OLA1_HUMAN
ID OLA1_HUMAN Reviewed; 396 AA.
AC Q9NTK5; D7EHM2; Q5BJD7; Q8NCI8; Q96CU1; Q96SV2; Q9P1D3; Q9UNY9; Q9Y6G4;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
DE AltName: Full=DNA damage-regulated overexpressed in cancer 45;
DE Short=DOC45;
DE AltName: Full=GTP-binding protein 9;
GN Name=OLA1 {ECO:0000255|HAMAP-Rule:MF_03167}; Synonyms=GTPBP9;
GN ORFNames=PRO2455, PTD004;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 putative
RT 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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 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 deduced by
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, SUBUNIT,
RP 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., Kostrewa D.,
RA Kutay U., Kambach C.;
RT "Human OLA1 defines an ATPase subfamily in the Obg family of GTP-binding
RT proteins.";
RL J. Biol. Chem. 282:19928-19937(2007).
RN [14]
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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal 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. {ECO:0000255|HAMAP-
CC Rule:MF_03167}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01047};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03167,
CC ECO:0000269|PubMed:17430889}.
CC -!- INTERACTION:
CC Q9NTK5; PRO_0000038593 [P04591]: gag; Xeno; NbExp=4; IntAct=EBI-766468, EBI-6179719;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03167,
CC ECO:0000269|PubMed:20053727}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03167,
CC ECO:0000269|PubMed:20053727}. Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03167, ECO:0000269|PubMed:20053727}. Note=Predominantly
CC cytoplasmic, shuttles between the nucleus and the cytoplasm.
CC {ECO:0000255|HAMAP-Rule:MF_03167}.
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 -!- TISSUE SPECIFICITY: Expressed in all tissues tested but its expression
CC is more abundant in testis, liver, lung, and brain. Overexpressed in
CC several malignancies, including cancers of the colon, rectum, ovary,
CC lung, stomach, and uterus.
CC -!- INDUCTION: Strongly down-regulated by DNA damage-inducing agents.
CC {ECO:0000269|PubMed:20053727}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03167}.
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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 CCDS; CCDS2255.1; -. [Q9NTK5-1]
DR CCDS; CCDS42779.1; -. [Q9NTK5-2]
DR PIR; T46901; T46901.
DR RefSeq; NP_001011708.1; NM_001011708.2. [Q9NTK5-2]
DR RefSeq; NP_037473.3; NM_013341.4. [Q9NTK5-1]
DR PDB; 2OHF; X-ray; 2.70 A; A=1-396.
DR PDBsum; 2OHF; -.
DR AlphaFoldDB; Q9NTK5; -.
DR SMR; Q9NTK5; -.
DR BioGRID; 118917; 91.
DR DIP; DIP-34591N; -.
DR IntAct; Q9NTK5; 27.
DR MINT; Q9NTK5; -.
DR STRING; 9606.ENSP00000284719; -.
DR ChEMBL; CHEMBL4105704; -.
DR GlyGen; Q9NTK5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NTK5; -.
DR MetOSite; Q9NTK5; -.
DR PhosphoSitePlus; Q9NTK5; -.
DR SwissPalm; Q9NTK5; -.
DR BioMuta; OLA1; -.
DR DMDM; 25453240; -.
DR OGP; Q9NTK5; -.
DR UCD-2DPAGE; Q9NTK5; -.
DR EPD; Q9NTK5; -.
DR jPOST; Q9NTK5; -.
DR MassIVE; Q9NTK5; -.
DR MaxQB; Q9NTK5; -.
DR PaxDb; Q9NTK5; -.
DR PeptideAtlas; Q9NTK5; -.
DR PRIDE; Q9NTK5; -.
DR ProteomicsDB; 82622; -. [Q9NTK5-1]
DR ProteomicsDB; 82623; -. [Q9NTK5-2]
DR ProteomicsDB; 82624; -. [Q9NTK5-3]
DR Antibodypedia; 19452; 293 antibodies from 27 providers.
DR DNASU; 29789; -.
DR Ensembl; ENST00000284719.8; ENSP00000284719.3; ENSG00000138430.16. [Q9NTK5-1]
DR Ensembl; ENST00000344357.9; ENSP00000340167.5; ENSG00000138430.16. [Q9NTK5-2]
DR Ensembl; ENST00000428402.6; ENSP00000410385.2; ENSG00000138430.16. [Q9NTK5-3]
DR GeneID; 29789; -.
DR KEGG; hsa:29789; -.
DR MANE-Select; ENST00000284719.8; ENSP00000284719.3; NM_013341.5; NP_037473.3.
DR UCSC; uc002uih.4; human. [Q9NTK5-1]
DR CTD; 29789; -.
DR DisGeNET; 29789; -.
DR GeneCards; OLA1; -.
DR HGNC; HGNC:28833; OLA1.
DR HPA; ENSG00000138430; Low tissue specificity.
DR MIM; 611175; gene.
DR neXtProt; NX_Q9NTK5; -.
DR OpenTargets; ENSG00000138430; -.
DR PharmGKB; PA162398388; -.
DR VEuPathDB; HostDB:ENSG00000138430; -.
DR eggNOG; KOG1491; Eukaryota.
DR GeneTree; ENSGT00390000000673; -.
DR HOGENOM; CLU_018395_1_0_1; -.
DR InParanoid; Q9NTK5; -.
DR OrthoDB; 738371at2759; -.
DR PhylomeDB; Q9NTK5; -.
DR TreeFam; TF300774; -.
DR PathwayCommons; Q9NTK5; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q9NTK5; -.
DR BioGRID-ORCS; 29789; 173 hits in 1078 CRISPR screens.
DR ChiTaRS; OLA1; human.
DR EvolutionaryTrace; Q9NTK5; -.
DR GeneWiki; OLA1; -.
DR GenomeRNAi; 29789; -.
DR Pharos; Q9NTK5; Tchem.
DR PRO; PR:Q9NTK5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NTK5; protein.
DR Bgee; ENSG00000138430; Expressed in cervix squamous epithelium and 210 other tissues.
DR ExpressionAtlas; Q9NTK5; baseline and differential.
DR Genevisible; Q9NTK5; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IDA:HGNC-UCL.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046034; P:ATP metabolic process; IDA:BHF-UCL.
DR CDD; cd04867; TGS_YchF_OLA1; 1.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 1.10.150.300; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom_sf.
DR InterPro; IPR013029; YchF_C.
DR InterPro; IPR041706; YchF_N.
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.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..396
FT /note="Obg-like ATPase 1"
FT /id="PRO_0000122456"
FT DOMAIN 23..283
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 304..387
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT MOTIF 267..274
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT BINDING 32..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17430889"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17430889"
FT MOD_RES 294
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.5"
FT /id="VSP_002049"
FT VAR_SEQ 245..278
FT /note="IKIKEWVDKYDPGALVIPFSGALELKLQELSAEE -> LESTDNKAEIILLK
FT MEILSSSNLTHLNNRRRNKI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_002050"
FT VAR_SEQ 279..396
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_002051"
FT VARIANT 168
FT /note="E -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036613"
FT MUTAGEN 127
FT /note="F->A: Loss of ATP-binding."
FT /evidence="ECO:0000269|PubMed:17430889"
FT MUTAGEN 230
FT /note="N->A: Loss of ATP-binding."
FT /evidence="ECO:0000269|PubMed:17430889"
FT MUTAGEN 231..233
FT /note="LSE->KSD: Retention of ATP-binding specificity."
FT /evidence="ECO:0000269|PubMed:17430889"
FT CONFLICT 33
FT /note="V -> A (in Ref. 6; BAB55174)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="V -> A (in Ref. 4; AAD44500)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="Y -> C (in Ref. 3; CAB66481)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="Q -> R (in Ref. 5; AAF71123)"
FT /evidence="ECO:0000305"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 142..165
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 305..322
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:2OHF"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:2OHF"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:2OHF"
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
