn R., Marquardt T., Gail R., Wittinghofer A.,
RA Kostrewa D., Kutay U., Kambach C.;
RT "Human OLA1 defines an ATPase subfamily in the Obg family of GTP-
RT binding proteins.";
RL J. Biol. Chem. 282:19928-19937(2007).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-168.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC efficiency. Has lower affinity for GTP.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P04591:gag (xeno); NbExp=4; IntAct=EBI-766468, EBI-6179719;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
CC Note=Predominantly cytoplasmic, shuttles between the nucleus and
CC the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NTK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTK5-2; Sequence=VSP_002049;
CC Name=3;
CC IsoId=Q9NTK5-3; Sequence=VSP_002050, VSP_002051;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested but its
CC expression is more abundant in testis, liver, lung, and brain.
CC Overexpressed in several malignancies, including cancers of the
CC colon, rectum, ovary, lung, stomach, and uterus.
CC -!- INDUCTION: Strongly down-regulated by DNA damage-inducing agents.
CC -!- SIMILARITY: Belongs to the GTP1/OBG family. YchF/OLA1 subfamily.
CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
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DR EMBL; DQ250006; ABB72766.1; -; mRNA.
DR EMBL; AF134478; AAP97255.1; -; mRNA.
DR EMBL; AL136546; CAB66481.1; -; mRNA.
DR EMBL; AF078859; AAD44491.1; -; mRNA.
DR EMBL; AF078868; AAD44500.1; -; mRNA.
DR EMBL; AF116703; AAF71123.1; -; mRNA.
DR EMBL; AK027523; BAB55174.1; -; mRNA.
DR EMBL; AK074710; BAC11153.1; -; mRNA.
DR EMBL; CH471058; EAX11151.1; -; Genomic_DNA.
DR EMBL; BC012842; AAH12842.1; -; mRNA.
DR EMBL; BC013925; AAH13925.1; -; mRNA.
DR EMBL; BC029376; AAH29376.1; -; mRNA.
DR EMBL; BC091522; AAH91522.1; -; mRNA.
DR PIR; T46901; T46901.
DR RefSeq; NP_001011708.1; NM_001011708.1.
DR RefSeq; NP_037473.3; NM_013341.3.
DR RefSeq; XP_005246538.1; XM_005246481.1.
DR UniGene; Hs.157351; -.
DR PDB; 2OHF; X-ray; 2.70 A; A=1-396.
DR PDBsum; 2OHF; -.
DR ProteinModelPortal; Q9NTK5; -.
DR SMR; Q9NTK5; 16-388.
DR IntAct; Q9NTK5; 8.
DR MINT; MINT-1407274; -.
DR STRING; 9606.ENSP00000284719; -.
DR PhosphoSite; Q9NTK5; -.
DR DMDM; 25453240; -.
DR OGP; Q9NTK5; -.
DR UCD-2DPAGE; Q9NTK5; -.
DR PaxDb; Q9NTK5; -.
DR PRIDE; Q9NTK5; -.
DR DNASU; 29789; -.
DR Ensembl; ENST00000284719; ENSP00000284719; ENSG00000138430.
DR Ensembl; ENST00000344357; ENSP00000340167; ENSG00000138430.
DR Ensembl; ENST00000428402; ENSP00000410385; ENSG00000138430.
DR GeneID; 29789; -.
DR KEGG; hsa:29789; -.
DR UCSC; uc002uih.3; human.
DR CTD; 29789; -.
DR GeneCards; GC02M174937; -.
DR HGNC; HGNC:28833; OLA1.
DR HPA; HPA035790; -.
DR MIM; 611175; gene.
DR neXtProt; NX_Q9NTK5; -.
DR PharmGKB; PA162398388; -.
DR eggNOG; COG0012; -.
DR HOVERGEN; HBG031861; -.
DR InParanoid; Q9NTK5; -.
DR KO; K06942; -.
DR OrthoDB; EOG7X3QQF; -.
DR PhylomeDB; Q9NTK5; -.
DR ChiTaRS; OLA1; human.
DR EvolutionaryTrace; Q9NTK5; -.
DR GeneWiki; OLA1; -.
DR GenomeRNAi; 29789; -.
DR NextBio; 52323; -.
DR PRO; PR:Q9NTK5; -.
DR ArrayExpress; Q9NTK5; -.
DR Bgee; Q9NTK5; -.
DR CleanEx; HS_OLA1; -.
DR Genevestigator; Q9NTK5; -.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:HGNC.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006200; P:ATP catabolic process; IDA:HGNC.
DR Gene3D; 1.10.150.300; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1; -.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom.
DR InterPro; IPR013029; DUF933.
DR InterPro; IPR006073; GTP_binding_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00092; TIGR00092; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus;
KW Polymorphism; Reference proteome.
FT CHAIN 1 396 Obg-like ATPase 1.
FT /FTId=PRO_0000122456.
FT DOMAIN 24 131 G.
FT NP_BIND 32 37 ATP.
FT MOTIF 267 274 Nuclear export signal (Potential).
FT BINDING 231 231 ATP; via carbonyl oxygen.
FT MOD_RES 294 294 N6-acetyllysine.
FT VAR_SEQ 1 158 Missing (in isoform 2).
FT /FTId=VSP_002049.
FT VAR_SEQ 245 278 IKIKEWVDKYDPGALVIPFSGALELKLQELSAEE -> LES
FT TDNKAEIILLKMEILSSSNLTHLNNRRRNKI (in
FT isoform 3).
FT /FTId=VSP_002050.
FT VAR_SEQ 279 396 Missing (in isoform 3).
FT /FTId=VSP_002051.
FT VARIANT 168 168 E -> Q (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036613.
FT MUTAGEN 127 127 F->A: Loss of ATP-binding.
FT MUTAGEN 230 230 N->A: Loss of ATP-binding.
FT MUTAGEN 231 233 LSE->KSD: Retention of ATP-binding
FT specificity.
FT CONFLICT 33 33 V -> A (in Ref. 6; BAB55174).
FT CONFLICT 97 97 V -> A (in Ref. 4; AAD44500).
FT CONFLICT 254 254 Y -> C (in Ref. 3; CAB66481).
FT CONFLICT 391 391 Q -> R (in Ref. 5; AAF71123).
FT STRAND 19 21
FT STRAND 25 28
FT STRAND 31 34
FT HELIX 35 43
FT STRAND 60 65
FT HELIX 69 78
FT STRAND 81 84
FT STRAND 87 92
FT HELIX 109 115
FT STRAND 117 125
FT HELIX 142 165
FT HELIX 182 192
FT HELIX 200 202
FT HELIX 208 217
FT HELIX 220 222
FT STRAND 225 230
FT HELIX 233 238
FT HELIX 242 254
FT STRAND 259 263
FT HELIX 265 273
FT HELIX 276 285
FT HELIX 292 302
FT STRAND 305 322
FT HELIX 327 332
FT HELIX 337 341
FT STRAND 342 348
FT HELIX 350 356
FT HELIX 359 364
FT STRAND 369 371
FT STRAND 382 387
SQ SEQUENCE 396 AA; 44744 MW; 4C7629BFC27CBEB2 CRC64;
MPPKKGGDGI KPPPIIGRFG TSLKIGIVGL PNVGKSTFFN VLTNSQASAE NFPFCTIDPN
ESRVPVPDER FDFLCQYHKP ASKIPAFLNV VDIAGLVKGA HNGQGLGNAF LSHISACDGI
FHLTRAFEDD DITHVEGSVD PIRDIEIIHE ELQLKDEEMI GPIIDKLEKV AVRGGDKKLK
PEYDIMCKVK SWVIDQKKPV RFYHDWNDKE IEVLNKHLFL TSKPMVYLVN LSEKDYIRKK
NKWLIKIKEW VDKYDPGALV IPFSGALELK LQELSAEERQ KYLEANMTQS ALPKIIKAGF
AALQLEYFFT AGPDEVRAWT IRKGTKAPQA AGKIHTDFEK GFIMAEVMKY EDFKEEGSEN
AVKAAGKYRQ QGRNYIVEDG DIIFFKFNTP QQPKKK
//
MIM
611175
*RECORD*
*FIELD* NO
611175
*FIELD* TI
*611175 OBG-LIKE ATPase 1; OLA1
;;GTP-BINDING PROTEIN 9; GTPBP9
*FIELD* TX
CLONING
read more
Koller-Eichhorn et al. (2007) identified human GTPBP9, which they called
OLA1, as the homolog of the E. coli P-loop NTPase YchF, a member of the
Obg-related family of GTPases belonging to the TRAFAC (translation
factors) class. The deduced 396-amino acid protein consists of an
N-terminal G domain, flanked on either side by an inserted coiled-coil,
and a C-terminal TGS domain.
GENE FUNCTION
Koller-Eichhorn et al. (2007) demonstrated that OLA1 binds and
hydrolyzes ATP more efficiently than GTP and thus is a member of a new
subclass of NTPases in the Obg family of GTPases. They showed that
members of this protein family from different species also have ATPase
activity and are not exclusively GTPases. By performing x-ray
crystallography with AMPPCP, a nonhydrolyzable analog of ATP,
Koller-Eichhorn et al. (2007) found that one cause of the altered
nucleotide specificity of this subclass of NTPases is a substitution of
a hydrophobic amino acid for a glutamine in all members of the Obg
family. They noted that the same substitution inactivates Ras-like
GTPases.
MAPPING
Scott (2007) mapped the GTPBP9 gene to chromosome 2q31.1 based on an
alignment of the GTPBP9 sequence (GenBank GENBANK AC013467) with the
genomic sequence (build 36.2).
*FIELD* RF
1. Koller-Eichhorn, R.; Marquardt, T.; Gail, R.; Wittinghofer, A.;
Kostrewa, D.; Kutay, U.; Kambach, C.: Human OLA1 defines an ATPase
subfamily in the OBG family of GTP-binding proteins. J. Biol. Chem. 282:
19928-19937, 2007.
2. Scott, A. F.: Personal Communication. Baltimore, Md. 6/29/2007.
*FIELD* CD
Alan F. Scott: 7/6/2007
*FIELD* ED
alopez: 08/26/2011
carol: 7/6/2007
*RECORD*
*FIELD* NO
611175
*FIELD* TI
*611175 OBG-LIKE ATPase 1; OLA1
;;GTP-BINDING PROTEIN 9; GTPBP9
*FIELD* TX
CLONING
read more
Koller-Eichhorn et al. (2007) identified human GTPBP9, which they called
OLA1, as the homolog of the E. coli P-loop NTPase YchF, a member of the
Obg-related family of GTPases belonging to the TRAFAC (translation
factors) class. The deduced 396-amino acid protein consists of an
N-terminal G domain, flanked on either side by an inserted coiled-coil,
and a C-terminal TGS domain.
GENE FUNCTION
Koller-Eichhorn et al. (2007) demonstrated that OLA1 binds and
hydrolyzes ATP more efficiently than GTP and thus is a member of a new
subclass of NTPases in the Obg family of GTPases. They showed that
members of this protein family from different species also have ATPase
activity and are not exclusively GTPases. By performing x-ray
crystallography with AMPPCP, a nonhydrolyzable analog of ATP,
Koller-Eichhorn et al. (2007) found that one cause of the altered
nucleotide specificity of this subclass of NTPases is a substitution of
a hydrophobic amino acid for a glutamine in all members of the Obg
family. They noted that the same substitution inactivates Ras-like
GTPases.
MAPPING
Scott (2007) mapped the GTPBP9 gene to chromosome 2q31.1 based on an
alignment of the GTPBP9 sequence (GenBank GENBANK AC013467) with the
genomic sequence (build 36.2).
*FIELD* RF
1. Koller-Eichhorn, R.; Marquardt, T.; Gail, R.; Wittinghofer, A.;
Kostrewa, D.; Kutay, U.; Kambach, C.: Human OLA1 defines an ATPase
subfamily in the OBG family of GTP-binding proteins. J. Biol. Chem. 282:
19928-19937, 2007.
2. Scott, A. F.: Personal Communication. Baltimore, Md. 6/29/2007.
*FIELD* CD
Alan F. Scott: 7/6/2007
*FIELD* ED
alopez: 08/26/2011
carol: 7/6/2007